混纺纱以及该混纺纱的织物和该织物的制造方法与流程

本发明涉及混纺纱、以及该混纺纱的织物和该织物的制造方法。
背景技术：
：作为再生纤维素纤维的人造丝、铜氨纤维、莱赛尔等纤维具有柔软的手感，因此进行针织或机织而形成织物，用于衣料用途等各种各样的用途中(例如，参照专利文献1)。现有技术文献专利文献专利文献1：日本专利第6162566号公报技术实现要素：发明所要解决的问题发明人等对于使用再生纤维素纤维的织物进行了各种各样的研究，结果获知存在下述情况：若被水润湿后干燥，则再生纤维素纤维的织物的弹力和硬挺度下降。为了防止这样的、再生纤维素纤维的织物的弹力和硬挺度的下降，考虑例如对织物实施防水或斥水涂敷等常规的防水加工。但是，这种情况下，存在损害再生纤维素纤维所具有的柔软的手感的可能性。本发明的目的在于，提供即使在将混纺纱用于织物的制造的情况下也能够制造减少了由湿润导致的弹力和硬挺度的下降的织物的混纺纱、以及该混纺纱的织物和该织物的制造方法。用于解决问题的方法本发明例如涉及以下的各发明。[1]一种混纺纱，其包含改造丝心蛋白纤维和再生纤维素纤维。[2]根据[1]所述的混纺纱，其中，上述改造丝心蛋白纤维的、由下式定义的收缩率超过7％。收缩率＝{1-(与水性介质接触之后的改造丝心蛋白纤维的长度/与水性介质接触之前的改造丝心蛋白纤维的长度)}×100(％)[3]根据[1]或[2]所述的混纺纱，其中，上述改造丝心蛋白纤维的量为5～40质量％。[4]根据[1]～[3]中任一项所述的混纺纱，其中，上述改造丝心蛋白纤维为改造蛛丝丝心蛋白纤维。[5]根据[1]～[4]中任一项所述的混纺纱，其中，上述再生纤维素纤维为莱赛尔纤维。[6]一种织物，其为[1]～[5]中任一项所述的混纺纱的织物。[7]一种织物的制造方法，其具备：对改造丝心蛋白纤维和再生纤维素纤维进行混纺而得到混纺纱的工序；以及对上述混纺纱进行针织或机织而得到未加工织物的工序。[8]根据[7]所述的制造方法，其中，上述改造丝心蛋白纤维的、由下式定义的收缩率超过7％。收缩率＝{1-(与水性介质接触之后的改造丝心蛋白纤维的长度/与水性介质接触之前的改造丝心蛋白纤维的长度)}×100(％)[9]根据[7]或[8]所述的制造方法，其中，进一步具备使上述未加工织物与水性介质接触而使上述未加工织物中含有的上述改造丝心蛋白纤维收缩的工序。[10]根据[7]～[9]中任一项所述的制造方法，其中，在得到上述混纺纱的上述工序中，以使上述混纺纱中的上述改造丝心蛋白纤维的量达到5～40质量％的方式对上述改造丝心蛋白纤维和上述再生纤维素纤维进行混纺。[11]根据[7]～[10]中任一项所述的制造方法，其中，上述改造丝心蛋白纤维为改造蛛丝丝心蛋白纤维。[12]根据[7]～[11]中任一项所述的制造方法，其中，上述再生纤维素纤维为莱赛尔纤维。[13]根据[1]～[5]中任一项所述的混纺纱、根据[6]所述的织物或根据[7]～[12]中任一项所述的制造方法，其中，上述改造丝心蛋白纤维包含改造丝心蛋白，上述改造丝心蛋白包含式1：[(a)n基序-rep]m所示的结构域序列，上述结构域序列具有与天然来源的丝心蛋白相比相当于缺失了至少一个或两个以上(a)n基序的、降低了(a)n基序的含量的氨基酸序列。[式1中，(a)n基序表示由2～27个氨基酸残基构成的氨基酸序列，且(a)n基序中的丙氨酸残基数相对于全部氨基酸残基数为83％以上。rep表示由10～200个氨基酸残基构成的氨基酸序列。m表示2～300的整数。两个以上存在的(a)n基序彼此可以为相同的氨基酸序列，也可以为不同的氨基酸序列。两个以上存在的rep彼此可以为相同的氨基酸序列，也可以为不同的氨基酸序列。][14]根据[13]所述的混纺纱、织物或制造方法，其中，上述结构域序列具有与天然来源的丝心蛋白相比相当于从n末端侧向c末端侧至少每1～3个(a)n基序中缺失了一个(a)n基序的氨基酸序列。[15]根据[13]所述的混纺纱、织物或制造方法，其中，上述结构域序列具有与天然来源的丝心蛋白相比相当于从n末端侧向c末端侧至少依次重复发生了两个连续的(a)n基序的缺失和一个(a)n基序的缺失的氨基酸序列。[16]根据[1]～[5]中任一项所述的混纺纱、根据[6]所述的织物或根据[7]～[12]中任一项所述的制造方法，其中，上述改造丝心蛋白纤维包含改造丝心蛋白，上述改造丝心蛋白包含式1：[(a)n基序-rep]m所示的结构域序列，从n末端侧向c末端侧将相邻的两个[(a)n基序-rep]单元的rep的氨基酸残基数依次进行比较，将设氨基酸残基数少的rep的氨基酸残基数为1时另一者的rep的氨基酸残基数之比为1.8～11.3的相邻的两个[(a)n基序-rep]单元的氨基酸残基数相加得到的合计值的最大值设为x、将上述结构域序列的总氨基酸残基数设为y时，x/y为50％以上。[式1中，(a)n基序表示由2～27个氨基酸残基构成的氨基酸序列，且(a)n基序中的丙氨酸残基数相对于全部氨基酸残基数为83％以上。rep表示由10～200个氨基酸残基构成的氨基酸序列。m表示2～300的整数。两个以上存在的(a)n基序彼此可以为相同的氨基酸序列，也可以为不同的氨基酸序列。两个以上存在的rep彼此可以为相同的氨基酸序列，也可以为不同的氨基酸序列。][17]根据[1]～[5]中任一项所述的混纺纱、根据[6]所述的织物或根据[7]～[12]中任一项所述的制造方法，其中，上述改造丝心蛋白纤维包含改造丝心蛋白，上述改造丝心蛋白包含式1：[(a)n基序-rep]m所示的结构域序列，上述结构域序列具有与天然来源的丝心蛋白相比相当于至少rep中的一个或两个以上甘氨酸残基被置换为了其他氨基酸残基的、降低了甘氨酸残基的含量的氨基酸序列。[式1中，(a)n基序表示由2～27个氨基酸残基构成的氨基酸序列，且(a)n基序中的丙氨酸残基数相对于全部氨基酸残基数为83％以上。rep表示由10～200个氨基酸残基构成的氨基酸序列。m表示2～300的整数。两个以上存在的(a)n基序彼此可以为相同的氨基酸序列，也可以为不同的氨基酸序列。两个以上存在的rep彼此可以为相同的氨基酸序列，也可以为不同的氨基酸序列。][18]根据[17]所述的混纺纱、织物或制造方法，其中，上述结构域序列具有与天然来源的丝心蛋白相比相当于在rep中的选自ggx和gpgxx(其中，x表示甘氨酸以外的氨基酸残基。)中的至少一个基序序列中至少一个或两个以上该基序序列中的一个甘氨酸残基被置换为了其他氨基酸残基的氨基酸序列。[19]根据[18]所述的混纺纱、织物或制造方法，其中，甘氨酸残基被置换为了其他氨基酸残基的基序序列的比例相对于全部基序序列为10％以上。[20]根据[1]～[5]中任一项所述的混纺纱、根据[6]所述的织物或根据[7]～[12]中任一项所述的制造方法，其中，上述改造丝心蛋白纤维包含改造丝心蛋白，上述改造丝心蛋白包含式1：[(a)n基序-rep]m所示的结构域序列，将从上述结构域序列中除去位于最靠c末端侧的(a)n基序至上述结构域序列的c末端为止的序列而得到的序列中的全部rep中含有的由xgx(其中，x表示甘氨酸以外的氨基酸残基。)构成的氨基酸序列的总氨基酸残基数设为z，将从上述结构域序列中除去位于最靠c末端侧的(a)n基序至上述结构域序列的c末端为止的序列而得到的序列中的总氨基酸残基数设为w时，z/w为50.9％以上。[式1中，(a)n基序表示由2～27个氨基酸残基构成的氨基酸序列，且(a)n基序中的丙氨酸残基数相对于全部氨基酸残基数为83％以上。rep表示由10～200个氨基酸残基构成的氨基酸序列。m表示2～300的整数。两个以上存在的(a)n基序彼此可以为相同的氨基酸序列，也可以为不同的氨基酸序列。两个以上存在的rep彼此可以为相同的氨基酸序列，也可以为不同的氨基酸序列。][21]根据[17]～[20]中任一项所述的混纺纱、织物或制造方法，其中，上述改造丝心蛋白具有与天然来源的丝心蛋白相比相当于在rep中的一个或两个以上甘氨酸残基被置换为了其他氨基酸残基的基础上、进一步置换、缺失、插入和/或添加了一个或两个以上氨基酸残基的氨基酸序列。[22]根据[1]～[5]中任一项所述的混纺纱、根据[6]所述的织物或根据[7]～[12]中任一项所述的制造方法，其中，上述改造丝心蛋白纤维包含改造丝心蛋白，上述改造丝心蛋白包含式1：[(a)n基序-rep]m所示的结构域序列，上述结构域序列具有与天然来源的丝心蛋白相比相当于rep中的一个或两个以上氨基酸残基被置换为了疏水性指数大的氨基酸残基、和/或在rep中插入了一个或两个以上疏水性指数大的氨基酸残基的、包含在局部疏水性指数大的区域的氨基酸序列。[式1中，(a)n基序表示由2～27个氨基酸残基构成的氨基酸序列，且(a)n基序中的丙氨酸残基数相对于全部氨基酸残基数为83％以上。rep表示由10～200个氨基酸残基构成的氨基酸序列。m表示2～300的整数。两个以上存在的(a)n基序彼此可以为相同的氨基酸序列，也可以为不同的氨基酸序列。两个以上存在的rep彼此可以为相同的氨基酸序列，也可以为不同的氨基酸序列。][23]根据[22]所述的混纺纱、织物或制造方法，其中，上述在局部疏水性指数大的区域由连续的2～4个氨基酸残基构成。[24]根据[22]或[23]所述的混纺纱、织物或制造方法，其中，上述疏水性指数大的氨基酸残基选自异亮氨酸(i)、缬氨酸(v)、亮氨酸(l)、苯丙氨酸(f)、半胱氨酸(c)、甲硫氨酸(m)和丙氨酸(a)。[25]根据[1]～[5]中任一项所述的混纺纱、根据[6]所述的织物或根据[7]～[12]中任一项所述的制造方法，其中，上述改造丝心蛋白纤维包含改造丝心蛋白，上述改造丝心蛋白包含式1：[(a)n基序-rep]m所示的结构域序列，将从上述结构域序列除去位于最靠c末端侧的(a)n基序至上述结构域序列的c末端为止的序列而得到的序列中含有的全部rep中连续的4个氨基酸残基的疏水性指数的平均值为2.6以上的区域中含有的氨基酸残基的总数设为p、将从上述结构域序列中除去位于最靠c末端侧的(a)n基序至上述结构域序列的c末端为止的序列而得到的序列中含有的氨基酸残基的总数设为q时，p/q为6.2％以上。[式1中，(a)n基序表示由2～27个氨基酸残基构成的氨基酸序列，且(a)n基序中的丙氨酸残基数相对于全部氨基酸残基数为83％以上。rep表示由10～200个氨基酸残基构成的氨基酸序列。m表示2～300的整数。两个以上存在的(a)n基序彼此可以为相同的氨基酸序列，也可以为不同的氨基酸序列。两个以上存在的rep彼此可以为相同的氨基酸序列，也可以为不同的氨基酸序列。][26]根据[22]～[25]中任一项所述的混纺纱、织物或制造方法，其中，上述改造丝心蛋白具有与天然来源的丝心蛋白相比相当于在rep中的一个或两个以上氨基酸残基被置换为了疏水性指数大的氨基酸残基和/或在rep中插入了一个或两个以上疏水性指数大的氨基酸残基的基础上、进一步置换、缺失、插入和/或添加了一个或两个以上氨基酸残基的氨基酸序列。[27]根据[1]～[5]中任一项所述的混纺纱、根据[6]所述的织物或根据[7]～[12]中任一项所述的制造方法，其中，上述改造丝心蛋白纤维包含改造丝心蛋白，上述改造丝心蛋白包含式1：[(a)n基序-rep]m或式2：[(a)n基序-rep]m-(a)n基序所示的结构域序列，上述结构域序列具有与天然来源的丝心蛋白相比相当于rep中的一个或两个以上谷氨酰胺残基发生了缺失或者被置换为了其他氨基酸残基的、降低了谷氨酰胺残基的含量的氨基酸序列。[式1和式2中，(a)n基序表示由2～27个氨基酸残基构成的氨基酸序列，且(a)n基序中的丙氨酸残基数相对于全部氨基酸残基数为80％以上。rep表示由10～200个氨基酸残基构成的氨基酸序列。m表示2～300的整数。两个以上存在的(a)n基序彼此可以为相同的氨基酸序列，也可以为不同的氨基酸序列。两个以上存在的rep彼此可以为相同的氨基酸序列，也可以为不同的氨基酸序列。][28]根据[27]所述的混纺纱、织物或制造方法，其中，上述改造丝心蛋白在rep中包含gpgxx(其中，x表示甘氨酸残基以外的氨基酸残基。)基序，gpgxx基序含有率为10％以上。[29]根据[27]或[28]所述的混纺纱、织物或制造方法，其中，上述改造丝心蛋白的谷氨酰胺残基含有率为9％以下。[30]根据[27]～[29]中任一项所述的混纺纱、织物或制造方法，其中，上述其他氨基酸残基为选自由异亮氨酸(i)、缬氨酸(v)、亮氨酸(l)、苯丙氨酸(f)、半胱氨酸(c)、甲硫氨酸(m)、丙氨酸(a)、甘氨酸(g)、苏氨酸(t)、丝氨酸(s)、色氨酸(w)、酪氨酸(y)、脯氨酸(p)和组氨酸(h)组成的组中的氨基酸残基。[31]根据[27]～[30]中任一项所述的混纺纱、织物或制造方法，其中，上述改造丝心蛋白的rep的疏水度为-0.8以上。[32]根据[27]～[31]中任一项所述的混纺纱、织物或制造方法，其中，上述改造丝心蛋白具有与天然来源的丝心蛋白相比相当于在rep中的一个或两个以上谷氨酰胺残基发生了缺失或者被置换为了其他氨基酸残基的基础上、进一步置换、缺失、插入和/或添加了一个或两个以上氨基酸残基的氨基酸序列。[33]根据[1]～[5]中任一项所述的混纺纱、根据[6]所述的织物或根据[7]～[12]中任一项所述的制造方法，其中，上述改造丝心蛋白纤维包含改造丝心蛋白，上述改造丝心蛋白具有26.0以上的极限氧指数(loi)值。[34]根据[1]～[5]中任一项所述的混纺纱、根据[6]所述的织物或根据[7]～[12]中任一项所述的制造方法，其中，上述改造丝心蛋白纤维包含改造丝心蛋白，上述改造丝心蛋白的根据下述式a求出的最高吸湿发热度超过0.025℃/g。式a：最高吸湿发热度＝{(将试样置于低湿度环境下直至试样温度达到平衡后转移到高湿度环境下之后的试样温度的最高值)-(将试样置于低湿度环境下直至试样温度达到平衡后转移到高湿度环境下时的试样温度)}(℃)/试样重量(g)[式a中，低湿度环境是指温度为20℃且相对湿度为40％的环境，高湿度环境是指温度为20℃且相对湿度为90％的环境。]发明效果根据本发明的混纺纱和方法，可以提供减少了由湿润导致的弹力和硬挺度的下降的织物。因此，根据本发明，可期待能够控制与弹力、硬挺度的下降相伴随的织物的垂坠性下降。另外，根据本发明，可以尽可能地维持再生纤维素纤维特有的优良手感。附图说明图1为示出改造丝心蛋白的结构域序列的一例的示意图。图2为示出天然来源的丝心蛋白的z/w(％)的值的分布的图。图3为示出天然来源的丝心蛋白的x/y(％)的值的分布的图。图4为示出改造丝心蛋白的结构域序列的一例的示意图。图5为示出改造丝心蛋白的结构域序列的一例的示意图。图6为示意性示出用于制造改造丝心蛋白长丝的纺丝装置的一例的说明图。图7为示出实施例中的针织物的照片。图8为示出比较例中的针织物的照片。图9为示出吸湿发热性试验的结果的一例的图。