FA10_CHICK
ID FA10_CHICK Reviewed; 475 AA.
AC P25155;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 1.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Coagulation factor X;
DE EC=3.4.21.6;
DE AltName: Full=Stuart factor;
DE AltName: Full=Virus-activating protease;
DE Short=VAP;
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; Synonyms=FX;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Chorioallantoic membrane;
RX PubMed=2044767; DOI=10.1016/0014-5793(91)80608-6;
RA Suzuki H., Harada A., Hayashi Y., Wada K., Asaka J., Gotoh B.,
RA Ogasawara T., Nagai Y.;
RT "Primary structure of the virus activating protease from chick embryo. Its
RT identity with the blood clotting factor Xa.";
RL FEBS Lett. 283:281-285(1991).
RN [2]
RP PROTEIN SEQUENCE OF 41-55 AND 241-261.
RC TISSUE=Allantoic fluid;
RX PubMed=2174359; DOI=10.1002/j.1460-2075.1990.tb07643.x;
RA Gotoh B., Ogasawara T., Toyoda T., Inocencio N.M., Hamaguchi M., Nagai Y.;
RT "An endoprotease homologous to the blood clotting factor X as a determinant
RT of viral tropism in chick embryo.";
RL EMBO J. 9:4189-4195(1990).
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. VAP cleaves the fusion proteins of
CC Sendai virus, NDV, and influenza virus a at a specific single arginine-
CC containing site, and plays a key role in the viral spreading in the
CC allantoic sac.
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 -!- 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.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Liver and chorioallantoic membrane.
CC -!- PTM: The vitamin K-dependent, enzymatic carboxylation of some glutamate
CC residues allows the modified protein to bind calcium.
CC -!- PTM: The activation peptide is cleaved by factor IXa (in the intrinsic
CC pathway), or by factor VIIa (in the extrinsic pathway).
CC -!- PTM: The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate
CC and asparagine is (R) stereospecific within EGF domains. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00274}.
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DR EMBL; D00844; BAA00724.1; -; mRNA.
DR PIR; S15838; EXCH.
DR RefSeq; NP_990353.1; NM_205022.1.
DR AlphaFoldDB; P25155; -.
DR SMR; P25155; -.
DR STRING; 9031.ENSGALP00000042191; -.
DR MEROPS; S01.216; -.
DR Ensembl; ENSGALT00000044622; ENSGALP00000042191; ENSGALG00000026677.
DR GeneID; 395876; -.
DR KEGG; gga:395876; -.
DR CTD; 2159; -.
DR VEuPathDB; HostDB:geneid_395876; -.
DR eggNOG; ENOG502QS4N; Eukaryota.
DR GeneTree; ENSGT00940000157694; -.
DR HOGENOM; CLU_006842_19_5_1; -.
DR InParanoid; P25155; -.
DR OMA; HCLHQAK; -.
DR OrthoDB; 1314811at2759; -.
DR PhylomeDB; P25155; -.
DR Reactome; R-GGA-140834; Extrinsic Pathway of Fibrin Clot Formation.
DR Reactome; R-GGA-140837; Intrinsic Pathway of Fibrin Clot Formation.
DR Reactome; R-GGA-140875; Common Pathway of Fibrin Clot Formation.
DR Reactome; R-GGA-159763; Transport of gamma-carboxylated protein precursors from the endoplasmic reticulum to the Golgi apparatus.
DR Reactome; R-GGA-159782; Removal of aminoterminal propeptides from gamma-carboxylated proteins.
DR PRO; PR:P25155; -.
DR Proteomes; UP000000539; Chromosome 1.
DR Bgee; ENSGALG00000026677; Expressed in liver and 9 other tissues.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0005543; F:phospholipid binding; IEA:Ensembl.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0007596; P:blood coagulation; IEA:UniProtKB-KW.
DR GO; GO:0051897; P:positive regulation of protein kinase B signaling; IEA:Ensembl.
