Coagulation factor X (EC 3.4.21.6) (Stuart factor) (Virus-activating protease) (VAP) [Cleaved into: Factor X light chain; Factor X heavy chain; Activated factor Xa heavy chain]

 FA10_CHICK              Reviewed;         475 AA.
 P25155;
 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
 01-MAY-1992, sequence version 1.
 02-JUN-2021, entry version 170.
 RecName: Full=Coagulation factor X;
          EC=3.4.21.6;
 AltName: Full=Stuart factor;
 AltName: Full=Virus-activating protease;
          Short=VAP;
 Contains:
   RecName: Full=Factor X light chain;
 Contains:
   RecName: Full=Factor X heavy chain;
 Contains:
   RecName: Full=Activated factor Xa heavy chain;
 Flags: Precursor;
 Name=F10; Synonyms=FX;
 Gallus gallus (Chicken).
 Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
 Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
 Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
 Phasianinae; Gallus.
 NCBI_TaxID=9031;
 [1]
 NUCLEOTIDE SEQUENCE [MRNA].
 TISSUE=Chorioallantoic membrane;
 PubMed=2044767; DOI=10.1016/0014-5793(91)80608-6;
 Suzuki H., Harada A., Hayashi Y., Wada K., Asaka J., Gotoh B.,
 Ogasawara T., Nagai Y.;
 "Primary structure of the virus activating protease from chick embryo. Its
 identity with the blood clotting factor Xa.";
 FEBS Lett. 283:281-285(1991).
 [2]
 PROTEIN SEQUENCE OF 41-55 AND 241-261.
 TISSUE=Allantoic fluid;
 PubMed=2174359; DOI=10.1002/j.1460-2075.1990.tb07643.x;
 Gotoh B., Ogasawara T., Toyoda T., Inocencio N.M., Hamaguchi M., Nagai Y.;
 "An endoprotease homologous to the blood clotting factor X as a determinant
 of viral tropism in chick embryo.";
 EMBO J. 9:4189-4195(1990).
 -!- FUNCTION: Factor Xa is a vitamin K-dependent glycoprotein that converts
     prothrombin to thrombin in the presence of factor Va, calcium and
     phospholipid during blood clotting. VAP cleaves the fusion proteins of
     Sendai virus, NDV, and influenza virus a at a specific single arginine-
     containing site, and plays a key role in the viral spreading in the
     allantoic sac.
 -!- CATALYTIC ACTIVITY:
     Reaction=Selective cleavage of Arg-|-Thr and then Arg-|-Ile bonds in
       prothrombin to form thrombin.; EC=3.4.21.6;
 -!- SUBUNIT: The two chains are formed from a single-chain precursor by the
     excision of two Arg residues and are held together by 1 or more
     disulfide bonds.
 -!- SUBCELLULAR LOCATION: Secreted.
 -!- TISSUE SPECIFICITY: Liver and chorioallantoic membrane.
 -!- PTM: The vitamin K-dependent, enzymatic carboxylation of some glutamate
     residues allows the modified protein to bind calcium.
 -!- PTM: The activation peptide is cleaved by factor IXa (in the intrinsic
     pathway), or by factor VIIa (in the extrinsic pathway).
 -!- PTM: The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate
     and asparagine is (R) stereospecific within EGF domains. {ECO:0000250}.
 -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
     ProRule:PRU00274}.
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 EMBL; D00844; BAA00724.1; -; mRNA.
 PIR; S15838; EXCH.
 RefSeq; NP_990353.1; NM_205022.1.
 SMR; P25155; -.
 STRING; 9031.ENSGALP00000042191; -.
 MEROPS; S01.216; -.
 Ensembl; ENSGALT00000044622; ENSGALP00000042191; ENSGALG00000026677.
 GeneID; 395876; -.
 KEGG; gga:395876; -.
 CTD; 2159; -.
 eggNOG; ENOG502QS4N; Eukaryota.
 GeneTree; ENSGT00940000157694; -.
 HOGENOM; CLU_006842_19_5_1; -.
 InParanoid; P25155; -.
 OMA; CAGYDAK; -.
 OrthoDB; 1314811at2759; -.
 PhylomeDB; P25155; -.
 Reactome; R-GGA-140834; Extrinsic Pathway of Fibrin Clot Formation.
