FA10_BOVIN
ID FA10_BOVIN Reviewed; 492 AA.
AC P00743;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-1987, sequence version 1.
DT 03-AUG-2022, entry version 226.
DE RecName: Full=Coagulation factor X;
DE EC=3.4.21.6;
DE AltName: Full=Stuart factor;
DE Contains:
DE RecName: Full=Factor X light chain;
DE Contains:
DE RecName: Full=Factor X heavy chain;
DE Contains:
DE RecName: Full=Activated factor Xa heavy chain;
DE Flags: Precursor;
GN Name=F10;
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] OF 1-487.
RX PubMed=6330671; DOI=10.1093/nar/12.11.4481;
RA Fung M.R., Campbell R.M., McGillivray R.T.A.;
RT "Blood coagulation factor X mRNA encodes a single polypeptide chain
RT containing a prepro leader sequence.";
RL Nucleic Acids Res. 12:4481-4492(1984).
RN [2]
RP PROTEIN SEQUENCE OF 41-180, AND GAMMA-CARBOXYGLUTAMATION AT GLU-46; GLU-47;
RP GLU-54; GLU-56; GLU-59; GLU-60; GLU-65; GLU-66; GLU-69; GLU-72; GLU-75 AND
RP GLU-79.
RX PubMed=6766735; DOI=10.1021/bi00545a009;
RA Enfield D.L., Ericsson L.H., Fujikawa K., Walsh K.A., Neurath H.,
RA Titani K.;
RT "Amino acid sequence of the light chain of bovine factor X1 (Stuart
RT factor).";
RL Biochemistry 19:659-667(1980).
RN [3]
RP HYDROXYLATION AT ASP-103.
RX PubMed=6688526; DOI=10.1016/0006-291x(83)90961-0;
RA McMullen B.A., Fujikawa K., Kisiel W.;
RT "The occurrence of beta-hydroxyaspartic acid in the vitamin K-dependent
RT blood coagulation zymogens.";
RL Biochem. Biophys. Res. Commun. 115:8-14(1983).
RN [4]
RP PROTEIN SEQUENCE OF 183-492, GLYCOSYLATION AT ASN-218 AND THR-485, AND
RP DISULFIDE BONDS.
RX PubMed=1059093; DOI=10.1073/pnas.72.8.3082;
RA Titani K., Fujikawa K., Enfield D.L., Ericsson L.H., Walsh K.A.,
RA Neurath H.;
RT "Bovine factor X1 (Stuart factor): amino-acid sequence of heavey chain.";
RL Proc. Natl. Acad. Sci. U.S.A. 72:3082-3086(1975).
RN [5]
RP PROTEIN SEQUENCE OF 183-233, AND GLYCOSYLATION AT THR-208.
RX PubMed=8243461; DOI=10.1111/j.1432-1033.1993.tb18361.x;
RA Inoue K., Morita T.;
RT "Identification of O-linked oligosaccharide chains in the activation
RT peptides of blood coagulation factor X. The role of the carbohydrate
RT moieties in the activation of factor X.";
RL Eur. J. Biochem. 218:153-163(1993).
RN [6]
RP ACTIVE SITE.
RX PubMed=4264286; DOI=10.1021/bi00776a004;
RA Titani K., Hermodson M.A., Fujikawa K., Ericsson L.H., Walsh K.A.,
RA Neurath H., Davie E.W.;
RT "Bovine factor X 1a (activated Stuart factor). Evidence of homology with
RT mammalian serine proteases.";
RL Biochemistry 11:4899-4903(1972).
RN [7]
RP PROTEOLYTIC PROCESSING.
RX PubMed=1059122; DOI=10.1073/pnas.72.9.3359;
RA Fujikawa K., Titani K., Davie E.W.;
RT "Activation of bovine factor X (Stuart factor): conversion of factor Xa-
RT alpha to factor Xa-beta.";
RL Proc. Natl. Acad. Sci. U.S.A. 72:3359-3363(1975).
RN [8]
RP CALCIUM-BINDING.
RX PubMed=6546930; DOI=10.1016/s0021-9258(18)91071-9;
RA Sugo T., Bjoerk I., Holmgren A., Stenflo J.;
RT "Calcium-binding properties of bovine factor X lacking the gamma-
RT carboxyglutamic acid-containing region.";
RL J. Biol. Chem. 259:5705-5710(1984).