具体实施方式＜混纺纱＞本发明的一个方式涉及包含改造丝心蛋白纤维和再生纤维素纤维的混纺纱。改造丝心蛋白纤维包含后述的改造丝心蛋白作为主要成分，可以是长丝(长纤维)，也可以是短纤维(staple)。改造丝心蛋白纤维中可以包含改造丝心蛋白以外的蛋白质等改造丝心蛋白以外的成分和杂质。需要说明的是，本发明中，混纺纱中包含具有利用湿润后的干燥而进行收缩的特性的改造丝心蛋白纤维，因此，若使使用这样的混纺纱的织物湿润和干燥，则针织密度、机织密度等会由于改造丝心蛋白纤维的收缩而增大，其结果是可发挥上述的效果。改造丝心蛋白纤维的、后述的与水性介质接触时的收缩率可以为超过7％、15％以上、25％以上、32％以上、40％以上、48％以上、56％以上、64％以上或72％以上。收缩率通常为80％以下。在此，改造丝心蛋白纤维的收缩率由下式定义。收缩率＝{1-(与水性介质接触之后的改造丝心蛋白纤维的长度/与水性介质接触之前的改造丝心蛋白纤维的长度)}×100(％)改造丝心蛋白纤维可以为具有卷曲(crimp)的改造丝心蛋白卷曲纤维。卷曲的程度没有限制，卷曲数可以为例如10～100个/40mm，可以为20～40个/40mm。改造丝心蛋白纤维优选具有优良的阻燃性，极限氧指数(loi)值可以为18以上、20以上、22以上、24以上、26以上、28以上、29以上或30以上。本说明书中，loi值为基于日本“消防危50号(1995年5月31日)”中记载的“粉粒状或熔点低的合成树脂的试验方法”测得的值。在发挥充分的阻燃性的方面考虑，改造丝心蛋白纤维可以包含亲水性改造丝心蛋白、和/或可以包含疏水性指数的平均值(平均hi)为0以下的改造丝心蛋白。改造丝心蛋白纤维优选具有优良的吸湿发热性，根据下述式a求出的最高吸湿发热度可以超过0.025℃/g。在此，式a中的试样是指改造丝心蛋白纤维。式a：最高吸湿发热度＝{(将试样置于低湿度环境下直至试样温度达到平衡后转移到高湿度环境下之后的试样温度的最高值)-(将试样置于低湿度环境下直至试样温度达到平衡后转移到高湿度环境下时的试样温度)}(℃)/试样重量(g)[式a中，低湿度环境是指温度为20℃且相对湿度为40％的环境，高湿度环境是指温度为20℃且相对湿度为90％的环境。]改造丝心蛋白纤维的最高吸湿发热度可以为0.026℃/g以上、0.027℃/g以上、0.028℃/g以上、0.029℃/g以上、0.030℃/g以上、0.035℃/g以上或0.040℃/g以上。最高吸湿发热度的上限没有特别限制，通常为0.060℃/g以下。在发挥充分的吸湿发热性的方面考虑，改造丝心蛋白纤维可以包含疏水性改造丝心蛋白、和/或可以包含疏水性指数的平均值(平均hi)超过0的改造丝心蛋白。本实施方式的改造丝心蛋白纤维优选具有优良的保温性，按照下述式b求出的保温性指数可以为0.20以上。式b：保温性指数＝保温率(％)/试样的基重(g/m2)在此，本说明书中，保温率是指通过使用thermo-laboii型试验机(30cm/秒的有风下)的干接触法测得的保温率，是通过后述的参考例中记载的方法测得的值。本实施方式的改造丝心蛋白纤维的保温性指数可以为0.22以上，可以为0.24以上，可以为0.26以上，可以为0.28以上，可以为0.30以上，可以为0.32以上。保温性指数的上限没有特别限制，可以为例如0.60以下或0.40以下。再生纤维素纤维没有特别限制，可以为例如人造丝、铜氨纤维、莱赛尔、醋酸纤维等公知的再生纤维素的纤维。再生纤维素纤维中，从具有更柔软的手感和更高的强度的观点出发，优选莱赛尔纤维。再生纤维素纤维可以为长丝，也可以为短纤维。再生纤维素纤维可以利用与再生纤维素纤维的分子内的羟基反应的化合物、树脂等交联剂进行了交联。再生纤维素纤维可以为具有卷曲的再生纤维素卷曲纤维。卷曲的程度没有限制，卷曲数可以为例如10～100个/40mm，可以为20～40个/40mm。再生纤维素纤维优选莱赛尔卷曲纤维。混纺纱可以仅由改造丝心蛋白纤维和再生纤维素纤维构成，也可以包含改造丝心蛋白纤维和再生纤维素纤维以外的其他纤维。其他纤维可以为天然纤维，也可以为化学纤维。混纺纱中的改造丝心蛋白纤维的量和再生纤维素纤维的量没有特别限定，从防止或抑制织物的由湿润导致的弹力和硬挺度的下降的观点出发，混纺纱中的改造丝心蛋白纤维的量可以为例如5～90质量％、5～40质量％、10～70质量％、10～50质量％、20～40质量％、20～30质量％或15～25质量％。另外，从维持再生纤维素纤维特有的优良手感的观点出发，混纺纱中的再生纤维素纤维的量可以为例如60～95质量％、70～90质量％、70～85质量％或75～85质量％。混纺纱中的其他纤维的量可以为例如5～30质量％、5～20质量％、5～10质量％或5～15质量％。＜改造丝心蛋白＞本实施方式的改造丝心蛋白为包含式1：[(a)n基序-rep]m或式2：[(a)n基序-rep]m-(a)n基序所示的结构域序列的蛋白质。改造丝心蛋白可以在结构域序列的n末端侧和c末端侧中的任意一个末端侧或两个末端侧进一步添加有氨基酸序列(n末端序列和c末端序列)。n末端序列和c末端序列典型地为不具有丝心蛋白中特征性的氨基酸基序的重复的区域，由约100个残基的氨基酸构成，但不限于此。本说明书中，“改造丝心蛋白”是指人为地制造的丝心蛋白(人造丝心蛋白)。改造丝心蛋白可以为其结构域序列与天然来源的丝心蛋白的氨基酸序列不同的丝心蛋白，也可以为其结构域序列与天然来源的丝心蛋白的氨基酸序列相同的丝心蛋白。本说明书中所说的“天然来源的丝心蛋白”也为包含式1：[(a)n基序-rep]m或式2：[(a)n基序-rep]m-(a)n基序所示的结构域序列的蛋白质。“改造丝心蛋白”可以为直接利用天然来源的丝心蛋白的氨基酸序列的改造丝心蛋白，也可以为依据天然来源的丝心蛋白的氨基酸序列对其氨基酸序列进行了改造的丝心蛋白(例如，通过对克隆出的天然来源的丝心蛋白的基因序列进行改造而改造了氨基酸序列的丝心蛋白)，另外还可以为不依赖于天然来源的丝心蛋白而人为地设计和合成的改造丝心蛋白(例如，通过化学合成编码所设计的氨基酸序列的核酸而具有所期望的氨基酸序列的丝心蛋白)。本说明书中，“结构域序列”为生成丝心蛋白特有的结晶区(典型地，相当于氨基酸序列的(a)n基序)和非晶区(典型地，相当于氨基酸序列的rep)的氨基酸序列，是指式1：[(a)n基序-rep]m或式2：[(a)n基序-rep]m-(a)n基序所示的氨基酸序列。在此，(a)n基序表示以丙氨酸残基为主的氨基酸序列，氨基酸残基数为2～27。(a)n基序的氨基酸残基数可以为2～20、4～27、4～20、8～20、10～20、4～16、8～16或10～16的整数。另外，(a)n基序中的丙氨酸残基数相对于全部氨基酸残基数的比例为40％以上即可，可以为60％以上、70％以上、80％以上、83％以上、85％以上、86％以上、90％以上、95％以上或100％(意味着仅由丙氨酸残基构成)。在结构域序列中两个以上存在的(a)n基序中的至少7个可以仅由丙氨酸残基构成。rep表示由2～200个氨基酸残基构成的氨基酸序列。rep可以为由10～200个氨基酸残基构成的氨基酸序列，可以为由10～40、10～60、10～80、10～100、10～120、10～140、10～160或10～180个氨基酸残基构成的氨基酸序列。m表示2～300的整数，可以为8～300、10～300、20～300、40～300、60～300、80～300、100～300、10～200、20～200、20～180、20～160、20～140或20～120的整数。两个以上存在的(a)n基序彼此可以为相同的氨基酸序列，也可以为不同的氨基酸序列。两个以上存在的rep彼此可以为相同的氨基酸序列，也可以为不同的氨基酸序列。本实施方式的改造丝心蛋白例如可以通过对克隆出的天然来源的丝心蛋白的基因序列进行相当于例如置换、缺失、插入和/或添加一个或两个以上的氨基酸残基的氨基酸序列的改造而得到。氨基酸残基的置换、缺失、插入和/或添加可以利用定点诱变法等本领域技术人员公知的方法进行。具体而言，可以依据nucleicacidres.10,6487(1982)、methodsinenzymology,100,448(1983)等文献中记载的方法进行。天然来源的丝心蛋白为包含式1：[(a)n基序-rep]m或式2：[(a)n基序-rep]m-(a)n基序所示的结构域序列的蛋白质，具体而言，可列举例如昆虫或蜘蛛类产生的丝心蛋白。作为昆虫产生的丝心蛋白，可列举例如家蚕(bombyxmori)、野桑蚕(bombyxmandarina)、天蚕(antheraeayamamai)、柞蚕(anteraeapernyi)、枫蚕(eriogynapyretorum)、蓖麻蚕(pilosamiacynthiaricini)、樗蚕(samiacynthia)、樟蚕(caligurajaponica)、印度柞蚕(antheraeamylitta)、琥珀蚕(antheraeaassama)等蚕产生的蚕丝蛋白和雀蜂(vespasimillimaxanthoptera)的幼虫吐出的蜂丝蛋白。作为昆虫产生的丝心蛋白的更具体的例子，可列举例如蚕·丝心蛋白l链(genbank登录号m76430(碱基序列)和aaa27840.1(氨基酸序列))。作为蜘蛛类产生的丝心蛋白，可列举例如大腹园蛛、十字园蛛、肥胖园蛛、五纹园蛛和野岛园蛛(araneusnojimai)等属于园蛛属(araneus属)的蜘蛛、青新园蛛、嗜水新园蛛、灌木新园蛛和类青新园蛛等属于新园蛛属(neoscona属)的蜘蛛、小岬蛛等属于岬蛛属(pronus属)的蜘蛛、蟾蜍曲腹蛛和对称曲腹蛛等属于曲腹蛛属(cyrtarachne属)的蜘蛛、库氏棘腹蛛和乳突棘腹蛛等属于棘腹蛛属(gasteracantha属)的蜘蛛、何氏瘤腹蛛和六刺瘤腹蛛等属于瘤腹蛛属(ordgarius属)的蜘蛛、悦目金蛛、小悦目金蛛和横纹金蛛等属于金蛛属(argiope属)的蜘蛛、双峰尾园蛛等属于尾园蛛属(arachnura属)的蜘蛛、褐吊叶蛛等属于吊叶蛛属(acusilas属)的蜘蛛、红云斑蛛、花云斑蛛和全色云斑蛛等属于云斑蛛属(cytophora属)的蜘蛛、丑锥头蛛等属于锥头蛛属(poltys属)的蜘蛛、八瘤艾蛛、四突艾蛛、圆腹艾蛛和黑尾艾蛛等属于艾蛛属(cyclosa属)的蜘蛛和日本壮头蛛等属于壮头蛛属(chorizopes属)的蜘蛛所产生的蛛丝蛋白、以及前齿肖蛸、锥腹肖蛸、直伸肖蛸和鳞纹肖蛸等属于肖蛸属(tetragnatha属)的蜘蛛、纵条银鳞蛛、肩斑银鳞蛛和小肩斑银鳞蛛等属于银鳞蛛属(leucauge属)的蜘蛛、棒络新妇和斑络新妇等属于络新妇属(nephila属)的蜘蛛、美丽麦蛛等属于麦蛛属(menosira属)的蜘蛛、柔弱粗螯蛛等属于锯螯蛛属(dyschiriognatha属)的蜘蛛、红斑寇蛛、哈氏寇蛛、几何寇蛛和间斑寇蛛等属于冠蛛属(latrodectus属)的蜘蛛、以及属于育儿网蛛属(euprosthenops属)的蜘蛛等属于肖蛸科(tetragnathidae科)的蜘蛛所产生的蛛丝蛋白。作为蛛丝蛋白，可列举例如masp(masp1和masp2)、adf(adf3和adf4)等牵引丝蛋白、misp(misp1和misp2)等。作为蜘蛛类产生的蛛丝蛋白的更具体的例子，可列举例如丝心蛋白-3(fibroin-3，adf-3)[十字园蛛(araneusdiadematus)来源](genbank登录号aac47010(氨基酸序列)、u47855(碱基序列))、丝心蛋白-4(fibroin-4，adf-4)[十字园蛛来源](genbank登录号aac47011(氨基酸序列)、u47856(碱基序列))、牵引丝蛋白蛛丝蛋白1(draglinesilkproteinspidroin1)[金纺蜘蛛(nephilaclavipes)来源](genbank登录号aac04504(氨基酸序列)、u37520(碱基序列))、大壶状腺蛛丝蛋白1(majorampullatespidroin1)[黑寡妇蜘蛛(latrodectushesperus)来源](genbank登录号abr68856(氨基酸序列)、ef595246(碱基序列))、牵引丝蛋白蛛丝蛋白2(draglinesilkproteinspidroin2)[棒络新妇(nephilaclavata)来源](genbank登录号aal32472(氨基酸序列)、af441245(碱基序列))、大壶状腺蛛丝蛋白1[非洲育儿网蛛(euprosthenopsaustralis)来源](genbank登录号caj00428(氨基酸序列)、aj973155(碱基序列))和大壶状腺蛛丝蛋白2(majorampullatespidroin2)[非洲育儿网蛛](genbank登录号cam32249.1(氨基酸序列)、am490169(碱基序列))、小壶状腺丝蛋白1(minorampullatesilkprotein1)[金纺蜘蛛](genbank登录号aac14589.1(氨基酸序列))、小壶状腺丝蛋白2(minorampullatesilkprotein2)[金纺蜘蛛](genbank登录号aac14591.1(氨基酸序列))、小壶状腺蛛丝蛋白样蛋白质(minorampullatespidroin-likeprotein)[nephilengyscruentata](genbank登录号abr37278.1(氨基酸序列)等。作为天然来源的丝心蛋白的更具体的例子，可以进一步列举在ncbigenbank中登记了序列信息的丝心蛋白。例如，可以通过从ncbigenbank中登记的序列信息中包含inv作为分类码(division)的序列中提取出在定义(definition)中记载了蛛丝蛋白、壶状腺、丝心蛋白、“丝和多肽”或“丝和蛋白质”作为关键词的序列、从cds中提取出指定产物的字符串、从来源(source)中提取出在组织类型(tissuetype)中记载了指定字符串的序列来确认。本实施方式的改造丝心蛋白可以为改造蚕丝(silk)丝心蛋白(对蚕产生的蚕丝蛋白的氨基酸序列进行改造而得到的丝心蛋白)，也可以为改造蛛丝丝心蛋白(对蜘蛛类产生的蛛丝蛋白的氨基酸序列进行改造而得到的丝心蛋白)。作为改造丝心蛋白，优选改造蛛丝丝心蛋白。改造蛛丝丝心蛋白的保温性、吸湿发热性和/或阻燃性也优良。作为改造丝心蛋白的具体例，可列举来源于蜘蛛的大壶状腺中产生的大吐丝管牵引丝蛋白的改造丝心蛋白(第一改造丝心蛋白)、具有降低了甘氨酸残基的含量的结构域序列的改造丝心蛋白(第二改造丝心蛋白)、具有降低了(a)n基序的含量的结构域序列的改造丝心蛋白(第三改造丝心蛋白)、降低了甘氨酸残基的含量和(a)n基序的含量的改造丝心蛋白(第四改造丝心蛋白)、具有包含在局部疏水性指数大的区域的结构域序列的改造丝心蛋白(第五改造丝心蛋白)、以及具有降低了谷氨酰胺残基的含量的结构域序列的改造丝心蛋白(第六改造丝心蛋白)。