 Reactome; R-GGA-140837; Intrinsic Pathway of Fibrin Clot Formation.
 Reactome; R-GGA-140875; Common Pathway of Fibrin Clot Formation.
 Reactome; R-GGA-159763; Transport of gamma-carboxylated protein precursors from the endoplasmic reticulum to the Golgi apparatus.
 Reactome; R-GGA-159782; Removal of aminoterminal propeptides from gamma-carboxylated proteins.
 PRO; PR:P25155; -.
 Proteomes; UP000000539; Chromosome 1.
 Bgee; ENSGALG00000026677; Expressed in spleen and 10 other tissues.
 GO; GO:0005615; C:extracellular space; IBA:GO_Central.
 GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
 GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC.
 GO; GO:0007596; P:blood coagulation; IEA:UniProtKB-KW.
 CDD; cd00190; Tryp_SPc; 1.
 Gene3D; 2.40.10.10; -; 2.
 Gene3D; 4.10.740.10; -; 1.
 InterPro; IPR017857; Coagulation_fac-like_Gla_dom.
 InterPro; IPR001881; EGF-like_Ca-bd_dom.
 InterPro; IPR000742; EGF-like_dom.
 InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
 InterPro; IPR018097; EGF_Ca-bd_CS.
 InterPro; IPR035972; GLA-like_dom_SF.
 InterPro; IPR000294; GLA_domain.
 InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
 InterPro; IPR012224; Pept_S1A_FX.
 InterPro; IPR009003; Peptidase_S1_PA.
 InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
 InterPro; IPR001314; Peptidase_S1A.
 InterPro; IPR001254; Trypsin_dom.
 InterPro; IPR018114; TRYPSIN_HIS.
 InterPro; IPR033116; TRYPSIN_SER.
 Pfam; PF00008; EGF; 1.
 Pfam; PF00594; Gla; 1.
 Pfam; PF00089; Trypsin; 1.
 PIRSF; PIRSF001143; Factor_X; 1.
 PRINTS; PR00722; CHYMOTRYPSIN.
 PRINTS; PR00001; GLABLOOD.
 SMART; SM00181; EGF; 2.
 SMART; SM00179; EGF_CA; 1.
 SMART; SM00069; GLA; 1.
 SMART; SM00020; Tryp_SPc; 1.
 SUPFAM; SSF50494; SSF50494; 1.
 SUPFAM; SSF57184; SSF57184; 1.
 SUPFAM; SSF57630; SSF57630; 1.
 PROSITE; PS00010; ASX_HYDROXYL; 1.
 PROSITE; PS00022; EGF_1; 1.
 PROSITE; PS01186; EGF_2; 2.
 PROSITE; PS50026; EGF_3; 1.
 PROSITE; PS01187; EGF_CA; 1.
 PROSITE; PS00011; GLA_1; 1.
 PROSITE; PS50998; GLA_2; 1.
 PROSITE; PS50240; TRYPSIN_DOM; 1.
 PROSITE; PS00134; TRYPSIN_HIS; 1.
 PROSITE; PS00135; TRYPSIN_SER; 1.
 1: Evidence at protein level;
 Blood coagulation; Calcium; Cleavage on pair of basic residues;
 Direct protein sequencing; Disulfide bond; EGF-like domain;
 Gamma-carboxyglutamic acid; Glycoprotein; Hemostasis; Hydrolase;
 Hydroxylation; Protease; Reference proteome; Repeat; Secreted;
 Serine protease; Signal; Zymogen.