RN [9]
RP SULFATION AT TYR-200.
RX PubMed=3949800; DOI=10.1016/s0021-9258(17)35614-4;
RA Morita T., Jackson C.M.;
RT "Localization of the structural difference between bovine blood coagulation
RT factors X1 and X2 to tyrosine 18 in the activation peptide.";
RL J. Biol. Chem. 261:4008-4014(1986).
RN [10]
RP STRUCTURE BY NMR OF 85-126.
RX PubMed=2261466; DOI=10.1021/bi00487a018;
RA Selander M., Persson E., Stenflo J., Drakenberg T.;
RT "1H NMR assignment and secondary structure of the Ca2(+)-free form of the
RT amino-terminal epidermal growth factor like domain in coagulation factor
RT X.";
RL Biochemistry 29:8111-8118(1990).
RN [11]
RP STRUCTURE BY NMR OF 85-126.
RX PubMed=1627540; DOI=10.1021/bi00141a004;
RA Ullner M., Selander M., Persson E., Stenflo J., Drakenberg T., Teleman O.;
RT "Three-dimensional structure of the apo form of the N-terminal EGF-like
RT module of blood coagulation factor X as determined by NMR spectroscopy and
RT simulated folding.";
RL Biochemistry 31:5974-5983(1992).
RN [12]
RP STRUCTURE BY NMR OF 85-126.
RX PubMed=1527084; DOI=10.2210/pdb1ccf/pdb;
RA Selander-Sunnerhagen M., Ullner M., Persson E., Teleman O., Stenflo J.,
RA Drakenberg T.;
RT "How an epidermal growth factor (EGF)-like domain binds calcium. High
RT resolution NMR structure of the calcium form of the NH2-terminal EGF-like
RT domain in coagulation factor X.";
RL J. Biol. Chem. 267:19642-19649(1992).
RN [13]
RP STRUCTURE BY NMR OF 41-126.
RX PubMed=8794734; DOI=10.1021/bi960633j;
RA Sunnerhagen M., Olah G.A., Stenflo J., Forsen S., Drakenberg T.,
RA Trewhella J.;
RT "The relative orientation of Gla and EGF domains in coagulation factor X is
RT altered by Ca2+ binding to the first EGF domain. A combined NMR-small angle
RT X-ray scattering study.";
RL Biochemistry 35:11547-11559(1996).
CC -!- FUNCTION: Factor Xa is a vitamin K-dependent glycoprotein that converts
CC prothrombin to thrombin in the presence of factor Va, calcium and
CC phospholipid during blood clotting.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Selective cleavage of Arg-|-Thr and then Arg-|-Ile bonds in
CC prothrombin to form thrombin.; EC=3.4.21.6;
CC -!- ACTIVITY REGULATION: Inhibited by SERPINA5. {ECO:0000250}.
CC -!- SUBUNIT: The two chains are formed from a single-chain precursor by the
CC excision of two Arg residues and are held together by 1 or more
CC disulfide bonds. Forms a heterodimer with SERPINA5 (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- PTM: The vitamin K-dependent, enzymatic carboxylation of some glutamate
CC residues allows the modified protein to bind calcium.
CC -!- PTM: N- and O-glycosylated. {ECO:0000269|PubMed:1059093,
CC ECO:0000269|PubMed:8243461}.
CC -!- PTM: Proteolytically cleaved and activated by cathepsin CTSG (By
CC similarity). The activation peptide is cleaved by factor IXa (in the
CC intrinsic pathway), or by factor VIIa (in the extrinsic pathway)
CC (PubMed:1059122). {ECO:0000250|UniProtKB:P00742,
CC ECO:0000269|PubMed:1059122}.
CC -!- PTM: The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate
CC and asparagine is (R) stereospecific within EGF domains.
CC {ECO:0000269|PubMed:6688526}.
CC -!- MISCELLANEOUS: Calcium also binds, with stronger affinity to another
CC site, beyond the GLA domain.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00274}.
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DR EMBL; X00673; CAA25286.1; -; mRNA.
DR PIR; A22867; EXBO.
DR RefSeq; NP_001073682.1; NM_001080213.1.
DR PDB; 1APO; NMR; -; A=85-126.