作为第一改造丝心蛋白，可列举包含式1：[(a)n基序-rep]m所示的结构域序列的蛋白质。在第一改造丝心蛋白中，(a)n基序的氨基酸残基数优选为3～20的整数，更优选为4～20的整数，进一步优选为8～20的整数，进一步更优选为10～20的整数，进一步更优选为4～16的整数，特别优选为8～16的整数，最优选为10～16的整数。第一改造丝心蛋白中，式1中构成rep的氨基酸残基数优选为10～200个残基，更优选为10～150个残基，进一步优选为20～100个残基，进一步更优选为20～75个残基。第一改造丝心蛋白中，式1：[(a)n基序-rep]m所示的氨基酸序列中含有的甘氨酸残基、丝氨酸残基和丙氨酸残基的合计残基数相对于氨基酸残基数总体优选为40％以上，更优选为60％以上，进一步优选为70％以上。第一改造丝心蛋白可以为包含式1：[(a)n基序-rep]m所示的氨基酸序列的单元、并且c末端序列为序列号1～3中任一者所示的氨基酸序列或与序列号1～3中任一者所示的氨基酸序列具有90％以上的同源性的氨基酸序列的多肽。序列号1所示的氨基酸序列与由adf3(gi：1263287、ncbi)的氨基酸序列的c末端的50个残基的氨基酸构成的氨基酸序列相同，序列号2所示的氨基酸序列与从序列号1所示的氨基酸序列的c末端去除20个残基而得到的氨基酸序列相同，序列号3所示的氨基酸序列与从序列号1所示的氨基酸序列的c末端去除29个残基而得到的氨基酸序列相同。作为第一改造丝心蛋白的更具体的例子，可列举(1-i)包含序列号4(重组蛛丝蛋白adf3kailargenrsh1)所示的氨基酸序列的改造丝心蛋白、或者(1-ii)包含与序列号4所示的氨基酸序列具有90％以上的序列一致性的氨基酸序列的改造丝心蛋白。序列一致性优选为95％以上。序列号4所示的氨基酸序列是在n末端添加有由起始密码子、his10标签和hrv3c蛋白酶(人鼻病毒(humanrhinovirus)3c蛋白酶)识别位点构成的氨基酸序列(序列号5)的adf3的氨基酸序列中以使第1～13个重复区域增加为约2倍、并且在第1154位氨基酸残基处终止翻译的方式发生突变而得到的氨基酸序列。序列号4所示的氨基酸序列的c末端的氨基酸序列与序列号3所示的氨基酸序列相同。(1-i)的改造丝心蛋白可以由序列号4所示的氨基酸序列构成。第二改造丝心蛋白中，其结构域序列具有与天然来源的丝心蛋白相比降低了甘氨酸残基的含量的氨基酸序列。第二改造丝心蛋白可以说具有与天然来源的丝心蛋白相比相当于至少rep中的一个或两个以上甘氨酸残基被置换为了其他氨基酸残基的氨基酸序列。第二改造丝心蛋白中，其结构域序列可以具有与天然来源的丝心蛋白相比相当于在rep中的选自ggx和gpgxx(其中，g表示甘氨酸残基、p表示脯氨酸残基、x表示甘氨酸以外的氨基酸残基)中的至少一种基序序列中至少一个或两个以上该基序序列中的一个甘氨酸残基被置换为了其他氨基酸残基的氨基酸序列。第二改造丝心蛋白中，上述甘氨酸残基被置换为了其他氨基酸残基的基序序列的比例相对于全部基序序列可以为10％以上。第二改造丝心蛋白可以包含式1：[(a)n基序-rep]m所示的结构域序列，并且具有下述氨基酸序列：将从上述结构域序列中除去位于最靠c末端侧的(a)n基序至上述结构域序列的c末端为止的序列而得到的序列中的全部rep中含有的由xgx(其中，x表示甘氨酸以外的氨基酸残基)构成的氨基酸序列的总氨基酸残基数设为z，将从上述结构域序列中除去位于最靠c末端侧的(a)n基序至上述结构域序列的c末端为止的序列而得到的序列中的总氨基酸残基数设为w时，z/w为30％以上、40％以上、50％以上或50.9％以上。(a)n基序中的丙氨酸残基数相对于全部氨基酸残基数可以为83％以上，优选为86％以上，更优选为90％以上，进一步优选为95％以上，进一步更优选为100％(意味着仅由丙氨酸残基构成)。第二改造丝心蛋白优选为通过将ggx基序的一个甘氨酸残基置换为其他氨基酸残基而提高了由xgx构成的氨基酸序列的含有比例的改造丝心蛋白。第二改造丝心蛋白中，结构域序列中的由ggx构成的氨基酸序列的含有比例优选为30％以下，更优选为20％以下，进一步优选为10％以下，进一步更优选为6％以下，进一步更优选为4％以下，特别优选为2％以下。结构域序列中的由ggx构成的氨基酸序列的含有比例可以利用与下述由xgx构成的氨基酸序列的含有比例(z/w)的计算方法同样的方法算出。进一步详细地说明z/w的计算方法。首先，在包含式1：[(a)n基序-rep]m所示的结构域序列的丝心蛋白(改造丝心蛋白或天然来源的丝心蛋白)中，从结构域序列中除去位于最靠c末端侧的(a)n基序至结构域序列的c末端为止的序列，从所得到的序列中含有的全部rep中提取出由xgx构成的氨基酸序列。构成xgx的氨基酸残基的总数为z。例如，在提取出50个由xgx构成的氨基酸序列的情况下(无重复)，z为50×3＝150。另外，例如在如由xgxgx构成的氨基酸序列的情况这样存在包含于两个xgx中的x(中央的x)的情况下，扣除重复量来进行计算(xgxgx的情况下为5个氨基酸残基)。w为从结构域序列中除去位于最靠c末端侧的(a)n基序至结构域序列的c末端为止的序列而得到的序列中含有的总氨基酸残基数。例如，在图1所示的结构域序列的情况下，w为4+50+4+100+4+10+4+20+4+30＝230(除去了位于最靠c末端侧的(a)n基序)。接着，将z除以w，由此能够算出z/w(％)。在此，对天然来源的丝心蛋白中的z/w进行说明。首先，如上所述，利用例示出在ncbigenbank中登记了氨基酸序列信息的丝心蛋白的方法进行确认，结果提取出663种丝心蛋白(其中，蜘蛛类来源的丝心蛋白为415种)。由所提取的全部丝心蛋白中包含式1：[(a)n基序-rep]m所示的结构域序列且丝心蛋白中的由ggx构成的氨基酸序列的含有比例为6％以下的天然来源的丝心蛋白的氨基酸序列，利用上述计算方法算出z/w。将其结果示于图2中。图2的横轴表示z/w(％)，纵轴表示频率。由图2明确了天然来源的丝心蛋白中的z/w均小于50.9％(最高为50.86％)。第二改造丝心蛋白中，z/w优选为50.9％以上，更优选为56.1％以上，进一步优选为58.7％以上，进一步更优选为70％以上，进一步更优选为80％以上。对z/w的上限没有特别限制，例如可以为95％以下。第二改造丝心蛋白例如可以通过以下述方式进行改造而得到：从克隆出的天然来源的丝心蛋白的基因序列中对编码甘氨酸残基的碱基序列的至少一部分进行置换，使其编码其他氨基酸残基。此时，可以选择ggx基序和gpgxx基序中的一个甘氨酸残基作为进行改造的甘氨酸残基，另外也可以进行置换以使z/w为50.9％以上。另外，例如也可以通过由天然来源的丝心蛋白的氨基酸序列设计出满足上述方式的氨基酸序列、并化学合成出编码所设计的氨基酸序列的核酸而得到。在任何一种情况下，都可以在相当于从天然来源的丝心蛋白的氨基酸序列中将rep中的甘氨酸残基置换为其他氨基酸残基的改造的基础上，进一步进行相当于置换、缺失、插入和/或添加一个或两个以上氨基酸残基的氨基酸序列的改造。作为上述的其他氨基酸残基，只要是甘氨酸残基以外的氨基酸残基则没有特别限制，优选缬氨酸(v)残基、亮氨酸(l)残基、异亮氨酸(i)残基、甲硫氨酸(m)残基、脯氨酸(p)残基、苯丙氨酸(f)残基和色氨酸(w)残基等疏水性氨基酸残基、谷氨酰胺(q)残基、天冬酰胺(n)残基、丝氨酸(s)残基、赖氨酸(k)残基和谷氨酸(e)残基等亲水性氨基酸残基，更优选缬氨酸(v)残基、亮氨酸(l)残基、异亮氨酸(i)残基、苯丙氨酸(f)残基和谷氨酰胺(q)残基，进一步优选谷氨酰胺(q)残基。作为第二改造丝心蛋白的更具体的例子，可列举(2-i)包含序列号6(met-prt380)、序列号7(met-prt410)、序列号8(met-prt525)或序列号9(met-prt799)所示的氨基酸序列的改造丝心蛋白、或者(2-ii)包含与序列号6、序列号7、序列号8或序列号9所示的氨基酸序列具有90％以上的序列一致性的氨基酸序列的改造丝心蛋白。对(2-i)的改造丝心蛋白进行说明。序列号6所示的氨基酸序列为将相当于天然来源的丝心蛋白的序列号10(met-prt313)所示的氨基酸序列的rep中的全部ggx置换为gqx而得到的氨基酸序列。序列号7所示的氨基酸序列是从序列号6所示的氨基酸序列中从n末端侧向c末端侧使(a)n基序每隔两个发生缺失、进一步在c末端序列的近前处插入一个[(a)n基序-rep]而得到的氨基酸序列。序列号8所示的氨基酸序列是在序列号7所示的氨基酸序列的各(a)n基序的c末端侧插入两个丙氨酸残基、进一步将一部分谷氨酰胺(q)残基置换为丝氨酸(s)残基、并使c末端侧的一部分氨基酸缺失以使其与序列号7的分子量大致相同而得到的氨基酸序列。序列号9所示的氨基酸序列是在将序列号7所示的氨基酸序列中存在的20个结构域序列的区域(其中，该区域的c末端侧的几个氨基酸残基被进行了置换)重复4次而得到的序列的c末端添加规定的铰链序列和his标签序列而得到的氨基酸序列。序列号10所示的氨基酸序列(相当于天然来源的丝心蛋白)中的z/w的值为46.8％。序列号6所示的氨基酸序列、序列号7所示的氨基酸序列、序列号8所示的氨基酸序列和序列号9所示的氨基酸序列中的z/w的值分别为58.7％、70.1％、66.1％和70.0％。另外，序列号10、序列号6、序列号7、序列号8和序列号9所示的氨基酸序列的锯齿比率(在下文说明)为1:1.8～11.3时的x/y的值分别为15.0％、15.0％、93.4％、92.7％和89.8％。(2-i)的改造丝心蛋白可以由序列号6、序列号7、序列号8或序列号9所示的氨基酸序列构成。(2-ii)的改造丝心蛋白包含与序列号6、序列号7、序列号8或序列号9所示的氨基酸序列具有90％以上的序列一致性的氨基酸序列。(2-ii)的改造丝心蛋白也为包含式1：[(a)n基序-rep]m所示的结构域序列的蛋白质。上述序列一致性优选为95％以上。(2-ii)的改造丝心蛋白优选：与序列号6、序列号7、序列号8或序列号9所示的氨基酸序列具有90％以上的序列一致性，并且将rep中含有的xgx(其中，x表示甘氨酸以外的氨基酸残基)构成的氨基酸序列的总氨基酸残基数设为z、将上述结构域序列中的rep的总氨基酸残基数设为w时，z/w为50.9％以上。第二改造丝心蛋白可以在n末端和c末端中的任意一个末端或两个末端包含标签序列。由此，能够进行改造丝心蛋白的分离、固定化、检测和可见化等。作为标签序列，可列举例如利用与其他分子的特异性亲和性(结合性、affinity)的亲和性标签。作为亲和性标签的具体例，可列举组氨酸标签(his标签)。his标签是由约4至10个组氨酸残基排列而成的短肽，具有与镍等金属离子特异性地结合的性质，因此能够用于通过金属螯合层析(chelatingmetalchromatography)进行的改造丝心蛋白的分离。作为标签序列的具体例，可列举例如序列号11所示的氨基酸序列(包含his标签序列和铰链序列的氨基酸序列)。另外，也可以利用与谷胱甘肽特异性地结合的谷胱甘肽-s-转移酶(gst)、与麦芽糖特异性地结合的麦芽糖结合蛋白(mbp)等标签序列。此外，也可以使用利用抗原抗体反应的“表位标签”。通过添加显示抗原性的肽(表位)作为标签序列，能够使针对该表位的抗体进行结合。作为表位标签，可列举ha(流感病毒的血凝素的肽序列)标签、myc标签、flag标签等。通过利用表位标签，能够以高特异性容易地对改造丝心蛋白进行纯化。也可以使用进一步利用特定的蛋白酶将标签序列切除而得到的改造丝心蛋白。也可以通过对经由该标签序列吸附的蛋白质进行蛋白酶处理而回收切除标签序列后的改造丝心蛋白。作为包含标签序列的改造丝心蛋白的更具体的例子，可列举(2-iii)包含序列号12(prt380)、序列号13(prt410)、序列号14(prt525)或序列号15(prt799)所示的氨基酸序列的改造丝心蛋白、或者(2-iv)包含与序列号12、序列号13、序列号14或序列号15所示的氨基酸序列具有90％以上的序列一致性的氨基酸序列的改造丝心蛋白。序列号16(prt313)、序列号12、序列号13、序列号14和序列号15所示的氨基酸序列分别为在序列号10、序列号6、序列号7、序列号8和序列号9所示的氨基酸序列的n末端添加序列号11所示的氨基酸序列(包含his标签序列和铰链序列)而得到的氨基酸序列。(2-iii)的改造丝心蛋白可以由序列号12、序列号13、序列号14或序列号15所示的氨基酸序列构成。(2-iv)的改造丝心蛋白包含与序列号12、序列号13、序列号14或序列号15所示的氨基酸序列具有90％以上的序列一致性的氨基酸序列。另外，(2-iv)的改造丝心蛋白也为包含式1：[(a)n基序-rep]m所示的结构域序列的蛋白质。上述序列一致性优选为95％以上。(2-iv)的改造丝心蛋白优选：与序列号12、序列号13、序列号14或序列号15所示的氨基酸序列具有90％以上的序列一致性，并且将rep中含有的由xgx(其中，x表示甘氨酸以外的氨基酸残基)构成的氨基酸序列的总氨基酸残基数设为z、将上述结构域序列中的rep的总氨基酸残基数设为w时，z/w为50.9％以上。第二改造丝心蛋白可以包含用于将重组蛋白生产系统中生产的蛋白质释放到宿主的外部的分泌信号。分泌信号的序列可以根据宿主的种类适当设定。第三改造丝心蛋白中，其结构域序列具有与天然来源的丝心蛋白相比降低了(a)n基序的含量的氨基酸序列。第三改造丝心蛋白的结构域序列可以说具有与天然来源的丝心蛋白相比相当于缺失了至少一个或两个以上(a)n基序的氨基酸序列。第三改造丝心蛋白可以具有相当于从天然来源的丝心蛋白中缺失了10～40％的(a)n基序的氨基酸序列。第三改造丝心蛋白中，其结构域序列可以具有与天然来源的丝心蛋白相比相当于从n末端侧向c末端侧至少每1～3个(a)n基序中缺失了一个(a)n基序的氨基酸序列。第三改造丝心蛋白中，其结构域序列可以具有与天然来源的丝心蛋白相比相当于从n末端侧向c末端侧至少依次重复发生了两个连续的(a)n基序的缺失和一个(a)n基序的缺失的氨基酸序列。第三改造丝心蛋白中，其结构域序列可以具有相当于从n末端侧向c末端侧至少使(a)n基序每隔两个发生了缺失的氨基酸序列。第三改造丝心蛋白可以包含式1：[(a)n基序-rep]m所示的结构域序列，并且具有下述氨基酸序列：从n末端侧向c末端侧将相邻的两个[(a)n基序-rep]单元的rep的氨基酸残基数依次进行比较，将设氨基酸残基数少的rep的氨基酸残基数为1时另一者的rep的氨基酸残基数之比为1.8～11.3的相邻的两个[(a)n基序-rep]单元的氨基酸残基数相加得到的合计值的最大值设为x、将结构域序列的总氨基酸残基数设为y时，x/y为20％以上、30％以上、40％以上或50％以上。