ID FA8_PIG Reviewed; 2133 AA. AC P12263; Q95243; DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 2. DT 04-NOV-2026, entry version 161. DE RecName: Full=Coagulation factor VIII; DE AltName: Full=Procoagulant component; DE Flags: Precursor; GN Name=F8; Synonyms=CF8; OS Sus scrofa (Pig). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus. OX NCBI_TaxID=9823; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RA Healey J.F., Lubin I.M., Lollar P.; RL Submitted (MAY-1996) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] OF 705-1573. RX PubMed=3016730; DOI=10.1073/pnas.83.16.5939; RA Toole J.J., Pittman D.D., Orr E.C., Murtha P., Wasley L.C., Kaufman R.J.; RT "A large region (approximately equal to 95 kDa) of human factor VIII is RT dispensable for in vitro procoagulant activity."; RL Proc. Natl. Acad. Sci. U.S.A. 83:5939-5942(1986). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] OF 392-759. RX PubMed=7510693; DOI=10.1016/s0021-9258(17)37014-x; RA Lubin I.M., Healey J.F., Scandella D., Runge M.S., Lollar P.; RT "Elimination of a major inhibitor epitope in factor VIII."; RL J. Biol. Chem. 269:8639-8641(1994). CC -!- FUNCTION: Factor VIII, along with calcium and phospholipid, acts as a CC cofactor for factor IXa when it converts factor X to the activated CC form, factor Xa. CC -!- SUBUNIT: Interacts with vWF. vWF binding is essential for the CC stabilization of F8 in circulation (By similarity). {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space. CC -!- PTM: Proteolytically cleaved by cathepsin CTSG to produce a partially CC activated form. {ECO:0000250|UniProtKB:P00451}. CC -!- SIMILARITY: Belongs to the multicopper oxidase family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U49517; AAB06705.1; -; mRNA. DR PIR; A25945; A25945. DR PIR; T42763; T42763. DR RefSeq; NP_999332.3; NM_214167.3. DR PDB; 4MO3; X-ray; 1.70 A; M=1971-2129. DR PDB; 6MF0; X-ray; 3.20 A; A/B=3-405, A/B=762-1820. DR PDB; 7K66; X-ray; 3.92 A; A=1-405, A=1438-1820. DR PDB; 7KBT; X-ray; 4.15 A; A=1-405, A=762-1820. DR PDB; 7S0P; X-ray; 1.30 A; M=1974-2129. DR PDB; 8G6I; EM; 4.23 A; A=1-405, A=1438-1820. DR PDB; 8TY1; EM; 3.46 A; A=1-405, A=762-1820. DR AlphaFoldDB; P12263; -. DR SMR; P12263; -. DR FunCoup; P12263; 192. DR STRING; 9823.ENSSSCP00000028556; -. DR GlyConnect; P12263; 22 N-Linked glycans. DR GlyCosmos; P12263; 16 sites, 41 glycans. DR GlyGen; P12263; 17 sites, 41 N-linked glycans (1 site). DR PaxDb; 9823-ENSSSCP00000028556; -. DR ABCD; P12263; 1 sequenced antibody. DR GeneID; 397339; -. DR KEGG; ssc:397339; -. DR CTD; 2157; -. DR eggNOG; ENOG502QSFZ; Eukaryota. DR InParanoid; P12263; -. DR OMA; AAHSNEG; -. DR OrthoDB; 2121828at2759; -. DR EvolutionaryTrace; P12263; -. DR Proteomes; UP000008227; Unplaced. DR GO; GO:0005576; C:extracellular region; IBA:GO_Central. DR GO; GO:0031091; C:platelet alpha granule; IEA:UniProtKB-ARBA. DR GO; GO:0005507; F:copper ion binding; IEA:InterPro. DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro. DR GO; GO:0007597; P:blood coagulation, intrinsic pathway; IBA:GO_Central. DR CDD; cd00057; FA58C; 2. DR FunFam; 2.60.120.260:FF:000002; Coagulation factor VIII; 