DR PDB; 1CCF; NMR; -; A=85-126.
DR PDB; 1IOD; X-ray; 2.30 A; G=41-84.
DR PDB; 1KIG; X-ray; 3.00 A; H=234-474, L=129-179.
DR PDB; 1WHE; NMR; -; A=41-126.
DR PDB; 1WHF; NMR; -; A=41-126.
DR PDBsum; 1APO; -.
DR PDBsum; 1CCF; -.
DR PDBsum; 1IOD; -.
DR PDBsum; 1KIG; -.
DR PDBsum; 1WHE; -.
DR PDBsum; 1WHF; -.
DR AlphaFoldDB; P00743; -.
DR BMRB; P00743; -.
DR SMR; P00743; -.
DR ELM; P00743; -.
DR IntAct; P00743; 1.
DR STRING; 9913.ENSBTAP00000021789; -.
DR BindingDB; P00743; -.
DR ChEMBL; CHEMBL3656; -.
DR MEROPS; S01.216; -.
DR GlyConnect; 101; 2 N-Linked glycans (1 site), 9 O-Linked glycans.
DR iPTMnet; P00743; -.
DR PaxDb; P00743; -.
DR PRIDE; P00743; -.
DR GeneID; 280787; -.
DR KEGG; bta:280787; -.
DR CTD; 2159; -.
DR eggNOG; ENOG502QS4N; Eukaryota.
DR HOGENOM; CLU_006842_19_5_1; -.
DR InParanoid; P00743; -.
DR OrthoDB; 1314811at2759; -.
DR TreeFam; TF327329; -.
DR SABIO-RK; P00743; -.
DR EvolutionaryTrace; P00743; -.
DR PRO; PR:P00743; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0007596; P:blood coagulation; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 2.40.10.10; -; 2.
DR Gene3D; 4.10.740.10; -; 1.
DR InterPro; IPR017857; Coagulation_fac-like_Gla_dom.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR InterPro; IPR018097; EGF_Ca-bd_CS.
DR InterPro; IPR035972; GLA-like_dom_SF.
DR InterPro; IPR000294; GLA_domain.
DR InterPro; IPR012224; Pept_S1A_FX.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001314; Peptidase_S1A.
DR InterPro; IPR001254; Trypsin_dom.
DR InterPro; IPR018114; TRYPSIN_HIS.
DR InterPro; IPR033116; TRYPSIN_SER.
DR Pfam; PF00008; EGF; 1.
DR Pfam; PF00594; Gla; 1.
DR Pfam; PF00089; Trypsin; 1.
DR PIRSF; PIRSF001143; Factor_X; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR PRINTS; PR00001; GLABLOOD.
DR SMART; SM00181; EGF; 2.
DR SMART; SM00179; EGF_CA; 1.
DR SMART; SM00069; GLA; 1.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF50494; SSF50494; 1.
DR SUPFAM; SSF57630; SSF57630; 1.
DR PROSITE; PS00010; ASX_HYDROXYL; 1.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS01186; EGF_2; 2.
DR PROSITE; PS50026; EGF_3; 1.
DR PROSITE; PS01187; EGF_CA; 1.
DR PROSITE; PS00011; GLA_1; 1.
DR PROSITE; PS50998; GLA_2; 1.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
DR PROSITE; PS00134; TRYPSIN_HIS; 1.