(a)n基序中的丙氨酸残基数相对于全部氨基酸残基数可以为83％以上，优选为86％以上，更优选为90％以上，进一步优选为95％以上，进一步更优选为100％(意味着仅由丙氨酸残基构成)。参考图1进一步详细地说明x/y的计算方法。图1中示出从改造丝心蛋白除去n末端序列和c末端序列后的结构域序列。该结构域序列从n末端侧(左侧)起具有(a)n基序-第一rep(50个氨基酸残基)-(a)n基序-第二rep(100个氨基酸残基)-(a)n基序-第三rep(10个氨基酸残基)-(a)n基序-第四rep(20个氨基酸残基)-(a)n基序-第五rep(30个氨基酸残基)-(a)n基序这样的序列。从n末端侧向c末端侧按照没有重复的方式依次选择相邻的两个[(a)n基序-rep]单元。此时，可以存在未被选择的[(a)n基序-rep]单元。图1中示出了方式1(第一rep与第二rep的比较、以及第三rep与第四rep的比较)、方式2(第一rep与第二rep的比较、以及第四rep与第五rep的比较)、方式3(第二rep与第三rep的比较、以及第四rep与第五rep的比较)、方式4(第一rep与第二rep的比较)。需要说明的是，也存在除此以外的选择方法。接着，对于各方式，将所选择的相邻的两个[(a)n基序-rep]单元中的各rep的氨基酸残基数进行比较。比较通过求出将氨基酸残基数更少的一者设为1时的、另一者的氨基酸残基数之比来进行。例如，在第一rep(50个氨基酸残基)与第二rep(100个氨基酸残基)的比较的情况下，将氨基酸残基数更少的第一rep设为1时，第二rep的氨基酸残基数之比为100/50＝2。同样地，在第四rep(20个氨基酸残基)与第五rep(30个氨基酸残基)的比较的情况下，将氨基酸残基数更少的第四rep设为1时，第五rep的氨基酸残基数之比为30/20＝1.5。图1中，用实线示出了将氨基酸残基数更少的一者设为1时、另一者的氨基酸残基数之比为1.8～11.3的[(a)n基序-rep]单元的组。本说明书中，将该比称为锯齿比率。将氨基酸残基数更少的一者设为1时、另一者的氨基酸残基数之比小于1.8或大于11.3的[(a)n基序-rep]单元的组用虚线表示。在各方式中，将用实线表示的相邻的两个[(a)n基序-rep]单元的全部氨基酸残基数相加(不仅是rep的氨基酸残基数，还有(a)n基序的氨基酸残基数)。并且，对相加得到的合计值进行比较，将该合计值最大的方式的合计值(合计值的最大值)设为x。在图1所示的例子中，方式1的合计值最大。接着，将x除以结构域序列的总氨基酸残基数y，由此可以算出x/y(％)。第三改造丝心蛋白中，x/y优选为50％以上，更优选为60％以上，进一步优选为65％以上，进一步更优选为70％以上，进一步更优选为75％以上，特别优选为80％以上。对x/y的上限没有特别限制，例如可以为100％以下。锯齿比率为1:1.9～11.3的情况下，x/y优选为89.6％以上，锯齿比率为1:1.8～3.4的情况下，x/y优选为77.1％以上，锯齿比率为1:1.9～8.4的情况下，x/y优选为75.9％以上，锯齿比率为1:1.9～4.1的情况下，x/y优选为64.2％以上。在第三改造丝心蛋白为在结构域序列中两个以上存在的(a)n基序中的至少7个仅由丙氨酸残基构成的改造丝心蛋白的情况下，x/y优选为46.4％以上，更优选为50％以上，进一步优选为55％以上，进一步更优选为60％以上，进一步更优选为70％以上，特别优选为80％以上。对x/y的上限没有特别限制，只要为100％以下即可。在此，对天然来源的丝心蛋白中的x/y进行说明。首先，如上所述，利用例示出在ncbigenbank中登记了氨基酸序列信息的丝心蛋白的方法进行确认，结果提取出663种丝心蛋白(其中，蜘蛛类来源的丝心蛋白为415种)。根据所提取的全部丝心蛋白中由式1：[(a)n基序-rep]m所示的结构域序列构成的天然来源的丝心蛋白的氨基酸序列，利用上述的计算方法算出x/y。将锯齿比率为1:1.9～4.1的情况下的结果示于图3中。图3的横轴表示x/y(％)，纵轴表示频率。由图3明确了天然来源的丝心蛋白中的x/y均小于64.2％(最高为64.14％)。第三改造丝心蛋白例如可以通过从克隆出的天然来源的丝心蛋白的基因序列中使编码(a)n基序的序列中的一个或两个以上发生缺失以使x/y为64.2％以上而得到。另外，例如也可以通过设计出相当于从天然来源的丝心蛋白的氨基酸序列中使一个或两个以上(a)n基序发生缺失以使x/y为64.2％以上的氨基酸序列、并化学合成出编码所设计的氨基酸序列的核酸而得到。在任何一种情况下，都可以在相当于从天然来源的丝心蛋白的氨基酸序列中使(a)n基序发生了缺失的改造的基础上，进一步进行相当于置换、缺失、插入和/或添加一个或两个以上氨基酸残基的氨基酸序列的改造。作为第三改造丝心蛋白的更具体的例子，可列举(3-i)包含序列号17(met-prt399)、序列号7(met-prt410)、序列号8(met-prt525)或序列号9(met-prt799)所示的氨基酸序列的改造丝心蛋白、或者(3-ii)包含与序列号17、序列号7、序列号8或序列号9所示的氨基酸序列具有90％以上的序列一致性的氨基酸序列的改造丝心蛋白。对(3-i)的改造丝心蛋白进行说明。序列号17所示的氨基酸序列是从相当于天然来源的丝心蛋白的序列号10(met-prt313)所示的氨基酸序列中从n末端侧向c末端侧使(a)n基序每隔两个发生缺失、进一步在c末端序列的近前处插入一个[(a)n基序-rep]而得到的氨基酸序列。序列号7、序列号8或序列号9所示的氨基酸序列如第二改造丝心蛋白中所说明的那样。序列号10所示的氨基酸序列(相当于天然来源的丝心蛋白)的锯齿比率为1:1.8～11.3时的x/y的值为15.0％。序列号17所示的氨基酸序列和序列号7所示的氨基酸序列中的x/y的值均为93.4％。序列号8所示的氨基酸序列中的x/y的值为92.7％。序列号9所示的氨基酸序列中的x/y的值为89.8％。序列号10、序列号17、序列号7、序列号8和序列号9所示的氨基酸序列中的z/w的值分别为46.8％、56.2％、70.1％、66.1％和70.0％。(3-i)的改造丝心蛋白可以由序列号17、序列号7、序列号8或序列号9所示的氨基酸序列构成。(3-ii)的改造丝心蛋白包含与序列号17、序列号7、序列号8或序列号9所示的氨基酸序列具有90％以上的序列一致性的氨基酸序列。另外，(3-ii)的改造丝心蛋白也为包含式1：[(a)n基序-rep]m所示的结构域序列的蛋白质。上述序列一致性优选为95％以上。(3-ii)的改造丝心蛋白优选：与序列号17、序列号7、序列号8或序列号9所示的氨基酸序列具有90％以上的序列一致性，并且从n末端侧向c末端侧将相邻的两个[(a)n基序-rep]单元的rep的氨基酸残基数依次进行比较，将设氨基酸残基数少的rep的氨基酸残基数为1时另一者的rep的氨基酸残基数之比为1.8～11.3(锯齿比率为1:1.8～11.3)的相邻的两个[(a)n基序-rep]单元的氨基酸残基数相加得到的合计值的最大值设为x、将结构域序列的总氨基酸残基数设为y时，x/y为64.2％以上。第三改造丝心蛋白可以在n末端和c末端中的任意一个末端或两个末端包含上述标签序列。作为包含标签序列的改造丝心蛋白的更具体的例子，可列举(3-iii)包含序列号18(prt399)、序列号13(prt410)、序列号14(prt525)或序列号15(prt799)所示的氨基酸序列的改造丝心蛋白、或者(3-iv)包含与序列号18、序列号13、序列号14或序列号15所示的氨基酸序列具有90％以上的序列一致性的氨基酸序列的改造丝心蛋白。序列号18、序列号13、序列号14和序列号15所示的氨基酸序列为分别在序列号17、序列号7、序列号8和序列号9所示的氨基酸序列的n末端添加序列号11所示的氨基酸序列(包含his标签序列和铰链序列)而得到的氨基酸序列。(3-iii)的改造丝心蛋白可以由序列号18、序列号13、序列号14或序列号15所示的氨基酸序列构成。(3-iv)的改造丝心蛋白包含与序列号18、序列号13、序列号14或序列号15所示的氨基酸序列具有90％以上的序列一致性的氨基酸序列。(3-iv)的改造丝心蛋白也为包含式1：[(a)n基序-rep]m所示的结构域序列的蛋白质。上述序列一致性优选为95％以上。(3-iv)的改造丝心蛋白优选：与序列号18、序列号13、序列号14或序列号15所示的氨基酸序列具有90％以上的序列一致性，并且从n末端侧向c末端侧将相邻的两个[(a)n基序-rep]单元的rep的氨基酸残基数依次进行比较，将设氨基酸残基数少的rep的氨基酸残基数为1时另一者的rep的氨基酸残基数之比为1.8～11.3的相邻的两个[(a)n基序-rep]单元的氨基酸残基数相加得到的合计值的最大值设为x、将结构域序列的总氨基酸残基数设为y时，x/y为64.2％以上。第三改造丝心蛋白可以包含用于将重组蛋白生产系统中生产的蛋白质释放到宿主的外部的分泌信号。分泌信号的序列可以根据宿主的种类适当设定。第四改造丝心蛋白中，其结构域序列具有与天然来源的丝心蛋白相比在降低了(a)n基序的含量的基础上还降低了甘氨酸残基的含量的氨基酸序列。第四改造丝心蛋白的结构域序列可以说具有与天然来源的丝心蛋白相比相当于在缺失了至少一个或两个以上(a)n基序的基础上、进一步至少将rep中的一个或两个以上甘氨酸残基置换为其他氨基酸残基的氨基酸序列。即，第四改造丝心蛋白为兼具上述第二改造丝心蛋白和第三改造丝心蛋白的特征的改造丝心蛋白。具体方式等如第二改造丝心蛋白和第三改造丝心蛋白中所说明的那样。作为第四改造丝心蛋白的更具体的例子，可列举(4-i)包含序列号7(met-prt410)、序列号8(met-prt525)、序列号9(met-prt799)、序列号13(prt410)、序列号14(prt525)或序列号15(prt799)所示的氨基酸序列的改造丝心蛋白、或者(4-ii)包含与序列号7、序列号8、序列号9、序列号13、序列号14或序列号15所示的氨基酸序列具有90％以上的序列一致性的氨基酸序列的改造丝心蛋白。包含序列号7、序列号8、序列号9、序列号13、序列号14或序列号15所示的氨基酸序列的改造丝心蛋白的具体方式如上所述。第五改造丝心蛋白中，其结构域序列可以具有与天然来源的丝心蛋白相比相当于rep中的一个或两个以上氨基酸残基被置换为了疏水性指数大的氨基酸残基、和/或在rep中插入了一个或两个以上疏水性指数大的氨基酸残基的、包含在局部疏水性指数大的区域的氨基酸序列。在局部疏水性指数大的区域优选由连续的2～4个氨基酸残基构成。上述疏水性指数大的氨基酸残基更优选为选自异亮氨酸(i)、缬氨酸(v)、亮氨酸(l)、苯丙氨酸(f)、半胱氨酸(c)、甲硫氨酸(m)和丙氨酸(a)中的氨基酸残基。第五改造丝心蛋白中，可以在与天然来源的丝心蛋白相比相当于rep中的一个或两个以上氨基酸残基被置换为了疏水性指数大的氨基酸残基、和/或在rep中插入了一个或两个以上疏水性指数大的氨基酸残基的改造的基础上，进一步进行与天然来源的丝心蛋白相比相当于置换、缺失、插入和/或添加一个或两个以上氨基酸残基的氨基酸序列的改造。第五改造丝心蛋白例如可以通过从克隆出的天然来源的丝心蛋白的基因序列中将rep中的一个或两个以上亲水性氨基酸残基(例如疏水性指数为负的氨基酸残基)置换为疏水性氨基酸残基(例如疏水性指数为正的氨基酸残基)、和/或在rep中插入一个或两个以上疏水性氨基酸残基而得到。另外，例如也可以通过设计出相当于从天然来源的丝心蛋白的氨基酸序列中将rep中的一个或两个以上亲水性氨基酸残基置换为疏水性氨基酸残基、和/或在rep中插入一个或两个以上疏水性氨基酸残基的氨基酸序列、并化学合成出编码所设计的氨基酸序列的核酸而得到。在任何一种情况下，都可以在相当于从天然来源的丝心蛋白的氨基酸序列中将rep中的一个或两个以上亲水性氨基酸残基置换为疏水性氨基酸残基、和/或在rep中插入一个或两个以上疏水性氨基酸残基的改造的基础上，进一步进行相当于置换、缺失、插入和/或添加一个或两个以上氨基酸残基的氨基酸序列的改造。第五改造丝心蛋白可以包含式1：[(a)n基序-rep]m所示的结构域序列，并且具有下述氨基酸序列：将从上述结构域序列中除去位于最靠c末端侧的(a)n基序至上述结构域序列的c末端为止的序列而得到的序列中含有的全部rep中连续的4个氨基酸残基的疏水性指数的平均值为2.6以上的区域中含有的氨基酸残基的总数设为p、将从上述结构域序列中除去位于最靠c末端侧的(a)n基序至上述结构域序列的c末端为止的序列而得到的序列中含有的氨基酸残基的总数设为q时，p/q为6.2％以上。关于氨基酸残基的疏水性指数，使用公知的指数(hydropathyindex:kytej,&doolittler(1982)“asimplemethodfordisplayingthehydropathiccharacterofaprotein”,j.mol.biol.,157,pp.105-132)。具体而言，各氨基酸的疏水性指数(hydropathyindex、以下也记为“hi”)如下述表1所示。[表1]氨基酸hi氨基酸hi异亮氨酸(ile)4.5色氨酸(trp)-0.9缬氨酸(val)4.2酪氨酸(tyr)-1.3亮氨酸(leu)3.8脯氨酸(pro)-1.6苯丙氨酸(phe)2.8组氨酸(his)-3.2半胱氨酸(cys)2.5天冬酰胺(asn)-3.5甲硫氨酸(met)1.9天冬氨酸(asp)-3.5丙氨酸(ala)1.8谷氨酰胺(gln)-3.5甘氨酸(gly)-0.4谷氨酸(glu)-3.5苏氨酸(thr)-0.7赖氨酸(lys)-3.9丝氨酸(ser)-0.8精氨酸(arg)-4.5进一步详细地说明p/q的计算方法。计算中，使用从式1：[(a)n基序-rep]m所示的结构域序列中除去位于最靠c末端侧的(a)n基序至结构域序列的c末端为止的序列而得到的序列(以下记为“序列a”)。首先，算出序列a中含有的全部rep中连续的4个氨基酸残基的疏水性指数的平均值。疏水性指数的平均值用连续的4个氨基酸残基中含有的各氨基酸残基的hi的总和除以4(氨基酸残基数)而求出。对全部的连续的4个氨基酸残基求出疏水性指数的平均值(各氨基酸残基被用于1～4次平均值的计算)。接着，确定出连续的4个氨基酸残基的疏水性指数的平均值为2.6以上的区域。即使在某一氨基酸残基对应于多个“疏水性指数的平均值为2.6以上的连续的4个氨基酸残基”的情况下，在区域中也作为1个氨基酸残基而含有。并且，该区域中含有的氨基酸残基的总数为p。另外，序列a中含有的氨基酸残基的总数为q。