2. DR FunFam; 2.60.40.420:FF:000047; Coagulation factor VIII; 1. DR FunFam; 2.60.40.420:FF:000051; Coagulation factor VIII; 1. DR FunFam; 2.60.40.420:FF:000011; Coagulation factor VIII (Predicted); 1. DR FunFam; 2.60.40.420:FF:000026; Coagulation factor VIII (Predicted); 1. DR FunFam; 2.60.40.420:FF:000032; Coagulation factor VIII (Predicted); 1. DR FunFam; 2.60.40.420:FF:000035; Coagulation factor VIII (Predicted); 1. DR Gene3D; 2.60.40.420; Cupredoxins - blue copper proteins; 6. DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 2. DR InterPro; IPR011707; Cu-oxidase-like_N. DR InterPro; IPR001117; Cu-oxidase_2nd. DR InterPro; IPR011706; Cu-oxidase_C. DR InterPro; IPR033138; Cu_oxidase_CS. DR InterPro; IPR008972; Cupredoxin. DR InterPro; IPR000421; FA58C. DR InterPro; IPR024715; Factor_5/8-like. DR InterPro; IPR008979; Galactose-bd-like_sf. DR InterPro; IPR050633; Neuropilin_MCO_CoagFactor. DR PANTHER; PTHR46806:SF7; COAGULATION FACTOR VIII; 1. DR PANTHER; PTHR46806; F5/8 TYPE C DOMAIN-CONTAINING PROTEIN; 1. DR Pfam; PF00394; Cu-oxidase; 1. DR Pfam; PF07731; Cu-oxidase_2; 1. DR Pfam; PF07732; Cu-oxidase_3; 2. DR Pfam; PF00754; F5_F8_type_C; 2. DR PIRSF; PIRSF000354; Factors_V_VIII; 1. DR SMART; SM00231; FA58C; 2. DR SUPFAM; SSF49503; Cupredoxins; 6. DR SUPFAM; SSF49785; Galactose-binding domain-like; 2. DR PROSITE; PS01285; FA58C_1; 2. DR PROSITE; PS01286; FA58C_2; 2. DR PROSITE; PS50022; FA58C_3; 2. DR PROSITE; PS00079; MULTICOPPER_OXIDASE1; 3. PE 1: Evidence at protein level; KW 3D-structure; Acute phase; Blood coagulation; Calcium; Disulfide bond; KW Glycoprotein; Hemostasis; Metal-binding; Reference proteome; Repeat; KW Secreted; Signal; Sulfation. FT SIGNAL 1..19 FT /evidence="ECO:0000255" FT CHAIN 20..2133 FT /note="Coagulation factor VIII" FT /id="PRO_0000002973" FT DOMAIN 20..357 FT /note="F5/8 type A 1" FT DOMAIN 20..199 FT /note="Plastocyanin-like 1" FT DOMAIN 207..357 FT /note="Plastocyanin-like 2" FT DOMAIN 399..730 FT /note="F5/8 type A 2" FT DOMAIN 399..573 FT /note="Plastocyanin-like 3" FT DOMAIN 583..730 FT /note="Plastocyanin-like 4" FT DOMAIN 1495..1822 FT /note="F5/8 type A 3" FT DOMAIN 1495..1659 FT /note="Plastocyanin-like 5" FT DOMAIN 1669..1822 FT /note="Plastocyanin-like 6" FT DOMAIN 1822..1970 FT /note="F5/8 type C 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00081" FT DOMAIN 1975..2127 FT /note="F5/8 type C 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00081" FT REGION 760..1599 FT /note="B" FT REGION 760..790 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 804..914 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1042..1078 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1160..1179 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1200..1221 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1358..1391 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1406..1441 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 761..780 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 853..862 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 868..878 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 879..888 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 