FA5_BOVIN
ID FA5_BOVIN Reviewed; 2211 AA.
AC Q28107; Q28108;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Coagulation factor V;
DE AltName: Full=Activated protein C cofactor;
DE Contains:
DE RecName: Full=Coagulation factor V heavy chain;
DE Contains:
DE RecName: Full=Coagulation factor V light chain;
DE Flags: Precursor;
GN Name=F5;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=1737753; DOI=10.1016/s0021-9258(19)50682-2;
RA Guinto E.R., Esmon C.T., Mann K.G., Macgillivray R.T.;
RT "The complete cDNA sequence of bovine coagulation factor V.";
RL J. Biol. Chem. 267:2971-2978(1992).
RN [2]
RP DISULFIDE BONDS.
RX PubMed=7947716; DOI=10.1021/bi00248a021;
RA Xue J., Kalafatis M., Silveira J.R., Kung C., Mann K.G.;
RT "Determination of the disulfide bridges in factor Va heavy chain.";
RL Biochemistry 33:13109-13116(1994).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 29-2211, GLYCOSYLATION AT ASN-225
RP AND ASN-239, DISULFIDE BONDS, AND METAL-BINDING SITES.
RX PubMed=15184653; DOI=10.1073/pnas.0403072101;
RA Adams T.E., Hockin M.F., Mann K.G., Everse S.J.;
RT "The crystal structure of activated protein C-inactivated bovine factor Va:
RT Implications for cofactor function.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:8918-8923(2004).
CC -!- FUNCTION: Central regulator of hemostasis. It serves as a critical
CC cofactor for the prothrombinase activity of factor Xa that results in
CC the activation of prothrombin to thrombin.
CC -!- ACTIVITY REGULATION: Inhibited by SERPINA5. {ECO:0000250}.
CC -!- SUBUNIT: Factor Va, the activated form of factor V, is composed of a
CC heavy chain and a light chain, non-covalently bound. The interaction
CC between the two chains is calcium-dependent. Forms heterodimer with
CC SERPINA5 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- DOMAIN: Domain B contains 29.5 X 9 AA tandem repeats, and 2 X 14 AA
CC repeats.
CC -!- PTM: Thrombin activates factor V proteolytically to the active
CC cofactor, factor Va (formation of a heavy chain at the N-terminus and a
CC light chain at the C-terminus).
CC -!- PTM: Sulfation is required for efficient thrombin cleavage and
CC activation and for full procoagulant activity. {ECO:0000250}.
CC -!- PTM: Activated protein C inactivates factor V and factor Va by
CC proteolytic degradation. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the multicopper oxidase family. {ECO:0000305}.
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DR EMBL; M81440; AAA30512.1; -; mRNA.
DR EMBL; M81441; AAA30513.1; -; mRNA.
DR PIR; A42580; KFBO5.
DR RefSeq; NP_776304.1; NM_173879.2.
DR PDB; 1SDD; X-ray; 2.80 A; A=29-334, B=1565-2211.
DR PDBsum; 1SDD; -.
DR AlphaFoldDB; Q28107; -.
DR SMR; Q28107; -.
DR STRING; 9913.ENSBTAP00000023573; -.
DR iPTMnet; Q28107; -.
DR PRIDE; Q28107; -.
DR GeneID; 280687; -.
DR KEGG; bta:280687; -.
DR CTD; 2153; -.
DR eggNOG; ENOG502QSUG; Eukaryota.
DR InParanoid; Q28107; -.
DR OrthoDB; 454773at2759; -.
DR EvolutionaryTrace; Q28107; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0031091; C:platelet alpha granule; IBA:GO_Central.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0008015; P:blood circulation; IBA:GO_Central.
DR GO; GO:0007596; P:blood coagulation; IBA:GO_Central.
DR CDD; cd00057; FA58C; 2.
DR Gene3D; 2.60.40.420; -; 5.
DR InterPro; IPR009271; Coagulation_factor_V_LSPD.