 SIGNAL          1..20
                 /evidence="ECO:0000255"
 PROPEP          21..40
                 /evidence="ECO:0000269|PubMed:2174359"
                 /id="PRO_0000027810"
 CHAIN           41..475
                 /note="Coagulation factor X"
                 /id="PRO_0000027811"
 CHAIN           41..180
                 /note="Factor X light chain"
                 /id="PRO_0000027812"
 CHAIN           186..475
                 /note="Factor X heavy chain"
                 /id="PRO_0000027813"
 PROPEP          186..240
                 /note="Activation peptide"
                 /evidence="ECO:0000269|PubMed:2174359"
                 /id="PRO_0000027814"
 CHAIN           241..475
                 /note="Activated factor Xa heavy chain"
                 /id="PRO_0000027815"
 DOMAIN          41..85
                 /note="Gla"
                 /evidence="ECO:0000255|PROSITE-ProRule:PRU00463"
 DOMAIN          86..122
                 /note="EGF-like 1; calcium-binding"
                 /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
 DOMAIN          125..168
                 /note="EGF-like 2"
                 /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
 DOMAIN          241..473
                 /note="Peptidase S1"
                 /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
 REGION          216..237
                 /note="Disordered"
                 /evidence="ECO:0000256|SAM:MobiDB-lite"
 ACT_SITE        282
                 /note="Charge relay system"
                 /evidence="ECO:0000250"
 ACT_SITE        328
                 /note="Charge relay system"
                 /evidence="ECO:0000250"
 ACT_SITE        425
                 /note="Charge relay system"
                 /evidence="ECO:0000250"
 MOD_RES         46
                 /note="4-carboxyglutamate"
                 /evidence="ECO:0000255|PROSITE-ProRule:PRU00463"
 MOD_RES         47
                 /note="4-carboxyglutamate"
                 /evidence="ECO:0000255|PROSITE-ProRule:PRU00463"
 MOD_RES         54
                 /note="4-carboxyglutamate"
                 /evidence="ECO:0000255|PROSITE-ProRule:PRU00463"
 MOD_RES         56
                 /note="4-carboxyglutamate"
                 /evidence="ECO:0000255|PROSITE-ProRule:PRU00463"
 MOD_RES         59
                 /note="4-carboxyglutamate"
                 /evidence="ECO:0000255|PROSITE-ProRule:PRU00463"
 MOD_RES         60
                 /note="4-carboxyglutamate"
                 /evidence="ECO:0000255|PROSITE-ProRule:PRU00463"
 MOD_RES         65
                 /note="4-carboxyglutamate"
                 /evidence="ECO:0000255|PROSITE-ProRule:PRU00463"
 MOD_RES         66
                 /note="4-carboxyglutamate"
                 /evidence="ECO:0000255|PROSITE-ProRule:PRU00463"
 MOD_RES         69
                 /note="4-carboxyglutamate"
                 /evidence="ECO:0000255|PROSITE-ProRule:PRU00463"
 MOD_RES         72
                 /note="4-carboxyglutamate"
                 /evidence="ECO:0000255|PROSITE-ProRule:PRU00463"
 MOD_RES         79
                 /note="4-carboxyglutamate"
                 /evidence="ECO:0000255|PROSITE-ProRule:PRU00463"
 MOD_RES         103
                 /note="(3R)-3-hydroxyaspartate"
                 /evidence="ECO:0000250"
 CARBOHYD        196
                 /note="N-linked (GlcNAc...) asparagine"
                 /evidence="ECO:0000255"
 CARBOHYD        207
                 /note="N-linked (GlcNAc...) asparagine"
                 /evidence="ECO:0000255"
 CARBOHYD        228
                 /note="N-linked (GlcNAc...) asparagine"
                 /evidence="ECO:0000255"
 CARBOHYD        285
                 /note="N-linked (GlcNAc...) asparagine"
                 /evidence="ECO:0000255"
 DISULFID        57..62
                 /evidence="ECO:0000250"
 DISULFID        90..101
                 /evidence="ECO:0000250"
 DISULFID        95..110
                 /evidence="ECO:0000250"
 DISULFID        112..121
                 /evidence="ECO:0000250"
 DISULFID        129..140
                 /evidence="ECO:0000250"
 DISULFID        136..152
                 /evidence="ECO:0000250"
 DISULFID        154..167
                 /evidence="ECO:0000250"
 DISULFID        175..348
                 /note="Interchain (between light and heavy chains)"
                 /evidence="ECO:0000255|PROSITE-ProRule:PRU00076,
                 ECO:0000255|PROSITE-ProRule:PRU00274, ECO:0000255|PROSITE-
                 ProRule:PRU00463"
 DISULFID        247..252
                 /evidence="ECO:0000250"
 DISULFID        267..283
                 /evidence="ECO:0000250"
 DISULFID        396..410
                 /evidence="ECO:0000250"
 DISULFID        421..449
                 /evidence="ECO:0000250"
 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

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