889..900 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1060..1075 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1378..1387 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT SITE 391..392 FT /note="Cleavage; by thrombin" FT /evidence="ECO:0000250" FT SITE 759..760 FT /note="Cleavage; by thrombin" FT /evidence="ECO:0000250" FT SITE 1449..1450 FT /note="Cleavage (activation)" FT /evidence="ECO:0000250" FT SITE 1490..1491 FT /note="Cleavage; by thrombin" FT /evidence="ECO:0000250" FT MOD_RES 737 FT /note="Sulfotyrosine" FT /evidence="ECO:0000250" FT MOD_RES 738 FT /note="Sulfotyrosine" FT /evidence="ECO:0000250" FT MOD_RES 742 FT /note="Sulfotyrosine" FT /evidence="ECO:0000250" FT CARBOHYD 233 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 259 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 601 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 929 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 985 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 1025 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 1111 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 1181 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 1208 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 1245 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 1265 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 1335 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 1408 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 1611 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 1919 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 173..199 FT /evidence="ECO:0000305" FT DISULFID 547..573 FT /evidence="ECO:0000305" FT DISULFID 1633..1659 FT /evidence="ECO:0000305" FT DISULFID 1822..1970 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00081" FT DISULFID 1975..2127 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00081" FT CONFLICT 713 FT /note="N -> M (in Ref. 2; no nucleotide entry)" FT /evidence="ECO:0000305" FT CONFLICT 734 FT /note="I -> T (in Ref. 2; no nucleotide entry)" FT /evidence="ECO:0000305" FT CONFLICT 792 FT /note="G -> Q (in Ref. 2; no nucleotide entry)" FT /evidence="ECO:0000305" FT CONFLICT 1133 FT /note="E -> F (in Ref. 2; no nucleotide entry)" FT /evidence="ECO:0000305" FT CONFLICT 1191 FT /note="I -> L (in Ref. 2; no nucleotide entry)" FT /evidence="ECO:0000305" FT CONFLICT 1209 FT /note="R -> F (in Ref. 2; no nucleotide entry)" FT /evidence="ECO:0000305" FT CONFLICT 1437 FT /note="C -> G (in Ref. 2; no nucleotide entry)" FT /evidence="ECO:0000305" FT CONFLICT 1456 FT /note="F -> R (in Ref. 2; no nucleotide entry)" FT /evidence="ECO:0000305" FT CONFLICT 1539 FT /note="F -> R (in Ref. 2; no nucleotide entry)" FT /evidence="ECO:0000305" FT CONFLICT 1546 FT /note="Q -> N (in Ref. 2; no nucleotide entry)" FT /evidence="ECO:0000305" FT STRAND 21..24 FT /evidence="ECO:0007829|PDB:6MF0" FT STRAND 27..33 FT /evidence="ECO:0007829|PDB:6MF0" FT STRAND 35..37 FT /evidence="ECO:0007829|PDB:8TY1" FT HELIX 40..42 FT /evidence="ECO:0007829|PDB:6MF0" FT STRAND 61..63 FT /evidence="ECO:0007829|PDB:6MF0" FT STRAND 66..72 FT /evidence="ECO:0007829|PDB:6MF0" FT STRAND 74..76 FT /evidence="ECO:0007829|PDB:6MF0" FT TURN 87..91 FT /evidence="ECO:0007829|PDB:6MF0" FT STRAND 93..99 FT /evidence="ECO:0007829|PDB:6MF0" FT STRAND 103..107 FT /evidence="ECO:0007829|PDB:6MF0" FT STRAND 109..114 FT /evidence="ECO:0007829|PDB:6MF0" FT STRAND 119..123 FT /evidence="ECO:0007829|PDB:6MF0" FT STRAND 127..129 FT /evidence="ECO:0007829|PDB:6MF0" FT HELIX 141..143 FT /evidence="ECO:0007829|PDB:6MF0" FT HELIX 144..146 FT /evidence="ECO:0007829|PDB:8TY1" FT STRAND 156..158 FT /evidence="ECO:0007829|PDB:8TY1" FT HELIX 162..164 FT /evidence="ECO:0007829|PDB:6MF0" FT STRAND 168..170 FT /evidence="ECO:0007829|PDB:6MF0" FT STRAND 172..179 FT /evidence="ECO:0007829|PDB:6MF0" FT HELIX 184..188 FT /evidence="ECO:0007829|PDB:6MF0" FT TURN 189..191 FT /evidence="ECO:0007829|PDB:6MF0" FT STRAND 193..199 FT /evidence="ECO:0007829|PDB:6MF0" FT STRAND 204..210 FT /evidence="ECO:0007829|PDB:8TY1" FT STRAND 211..223 FT /evidence="ECO:0007829|PDB:6MF0" FT HELIX 224..226 FT /evidence="ECO:0007829|PDB:6MF0" FT STRAND 227..229 FT /evidence="ECO:0007829|PDB:6MF0" FT STRAND 250..252 FT /evidence="ECO:0007829|PDB:6MF0" FT STRAND 266..268 FT /evidence="ECO:0007829|PDB:6MF0" FT STRAND 271..280 FT /evidence="ECO:0007829|PDB:6MF0" FT STRAND 287..291 FT /evidence="ECO:0007829|PDB:6MF0" FT STRAND 296..298 FT /evidence="ECO:0007829|PDB:6MF0" FT STRAND 301..308 FT /evidence="ECO:0007829|PDB:6MF0" FT STRAND 313..319 FT /evidence="ECO:0007829|PDB:6MF0" FT STRAND 324..330 FT /evidence="ECO:0007829|PDB:6MF0" FT STRAND 341..347 FT /evidence="ECO:0007829|PDB:6MF0" FT STRAND 400..405 FT /evidence="ECO:0007829|PDB:6MF0" FT STRAND 1496..1508 FT /evidence="ECO:0007829|PDB:6MF0" FT STRAND 1531..1543 FT /evidence="ECO:0007829|PDB:6MF0" FT HELIX 1555..1557 FT /evidence="ECO:0007829|PDB:6MF0" FT STRAND 1564..1566 FT /evidence="ECO:0007829|PDB:6MF0" FT STRAND 1568..1578 FT /evidence="ECO:0007829|PDB:6MF0" FT STRAND 1580..1582 FT /evidence="ECO:0007829|PDB:6MF0" FT STRAND 1597..1599 FT /evidence="ECO:0007829|PDB:8TY1" FT STRAND 1613..1619 FT /evidence="ECO:0007829|PDB:6MF0" FT HELIX 1622..1624 FT /evidence="ECO:0007829|PDB:6MF0" FT STRAND 1628..1630 FT /evidence="ECO:0007829|PDB:8TY1" FT STRAND 1632..1639 FT /evidence="ECO:0007829|PDB:6MF0" FT HELIX 1641..1643 FT /evidence="ECO:0007829|PDB:8TY1" FT HELIX 1646..1649 FT /evidence="ECO:0007829|PDB:6MF0" FT STRAND 1653..1659 FT /evidence="ECO:0007829|PDB:6MF0" FT TURN 1666..1669 FT /evidence="ECO:0007829|PDB:6MF0" FT STRAND 1673..1685 FT /evidence="ECO:0007829|PDB:6MF0" FT TURN 1686..1688 FT /evidence="ECO:0007829|PDB:6MF0" FT HELIX 1690..1692 FT /evidence="ECO:0007829|PDB:6MF0" FT HELIX 1694..1696 FT /evidence="ECO:0007829|PDB:6MF0" FT HELIX 1714..1716 FT /evidence="ECO:0007829|PDB:6MF0" FT STRAND 1717..1722 FT /evidence="ECO:0007829|PDB:6MF0" FT STRAND 1734..1738 FT /evidence="ECO:0007829|PDB:6MF0" FT STRAND 1741..1747 FT /evidence="ECO:0007829|PDB:6MF0" FT STRAND 1756..1759 FT /evidence="ECO:0007829|PDB:6MF0" FT STRAND 1764..1778 FT /evidence="ECO:0007829|PDB:6MF0" FT STRAND 1784..1789 FT /evidence="ECO:0007829|PDB:6MF0" FT STRAND 1795..1801 FT /evidence="ECO:0007829|PDB:6MF0" FT HELIX 1804..1808 FT /evidence="ECO:0007829|PDB:6MF0" FT STRAND 1813..1818 FT /evidence="ECO:0007829|PDB:6MF0" FT TURN 1981..1983 FT /evidence="ECO:0007829|PDB:7S0P" FT STRAND 1984..1986 FT /evidence="ECO:0007829|PDB:7S0P" FT HELIX 1988..1990 FT /evidence="ECO:0007829|PDB:7S0P" FT STRAND 1991..1994 FT /evidence="ECO:0007829|PDB:7S0P" FT HELIX 2006..2008 FT /evidence="ECO:0007829|PDB:7S0P" FT STRAND 2031..2047 FT /evidence="ECO:0007829|PDB:7S0P" FT STRAND 2049..2051 FT /evidence="ECO:0007829|PDB:7S0P" FT STRAND 2054..2071 FT /evidence="ECO:0007829|PDB:7S0P" FT STRAND 2088..2091 FT /evidence="ECO:0007829|PDB:7S0P" FT STRAND 2094..2117 FT /evidence="ECO:0007829|PDB:7S0P" FT STRAND 2120..2127 FT /evidence="ECO:0007829|PDB:7S0P" SQ SEQUENCE 2133 AA; 239305 MW; 152BBA8997F570DA CRC64; MQLELSTCVF LCLLPLGFSA IRRYYLGAVE LSWDYRQSEL LRELHVDTRF PATAPGALPL GPSVLYKKTV FVEFTDQLFS VARPRPPWMG LLGPTIQAEV YDTVVVTLKN MASHPVSLHA VGVSFWKSSE GAEYEDHTSQ REKEDDKVLP GKSQTYVWQV LKENGPTASD PPCLTYSYLS HVDLVKDLNS GLIGALLVCR EGSLTRERTQ NLHEFVLLFA VFDEGKSWHS ARNDSWTRAM DPAPARAQPA MHTVNGYVNR SLPGLIGCHK KSVYWHVIGM GTSPEVHSIF LEGHTFLVRH HRQASLEISP LTFLTAQTFL MDLGQFLLFC HISSHHHGGM EAHVRVESCA EEPQLRRKAD EEEDYDDNLY DSDMDVVRLD GDDVSPFIQI RSVAKKHPKT WVHYISAEEE DWDYAPAVPS PSDRSYKSLY LNSGPQRIGR KYKKARFVAY TDVTFKTRKA IPYESGILGP LLYGEVGDTL LIIFKNKASR PYNIYPHGIT DVSALHPGRL LKGWKHLKDM PILPGETFKY KWTVTVEDGP TKSDPRCLTR YYSSSINLEK DLASGLIGPL LICYKESVDQ RGNQMMSDKR NVILFSVFDE NQSWYLAENI QRFLPNPDGL QPQDPEFQAS NIMHSINGYV FDSLQLSVCL HEVAYWYILS VGAQTDFLSV FFSGYTFKHK MVYEDTLTLF PFSGETVFMS MENPGLWVLG CHNSDLRNRG MTALLKVYSC DRDIGDYYDN TYEDIPGFLL SGKNVIEPRS FAQNSRPPSA SQKQFQTITS PEDDVELDPQ SGERTQALEE LSVPSGDGSM LLGQNPAPHG SSSSDLQEAR NEADDYLPGA RERNTAPSAA ARLRPELHHS AERVLTPEPE KELKKLDSKM SSSSDLLKTS PTIPSDTLSA ETERTHSLGP PHPQVNFRSQ LGAIVLGKNS SHFIGAGVPL GSTEEDHESS LGENVSPVES DGIFEKERAH GPASLTKDDV LFKVNISLVK TNKARVYLKT NRKIHIDDAA LLTENRASAT FMDKNTTASG LNHVSNWIKG PLGKNPLSSE RGPSPELLTS SGSGKSVKGQ SSGQGRIRVA VEEEELSKGK EMMLPNSELT FLTNSADVQG NDTHSQGKKS REEMERREKL VQEKVDLPQV YTATGTKNFL RNIFHQSTEP SVEGFDGGSH APVPQDSRSL NDSAERAETH IAHFSAIREE APLEAPGNRT GPGPRSAVPR RVKQSLKQIR LPLEEIKPER GVVLNATSTR WSESSPILQG AKRNNLSLPF LTLEMAGGQG KISALGKSAA GPLASGKLEK AVLSSAGLSE ASGKAEFLPK VRVHREDLLP QKTSNVSCAH GDLGQEIFLQ KTRGPVNLNK VNRPGRTPSK LLGPPMPKEW ESLEKSPKST ALRTKDIISL PLDRHESNHS IAAKNEGQAE TQREAAWTKQ GGPGRLCAPK PPVLRRHQRD ISLPTFQPEE DKMDYDDIFS TETKGEDFDI YGEDENQDPR SFQKRTRHYF IAAVEQLWDY GMSESPRALR NRAQNGEVPR FKKVVFREFA DGSFTQPSYR GELNKHLGLL GPYIRAEVED NIMVTFKNQA SRPYSFYSSL ISYPDDQEQG AEPRHNFVQP NETRTYFWKV QHHMAPTEDE FDCKAWAYFS DVDLEKDVHS GLIGPLLICR ANTLNAAHGR QVTVQEFALF FTIFDETKSW YFTENVERNC RAPCHLQMED PTLKENYRFH AINGYVMDTL PGLVMAQNQR IRWYLLSMGS NENIHSIHFS GHVFSVRKKE EYKMAVYNLY PGVFETVEML PSKVGIWRIE CLIGEHLQAG MSTTFLVYSK ECQAPLGMAS GRIRDFQITA SGQYGQWAPK LARLHYSGSI NAWSTKDPHS WIKVDLLAPM IIHGIMTQGA RQKFSSLYIS QFIIMYSLDG RNWQSYRGNS TGTLMVFFGN VDASGIKHNI FNPPIVARYI RLHPTHYSIR STLRMELMGC DLNSCSMPLG MQNKAISDSQ ITASSHLSNI FATWSPSQAR LHLQGRTNAW RPRVSSAEEW LQVDLQKTVK VTGITTQGVK SLLSSMYVKE FLVSSSQDGR RWTLFLQDGH TKVFQGNQDS STPVVNALDP PLFTRYLRIH PTSWAQHIAL RLEVLGCEAQ DLY //