DR InterPro; IPR011707; Cu-oxidase_N.
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 Pfam; PF07732; Cu-oxidase_3; 2.
DR Pfam; PF00754; F5_F8_type_C; 2.
DR Pfam; PF06049; LSPR; 28.
DR PIRSF; PIRSF000354; Factors_V_VIII; 1.
DR SMART; SM00231; FA58C; 2.
DR SUPFAM; SSF49503; SSF49503; 6.
DR SUPFAM; SSF49785; SSF49785; 2.
DR PROSITE; PS01285; FA58C_1; 2.
DR PROSITE; PS01286; FA58C_2; 2.
DR PROSITE; PS50022; FA58C_3; 2.
DR PROSITE; PS00079; MULTICOPPER_OXIDASE1; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Blood coagulation; Calcium; Copper; Disulfide bond;
KW Glycoprotein; Hemostasis; Metal-binding; Phosphoprotein;
KW Reference proteome; Repeat; Secreted; Signal; Sulfation; Zymogen.
FT SIGNAL 1..28
FT /evidence="ECO:0000255"
FT CHAIN 29..2211
FT /note="Coagulation factor V"
FT /id="PRO_0000002974"
FT CHAIN 29..741
FT /note="Coagulation factor V heavy chain"
FT /evidence="ECO:0000250"
FT /id="PRO_0000002975"
FT PROPEP 742..1564
FT /note="Activation peptide (connecting region)"
FT /evidence="ECO:0000250"
FT /id="PRO_0000002976"
FT CHAIN 1565..2211
FT /note="Coagulation factor V light chain"
FT /evidence="ECO:0000250"
FT /id="PRO_0000002977"
FT DOMAIN 30..327
FT /note="F5/8 type A 1"
FT DOMAIN 30..193
FT /note="Plastocyanin-like 1"
FT DOMAIN 203..327
FT /note="Plastocyanin-like 2"
FT DOMAIN 348..686
FT /note="F5/8 type A 2"
FT DOMAIN 348..525
FT /note="Plastocyanin-like 3"
FT DOMAIN 535..686
FT /note="Plastocyanin-like 4"
FT REPEAT 1124..1137
FT /note="1-1"
FT REPEAT 1138..1151
FT /note="1-2"
FT REPEAT 1188..1196
FT /note="2-1"
FT REPEAT 1197..1205
FT /note="2-2"
FT REPEAT 1206..1214
FT /note="2-3"
FT REPEAT 1215..1223
FT /note="2-4"
FT REPEAT 1224..1232
FT /note="2-5"
FT REPEAT 1233..1241
FT /note="2-6"
FT REPEAT 1242..1250
FT /note="2-7"
FT REPEAT 1251..1259
FT /note="2-8"
FT REPEAT 1260..1268
FT /note="2-9"
FT REPEAT 1269..1277
FT /note="2-10"
FT REPEAT 1278..1286
FT /note="2-11"
FT REPEAT 1287..1295
FT /note="2-12"
FT REPEAT 1296..1304
FT /note="2-13"
FT REPEAT 1305..1313
FT /note="2-14"
FT REPEAT 1314..1322
FT /note="2-15"
FT REPEAT 1323..1331
FT /note="2-16"
FT REPEAT 1332..1340
FT /note="2-17"
FT REPEAT 1341..1349
FT /note="2-18"
FT REPEAT 1350..1358
FT /note="2-19"
FT REPEAT 1359..1367
FT /note="2-20"
FT REPEAT 1368..1376
FT /note="2-21"
FT REPEAT 1377..1385
FT /note="2-22"
FT REPEAT 1386..1394
FT /note="2-23"
FT REPEAT 1395..1403
FT /note="2-24"
FT REPEAT 1404..1412
FT /note="2-25"
FT REPEAT 1413..1421
FT /note="2-26"
FT REPEAT 1422..1430
FT /note="2-27"
FT REPEAT 1431..1439
FT /note="2-28"
FT REPEAT 1440..1444
FT /note="2-29; truncated"
FT REPEAT 1445..1453
FT /note="2-30"
FT DOMAIN 1569..1890
FT /note="F5/8 type A 3"
FT DOMAIN 1569..1738
FT /note="Plastocyanin-like 5"
FT DOMAIN 1748..1890
FT /note="Plastocyanin-like 6"
