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   02-SEP-2026, entry version 187.
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 (By similarity). VAP cleaves the
CC       fusion proteins of Sendai virus, NDV, and influenza virus a at a
CC       specific single arginine-containing site, and plays a key role in the
CC       viral spreading in the allantoic sac. {ECO:0000250|UniProtKB:P00742}.
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 (By similarity). {ECO:0000250|UniProtKB:P00742}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Liver and chorioallantoic membrane.
CC   -!- PTM: Carboxylated by vitamin K-dependent GGCX to form gamma-
CC       carboxyglutamate; these residues are essential for the binding of
CC       calcium. {ECO:0000250|UniProtKB:P00742}.
CC   -!- PTM: The activation peptide is cleaved by factor IXa (in the intrinsic
CC       pathway), or by factor VIIa (in the extrinsic pathway).
CC       {ECO:0000250|UniProtKB:P00742}.
CC   -!- PTM: The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate
CC       and asparagine is (R) stereospecific within EGF domains.
CC       {ECO:0000250|UniProtKB:P00742}.
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_205022.2.
DR   AlphaFoldDB; P25155; -.
DR   SMR; P25155; -.
DR   FunCoup; P25155; 1.
DR   STRING; 9031.ENSGALP00000042191; -.
DR   MEROPS; S01.216; -.
DR   GlyCosmos; P25155; 4 sites, No reported glycans.
DR   GlyGen; P25155; 5 sites.
DR   PaxDb; 9031-ENSGALP00000042191; -.
DR   Ensembl; ENSGALT00010035531.1; ENSGALP00010020645.1; ENSGALG00010014766.1.
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; QKDWAEA; -.
DR   OrthoDB; 6380398at2759; -.
DR   PhylomeDB; P25155; -.
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   Reactome; R-GGA-9769735; Initiation of coagulation cascade.
DR   Reactome; R-GGA-9769739; Regulation of clotting cascade.
DR   Reactome; R-GGA-9769743; Amplification and propagation of coagulation cascade.
DR   PRO; PR:P25155; -.
DR   Proteomes; UP000000539; Chromosome 1.
DR   Bgee; ENSGALG00000026677; Expressed in liver and 9 other cell types or tissues.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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; IBA:GO_Central.
DR   GO; GO:0007596; P:blood coagulation; IBA:GO_Central.
DR   GO; GO:0032008; P:positive regulation of TOR signaling; IEA:Ensembl.
DR   GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR   CDD; cd00054; EGF_CA; 1.
DR   CDD; cd00190; Tryp_SPc; 1.
DR   FunFam; 2.40.10.10:FF:000013; Coagulation factor X; 1.
DR   FunFam; 2.10.25.10:FF:000162; Coagulation factor X (Predicted); 1.
DR   FunFam; 4.10.740.10:FF:000001; vitamin K-dependent protein S; 1.
DR   Gene3D; 4.10.740.10; Coagulation Factor IX; 1.
DR   Gene3D; 2.10.25.10; Laminin; 2.
DR   Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
DR   InterPro; IPR017857; Coagulation_fac-like_Gla_dom.
DR   InterPro; IPR000742; EGF.
DR   InterPro; IPR001881; EGF-like_Ca-bd_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; IPR050442; Peptidase_S1_coag_factors.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR001314; Peptidase_S1A.
DR   InterPro; IPR001254; Trypsin_dom.
DR   InterPro; IPR018114; TRYPSIN_HIS.
DR   InterPro; IPR033116; TRYPSIN_SER.
DR   PANTHER; PTHR24278; COAGULATION FACTOR; 1.
DR   PANTHER; PTHR24278:SF28; COAGULATION FACTOR X; 1.
DR   Pfam; PF00008; EGF; 1.
DR   Pfam; PF14670; FXa_inhibition; 1.
DR   Pfam; PF00594; Gla; 1.
DR   Pfam; PF00089; Trypsin; 1.
DR   PIRSF; PIRSF001143; Factor_X; 1.
DR   PRINTS; PR00722; CHYMOTRYPSIN.
DR   PRINTS; PR00010; EGFBLOOD.
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; SSF57630; GLA-domain; 1.
DR   SUPFAM; SSF57184; Growth factor receptor domain; 1.
DR   SUPFAM; SSF50494; Trypsin-like serine proteases; 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
//