DR PROSITE; PS00135; TRYPSIN_SER; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Blood coagulation; Calcium;
KW Cleavage on pair of basic residues; Direct protein sequencing;
KW Disulfide bond; EGF-like domain; Gamma-carboxyglutamic acid; Glycoprotein;
KW Hemostasis; Hydrolase; Hydroxylation; Protease; Reference proteome; Repeat;
KW Secreted; Serine protease; Signal; Sulfation; Zymogen.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT PROPEP 24..40
FT /evidence="ECO:0000269|PubMed:6766735"
FT /id="PRO_0000027779"
FT CHAIN 41..492
FT /note="Coagulation factor X"
FT /id="PRO_0000027780"
FT CHAIN 41..180
FT /note="Factor X light chain"
FT /id="PRO_0000027781"
FT CHAIN 183..492
FT /note="Factor X heavy chain"
FT /id="PRO_0000027782"
FT PROPEP 183..233
FT /note="Activation peptide"
FT /id="PRO_0000027783"
FT CHAIN 234..492
FT /note="Activated factor Xa heavy chain"
FT /id="PRO_0000027784"
FT PROPEP 476..492
FT /note="May be removed but is not necessary for activation"
FT /id="PRO_0000027785"
FT DOMAIN 41..85
FT /note="Gla"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463"
FT DOMAIN 86..122
FT /note="EGF-like 1; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 125..165
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 234..466
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT REGION 472..492
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 275
FT /note="Charge relay system"
FT /evidence="ECO:0000269|PubMed:4264286"
FT ACT_SITE 321
FT /note="Charge relay system"
FT /evidence="ECO:0000269|PubMed:4264286"
FT ACT_SITE 418
FT /note="Charge relay system"
FT /evidence="ECO:0000269|PubMed:4264286"
FT SITE 233..234
FT /note="Cleavage; by coagulation factor IXa and coagulation
FT factor VIIa"
FT MOD_RES 46
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
FT ECO:0000269|PubMed:6766735"
FT MOD_RES 47
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
FT ECO:0000269|PubMed:6766735"
FT MOD_RES 54
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
FT ECO:0000269|PubMed:6766735"
FT MOD_RES 56
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
FT ECO:0000269|PubMed:6766735"
FT MOD_RES 59
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
FT ECO:0000269|PubMed:6766735"
FT MOD_RES 60
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
FT ECO:0000269|PubMed:6766735"
FT MOD_RES 65
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
FT ECO:0000269|PubMed:6766735"
FT MOD_RES 66
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
FT ECO:0000269|PubMed:6766735"
FT MOD_RES 69
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
FT ECO:0000269|PubMed:6766735"
FT MOD_RES 72
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
FT ECO:0000269|PubMed:6766735"
FT MOD_RES 75
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
FT ECO:0000269|PubMed:6766735"
FT MOD_RES 79
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463,
FT ECO:0000269|PubMed:6766735"
FT MOD_RES 103
FT /note="(3R)-3-hydroxyaspartate"
FT /evidence="ECO:0000269|PubMed:6688526"
FT MOD_RES 200
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000269|PubMed:3949800"
FT CARBOHYD 208
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:8243461"
FT CARBOHYD 218
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:1059093"
FT /id="CAR_000011"
FT CARBOHYD 485
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:1059093"
FT DISULFID 57..62
FT /evidence="ECO:0000250"
FT DISULFID 90..101
FT /evidence="ECO:0000269|PubMed:1059093"
FT DISULFID 95..110
FT /evidence="ECO:0000269|PubMed:1059093"
FT DISULFID 112..121
FT /evidence="ECO:0000269|PubMed:1059093"
FT DISULFID 129..140
FT /evidence="ECO:0000250"
FT DISULFID 136..149
FT /evidence="ECO:0000250"
FT DISULFID 151..164