例如，在提取到20处“疏水性指数的平均值为2.6以上的连续的4个氨基酸残基”的情况下(无重复)，在连续的4个氨基酸残基的疏水性指数的平均值为2.6以上的区域中含有20处连续的4个氨基酸残基(无重复)，p为20×4＝80。另外，例如，在2处“疏水性指数的平均值为2.6以上的连续的4个氨基酸残基”仅有1个氨基酸残基重复存在的情况下，在连续的4个氨基酸残基的疏水性指数的平均值为2.6以上的区域中含有7个氨基酸残基(p＝2×4-1＝7。“-1”为重复部分的扣除)。例如，在图4所示的结构域序列的情况下，“疏水性指数的平均值为2.6以上的连续的4个氨基酸残基”不重复地存在7个，因此p为7×4＝28。另外，例如，在图4所示的结构域序列的情况下，q为4+50+4+40+4+10+4+20+4+30＝170(不包括存在于c末端侧的最后的(a)n基序)。接着，将p除以q，由此能够算出p/q(％)。图4的情况下为28/170＝16.47％。第五改造丝心蛋白中，p/q优选为6.2％以上，更优选为7％以上，进一步优选为10％以上，进一步更优选为20％以上，进一步更优选为30％以上。p/q的上限没有特别限制，例如可以为45％以下。第五改造丝心蛋白例如可以通过如下方法得到：对于克隆出的天然来源的丝心蛋白的氨基酸序列，将rep中的一个或两个以上亲水性氨基酸残基(例如疏水性指数为负的氨基酸残基)置换为疏水性氨基酸残基(例如疏水性指数为正的氨基酸残基)、和/或在rep中插入一个或两个以上疏水性氨基酸残基，以使其满足上述p/q的条件，由此改造成包含在局部疏水性指数大的区域的氨基酸序列。另外，例如也可以通过由天然来源的丝心蛋白的氨基酸序列设计出满足上述p/q的条件的氨基酸序列、并化学合成出编码所设计的氨基酸序列的核酸而得到。在任何一种情况下，都可以在与天然来源的丝心蛋白相比相当于rep中的一个或两个以上氨基酸残基被置换为了疏水性指数大的氨基酸残基、和/或在rep中插入一个或两个以上疏水性指数大的氨基酸残基的改造的基础上，进一步进行相当于置换、缺失、插入和/或添加一个或两个以上氨基酸残基的改造。作为疏水性指数大的氨基酸残基，没有特别限制，优选异亮氨酸(i)、缬氨酸(v)、亮氨酸(l)、苯丙氨酸(f)、半胱氨酸(c)、甲硫氨酸(m)和丙氨酸(a)，更优选缬氨酸(v)、亮氨酸(l)和异亮氨酸(i)。作为第五改造丝心蛋白的更具体的例子，可列举(5-i)包含序列号19(met-prt720)、序列号20(met-prt665)或序列号21(met-prt666)所示的氨基酸序列的改造丝心蛋白、或者(5-ii)包含与序列号19、序列号20或序列号21所示的氨基酸序列具有90％以上的序列一致性的氨基酸序列的改造丝心蛋白。对(5-i)的改造丝心蛋白进行说明。序列号19所示的氨基酸序列为对于序列号7(met-prt410)所示的氨基酸序列，除c末端侧的末端的结构域序列以外每隔一个rep分别插入2处由3个氨基酸残基构成的氨基酸序列(vli)，进一步将一部分谷氨酰胺(q)残基置换为丝氨酸(s)残基，并且使c末端侧的一部分氨基酸发生缺失而得到的氨基酸序列。序列号20所示的氨基酸序列为对于序列号8(met-prt525)所示的氨基酸序列，每隔一个rep分别插入1处由3个氨基酸残基构成的氨基酸序列(vli)而得到的氨基酸序列。序列号21所示的氨基酸序列为对于序列号8所示的氨基酸序列，每隔一个rep分别插入2处由3个氨基酸残基构成的氨基酸序列(vli)而得到的氨基酸序列。(5-i)的改造丝心蛋白可以由序列号19、序列号20或序列号21所示的氨基酸序列构成。(5-ii)的改造丝心蛋白包含与序列号19、序列号20或序列号21所示的氨基酸序列具有90％以上的序列一致性的氨基酸序列。(5-ii)的改造丝心蛋白也为包含式1：[(a)n基序-rep]m所示的结构域序列的蛋白质。上述序列一致性优选为95％以上。(5-ii)的改造丝心蛋白优选：与序列号19、序列号20或序列号21所示的氨基酸序列具有90％以上的序列一致性，并且将从结构域序列中除去位于最靠c末端侧的(a)n基序至结构域序列的c末端为止的序列而得到的序列中含有的全部rep中连续的4个氨基酸残基的疏水性指数的平均值为2.6以上的区域中含有的氨基酸残基的总数设为p、将从结构域序列中除去位于最靠c末端侧的(a)n基序至结构域序列的c末端为止的序列而得到的序列中含有的氨基酸残基的总数设为q时，p/q为6.2％以上。第五改造丝心蛋白可以在n末端和c末端中的任意一个末端或两个末端包含标签序列。作为包含标签序列的改造丝心蛋白的更具体的例子，可列举(5-iii)包含序列号22(prt720)、序列号23(prt665)或序列号24(prt666)所示的氨基酸序列的改造丝心蛋白、或者(5-iv)包含与序列号22、序列号23或序列号24所示的氨基酸序列具有90％以上的序列一致性的氨基酸序列的改造丝心蛋白。序列号22、序列号23和序列号24所示的氨基酸序列为分别在序列号19、序列号20和序列号21所示的氨基酸序列的n末端添加序列号11所示的氨基酸序列(包含his标签序列和铰链序列)而得到的氨基酸序列。(5-iii)的改造丝心蛋白可以由序列号22、序列号23或序列号24所示的氨基酸序列构成。(5-iv)的改造丝心蛋白包含与序列号22、序列号23或序列号24所示的氨基酸序列具有90％以上的序列一致性的氨基酸序列。(5-iv)的改造丝心蛋白也为包含式1：[(a)n基序-rep]m所示的结构域序列的蛋白质。上述序列一致性优选为95％以上。(5-iv)的改造丝心蛋白优选：与序列号22、序列号23或序列号24所示的氨基酸序列具有90％以上的序列一致性，并且将从结构域序列中除去位于最靠c末端侧的(a)n基序至结构域序列的c末端为止的序列而得到的序列中含有的全部rep中连续的4个氨基酸残基的疏水性指数的平均值为2.6以上的区域中含有的氨基酸残基的总数设为p、将从结构域序列中除去位于最靠c末端侧的(a)n基序至结构域序列的c末端为止的序列而得到的序列中含有的氨基酸残基的总数设为q时，p/q为6.2％以上。第五改造丝心蛋白可以包含用于将重组蛋白生产系统中生产的蛋白质释放到宿主的外部的分泌信号。分泌信号的序列可以根据宿主的种类适当设定。第六改造丝心蛋白具有与天然来源的丝心蛋白相比降低了谷氨酰胺残基的含量的氨基酸序列。第六改造丝心蛋白优选在rep的氨基酸序列中包含选自ggx基序和gpgxx基序中的至少一种基序。第六改造丝心蛋白在rep中包含gpgxx基序的情况下，gpgxx基序含有率通常为1％以上，可以为5％以上，优选为10％以上。对gpgxx基序含有率的上限没有特别限制，可以为50％以下，也可以为30％以下。本说明书中，“gpgxx基序含有率”为利用下述方法算出的值。在包含式1：[(a)n基序-rep]m或式2：[(a)n基序-rep]m-(a)n基序所示的结构域序列的丝心蛋白(改造丝心蛋白或天然来源的丝心蛋白)中，在从结构域序列中除去位于最靠c末端侧的(a)n基序至结构域序列的c末端为止的序列而得到的序列中含有的全部rep中，将该区域中含有的gpgxx基序的个数的总数的3倍的数(即，相当于gpgxx基序中的g和p的总数)设为s，将从结构域序列中除去位于最靠c末端侧的(a)n基序至结构域序列的c末端为止的序列、进一步除去(a)n基序而得到的全部rep的氨基酸残基的总数设为t时，以s/t算出gpgxx基序含有率。gpgxx基序含有率的计算中，将“从结构域序列中除去位于最靠c末端侧的(a)n基序至结构域序列的c末端为止的序列而得到的序列”作为对象的原因在于，在“位于最靠c末端侧的(a)n基序至结构域序列的c末端为止的序列”(相当于rep的序列)中有时含有与丝心蛋白的特征性序列的相关性低的序列，在m小的情况下(即，结构域序列短的情况下)，会影响gpgxx基序含有率的计算结果，因此要排除该影响。需要说明的是，在“gpgxx基序”位于rep的c末端的情况下，即使在“xx”为例如“aa”的情况下，也作为“gpgxx基序”来处理。图5为示出改造丝心蛋白的结构域序列的示意图。参考图5对gpgxx基序含有率的计算方法具体地进行说明。首先，在图5所示的改造丝心蛋白的结构域序列(为“[(a)n基序-rep]m-(a)n基序”型)中，全部rep都包含在“从结构域序列中除去位于最靠c末端侧的(a)n基序至结构域序列的c末端为止的序列而得到的序列”(图5中“区域a”所示的序列)中，因此，用于计算s的gpgxx基序的个数为7，s为7×3＝21。同样地，由于全部rep都包含在“从结构域序列中除去位于最靠c末端侧的(a)n基序至结构域序列的c末端为止的序列而得到的序列”(图5中“区域a”所示的序列)中，因此，从该序列中进一步除去(a)n基序而得到的全部rep的氨基酸残基的总数t为50+40+10+20+30＝150。接着，将s除以t，由此能够算出s/t(％)，在图5的改造丝心蛋白的情况下为21/150＝14.0％。第六改造丝心蛋白的谷氨酰胺残基含有率优选为9％以下，更优选为7％以下，进一步优选为4％以下，特别优选为0％。本说明书中，“谷氨酰胺残基含有率”为利用下述方法算出的值。在包含式1：[(a)n基序-rep]m或式2：[(a)n基序-rep]m-(a)n基序所示的结构域序列的丝心蛋白(改造丝心蛋白或天然来源的丝心蛋白)中，在从结构域序列中除去位于最靠c末端侧的(a)n基序至结构域序列的c末端为止的序列而得到的序列(相当于图5的“区域a”的序列)中含有的全部rep中，将该区域中含有的谷氨酰胺残基的总数设为u，将从结构域序列中除去位于最靠c末端侧的(a)n基序至结构域序列的c末端为止的序列、进一步除去(a)n基序而得到的全部rep的氨基酸残基的总数设为t时，以u/t算出谷氨酰胺残基含有率。谷氨酰胺残基含有率的计算中，将“从结构域序列中除去位于最靠c末端侧的(a)n基序至结构域序列的c末端为止的序列而得到的序列”作为对象的原因与上述原因相同。第六改造丝心蛋白中，其结构域序列可以具有与天然来源的丝心蛋白相比相当于使rep中的一个或两个以上的谷氨酰胺残基发生了缺失或被置换为了其他氨基酸残基的氨基酸序列。“其他氨基酸残基”只要是谷氨酰胺残基以外的氨基酸残基即可，优选为疏水性指数比谷氨酰胺残基大的氨基酸残基。氨基酸残基的疏水性指数如表1所示。如表1所示，作为疏水性指数比谷氨酰胺残基大的氨基酸残基，可列举选自异亮氨酸(i)、缬氨酸(v)、亮氨酸(l)、苯丙氨酸(f)、半胱氨酸(c)、甲硫氨酸(m)、丙氨酸(a)、甘氨酸(g)、苏氨酸(t)、丝氨酸(s)、色氨酸(w)、酪氨酸(y)、脯氨酸(p)和组氨酸(h)中的氨基酸残基。这些之中，更优选为选自异亮氨酸(i)、缬氨酸(v)、亮氨酸(l)、苯丙氨酸(f)、半胱氨酸(c)、甲硫氨酸(m)和丙氨酸(a)中的氨基酸残基，进一步优选为选自异亮氨酸(i)、缬氨酸(v)、亮氨酸(l)和苯丙氨酸(f)中的氨基酸残基。第六改造丝心蛋白中，rep的疏水度优选为-0.8以上，更优选为-0.7以上，进一步优选为0以上，进一步更优选为0.3以上，特别优选为0.4以上。对rep的疏水度的上限没有特别限制，可以为1.0以下，也可以为0.7以下。本说明书中，“rep的疏水度”为利用下述方法算出的值。在包含式1：[(a)n基序-rep]m或式2：[(a)n基序-rep]m-(a)n基序所示的结构域序列的丝心蛋白(改造丝心蛋白或天然来源的丝心蛋白)中，在从结构域序列中除去位于最靠c末端侧的(a)n基序至结构域序列的c末端为止的序列而得到的序列(相当于图5的“区域a”的序列)中含有的全部rep中，将该区域的各氨基酸残基的疏水性指数的总和设为v，将从结构域序列中除去位于最靠c末端侧的(a)n基序至结构域序列的c末端为止的序列、进一步除去(a)n基序而得到的全部rep的氨基酸残基的总数设为t时，以v/t算出rep的疏水度。rep的疏水度的计算中，将“从结构域序列中除去位于最靠c末端侧的(a)n基序至结构域序列的c末端为止的序列而得到的序列”作为对象的原因与上述原因相同。第六改造丝心蛋白中，其结构域序列可以在与天然来源的丝心蛋白相比相当于使rep中的一个或两个以上的谷氨酰胺残基发生缺失、和/或将rep中的一个或两个以上的谷氨酰胺残基置换为其他氨基酸残基的氨基酸序列的改造的基础上，进一步具有相当于置换、缺失、插入和/或添加一个或两个以上氨基酸残基的氨基酸序列的改造。第六改造丝心蛋白例如可以通过从克隆出的天然来源的丝心蛋白的基因序列中使rep中的一个或两个以上谷氨酰胺残基发生缺失、和/或将rep中的一个或两个以上谷氨酰胺残基置换为其他氨基酸残基而得到。另外，例如也可以通过设计出相当于从天然来源的丝心蛋白的氨基酸序列中使rep中的一个或两个以上谷氨酰胺残基发生缺失、和/或将rep中的一个或两个以上谷氨酰胺残基置换为其他氨基酸残基的氨基酸序列、并化学合成出编码所设计的氨基酸序列的核酸而得到。作为第六改造丝心蛋白的更具体的例子，可列举(6-i)包含序列号25(met-prt888)、序列号26(met-prt965)、序列号27(met-prt889)、序列号28(met-prt916)、序列号29(met-prt918)、序列号30(met-prt699)、序列号31(met-prt698)、序列号32(met-prt966)、序列号41(met-prt917)或序列号42(met-prt1028)所示的氨基酸序列的改造丝心蛋白、或者(6-ii)包含与序列号25、序列号26、序列号27、序列号28、序列号29、序列号30、序列号31、序列号32、序列号41或序列号42所示的氨基酸序列具有90％以上的序列一致性的氨基酸序列的改造丝心蛋白。对(6-i)的改造丝心蛋白进行说明。序列号25所示的氨基酸序列为将序列号7所示的氨基酸序列(met-prt410)中的qq全部置换为vl而得到的氨基酸序列。序列号26所示的氨基酸序列为将序列号7所示的氨基酸序列中的qq全部置换为ts、并且将其余的q置换为a而得到的氨基酸序列。序列号27所示的氨基酸序列为将序列号7所示的氨基酸序列中的qq全部置换为vl、并且将其余的q置换为i而得到的氨基酸序列。序列号28所示的氨基酸序列为将序列号7所示的氨基酸序列中的qq全部置换为vi、并且将其余的q置换为l而得到的氨基酸序列。序列号29所示的氨基酸序列为将序列号7所示的氨基酸序列中的qq全部置换为vf、并且将其余的q置换为i而得到的氨基酸序列。序列号30所示的氨基酸序列为将序列号8所示的氨基酸序列(met-prt525)中的qq全部置换为vl而得到的氨基酸序列。序列号31所示的氨基酸序列为将序列号8所示的氨基酸序列中的qq全部置换为vl、并且将其余的q置换为i而得到的氨基酸序列。序列号32所示的氨基酸序列为将序列号7所示的氨基酸序列(met-prt410)中存在的20个结构域序列的区域重复2次而得到的序列中的qq全部置换为vf、并且将其余的q置换为i而得到的氨基酸序列。