FT DOMAIN 1894..2048
FT /note="F5/8 type C 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00081"
FT DOMAIN 2053..2208
FT /note="F5/8 type C 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00081"
FT REGION 696..1564
FT /note="B"
FT REGION 814..844
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 954..1039
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1084..1162
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1124..1151
FT /note="2 X 14 AA tandem repeats"
FT REGION 1188..1453
FT /note="30 X 9 AA approximate tandem repeats of [AS]-L-S-P-
FT D-[LP]-[GS]-Q-[TE]"
FT REGION 1195..1471
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 954..985
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 992..1028
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1084..1107
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1122..1162
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1215..1468
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 139
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT BINDING 140
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT BINDING 1830
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT BINDING 1832
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT BINDING 1872
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT SITE 334..335
FT /note="Cleavage; by activated protein C"
FT /evidence="ECO:0000250"
FT SITE 533..534
FT /note="Cleavage; by activated protein C"
FT /evidence="ECO:0000250"
FT SITE 741..742
FT /note="Cleavage; by thrombin"
FT /evidence="ECO:0000250"
FT SITE 1034..1035
FT /note="Cleavage; by thrombin"
FT /evidence="ECO:0000250"
FT SITE 1564..1565
FT /note="Cleavage; by thrombin"
FT MOD_RES 644
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P12259"
FT MOD_RES 697
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000255"
FT MOD_RES 701
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000255"
FT MOD_RES 730
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000255"
FT MOD_RES 1513
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000255"
FT MOD_RES 1529
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000255"
FT MOD_RES 1537
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000255"
FT MOD_RES 1541
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000255"
FT CARBOHYD 225
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:15184653"
FT CARBOHYD 239
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:15184653"
FT CARBOHYD 297
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 382
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 460
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 553
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 587
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 745
