(data stored in ACNUC3659 zone)

HOVERGEN: 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   22-SEP-2009, entry version 95.
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   Archosauria; Dinosauria; Saurischia; Theropoda; Coelurosauria; Aves;
OC   Neognathae; Galliformes; Phasianidae; Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Chorioallantoic membrane;
RX   MEDLINE=91257322; 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   MEDLINE=91065352; 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: Selective cleavage of Arg-|-Thr and then
CC       Arg-|-Ile bonds in prothrombin to form thrombin.
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       (By similarity).
CC   -!- SIMILARITY: Belongs to the peptidase S1 family.
CC   -!- SIMILARITY: Contains 2 EGF-like domains.
CC   -!- SIMILARITY: Contains 1 Gla (gamma-carboxy-glutamate) domain.
CC   -!- SIMILARITY: Contains 1 peptidase S1 domain.
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CC   -!- GENE_FAMILY: HBG013304 [ FAMILY / ALN / TREE ]
DR   EMBL; D00844; BAA00724.1; -; mRNA.
DR   IPI; IPI00587100; -.
DR   PIR; S15838; EXCH.
DR   RefSeq; NP_990353.1; -.
DR   UniGene; Gga.514; -.
DR   HSSP; P00742; 1HCG.
DR   GeneID; 395876; -.
DR   KEGG; gga:395876; -.
DR   CTD; 395876; -.
DR   HOVERGEN; P25155; -.
DR   BRENDA; 3.4.21.6; 4.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005509; F:calcium ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0007596; P:blood coagulation; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   InterPro; IPR002383; Coagulation_factor_Gla.
DR   InterPro; IPR006209; EGF.
DR   InterPro; IPR006210; EGF-like.
DR   InterPro; IPR013032; EGF-like_reg_CS.
DR   InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR   InterPro; IPR001438; EGF_2.
DR   InterPro; IPR000742; EGF_3.
DR   InterPro; IPR001881; EGF_Ca_bd.
DR   InterPro; IPR018097; EGF_Ca_bd_CS.
DR   InterPro; IPR000294; GLA_domain.
DR   InterPro; IPR012224; Pept_S1A_FX.
DR   InterPro; IPR018114; Peptidase_S1/S6_AS.
DR   InterPro; IPR001254; Peptidase_S1_S6.
DR   InterPro; IPR001314; Peptidase_S1A.
DR   Pfam; PF00008; EGF; 2.
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; 1.
DR   SMART; SM00179; EGF_CA; 1.
DR   SMART; SM00069; GLA; 1.
DR   SMART; SM00020; Tryp_SPc; 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;
DR   PRODOM; P25155.
DR   SWISS-2DPAGE; P25155.
KW   Blood coagulation; Calcium; Cleavage on pair of basic residues;
KW   Direct protein sequencing; Disulfide bond; EGF-like domain;
KW   Gamma-carboxyglutamic acid; Glycoprotein; Hydrolase; Hydroxylation;
KW   Protease; Repeat; Secreted; Serine protease; Signal; Zymogen.
FT   DOMAIN       41     92       PRODOM:2005.1:PD325296  86
FT   DOMAIN       93    122       PRODOM:2005.1:PD007207  861
FT   DOMAIN      179    240       PRODOM:2005.1:PD745314  1
FT   DOMAIN      241    282       PRODOM:2005.1:PD474467  1445
FT   DOMAIN      290    333       PRODOM:2005.1:PD331626  438
FT   DOMAIN      334    372       PRODOM:2005.1:PD774702  15
FT   DOMAIN      375    413       PRODOM:2005.1:PD623710  171
FT   DOMAIN      424    469       PRODOM:2005.1:PD000068  1525
FT   SIGNAL        1     20       Potential.
FT   PROPEP       21     40
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                                /FTId=PRO_0000027814.
FT   CHAIN       241    475       Activated factor Xa heavy chain.
FT                                /FTId=PRO_0000027815.
FT   DOMAIN       41     85       Gla.
FT   DOMAIN       86    122       EGF-like 1; calcium-binding (Potential).
FT   DOMAIN      125    168       EGF-like 2.
FT   DOMAIN      241    473       Peptidase S1.
FT   ACT_SITE    282    282       Charge relay system (By similarity).
FT   ACT_SITE    328    328       Charge relay system (By similarity).
FT   ACT_SITE    425    425       Charge relay system (By similarity).
FT   MOD_RES      46     46       4-carboxyglutamate (By similarity).
FT   MOD_RES      47     47       4-carboxyglutamate (By similarity).
FT   MOD_RES      54     54       4-carboxyglutamate (By similarity).
FT   MOD_RES      56     56       4-carboxyglutamate (By similarity).
FT   MOD_RES      59     59       4-carboxyglutamate (By similarity).
FT   MOD_RES      60     60       4-carboxyglutamate (By similarity).
FT   MOD_RES      65     65       4-carboxyglutamate (By similarity).
FT   MOD_RES      66     66       4-carboxyglutamate (By similarity).
FT   MOD_RES      69     69       4-carboxyglutamate (By similarity).
FT   MOD_RES      72     72       4-carboxyglutamate (By similarity).
FT   MOD_RES      79     79       4-carboxyglutamate (By similarity).
FT   MOD_RES     103    103       (3R)-3-hydroxyaspartate (By similarity).
FT   CARBOHYD    196    196       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    207    207       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    228    228       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    285    285       N-linked (GlcNAc...) (Potential).
FT   DISULFID     57     62       By similarity.
FT   DISULFID     90    101       By similarity.
FT   DISULFID     95    110       By similarity.
FT   DISULFID    112    121       By similarity.
FT   DISULFID    129    140       By similarity.
FT   DISULFID    136    152       By similarity.
FT   DISULFID    154    167       By similarity.
FT   DISULFID    175    348       Interchain (between light and heavy
FT                                chains) (By similarity).
FT   DISULFID    247    252       By similarity.
FT   DISULFID    267    283       By similarity.
FT   DISULFID    396    410       By similarity.
FT   DISULFID    421    449       By similarity.
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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