FT /evidence="ECO:0000250"
FT DISULFID 172..341
FT /note="Interchain (between light and heavy chains)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076,
FT ECO:0000255|PROSITE-ProRule:PRU00274, ECO:0000255|PROSITE-
FT ProRule:PRU00463, ECO:0000269|PubMed:1059093"
FT DISULFID 240..245
FT /evidence="ECO:0000269|PubMed:1059093"
FT DISULFID 260..276
FT /evidence="ECO:0000269|PubMed:1059093"
FT DISULFID 389..403
FT /evidence="ECO:0000269|PubMed:1059093"
FT DISULFID 414..442
FT /evidence="ECO:0000269|PubMed:1059093"
FT CONFLICT 103
FT /note="D -> N (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 293
FT /note="Missing (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 296..298
FT /note="EGN -> GDE (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 335
FT /note="Missing (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 349..350
FT /note="EA -> AE (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 355
FT /note="Missing (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 442..445
FT /note="CARK -> GKFG (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 46..48
FT /evidence="ECO:0007829|PDB:1IOD"
FT HELIX 53..57
FT /evidence="ECO:0007829|PDB:1IOD"
FT STRAND 58..61
FT /evidence="ECO:0007829|PDB:1WHE"
FT HELIX 64..71
FT /evidence="ECO:0007829|PDB:1IOD"
FT HELIX 74..82
FT /evidence="ECO:0007829|PDB:1IOD"
FT TURN 86..90
FT /evidence="ECO:0007829|PDB:1WHE"
FT STRAND 100..102
FT /evidence="ECO:0007829|PDB:1CCF"
FT STRAND 105..107
FT /evidence="ECO:0007829|PDB:1APO"
FT STRAND 109..111
FT /evidence="ECO:0007829|PDB:1CCF"
FT STRAND 116..118
FT /evidence="ECO:0007829|PDB:1APO"
FT STRAND 121..123
FT /evidence="ECO:0007829|PDB:1WHF"
FT TURN 131..134
FT /evidence="ECO:0007829|PDB:1KIG"
FT STRAND 135..138
FT /evidence="ECO:0007829|PDB:1KIG"
FT STRAND 155..157
FT /evidence="ECO:0007829|PDB:1KIG"
FT STRAND 164..166
FT /evidence="ECO:0007829|PDB:1KIG"
FT STRAND 168..170
FT /evidence="ECO:0007829|PDB:1KIG"
FT STRAND 235..237
FT /evidence="ECO:0007829|PDB:1KIG"
FT TURN 242..244
FT /evidence="ECO:0007829|PDB:1KIG"
FT STRAND 248..252
FT /evidence="ECO:0007829|PDB:1KIG"
FT STRAND 254..256
FT /evidence="ECO:0007829|PDB:1KIG"
FT STRAND 258..264
FT /evidence="ECO:0007829|PDB:1KIG"
FT STRAND 266..272
FT /evidence="ECO:0007829|PDB:1KIG"
FT STRAND 304..309
FT /evidence="ECO:0007829|PDB:1KIG"
FT TURN 315..317
FT /evidence="ECO:0007829|PDB:1KIG"
FT STRAND 323..329
FT /evidence="ECO:0007829|PDB:1KIG"
FT HELIX 345..350
FT /evidence="ECO:0007829|PDB:1KIG"
FT TURN 351..354
FT /evidence="ECO:0007829|PDB:1KIG"
FT STRAND 355..363
FT /evidence="ECO:0007829|PDB:1KIG"
FT STRAND 365..367
FT /evidence="ECO:0007829|PDB:1KIG"
FT STRAND 370..372
FT /evidence="ECO:0007829|PDB:1KIG"
FT STRAND 377..383
FT /evidence="ECO:0007829|PDB:1KIG"
FT HELIX 386..392
FT /evidence="ECO:0007829|PDB:1KIG"
FT STRAND 401..407
FT /evidence="ECO:0007829|PDB:1KIG"
FT STRAND 421..426
FT /evidence="ECO:0007829|PDB:1KIG"
FT STRAND 429..443
FT /evidence="ECO:0007829|PDB:1KIG"
FT STRAND 447..454
FT /evidence="ECO:0007829|PDB:1KIG"
FT HELIX 455..457
FT /evidence="ECO:0007829|PDB:1KIG"
FT HELIX 458..464
FT /evidence="ECO:0007829|PDB:1KIG"
SQ SEQUENCE 492 AA; 54510 MW; D5BD911FB72F1D30 CRC64;
MAGLLHLVLL STALGGLLRP AGSVFLPRDQ AHRVLQRARR ANSFLEEVKQ GNLERECLEE
ACSLEEAREV FEDAEQTDEF WSKYKDGDQC EGHPCLNQGH CKDGIGDYTC TCAEGFEGKN
CEFSTREICS LDNGGCDQFC REERSEVRCS CAHGYVLGDD SKSCVSTERF PCGKFTQGRS
RRWAIHTSED ALDASELEHY DPADLSPTES SLDLLGLNRT EPSAGEDGSQ VVRIVGGRDC
AEGECPWQAL LVNEENEGFC GGTILNEFYV LTAAHCLHQA KRFTVRVGDR NTEQEEGNEM
AHEVEMTVKH SRFVKETYDF DIAVLRLKTP IRFRRNVAPA CLPEKDWAEA TLMTQKTGIV
SGFGRTHEKG RLSSTLKMLE VPYVDRSTCK LSSSFTITPN MFCAGYDTQP EDACQGDSGG
PHVTRFKDTY FVTGIVSWGE GCARKGKFGV YTKVSNFLKW IDKIMKARAG AAGSRGHSEA
PATWTVPPPL PL