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 756
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 774
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 780
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 902
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 952
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 964
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1044
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1053
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1062
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1071
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1078
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1094
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1451
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1490
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1550
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1690
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1839
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1997
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2196
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 167..193
FT DISULFID 248..329
FT DISULFID 499..525
FT DISULFID 607..688
FT DISULFID 1712..1738
FT /evidence="ECO:0000305"
FT DISULFID 1894..2048
FT DISULFID 2053..2208
FT VARIANT 587..592
FT /note="NFTLPA -> T (in variant 2)"
FT STRAND 37..43
FT /evidence="ECO:0007829|PDB:1SDD"
FT STRAND 61..67
FT /evidence="ECO:0007829|PDB:1SDD"
FT TURN 71..73
FT /evidence="ECO:0007829|PDB:1SDD"
FT STRAND 90..93
FT /evidence="ECO:0007829|PDB:1SDD"
FT STRAND 97..104
FT /evidence="ECO:0007829|PDB:1SDD"
FT STRAND 106..108
FT /evidence="ECO:0007829|PDB:1SDD"
FT STRAND 113..117
FT /evidence="ECO:0007829|PDB:1SDD"
FT TURN 121..123
FT /evidence="ECO:0007829|PDB:1SDD"
FT HELIX 134..137
FT /evidence="ECO:0007829|PDB:1SDD"
FT STRAND 147..153
FT /evidence="ECO:0007829|PDB:1SDD"
FT HELIX 156..158
FT /evidence="ECO:0007829|PDB:1SDD"
FT STRAND 162..164
FT /evidence="ECO:0007829|PDB:1SDD"
FT STRAND 166..173
FT /evidence="ECO:0007829|PDB:1SDD"
FT STRAND 176..178
FT /evidence="ECO:0007829|PDB:1SDD"
FT HELIX 179..183
FT /evidence="ECO:0007829|PDB:1SDD"
FT STRAND 188..193
FT /evidence="ECO:0007829|PDB:1SDD"
FT STRAND 202..207
FT /evidence="ECO:0007829|PDB:1SDD"
FT STRAND 217..219
FT /evidence="ECO:0007829|PDB:1SDD"
FT STRAND 222..225
FT /evidence="ECO:0007829|PDB:1SDD"
FT STRAND 230..232
FT /evidence="ECO:0007829|PDB:1SDD"
FT STRAND 234..236
FT /evidence="ECO:0007829|PDB:1SDD"
FT STRAND 262..264
FT /evidence="ECO:0007829|PDB:1SDD"
FT TURN 313..315
FT /evidence="ECO:0007829|PDB:1SDD"
FT HELIX 316..318
FT /evidence="ECO:0007829|PDB:1SDD"
FT STRAND 1570..1583
FT /evidence="ECO:0007829|PDB:1SDD"
FT TURN 1584..1587
FT /evidence="ECO:0007829|PDB:1SDD"
FT STRAND 1601..1612