序列号41所示的氨基酸序列(met-prt917)为将序列号7所示的氨基酸序列中的qq全部置换为li、并且将其余的q置换为v而得到的氨基酸序列。序列号42所示的氨基酸序列(met-prt1028)为将序列号7所示的氨基酸序列中的qq全部置换为if、并且将其余的q置换为t而得到的氨基酸序列。序列号25、序列号26、序列号27、序列号28、序列号29、序列号30、序列号31、序列号32、序列号41和序列号42所示的氨基酸序列的谷氨酰胺残基含有率均为9％以下(表2)。[表2]改造丝心蛋白.谷氨酰胺残基含有率gpgxx基序含有率rep的疏水度met-prt410(序列号7)17.7％27.9％-1.52met-prt888(序列号25)6.3％27.9％-0.07met-prt965(序列号26)0.0％27.9％-0.65met-prt889(序列号27)0.0％27.9％0.35met-prt916(序列号28)0.0％27.9％0.47met-prt918(序列号29)0.0％27.9％0.45met-prt699(序列号30)3.6％26.4％-0.78met-prt698(序列号31)0.0％26.4％-0.03met-prt966(序列号32)0.0％28.0％0.35met-prt917(序列号41)0.0％27.9％0.46met-prt1028(序列号42)0.0％28.1％0.05(6-i)的改造丝心蛋白可以由序列号25、序列号26、序列号27、序列号28、序列号29、序列号30、序列号31、序列号32、序列号41或序列号42所示的氨基酸序列构成。(6-ii)的改造丝心蛋白包含与序列号25、序列号26、序列号27、序列号28、序列号29、序列号30、序列号31、序列号32、序列号41或序列号42所示的氨基酸序列具有90％以上的序列一致性的氨基酸序列。(6-ii)的改造丝心蛋白也为包含式1：[(a)n基序-rep]m或式2：[(a)n基序-rep]m-(a)n基序所示的结构域序列的蛋白质。上述序列一致性优选为95％以上。(6-ii)的改造丝心蛋白的谷氨酰胺残基含有率优选为9％以下。另外，(6-ii)的改造丝心蛋白的gpgxx基序含有率优选为10％以上。第六改造丝心蛋白可以在n末端和c末端中的任意一个末端或两个末端包含标签序列。由此，能够进行改造丝心蛋白的分离、固定化、检测和可见化等。作为包含标签序列的改造丝心蛋白的更具体的例子，可列举(6-iii)包含序列号33(prt888)、序列号34(prt965)、序列号35(prt889)、序列号36(prt916)、序列号37(prt918)、序列号38(prt699)、序列号39(prt698)、序列号40(prt966)、序列号43(prt917)或序列号44(prt1028)所示的氨基酸序列的改造丝心蛋白、或者(6-iv)包含与序列号33、序列号34、序列号35、序列号36、序列号37、序列号38、序列号39或序列号40、序列号43或序列号44所示的氨基酸序列具有90％以上的序列一致性的氨基酸序列的改造丝心蛋白。序列号33、序列号34、序列号35、序列号36、序列号37、序列号38、序列号39、序列号40、序列号43和序列号44所示的氨基酸序列分别为在序列号25、序列号26、序列号27、序列号28、序列号29、序列号30、序列号31、序列号32、序列号41和序列号42所示的氨基酸序列的n末端添加序列号11所示的氨基酸序列(包含his标签序列和铰链序列)而得到的氨基酸序列。由于仅在n末端添加了标签序列，因此谷氨酰胺残基含有率没有变化，序列号33、序列号34、序列号35、序列号36、序列号37、序列号38、序列号39、序列号40、序列号43和序列号44所示的氨基酸序列的谷氨酰胺残基含有率均为9％以下(表3)。[表3]改造丝心蛋白.谷氨酰胺残基含有率gpgxx基序含有率rep的疏水度prt888(序列号33)6.3％27.9％-0.07prt965(序列号34)0.0％27.9％-0.65prt889(序列号35)0.0％27.9％0.35prt916(序列号36)0.0％27.9％0.47prt918(序列号37)0.0％27.9％0.45prt699(序列号38)3.6％26.4％-0.78prt698(序列号39)0.0％26.4％-0.03prt966(序列号40)0.0％28.0％0.35prt917(序列号43)0.0％27.9％0.46prt1028(序列号44)0.0％28.1％0.05(6-iii)的改造丝心蛋白可以由序列号33、序列号34、序列号35、序列号36、序列号37、序列号38、序列号39、序列号40、序列号43或序列号44所示的氨基酸序列构成。(6-iv)的改造丝心蛋白包含与序列号33、序列号34、序列号35、序列号36、序列号37、序列号38、序列号39、序列号40、序列号43或序列号44所示的氨基酸序列具有90％以上的序列一致性的氨基酸序列。(6-iv)的改造丝心蛋白也为包含式1：[(a)n基序-rep]m或式2：[(a)n基序-rep]m-(a)n基序所示的结构域序列的蛋白质。上述序列一致性优选为95％以上。(6-iv)的改造丝心蛋白的谷氨酰胺残基含有率优选为9％以下。另外，(6-iv)的改造丝心蛋白的gpgxx基序含有率优选为10％以上。第六改造丝心蛋白可以包含用于将重组蛋白生产系统中生产的蛋白质释放到宿主的外部的分泌信号。分泌信号的序列可以根据宿主的种类适当设定。改造丝心蛋白可以为兼具第一改造丝心蛋白、第二改造丝心蛋白、第三改造丝心蛋白、第四改造丝心蛋白、第五改造丝心蛋白和第六改造丝心蛋白所具有的特征中的至少两个以上特征的改造丝心蛋白。从确保优良的阻燃性的观点出发，改造丝心蛋白可以为亲水性改造丝心蛋白。亲水性改造丝心蛋白优选为例如求出构成改造丝心蛋白的全部氨基酸残基的疏水性指数(hi)的总和、接着将该总和除以全部氨基酸残基数而得的值(平均hi)为0以下的改造丝心蛋白。hi如表1所示。作为亲水性改造丝心蛋白，可列举例如：包含序列号4所示的氨基酸序列的改造丝心蛋白；包含序列号6、序列号7、序列号8或序列号9所示的氨基酸序列的改造丝心蛋白；包含序列号13、序列号11、序列号14或序列号15所示的氨基酸序列的改造丝心蛋白；包含序列号18、序列号7、序列号8或序列号9所示的氨基酸序列的改造丝心蛋白；包含序列号17、序列号11、序列号14或序列号15所示的氨基酸序列的改造丝心蛋白；包含序列号19、序列号20或序列号21所示的氨基酸序列的改造丝心蛋白。本实施方式的改造丝心蛋白的loi值可以为18以上、20以上、22以上、24以上、26以上、28以上、29以上或30以上。本说明书中，loi值为基于日本“消防危50号(1995年5月31日)”中记载的“粉粒状或熔点低的合成树脂的试验方法”测得的值。从得到高的吸湿发热性的观点出发，改造丝心蛋白可以为疏水性改造丝心蛋白。疏水性改造丝心蛋白优选为例如平均hi超过0的改造丝心蛋白。作为疏水性改造丝心蛋白，可列举例如：包含序列号27、序列号28、序列号29、序列号30、序列号31、序列号32、序列号33或序列号43所示的氨基酸序列的改造丝心蛋白；包含序列号35、序列号37、序列号38、序列号39、序列号40、序列号41或序列号44所示的氨基酸序列的改造丝心蛋白。本实施方式的改造丝心蛋白的根据下述式a求出的最高吸湿发热度可以超过0.025℃/g。式a：最高吸湿发热度＝{(将试样置于低湿度环境下直至试样温度达到平衡后转移到高湿度环境下之后的试样温度的最高值)-(将试样置于低湿度环境下直至试样温度达到平衡后转移到高湿度环境下时的试样温度)}(℃)/试样重量(g)需要说明的是，式a中，低湿度环境是指温度为20℃且相对湿度为40％的环境，高湿度环境是指温度为20℃且相对湿度为90％的环境。本实施方式的改造丝心蛋白的最高吸湿发热度可以为0.026℃/g以上、0.027℃/g以上、0.028℃/g以上、0.029℃/g以上、0.030℃/g以上、0.035℃/g以上或0.040℃/g以上。最高吸湿发热度的上限没有特别限制，通常为0.060℃/g以下。＜改造丝心蛋白的制造方法＞上述任一实施方式的改造丝心蛋白(以下有时简称为“蛋白质”)例如也可以通过下述方法进行生产：利用具有编码该蛋白质的核酸序列和以能够工作的方式与该核酸序列连接的一个或两个以上调节序列的表达载体对宿主进行转化，利用转化后的宿主来表达该核酸。编码改造丝心蛋白的核酸的制造方法没有特别限制。例如可以通过利用编码天然丝心蛋白的基因，利用聚合酶链式反应(pcr)等进行扩增而进行克隆，利用基因工程方法进行改造的方法；或者进行化学合成的方法来制造该核酸。核酸的化学合成方法也没有特别限制，例如可以利用下述方法化学合成基因：基于由ncbi网络数据库等获得的蛋白质的氨基酸序列信息，利用aktaoligopilotplus10/100(通用电气医疗日本株式会社)等自动合成寡核苷酸，将所合成的寡核苷酸通过pcr等进行连接。此时，为了易于进行改造丝心蛋白的纯化和/或确认，可以合成编码由在上述氨基酸序列的n末端添加由起始密码子和his10标签构成的氨基酸序列而得到的氨基酸序列构成的改造丝心蛋白的核酸。调节序列是对宿主中的改造丝心蛋白的表达进行调控的序列(例如，启动子、增强子、核糖体结合序列、转录终止序列等)，可以根据宿主的种类适当选择。作为启动子，可以使用在宿主细胞中发挥功能、能够诱导改造丝心蛋白表达的诱导性启动子。诱导性启动子是能够根据诱导物质(表达诱导剂)的存在、阻遏物分子的不存在、或者温度、渗透压或ph值的上升或降低等物理因素对转录进行调控的启动子。表达载体的种类可以根据宿主的种类适当选择质粒载体、病毒载体、柯斯质粒(cosmid)载体、福斯质粒(fosmid)载体、人工染色体载体等。作为表达载体，优选使用在宿主细胞中能够自主复制、或者能够整合到宿主的染色体中、且在能够对编码改造丝心蛋白的核酸进行转录的位置含有启动子的表达载体。作为宿主，原核生物、以及酵母、丝状真菌、昆虫细胞、动物细胞和植物细胞等真核生物均可以优选使用。作为原核生物宿主的优选例，可列举属于埃希氏菌属、短芽孢杆菌属、沙雷氏菌属、芽孢杆菌属、微杆菌属、短杆菌属、棒杆菌属和假单胞菌属等的细菌。作为属于埃希氏菌属的微生物，可列举例如大肠杆菌(escherichiacoli)等。作为属于短芽孢杆菌属的微生物，可列举例如土壤短芽孢杆菌(brevibacillusagri)等。作为属于沙雷氏菌属的微生物，可列举例如液化沙雷氏菌(serratialiquefacience)等。作为属于芽孢杆菌属的微生物，可列举例如枯草芽孢杆菌(bacillussubtilis)等。作为属于微杆菌属的微生物，可列举例如嗜氨微杆菌(microbacteriumammoniaphilum)等。作为属于短杆菌属的微生物，可列举例如叉开短杆菌(brevivacteriumdivaricatum)等。作为属于棒杆菌属的微生物，可列举例如产氨棒杆菌(corynebacteriumammoniagenes)等。作为属于假单胞菌(pseudomonas)属的微生物，可列举例如恶臭假单胞菌(pseudomonasputida)等。在以原核生物作为宿主的情况下，作为导入编码改造丝心蛋白的核酸的载体，可列举例如pbtrp2(boehringermannheim公司制)、pgex(pharmacia公司制)、puc18、pbluescriptii、psupex、pet22b、pcold、pub110、pnco2(日本特开2002-238569号公报)等。作为真核生物的宿主，可列举例如酵母和丝状真菌(霉菌等)。作为酵母，可列举例如属于酵母属、毕赤酵母属、裂殖酵母属等的酵母。作为丝状真菌，可列举例如属于曲霉属、青霉属、木霉(trichoderma)属等的丝状真菌。在以真核生物作为宿主的情况下，作为导入编码改造丝心蛋白的核酸的载体，可列举例如yep13(atcc37115)、yep24(atcc37051)等。作为向上述宿主细胞中导入表达载体的方法，只要是将dna导入上述宿主细胞中的方法则均可以使用。可列举例如使用钙离子的方法[proc.natl.acad.sci.usa,69,2110(1972)]、电穿孔法、原生质球法、原生质体法、乙酸锂法、感受态细胞法等。作为利用以表达载体进行了转化的宿主的核酸的表达方法，除了直接表达以外，还可以依照分子克隆第二版中记载的方法等进行分泌生产、融合蛋白表达等。改造丝心蛋白例如可以通过将利用表达载体进行了转化的宿主在培养用培养基中培养，使该蛋白质在培养用培养基中生成和蓄积，并从该培养用培养基中采集来制造。将宿主在培养用培养基中培养的方法可以按照宿主的培养中通常使用的方法进行。在宿主为大肠杆菌等原核生物或酵母等真核生物的情况下，作为培养用培养基，只要是含有宿主可同化的碳源、氮源和无机盐类等、能够高效地进行宿主的培养的培养基，则可以使用天然培养基和合成培养基中的任意一种。作为碳源，只要是上述转化微生物可同化的碳源即可，可以使用例如葡萄糖、果糖、蔗糖以及含有这些糖的糖蜜、淀粉和淀粉水解物等碳水化合物、乙酸和丙酸等有机酸、以及乙醇和丙醇等醇类。作为氮源，可以使用例如氨、氯化铵、硫酸铵、乙酸铵和磷酸铵等无机酸或有机酸的铵盐、其他含氮化合物、以及蛋白胨、肉提取物、酵母提取物、玉米浆、酪蛋白水解物、豆粕和豆粕水解物、各种发酵菌体及其消化产物。作为无机盐，可以使用例如磷酸二氢钾、磷酸氢二钾、磷酸镁、硫酸镁、氯化钠、硫酸亚铁、硫酸锰、硫酸铜和碳酸钙。大肠杆菌等原核生物或酵母等真核生物的培养例如可以在振荡培养或深部通气搅拌培养等需氧条件下进行。培养温度例如为15～40℃。培养时间通常为16小时～7天。培养中的培养用培养基的ph优选保持于3.0～9.0。培养用培养基的ph的调节可以使用无机酸、有机酸、碱溶液、尿素、碳酸钙和氨等进行。另外，培养中，可以根据需要在培养用培养基中添加氨苄青霉素和四环素等抗生素。在对利用使用诱导性启动子作为启动子的表达载体进行了转化的微生物进行培养时，可以根据需要在培养基中添加诱导剂。例如，在对利用使用lac启动子的表达载体进行了转化的微生物进行培养时，可以在培养基中添加异丙基-β-d-硫代吡喃半乳糖苷等；在对利用使用trp启动子的表达载体进行了转化的微生物进行培养时，可以在培养基中添加吲哚丙烯酸等。所表达的改造丝心蛋白的分离和纯化可以利用通常使用的方法进行。例如，在该蛋白质以溶解状态在细胞内进行表达的情况下，在培养结束后，通过离心分离回收宿主细胞，悬浮于水系缓冲液中后，利用超声波破碎机、弗氏压碎器、manton-gaulin匀浆器和戴诺研磨机(dyno-mill)等将宿主细胞破碎，得到无细胞提取液。