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; IPR009030; Growth_fac_rcpt_cys_sf.
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; SSF57184; SSF57184; 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 Blood coagulation; Calcium; Cleavage on pair of basic residues;
KW Direct protein sequencing; Disulfide bond; EGF-like domain;
KW Gamma-carboxyglutamic acid; Glycoprotein; Hemostasis; Hydrolase;
KW Hydroxylation; Protease; Reference proteome; Repeat; Secreted;
KW Serine protease; Signal; Zymogen.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT PROPEP 21..40
FT /evidence="ECO:0000269|PubMed:2174359"
FT /id="PRO_0000027810"
FT CHAIN 41..475
FT /note="Coagulation factor X"
FT /id="PRO_0000027811"
FT CHAIN 41..180
FT /note="Factor X light chain"
FT /id="PRO_0000027812"
FT CHAIN 186..475
FT /note="Factor X heavy chain"
FT /id="PRO_0000027813"
FT PROPEP 186..240
FT /note="Activation peptide"
FT /evidence="ECO:0000269|PubMed:2174359"
FT /id="PRO_0000027814"
FT CHAIN 241..475
FT /note="Activated factor Xa heavy chain"
FT /id="PRO_0000027815"
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..168
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 241..473
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT REGION 216..237
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 282
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 328
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 425
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT MOD_RES 46
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463"
FT MOD_RES 47
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463"
FT MOD_RES 54
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463"
FT MOD_RES 56
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463"
FT MOD_RES 59
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463"
FT MOD_RES 60
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463"
FT MOD_RES 65
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463"
FT MOD_RES 66
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463"
FT MOD_RES 69
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463"
FT MOD_RES 72
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463"
FT MOD_RES 79
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463"
FT MOD_RES 103
FT /note="(3R)-3-hydroxyaspartate"
FT /evidence="ECO:0000250"
FT CARBOHYD 196
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 207
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 228
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 285
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 57..62
FT /evidence="ECO:0000250"
FT DISULFID 90..101
FT /evidence="ECO:0000250"
FT DISULFID 95..110
FT /evidence="ECO:0000250"
FT DISULFID 112..121
FT /evidence="ECO:0000250"
FT DISULFID 129..140
FT /evidence="ECO:0000250"
FT DISULFID 136..152
FT /evidence="ECO:0000250"
FT DISULFID 154..167
FT /evidence="ECO:0000250"
FT DISULFID 175..348
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"
FT DISULFID 247..252
FT /evidence="ECO:0000250"
FT DISULFID 267..283
FT /evidence="ECO:0000250"
FT DISULFID 396..410
FT /evidence="ECO:0000250"
FT DISULFID 421..449
FT /evidence="ECO:0000250"
SQ SEQUENCE 475 AA; 53142 MW; 570BF84956C5C74D CRC64;
MAGRLLLLLL CAALPDELRA EGGVFIKKES ADKFLERTKR ANSFLEEMKQ GNIERECNEE
RCSKEEAREA FEDNEKTEEF WNIYVDGDQC SSNPCHYGGQ CKDGLGSYTC SCLDGYQGKN
CEFVIPKYCK INNGDCEQFC SIKKSVQKDV VCSCTSGYEL AEDGKQCVSK VKYPCGKVLM
KRIKRSVILP TNSNTNATSD QDVPSTNGSI LEEVFTTTTE SPTPPPRNGS SITDPNVDTR
IVGGDECRPG ECPWQAVLIN EKGEEFCGGT ILNEDFILTA AHCINQSKEI KVVVGEVDRE
KEEHSETTHT AEKIFVHSKY IAETYDNDIA LIKLKEPIQF SEYVVPACLP QADFANEVLM
NQKSGMVSGF GREFEAGRLS KRLKVLEVPY VDRSTCKQST NFAITENMFC AGYETEQKDA
CQGDSGGPHV TRYKDTYFVT GIVSWGEGCA RKGKYGVYTK LSRFLRWVRT VMRQK