FT /evidence="ECO:0007829|PDB:1SDD"
FT HELIX 1626..1628
FT /evidence="ECO:0007829|PDB:1SDD"
FT STRAND 1635..1638
FT /evidence="ECO:0007829|PDB:1SDD"
FT STRAND 1642..1647
FT /evidence="ECO:0007829|PDB:1SDD"
FT STRAND 1651..1653
FT /evidence="ECO:0007829|PDB:1SDD"
FT STRAND 1658..1660
FT /evidence="ECO:0007829|PDB:1SDD"
FT TURN 1701..1703
FT /evidence="ECO:0007829|PDB:1SDD"
FT STRAND 1707..1709
FT /evidence="ECO:0007829|PDB:1SDD"
FT STRAND 1711..1718
FT /evidence="ECO:0007829|PDB:1SDD"
FT HELIX 1723..1727
FT /evidence="ECO:0007829|PDB:1SDD"
FT TURN 1728..1730
FT /evidence="ECO:0007829|PDB:1SDD"
FT STRAND 1732..1738
FT /evidence="ECO:0007829|PDB:1SDD"
FT STRAND 1755..1764
FT /evidence="ECO:0007829|PDB:1SDD"
FT HELIX 1765..1767
FT /evidence="ECO:0007829|PDB:1SDD"
FT STRAND 1791..1795
FT /evidence="ECO:0007829|PDB:1SDD"
FT STRAND 1798..1800
FT /evidence="ECO:0007829|PDB:1SDD"
FT STRAND 1806..1808
FT /evidence="ECO:0007829|PDB:1SDD"
FT STRAND 1812..1819
FT /evidence="ECO:0007829|PDB:1SDD"
FT STRAND 1827..1831
FT /evidence="ECO:0007829|PDB:1SDD"
FT STRAND 1836..1838
FT /evidence="ECO:0007829|PDB:1SDD"
FT STRAND 1840..1842
FT /evidence="ECO:0007829|PDB:1SDD"
FT STRAND 1844..1851
FT /evidence="ECO:0007829|PDB:1SDD"
FT STRAND 1855..1862
FT /evidence="ECO:0007829|PDB:1SDD"
FT STRAND 1865..1872
FT /evidence="ECO:0007829|PDB:1SDD"
FT HELIX 1876..1879
FT /evidence="ECO:0007829|PDB:1SDD"
FT TURN 1880..1882
FT /evidence="ECO:0007829|PDB:1SDD"
FT STRAND 1884..1890
FT /evidence="ECO:0007829|PDB:1SDD"
FT TURN 1900..1902
FT /evidence="ECO:0007829|PDB:1SDD"
FT HELIX 1907..1909
FT /evidence="ECO:0007829|PDB:1SDD"
FT STRAND 1910..1913
FT /evidence="ECO:0007829|PDB:1SDD"
FT HELIX 1921..1923
FT /evidence="ECO:0007829|PDB:1SDD"
FT STRAND 1930..1932
FT /evidence="ECO:0007829|PDB:1SDD"
FT STRAND 1934..1936
FT /evidence="ECO:0007829|PDB:1SDD"
FT STRAND 1950..1966
FT /evidence="ECO:0007829|PDB:1SDD"
FT STRAND 1968..1990
FT /evidence="ECO:0007829|PDB:1SDD"
FT STRAND 1999..2002
FT /evidence="ECO:0007829|PDB:1SDD"
FT STRAND 2009..2013
FT /evidence="ECO:0007829|PDB:1SDD"
FT STRAND 2015..2038
FT /evidence="ECO:0007829|PDB:1SDD"
FT STRAND 2040..2048
FT /evidence="ECO:0007829|PDB:1SDD"
FT TURN 2059..2061
FT /evidence="ECO:0007829|PDB:1SDD"
FT STRAND 2062..2064
FT /evidence="ECO:0007829|PDB:1SDD"
FT STRAND 2069..2072
FT /evidence="ECO:0007829|PDB:1SDD"
FT TURN 2078..2080
FT /evidence="ECO:0007829|PDB:1SDD"
FT HELIX 2085..2087
FT /evidence="ECO:0007829|PDB:1SDD"
FT STRAND 2089..2091
FT /evidence="ECO:0007829|PDB:1SDD"
FT STRAND 2094..2096
FT /evidence="ECO:0007829|PDB:1SDD"
FT STRAND 2098..2100
FT /evidence="ECO:0007829|PDB:1SDD"
FT STRAND 2110..2126
FT /evidence="ECO:0007829|PDB:1SDD"
FT STRAND 2128..2130
FT /evidence="ECO:0007829|PDB:1SDD"
FT STRAND 2133..2140