从通过将该无细胞提取液离心分离而得到的上清中，单独或组合使用蛋白质的分离纯化中通常使用的方法、即溶剂提取法、利用硫酸铵等的盐析法、脱盐法、利用有机溶剂的沉淀法、使用二乙基氨基乙基(deae)-琼脂糖、diaionhpa-75(三菱化成公司制)等树脂的阴离子交换层析法、使用s-琼脂糖ff(pharmacia公司制)等树脂的阳离子交换层析法、使用丁基琼脂糖、苯基琼脂糖等树脂的疏水性层析法、使用分子筛的凝胶过滤法、亲和层析法、聚焦层析法、等电聚焦电泳等电泳法等方法，能够得到纯化制备品。另外，在改造丝心蛋白在细胞内形成不溶体而进行表达的情况下，同样地回收宿主细胞后将其破碎并进行离心分离，由此以沉淀级分的形式回收改造丝心蛋白的不溶体。回收的改造丝心蛋白的不溶体可以利用蛋白变性剂进行可溶化。该操作后，利用与上述同样的分离纯化法能够得到改造丝心蛋白的纯化制备品。在该蛋白质被分泌到细胞外的情况下，可以从培养上清中回收该蛋白质。即，利用离心分离等方法对培养物进行处理，由此获得培养上清，通过使用与上述同样的分离纯化法，能够从该培养上清中得到纯化制备品。＜改造丝心蛋白纤维的制造方法＞在改造丝心蛋白纤维为改造丝心蛋白长丝的情况下，可以通过公知的纺丝方法制造改造丝心蛋白长丝。即，例如制造包含改造丝心蛋白作为主要成分的改造丝心蛋白长丝时，首先将依照上述方法制造的改造丝心蛋白根据需要与作为溶解促进剂的无机盐一起添加到二甲基亚砜(dmso)、n,n-二甲基甲酰胺(dmf)、甲酸或六氟异丙醇(hfip)等溶剂中，进行溶解，由此制作纺丝原液。接着，使用该纺丝原液，利用湿式纺丝、干式纺丝、干湿式纺丝或熔融纺丝等公知的纺丝方法进行纺丝，可以得到改造丝心蛋白长丝。作为优选的纺丝方法，可列举湿式纺丝或干湿式纺丝。图6为示意性示出用于制造改造丝心蛋白长丝的纺丝装置的一例的说明图。图6所示的纺丝装置10为干湿式纺丝用的纺丝装置的一例，具备挤出装置1、未拉伸丝制造装置2、湿热拉伸装置3和干燥装置4。对使用纺丝装置10的纺丝方法进行说明。首先，利用齿轮泵8将储藏于储槽7中的纺丝原液6从喷头9挤出。在实验室规模上，可以将纺丝原液填充至注射器中，使用注射泵从喷嘴挤出。接着，挤出的纺丝原液6经过气隙19被供给至凝固液槽20的凝固液11内，溶剂被除去，改造丝心蛋白发生凝固，形成纤维状凝固体。接着，纤维状凝固体被供给至拉伸浴槽21内的温水12中，进行拉伸。拉伸倍率由供给夹持辊13与引离夹持辊14的速度比决定。然后，拉伸后的纤维状凝固体被供给至干燥装置4，在丝路22内被干燥，以卷丝体5的形式得到改造丝心蛋白长丝36。18a～18g为导丝器。作为凝固液11，只要是能够脱溶剂的溶剂即可，可列举例如甲醇、乙醇和2-丙醇等碳原子数1～5的低级醇、以及丙酮等。凝固液11可以适当含有水。凝固液11的温度优选为0～30℃。在使用具有直径0.1～0.6mm的喷嘴作为喷头9的注射泵的情况下，挤出速度优选为每一孔0.2～6.0ml/小时，更优选为每一孔1.4～4.0ml/小时。凝固后的改造丝心蛋白在凝固液11中通过的距离(实质上为从导丝器18a至导丝器18b的距离)只要是能够高效地进行脱溶剂的长度即可，例如为200～500mm。未拉伸丝的引离速度例如可以为1～20m/分钟，优选为1～3m/分钟。在凝固液11中的停留时间例如可以为0.01～3分钟，优选为0.05～0.15分钟。另外，可以在凝固液11中进行拉伸(预拉伸)。凝固液槽20可以设置多段，并且可以根据需要在各段或特定的段中进行拉伸。需要说明的是，关于得到改造丝心蛋白长丝时实施的拉伸，除了例如上述的在凝固液槽20内进行的预拉伸和在拉伸浴槽21内进行的湿热拉伸以外，还可以采用干热拉伸。湿热拉伸可以在温水中、向温水中添加有机溶剂等而得到的溶液中或蒸汽加热中进行。作为温度，例如可以为50～90℃，优选为75～85℃。在湿热拉伸中，可以将未拉伸丝(或预拉伸丝)拉伸例如1～10倍，优选拉伸2～8倍。干热拉伸可以使用管式电热炉、干热板等来进行。作为温度，例如可以为140℃～270℃，优选为160℃～230℃。在干热拉伸中，可以将未拉伸丝(或预拉伸丝)拉伸例如0.5～8倍，优选拉伸1～4倍。湿热拉伸和干热拉伸可以分别单独进行，另外也可以将它们以多步或组合进行。即，可以以湿热拉伸进行第一步拉伸，以干热拉伸进行第二步拉伸；或者第一步拉伸进行湿热拉伸，第二步拉伸进行湿热拉伸，进一步以干热拉伸进行第三步拉伸等，可以将湿热拉伸和干热拉伸适当组合进行。关于最终拉伸倍率，其下限值相对于未拉伸丝(或预拉伸丝)优选为超过1倍、2倍以上、3倍以上、4倍以上、5倍以上、6倍以上、7倍以上、8倍以上、9倍以上中的任意一种，上限值优选为40倍以下、30倍以下、20倍以下、15倍以下、14倍以下、13倍以下、12倍以下、11倍以下、10倍以下。通过以上方法得到的改造丝心蛋白长丝的长度可根据纺丝的条件适宜地调节。改造丝心蛋白长丝的长度没有特别限制，也可以设为例如超过1500m、10000m以上、15000m以上或20000m以上。(切断工序)在改造丝心蛋白纤维为改造丝心蛋白短纤维的情况下，改造丝心蛋白短纤维可以通过将利用上述方法制造的改造丝心蛋白长丝切断来制造。需要说明的是，改造丝心蛋白长丝的切断可以在后述的卷曲工序之后或干燥工序之后进行。改造丝心蛋白短纤维的长度没有特别限制，可以为20mm以上、20～140mm、70～140mm或20～70mm。(卷曲工序)在改造丝心蛋白纤维为改造丝心蛋白卷曲纤维(改造丝心蛋白卷曲短纤维或改造丝心蛋白卷曲短纤维)的情况下，改造丝心蛋白卷曲纤维例如可以通过使未卷曲的改造丝心蛋白纤维卷曲来制造。改造丝心蛋白纤维可以利用以往的机械卷曲加工来进行卷曲，也可以通过与水性介质接触来进行卷曲。另外，也可以将这些加工方法组合使用。作为机械卷曲加工方法，可列举例如假捻法、压入法、刮擦法、空气喷射法(高压空气喷射法)和赋形法。发明中的改造丝心蛋白纤维通过与水接触而收缩、卷曲。因此，若利用与水性介质接触的加工方法，则可以不依靠外力而使改造丝心蛋白纤维卷曲。水性介质是指含有水(包括水蒸汽。)的液体或气体(蒸汽)的介质。水性介质可以为水，也可以为水与亲水性溶剂的混合液。另外，作为亲水性溶剂，还能够使用例如乙醇和甲醇等挥发性溶剂或其蒸气。水性介质优选水与乙醇的混合溶液。通过使用包含挥发性溶剂或其蒸气的水性介质，改造丝心蛋白纤维干燥得快，成为更有柔软感的成品。水与挥发性溶剂或其蒸气的比率没有特别限制，例如，水：挥发性溶剂或其蒸气以质量比计可以为10：90～90：10。在水性介质为液体时，水性介质中可以分散有例如工序通过用(例如防静电用等)或精加工用的油剂等公知的油剂。即，也可以使用包含水性介质和分散在水性介质中的油剂的油剂分散液来代替水性介质。通过使用这样的油剂分散液，可以在使改造丝心蛋白纤维卷曲的同时使油剂附着于改造丝心蛋白纤维。通过使油剂附着于改造丝心蛋白纤维，可以对改造丝心蛋白纤维赋予各种特性。需要说明的是，油剂的量没有特别限制，例如，相对于水性介质与油剂的总量可以为1～10质量％，或者可以为2～5质量％。水性介质的温度可以为10℃以上、25℃以上、40℃以上、60℃以上或100℃以上，可以为230℃以下、120℃以下或100℃以下。更具体而言，在水性介质为气体(蒸汽)的情况下，水性介质的温度优选为100～230℃，更优选为100～120℃。若水性介质的蒸汽为230℃以下，则可以防止改造丝心蛋白纤维的热变性。在水性介质为液体的情况下，从高效地赋予卷曲的观点出发，水性介质的温度优选为10℃以上、25℃以上或40℃以上，从使改造丝心蛋白纤维的纤维强度保持得较高的观点出发，优选为60℃以下。使改造丝心蛋白纤维与水性介质接触的时间没有特别限制，可以为30秒以上、1分钟以上或2分钟以上，从生产率的观点出发，优选为10分钟以下。水性介质与改造丝心蛋白纤维的接触可以在常压下进行，也可以在减压下(例如真空中)进行。作为使改造丝心蛋白纤维与水性介质接触的方法，可列举：将改造丝心蛋白纤维浸渍在水中的方法、对改造丝心蛋白纤维喷射水性介质的蒸汽的方法、使改造丝心蛋白纤维暴露于充满水性介质的蒸汽的环境中的方法等。在水性介质为蒸汽的情况下，水性介质与改造丝心蛋白纤维的接触可以使用常规的蒸汽定型装置。作为蒸汽定型装置的具体例，可列举产品名：fmsa型蒸汽机(福伸工业株式会社制)、产品名：eps-400(辻井染机工业株式会社制)等装置。作为通过水性介质的蒸汽使改造丝心蛋白纤维卷曲的方法的具体例，可列举：一面在规定的收容室内收容改造丝心蛋白纤维，一面向收容室内导入水性介质的蒸汽，将收容室内的温度调整为上述规定温度(例如100℃～230℃)且使蒸汽与改造丝心蛋白纤维接触。需要说明的是，通过与水性介质接触而进行的改造丝心蛋白纤维的卷曲工序优选在不对改造丝心蛋白纤维施加任何拉伸力(在纤维轴向上完全不绷紧)的状态或仅施加规定大小(在纤维轴向上以规定量绷紧)的状态下实施。此时，能够通过调整施加于改造丝心蛋白纤维的拉伸力来控制卷曲的程度。作为施加于改造丝心蛋白纤维的拉伸力的调整方法，可列举例如：对改造丝心蛋白纤维悬吊各种重量的重物等，从而调整对改造丝心蛋白纤维负载的载荷的方法；在使改造丝心蛋白纤维松弛的状态下固定两末端、并且对其松弛量进行各种变更的方法；将改造丝心蛋白纤维卷绕于纸筒或线轴等被卷绕体上、并且适当变更此时的卷绕力(对纸筒、线轴的缠绕力)的方法等。(干燥工序)在使改造丝心蛋白纤维与水性介质接触之后，可以对改造丝心蛋白纤维进行干燥。干燥方法没有特别限制，可以为自然干燥，也可以使用干燥设备强制干燥改造丝心蛋白纤维。利用水性介质进行的卷曲和此后的干燥可以连续地进行。具体而言，例如，可以一边从线轴退出改造丝心蛋白纤维一边浸渍于水性介质中后，吹送热风或送到热辊上而进行干燥。作为干燥温度，没有特别限制，可以为例如20～150℃，优选为40～120℃，更优选为60～100℃。＜织物＞本发明的一个方式涉及上述混纺纱的织物。织物为针织物和机织物的总称。构成织物的混纺纱可以为单丝，也可以为双丝。针织物可以为具有横编、圆编等纬编组织的针织物(也简称为“纬编针织物”)、具有特利科脱(tricot)、拉舍尔(raschel)等经编组织的针织物(也简称为“经针织物”)中的任意一种。机织物可以为具有平纹、斜纹或缎纹中的任一种组织的机织物。织物可以为通过针织或机织得到的未加工的织物本身，也可以为在针织或机织后实施了收缩加工等加工的织物。＜织物的制造方法＞本发明的织物可以通过具备对改造丝心蛋白纤维和再生纤维素纤维进行混纺而得到混纺纱的工序(混纺工序)和对混纺纱进行针织或机织而得到未加工织物的工序(针织或机织工序)的方法来制造。(混纺工序)本工序中，对改造丝心蛋白纤维和再生纤维素纤维进行混纺而得到混纺纱。改造丝心蛋白纤维、再生纤维素纤维和混纺纱的详细情况如上所述。混纺方法没有特别限制，可以采用公知的纺纱方法。(针织或机织工序)本工序中，对混纺纱进行针织或机织而得到未加工织物(未加工针织物或未加工机织物)。作为针织方法和机织方法，可以利用公知的方法。作为使用的针织机，可使用例如圆编机、经编机、横编机等，从生产率的观点出发，优选使用圆编机。作为横编机，有成型针织机、无缝制针织机等，特别是出于能够以最终产品的形态制造未加工针织物的原因，更优选使用无缝制针织机。作为使用的机织机，可列举例如有梭织机、以及片梭织机、剑杆织机、喷水织机、喷气织机等无梭织机。(收缩工序)可以对得到的未加工织物任意地进行各种加工。作为加工的一例，可列举使未加工织物与水性介质接触而使未加工织物中含有的改造丝心蛋白纤维收缩的加工。该加工可以通过与使改造丝心蛋白纤维与水性介质接触而卷曲的方法同样的方法来实施。即，可以通过将未加工织物浸渍在水中的方法、对未加工织物喷射水性介质的蒸汽的方法、使未加工织物暴露于充满水性介质的蒸汽的环境中的方法等来使未加工织物中含有的改造丝心蛋白纤维收缩，水性介质和各条件的详细情况如此前所述。更具体而言，可以通过使未加工织物与水性介质接触、接着进行干燥来使未加工织物中含有的改造丝心蛋白纤维收缩。经过收缩工序而得到的织物具有高密度，并且进一步减少了由湿润导致的弹力和硬挺度的下降。实施例以下基于实施例更具体地说明本发明。但是，本发明不受以下的实施例限定。＜改造蛛丝丝心蛋白的制造＞(1)质粒表达株的制作基于金纺蜘蛛(nephilaclavipes)来源的丝心蛋白(genbank登录号：p46804.1、gi：1174415)的碱基序列和氨基酸序列设计出具有序列号15(prt799)所示的氨基酸序列的改造丝心蛋白。另外，还设计出具有序列号37所示的氨基酸序列的改造丝心蛋白(prt918)和具有序列号40所示的氨基酸序列的改造丝心蛋白(prt966)。然后合成编码所设计的改造丝心蛋白的核酸。该核酸中，在5’末端添加有ndei位点，在终止密码子下游添加有ecori位点。将该核酸克隆到克隆载体(puc118)中。然后，用ndei和ecori进行限制酶处理而切出该核酸后，重组到蛋白质表达载体pet-22b(+)中，得到表达载体。(2)蛋白质的表达利用包含编码所设计的改造丝心蛋白的核酸的pet-22b(+)表达载体对大肠杆菌blr(de3)进行转化。将该转化大肠杆菌在含有氨苄青霉素的2ml的lb培养基中培养15小时。将该培养液添加到含有氨苄青霉素的100ml的种子培养用培养基(表4)中，使od600达到0.005。将培养液温度保持在30℃，进行烧瓶培养直至od600达到5为止(约15小时)，得到种子培养液。[表4]种子培养用培养基将该种子培养液添加到添加有500ml的生产培养基(表5)的发酵罐中，使od600达到0.05。使培养液温度保持在37℃，在ph6.9下控制恒定而进行培养。另外，将培养液中的溶解氧浓度维持于溶解氧饱和浓度的20％。[表5]生产培养基在生产培养基中的葡萄糖被完全消耗后，立即以1ml/分钟的速度添加补料液(葡萄糖455g/1l、酵母提取物120g/1l)。将培养液温度保持在37℃，在ph6.9下控制恒定而进行培养。另外，使得培养液中的溶解氧浓度维持于溶解氧饱和浓度的20％，进行20小时培养。然后，向培养液中添加1m的异丙基-β-硫代吡喃半乳糖苷(iptg)以使终浓度达到1mm，诱导表达改造丝心蛋白。在添加iptg后经过20小时的时刻，离心分离培养液，回收菌体。使用由添加iptg前和添加iptg后的培养液制备的菌体进行sds-page，根据依赖于iptg添加的目标改造丝心蛋白的大小的条带的出现，确认到目标改造丝心蛋白的表达。(3)蛋白质的纯化将添加iptg起2小时后回收的菌体用20mmtris-hcl缓冲液(ph7.4)进行清洗。使清洗后的菌体悬浮在包含约1mm的pmsf的20mmtris-hcl缓冲液(ph7.4)中，利用高压均质器(geanirosoavi公司制)将细胞破碎。将破碎的细胞离心分离，得到沉淀物。利用20mmtris-hcl缓冲液(ph7.4)清洗所得到的沉淀物，直至达到高纯度为止。