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Database: UniProt
Entry: P25155
LinkDB: P25155
Original site: P25155 
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   10-APR-2019, entry version 160.
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;
OC   Phasianidae; 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.
RT   Its 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;
RA   Gotoh B., Ogasawara T., Toyoda T., Inocencio N.M., Hamaguchi M.,
RA   Nagai Y.;
RT   "An endoprotease homologous to the blood clotting factor X as a
RT   determinant of viral tropism in chick embryo.";
RL   EMBO J. 9:4189-4195(1990).
CC   -!- FUNCTION: Factor Xa is a vitamin K-dependent glycoprotein that
CC       converts prothrombin to thrombin in the presence of factor Va,
CC       calcium and phospholipid during blood clotting. 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
CC       the viral spreading in the allantoic sac.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Selective cleavage of Arg-|-Thr and then Arg-|-Ile bonds
CC         in prothrombin to form thrombin.; EC=3.4.21.6;
CC   -!- SUBUNIT: The two chains are formed from a single-chain precursor
CC       by the excision of two Arg residues and are held together by 1 or
CC       more disulfide bonds.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Liver and chorioallantoic membrane.
CC   -!- PTM: The vitamin K-dependent, enzymatic carboxylation of some
CC       glutamate residues allows the modified protein to bind calcium.
CC   -!- PTM: The activation peptide is cleaved by factor IXa (in the
CC       intrinsic pathway), or by factor VIIa (in the extrinsic pathway).
CC   -!- PTM: The iron and 2-oxoglutarate dependent 3-hydroxylation of
CC       aspartate and asparagine is (R) stereospecific within EGF domains.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00274}.
DR   EMBL; D00844; BAA00724.1; -; mRNA.
DR   PIR; S15838; EXCH.
DR   RefSeq; NP_990353.1; NM_205022.1.
DR   UniGene; Gga.514; -.
DR   ProteinModelPortal; 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   GeneTree; ENSGT00940000157694; -.
DR   HOVERGEN; HBG013304; -.
DR   InParanoid; P25155; -.
DR   KO; K01314; -.
DR   OMA; CAGYDAK; -.
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 8 organ(s), highest expression level in spleen.
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:Ensembl.
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   CDD; cd00190; Tryp_SPc; 1.
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; IPR013032; EGF-like_CS.
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; 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   Complete proteome; Direct protein sequencing; Disulfide bond;
KW   EGF-like domain; Gamma-carboxyglutamic acid; Glycoprotein; Hemostasis;
KW   Hydrolase; Hydroxylation; Protease; Reference proteome; Repeat;
KW   Secreted; Serine protease; Signal; Zymogen.
FT   SIGNAL        1     20       {ECO:0000255}.
FT   PROPEP       21     40       {ECO:0000269|PubMed:2174359}.
FT                                /FTId=PRO_0000027810.
FT   CHAIN        41    475       Coagulation factor X.
FT                                /FTId=PRO_0000027811.
FT   CHAIN        41    180       Factor X light chain.
FT                                /FTId=PRO_0000027812.
FT   CHAIN       186    475       Factor X heavy chain.
FT                                /FTId=PRO_0000027813.
FT   PROPEP      186    240       Activation peptide.
FT                                {ECO:0000269|PubMed:2174359}.
FT                                /FTId=PRO_0000027814.
FT   CHAIN       241    475       Activated factor Xa heavy chain.
FT                                /FTId=PRO_0000027815.
FT   DOMAIN       41     85       Gla. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00463}.
FT   DOMAIN       86    122       EGF-like 1; calcium-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DOMAIN      125    168       EGF-like 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      241    473       Peptidase S1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00274}.
FT   ACT_SITE    282    282       Charge relay system. {ECO:0000250}.
FT   ACT_SITE    328    328       Charge relay system. {ECO:0000250}.
FT   ACT_SITE    425    425       Charge relay system. {ECO:0000250}.
FT   MOD_RES      46     46       4-carboxyglutamate. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00463}.
FT   MOD_RES      47     47       4-carboxyglutamate. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00463}.
FT   MOD_RES      54     54       4-carboxyglutamate. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00463}.
FT   MOD_RES      56     56       4-carboxyglutamate. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00463}.
FT   MOD_RES      59     59       4-carboxyglutamate. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00463}.
FT   MOD_RES      60     60       4-carboxyglutamate. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00463}.
FT   MOD_RES      65     65       4-carboxyglutamate. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00463}.
FT   MOD_RES      66     66       4-carboxyglutamate. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00463}.
FT   MOD_RES      69     69       4-carboxyglutamate. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00463}.
FT   MOD_RES      72     72       4-carboxyglutamate. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00463}.
FT   MOD_RES      79     79       4-carboxyglutamate. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00463}.
FT   MOD_RES     103    103       (3R)-3-hydroxyaspartate. {ECO:0000250}.
FT   CARBOHYD    196    196       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    207    207       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    228    228       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    285    285       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID     57     62       {ECO:0000250}.
FT   DISULFID     90    101       {ECO:0000250}.
FT   DISULFID     95    110       {ECO:0000250}.
FT   DISULFID    112    121       {ECO:0000250}.
FT   DISULFID    129    140       {ECO:0000250}.
FT   DISULFID    136    152       {ECO:0000250}.
FT   DISULFID    154    167       {ECO:0000250}.
FT   DISULFID    175    348       Interchain (between light and heavy
FT                                chains). {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076, ECO:0000255|PROSITE-
FT                                ProRule:PRU00274, ECO:0000255|PROSITE-
FT                                ProRule:PRU00463}.
FT   DISULFID    247    252       {ECO:0000250}.
FT   DISULFID    267    283       {ECO:0000250}.
FT   DISULFID    396    410       {ECO:0000250}.
FT   DISULFID    421    449       {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
//
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