FT /evidence="ECO:0007829|PDB:1SDD"
FT STRAND 2142..2149
FT /evidence="ECO:0007829|PDB:1SDD"
FT STRAND 2169..2172
FT /evidence="ECO:0007829|PDB:1SDD"
FT STRAND 2175..2190
FT /evidence="ECO:0007829|PDB:1SDD"
FT STRAND 2194..2198
FT /evidence="ECO:0007829|PDB:1SDD"
FT STRAND 2200..2208
FT /evidence="ECO:0007829|PDB:1SDD"
SQ SEQUENCE 2211 AA; 248983 MW; CBBF90B738667C45 CRC64;
MFLACPGFWV LVVLGSSWAG WGNLGAEAAK LRQFYVAAQS IRWNYRPEST HLSSKPFETS
FKKIVYREYE AYFQKEKPQS RTSGLLGPTL YAEVGDIMKV HFKNKAHKPL SIHAQGIKYS
KFSEGASYSD HTLPMEKMDD AVAPGQEYTY EWIISEHSGP THDDPPCLTH IYYSYVNLVE
DFNSGLIGPL LICKKGTLTE DGTQKMFEKQ HVLMFAVFDE SKSWNQTSSL MYTVNGYVNG
TMPDITVCAH DHISWHLIGM SSGPELFSIH FNGQVLEQNH HKISAITLVS ATSTTANMTV
SPEGRWTIAS LIPRHFQAGM QAYIDIKNCA KKTRNPKKLT RDQRRHIKRW EYFIAAEEVI
WDYAPIIPAN MDKKYRSLHL DNFSNRIGKH YKKVVYKQYQ DDSFTKRLED PSSEGDGILG
PIIRAQVRDT LKIVFKNMAS RSYSIYPHGV TFSPYDNEVN SSSTSGSNTM IRAVRPGETY
TYKWNILESD EPTENDAQCL TRPYYSNVDI TRDLASGLIG LLLICKSRSL DRRGIQRAAD
IEQQAVFAVF DENKSWYIED NIYKFCENPE KVKRDDPKFY ESNIMSNFTL PAINGYVPES
IPILGFCFDD TVQWHFCSVG TQNDILTIHF TGHSFIYGKR HEDTLTLFPM QGESVTVTMD
NVGTWMLTTM NSNPRSKKLR LRFRDAKCIR NDDDDSYEII YEPSGSTAMT TKKIHDSSEI
EDENDADSDY QDELALILGL RSFRNSSLNQ EKDELNLTAL ALEKDSEFIP PSANRSLDSN
SSSRSHVSRL IAKNFAESLK TLLHLEAPAA GSPLEHAGLD KNSALNPPMA EHSSPYSEDP
REDHPLSDVT GVSLLPFGTG FKNRKPAKHQ RFQVGRGQAA KHKFSQTRFP AHKTRTRLSQ
DNSSSSRMGP WEDIPSDLLL LQQKDPYKIL NGEWHLVSEK GSYEIIQDAN ENKTVNKLPN
SPQNDSRTWG ENIPFKNSHG KQSGHPTFLV TRRKPLQDRQ DRRNSRLKEG LPLIRTRRKK
KEEKPAYHVP LSPRSFHPLR GEVNASFSDR RHNHSLLLHA SNETSLSIDL NQTFPSMNLS
LAASLPDHDQ TSPNDTTSQT SSPPDLYPTV SPEEHYQIFP IQDSDPTHST TAPSNRSPDP
THSTTAPSNR SPPTQPSQIP NYDLRNRAIP TDVSQIFPSL ELEVWQTATS LDLSQPSISP
DLGQMALSPD PGQESLSPDL GQTSLSPDLS QESLSPDLGQ TALSPDPSQE SLSPDLGQTA
LSPDPSQESL SPDLGQTALS PDPGQESLSP DLGQTSLSPD LSQESLSPDL GQTALSPDPS
QESLSPDLGQ TALSPDPSQE SLSPDLGQTS LSPDLGQESL SPDLGQTALS PDPSQESLSP
DLGQTSLSPD LGQESLSPDL GQTALSPDLS QESLSPDLGQ TPLSPDLSLE SLSPDLSQLD
LKQTSPPLDL NQTSHTSESS QSLPLPEFGQ TFPNADIGQM PSPPPDSTLN NTFIPEEFNP
LVVVGLSRDD GDYIEIIPRQ KEESSEEDYG EFEFVAYNDP YQTDLRTDIN SSRNPDNIAA
WYLRSNTGNR KYYYIAAEEI SWDYSKFVQS DDVDYVPEDT VYKKVVFRKY LDSTFTKLDP
QGEYEEHLGI LGPVIRAEVD DVIQVRFKNL ASRPYSLHAH GLSYEKSSEG KTYEDDSPEW
FKEDNAIQPN KTYTYVWHAT TRSGPENPGS ACRAWAYYSA VNPEKDIHSG LIGPLLICRK
GTLDKETNMP VDMREFVLLF MVFDEKKSWY YDKKPTRSWR RASSEVKNSH EFHAINGMIY
NLPGLRMYEQ EWVRLHLLNL GGSRDIHVVH FHGQTLLENG TQQHQLGVWP LLPGSFKTLE
MKASKPGWWL LDTEVGEIQR AGMQTPFLIV DRECKMPMGL STGLIADSQI QASEFWGYWE
PKLARLNNGG SYNAWIAEKL STEFNPEPWI QVDMQKEVLL TGIQTQGAKH YLKPYYTTEF
CVAYSLDRKN WRIFKGNSTR NVMYFGGNSD ASTIKENQID PPVVARYIRI SPTGSYNKPA
LRLELQGCEV NGCSTPLGME SGKIENKQIT ASSFKKSWWG NYWEPFLARL NAQGRVNAWQ
AKANNNNQWL QIDLLKIKKI TAIVTQGCKS LSSEMYVKSY TIHYSDQGTD WKPYREKSSM
VDKIFEGNNN VRGHVKNFFN PPIISRFIRI IPKTWNQSIA LRLELFGCDM Y