将清洗后的沉淀物以达到100mg/ml的浓度的方式悬浮在8m胍缓冲液(8m胍盐酸盐、10mm磷酸二氢钠、20mmnacl、1mmtris-hcl、ph7.0)中，在60℃下用搅拌器搅拌30分钟，使其溶解。溶解后，使用透析管(三光纯药株式会社制造的纤维素管36/32)在水中进行透析。通过离心分离来回收透析后得到的白色凝集蛋白质，利用冷冻干燥机除去水分，回收冻干粉末，由此得到改造蛛丝丝心蛋白“prt799”、“prt918”和“prt966”。＜改造丝心蛋白长丝的制造＞(1)纺丝原液的制备向dmso中添加上述的改造丝心蛋白(prt799、prt918或prt966)，使浓度达到24质量％，然后添加作为溶解促进剂的licl，使浓度达到4.0质量％。然后，使用摇床用3小时溶解改造丝心蛋白，得到dmso溶液。除去得到的dmso溶液中的不溶物和气泡，作为纺丝原液。纺丝原液的溶液粘度在90℃下为5000cp(厘泊)。(2)纺丝使用如上述那样得到的纺丝原液和图6所示的纺丝装置10进行公知的干湿式纺丝，得到改造丝心蛋白长丝。将得到的改造丝心蛋白长丝卷绕在线轴上。需要说明的是，这里，按照下述的条件进行干湿式纺丝。凝固液(甲醇)的温度：5～10℃拉伸倍率：4.52倍干燥温度：80℃＜实施例＞将多根如上述那样得到的改造丝心蛋白长丝捆扎，用台式纤维切断机切成38mm的长度，制作改造丝心蛋白短纤维。将制作的改造丝心蛋白短纤维在40℃的水中浸渍1分钟而使其卷曲，接着在40℃下干燥18小时，得到改造丝心蛋白卷曲短纤维。通过浸渍于水中而得到的改造丝心蛋白短纤维的收缩率为50％。将该改造丝心蛋白卷曲短纤维和市售的莱赛尔卷曲短纤维用公知的纺纱设备进行纺纱，得到具有2/30nm的纤度和570t/m的捻度的混纺纱的双丝。混纺纱中的改造丝心蛋白卷曲短纤维的比例为20质量％。使用混纺纱的双丝，利用横编机通过天竺织制作针织物。使针织物浸渍于水中，观察干燥后的弹力和硬挺度的变化。具体而言，首先将预先测定了重量(初始重量)的上述针织物浸渍于温度37.5℃的水中。90秒后将针织物从水中取出，用纸巾去除针织物的水分。用干燥机(松下制eh5101p)进行干燥，使得重量恢复至初始重量。将干燥后的针织物的照片示于图7。干燥后的针织物与浸渍于水中之前相比稍稍变厚，成为硬挺状态。＜比较例＞使用具有2/30nm的纤度和295t/m的捻度的市售的莱赛尔短纤纱的双丝，利用横编机通过天竺织制作针织物。与实施例同样地，将针织物浸渍于水中，并观察干燥后的弹力和硬挺度的变化。将干燥后的针织物的照片示于图8。实施例的针织物与比较例的针织物相比，在水中浸渍并干燥后的弹力和硬挺度的下降得到抑制。＜参考例1＞将与上述实施例同样得到的改造丝心蛋白prt799的纺丝原液在60℃下用网眼为5μm的金属过滤器过滤，接着在30ml的不锈钢注射器内静置而脱泡后，从针直径为0.2mm的实心喷嘴向100质量％甲醇凝固浴槽中吐出。吐出温度为60℃。凝固后，将得到的原丝卷取，自然干燥，得到改造丝心蛋白纤维。使用得到的原料纤维，通过使用圆编机的圆编制造针织物。针织物的粗度为180旦尼尔、机号为18。从得到的针织物切出20g，作为试验片使用。基于日本“消防危50号(1995年5月31日)”中记载的“粉粒状或熔点低的合成树脂的试验方法”进行燃烧性试验。试验在温度22℃、相对湿度45％、气压1021hpa的条件下实施。将测定结果(氧浓度(％)、燃烧率(％)和换算燃烧率(％))示于表6。[表6]氧浓度(％)燃烧率(％)换算燃烧率(％)20.039.140.127.048.149.328.051.953.230.053.654.950.061.262.770.091.193.3100.097.6100.0燃烧性试验的结果为：用改造丝心蛋白(prt799)纤维编织得到的针织物的极限氧指数(loi)值为27.2。通常，若loi值为26以上，则视为有阻燃性。可知改造丝心蛋白的阻燃性优良。因此，可以说包含这样的改造丝心蛋白纤维的混纺纱及其织物的阻燃性优良。<参考例2>将与上述实施例同样得到的改造丝心蛋白(prt799或prt918)的纺丝原液在60℃下用网眼为5μm的金属过滤器过滤，接着在30ml的不锈钢注射器内静置而脱泡后，从针直径为0.2mm的实心喷嘴吐出到100质量％甲醇凝固浴槽中。吐出温度为60℃。凝固后，将得到的原丝卷取，自然干燥，得到改造丝心蛋白纤维(原料纤维)。为了比较，作为原料纤维，准备市售的羊毛纤维、棉纤维、天丝纤维、人造丝纤维和聚酯纤维。使用各原料纤维，通过使用横编机的横编分别制造针织物。使用prt918纤维作为原料纤维的针织物设为粗度：1/30n(毛支数单丝)、机号：18。使用prt799纤维作为原料纤维的针织物设为粗度：1/30n(毛支数单丝)、机号：16。调整使用其他原料纤维的针织物的粗度和机号，使得与使用prt918纤维和prt799纤维的针织物达到大致相同的覆盖系数。需要说明的是，使用改造丝心蛋白纤维以外的纤维的针织物的粗度和机号如下进行调整。羊毛纤维粗度：2/30n(双丝)、机号：14棉纤维粗度：2/34n(双丝)、机号：14天丝纤维粗度：2/30n(双丝)、机号：15人造丝纤维粗度：1/38n(单丝)、机号：14聚酯纤维粗度：1/60n(单丝)、机号：14将2片切成10cm×10cm的针织物重叠，将四条边缝合，制成试验片(试样)。将试验片在低湿度环境(温度20±2℃、相对湿度40±5％)下放置4小时以上后，转移到高湿度环境(温度20±2℃、相对湿度90±5％)下，利用安装在试验片内部中央的温度传感器以1分钟的间隔测定温度，测定30分钟。由测定结果按照下述式a求出最高吸湿发热度。式a：最高吸湿发热度＝{(将试样置于低湿度环境下直至试样温度达到平衡后转移到高湿度环境下之后的试样温度的最高值)-(将试样置于低湿度环境下直至试样温度达到平衡后转移到高湿度环境下时的试样温度)}(℃)/试样重量(g)图9为示出吸湿发热性试验的结果的一例的图。图的横轴是以将试样从低湿度环境转移到高湿度环境的时刻设为0来示出在高湿度环境下的放置时间(分钟)。图的纵轴表示用温度传感器测得的温度(试样温度)。图9所示的图中，m所表示的点对应于试样温度的最高值。将最高吸湿发热度的计算结果示于表7。[表7]原料纤维最高吸湿发热度(℃/g)prt9180.040prt7990.031羊毛0.020棉0.021天丝0.018人造丝0.025聚酯0.010如表7所示，可知：改造丝心蛋白(prt918和prt799)纤维与现有的材料相比，最高吸湿发热度高，吸湿发热性优良。因此，可以说包含这样的改造丝心蛋白纤维的混纺纱及其织物的吸湿发热性优良。<参考例3>将与上述实施例同样得到的改造丝心蛋白prt799和prt966的纺丝原液在60℃下用网眼5μm的金属过滤器过滤，接着在30ml的不锈钢注射器内静置而脱泡后，从针直径为0.2mm的实心喷嘴向100质量％甲醇凝固浴槽中吐出。吐出温度为60℃。凝固后，将得到的原丝卷取，自然干燥，得到改造丝心蛋白纤维(原料纤维)。为了比较，作为原料纤维，准备市售的羊毛纤维、蚕丝纤维、棉纤维、人造丝纤维和聚酯纤维。使用各原料纤维，通过使用横编机的横编分别制造针织物。将使用prt966纤维和prt799纤维的针织物的支数、加捻根数、机号和基重示于表8。调整使用其他原料纤维的针织物的粗度和机号，使得覆盖系数与改造丝心蛋白纤维的针织物的覆盖系数大致相同。具体如表8所示。[表8]使用katotech株式会社制的kes-f7thermo-laboii试验机，用干接触法评价保温性。干接触法为设定使皮肤与衣服在干燥状态下直接接触时的方法。使用1片切成20cm×20cm的矩形的针织物作为试验片(试样)。将试验片在设为恒定温度(30℃)的热板上定型，在风洞内风速为30cm/秒的条件下求出隔着试验片而发散的热量(a)。在未对试验片进行定型的状态下，以上述同样的条件求出发散的热量(b)，按照下式算出保温率(％)。保温率(％)＝(1-a/b)×100由测定结果按照下述式b求出保温性指数。式b：保温性指数＝保温率(％)/试样的基重(g/m2)将保温性指数的计算结果示于表9。保温性指数越高，则可以评价为保温性越优良的材料。[表9]原料纤维保温性指数prt9660.33prt7990.22羊毛0.16蚕丝0.11棉0.13人造丝0.02聚酯0.18如表9所示，可知：改造丝心蛋白(prt966和prt799)纤维与现有的材料相比，保温性指数高，保温性优良。符号说明1…挤出装置、2…未拉伸丝制造装置、3…湿热拉伸装置、4…干燥装置、6…纺丝原液、10…纺丝装置、20…凝固液槽、21…拉伸浴槽、36…改造丝心蛋白长丝。序列表<110>长谷虎纺绩株式会社（hasetoraspinningco.ltd.）丝芭博株式会社（spiberinc.）<120>混纺纱以及该混纺纱的织物和该织物的制造方法（amixedspunyarn,andaknittedorwovenfabricthereofandamethodforproducingthesame）<130>fp19-0337-00<150>jp2018-071886<151>2018-04-03<150>jp2018-185166<151>2018-09-28<160>44<170>patentinversion3.5<210>1<211>50<212>prt<213>十字园蛛（araneusdiadematus）<400>1serglycysaspvalleuvalglnalaleuleugluvalvalserala151015leuvalserileleuglyserserserileglyglnileasntyrgly202530alaseralaglntyrthrglnmetvalglyglnservalalaglnala354045leuala50<210>2<211>30<212>prt<213>十字园蛛<400>2serglycysaspvalleuvalglnalaleuleugluvalvalserala151015leuvalserileleuglyserserserileglyglnileasn202530<210>3<211>21<212>prt<213>十字园蛛<400>3serglycysaspvalleuvalglnalaleuleugluvalvalserala151015leuvalserileleu20<210>4<211>1154<212>prt<213>人工序列（artificialsequence）<220><223>重组蛛丝蛋白adf3kailargenrsh1（recombinantspidersilkproteinadf3kailargenrsh1）<400>4methishishishishishishishishishisserserglyserser151015leugluvalleupheglnglyproalaargalaglyserglyglngln202530glyproglyglnglnglyproglyglnglnglyproglyglnglngly354045protyrglyproglyalaseralaalaalaalaalaalaglyglytyr505560glyproglyserglyglnglnglyproserglnglnglyproglygln65707580glnglyproglyglyglnglyprotyrglyproglyalaseralaala859095alaalaalaalaglyglytyrglyproglyserglyglnglnglypro100105110glyglyglnglyprotyrglyproglyserseralaalaalaalaala115120125alaglyglyasnglyproglyserglyglnglnglyalaglyglngln130135140glyproglyglnglnglyproglyalaseralaalaalaalaalaala145150155160glyglytyrglyproglyserglyglnglnglyproglyglnglngly165170175proglyglyglnglyprotyrglyproglyalaseralaalaalaala180185190alaalaglyglytyrglyproglyserglyglnglyproglyglngln195200205glyproglyglyglnglyprotyrglyproglyalaseralaalaala210215220alaalaalaglyglytyrglyproglyserglyglnglnglyprogly225230235240glnglnglyproglyglnglnglyproglyglyglnglyprotyrgly245250255proglyalaseralaalaalaalaalaalaglyglytyrglyprogly260265270tyrglyglnglnglyproglyglnglnglyproglyglyglnglypro275280285tyrglyproglyalaseralaalaseralaalaserglyglytyrgly290295300proglyserglyglnglnglyproglyglnglnglyproglyglygln305310315320glyprotyrglyproglyalaseralaalaalaalaalaalaglygly325330335tyrglyproglyserglyglnglnglyproglyglnglnglyprogly340345350glnglnglyproglyglnglnglyproglyglyglnglyprotyrgly355360365proglyalaseralaalaalaalaalaalaglyglytyrglyprogly370375380serglyglnglnglyproglyglnglnglyproglyglnglnglypro385390395400glyglnglnglyproglyglnglnglyproglyglnglnglyprogly405410415glnglnglyproglyglnglnglyproglyglnglnglyproglygly420425430glnglyalatyrglyproglyalaseralaalaalaglyalaalagly435440445glytyrglyproglyserglyglnglnglyproglyglnglnglypro450455460glyglnglnglyproglygl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