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Database: UniProt
Entry: P22457
LinkDB: P22457
Original site: P22457 
ID   FA7_BOVIN               Reviewed;         447 AA.
AC   P22457; A6H6Y5; Q58DL3;
DT   01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT   13-JUN-2006, sequence version 2.
DT   16-JAN-2019, entry version 176.
DE   RecName: Full=Coagulation factor VII;
DE            EC=3.4.21.21;
DE   AltName: Full=Serum prothrombin conversion accelerator;
DE   Contains:
DE     RecName: Full=Factor VII light chain;
DE   Contains:
DE     RecName: Full=Factor VII heavy chain;
DE   Flags: Precursor;
GN   Name=F7;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
OC   Pecora; Bovidae; Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA   Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA   Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT   "Characterization of 954 bovine full-CDS cDNA sequences.";
RL   BMC Genomics 6:166-166(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   PROTEIN SEQUENCE OF 41-447, AND GAMMA-CARBOXYGLUTAMATION AT GLU-46;
RP   GLU-47; GLU-54; GLU-56; GLU-59; GLU-60; GLU-65; GLU-66; GLU-69; GLU-74
RP   AND GLU-75.
RX   PubMed=3049594;
RA   Takeya H., Kawabata S., Nakagawa K., Yamamichi Y., Miyata T.,
RA   Iwanaga S.;
RT   "Bovine factor VII. Its purification and complete amino acid
RT   sequence.";
RL   J. Biol. Chem. 263:14868-14877(1988).
RN   [4]
RP   GLYCOSYLATION AT SER-92, AND STRUCTURE OF CARBOHYDRATE ON SER-92.
RX   PubMed=3149637;
RA   Hase S., Kawabata S., Nishimura H., Takeya H., Sueyoshi T., Miyata T.,
RA   Iwanaga S., Takao T., Shimonishi Y., Ikenaka T.;
RT   "A new trisaccharide sugar chain linked to a serine residue in bovine
RT   blood coagulation factors VII and IX.";
RL   J. Biochem. 104:867-868(1988).
RN   [5]
RP   GLYCOSYLATION AT SER-92, AND STRUCTURE OF CARBOHYDRATE ON SER-92.
RX   PubMed=2129367;
RA   Iwanaga S., Nishimura H., Kawabata S., Kisiel W., Hase S., Ikenaka T.;
RT   "A new trisaccharide sugar chain linked to a serine residue in the
RT   first EGF-like domain of clotting factors VII and IX and protein Z.";
RL   Adv. Exp. Med. Biol. 281:121-131(1990).
CC   -!- FUNCTION: Initiates the extrinsic pathway of blood coagulation.
CC       Serine protease that circulates in the blood in a zymogen form.
CC       Factor VII is converted to factor VIIa by factor Xa, factor XIIa,
CC       factor IXa, or thrombin by minor proteolysis. In the presence of
CC       tissue factor and calcium ions, factor VIIa then converts factor X
CC       to factor Xa by limited proteolysis. Factor VIIa will also convert
CC       factor IX to factor IXa in the presence of tissue factor and
CC       calcium.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Selective cleavage of Arg-|-Ile bond in factor X to form
CC         factor Xa.; EC=3.4.21.21;
CC   -!- SUBUNIT: Heterodimer of a light chain and a heavy chain linked by
CC       a disulfide bond.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Plasma.
CC   -!- PTM: The vitamin K-dependent, enzymatic carboxylation of some
CC       glutamate residues allows the modified protein to bind calcium.
CC   -!- PTM: O-glycosylated. O-fucosylated by POFUT1 on a conserved serine
CC       or threonine residue found in the consensus sequence C2-X(4,5)-
CC       [S/T]-C3 of EGF domains, where C2 and C3 are the second and third
CC       conserved cysteines. {ECO:0000250}.
CC   -!- PTM: Can be either O-glucosylated or O-xylosylated at Ser-92 by
CC       POGLUT1. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00274}.
DR   EMBL; BT021584; AAX46431.1; -; mRNA.
DR   EMBL; BC146045; AAI46046.1; -; mRNA.
DR   PIR; A31979; KFBO7.
DR   RefSeq; NP_001029978.1; NM_001034806.1.
DR   UniGene; Bt.37397; -.
DR   ProteinModelPortal; P22457; -.
DR   ELM; P22457; -.
DR   STRING; 9913.ENSBTAP00000009746; -.
DR   MEROPS; S01.215; -.
DR   iPTMnet; P22457; -.
DR   PaxDb; P22457; -.
DR   PRIDE; P22457; -.
DR   Ensembl; ENSBTAT00000009746; ENSBTAP00000009746; ENSBTAG00000007411.
DR   GeneID; 617960; -.
DR   KEGG; bta:617960; -.
DR   CTD; 2155; -.
DR   VGNC; VGNC:28689; F7.
DR   eggNOG; ENOG410IIMB; Eukaryota.
DR   eggNOG; COG5640; LUCA.
DR   GeneTree; ENSGT00940000154474; -.
DR   HOGENOM; HOG000251821; -.
DR   HOVERGEN; HBG013304; -.
DR   InParanoid; P22457; -.
DR   KO; K01320; -.
DR   OMA; RNCETNK; -.
DR   OrthoDB; 1314811at2759; -.
DR   TreeFam; TF327329; -.
DR   Reactome; R-BTA-140834; Extrinsic Pathway of Fibrin Clot Formation.
DR   Reactome; R-BTA-159740; Gamma-carboxylation of protein precursors.
DR   Reactome; R-BTA-159763; Transport of gamma-carboxylated protein precursors from the endoplasmic reticulum to the Golgi apparatus.
DR   Reactome; R-BTA-159782; Removal of aminoterminal propeptides from gamma-carboxylated proteins.
DR   Proteomes; UP000009136; Chromosome 12.
DR   Bgee; ENSBTAG00000007411; Expressed in 5 organ(s), highest expression level in liver.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:1905286; C:serine-type peptidase complex; IEA:Ensembl.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:Ensembl.
DR   GO; GO:0007596; P:blood coagulation; IBA:GO_Central.
DR   GO; GO:0002690; P:positive regulation of leukocyte chemotaxis; IBA:GO_Central.
DR   GO; GO:0010641; P:positive regulation of platelet-derived growth factor receptor signaling pathway; IEA:Ensembl.
DR   GO; GO:0050927; P:positive regulation of positive chemotaxis; IEA:Ensembl.
DR   GO; GO:0051897; P:positive regulation of protein kinase B signaling; IEA:Ensembl.
DR   GO; GO:0016485; P:protein processing; 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; IPR033190; F7.
DR   InterPro; IPR035972; GLA-like_dom_SF.
DR   InterPro; IPR000294; GLA_domain.
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   PANTHER; PTHR44064:SF1; PTHR44064:SF1; 1.
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; 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; Protease; Reference proteome; Repeat; Secreted;
KW   Serine protease; Signal; Zymogen.
FT   SIGNAL        1     23       {ECO:0000255}.
FT   PROPEP       24     40       {ECO:0000269|PubMed:3049594}.
FT                                /FTId=PRO_0000240126.
FT   CHAIN        41    192       Factor VII light chain.
FT                                {ECO:0000269|PubMed:3049594}.
FT                                /FTId=PRO_0000027727.
FT   CHAIN       193    447       Factor VII heavy chain.
FT                                {ECO:0000269|PubMed:3049594}.
FT                                /FTId=PRO_0000027728.
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      127    168       EGF-like 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      193    432       Peptidase S1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00274}.
FT   ACT_SITE    233    233       Charge relay system. {ECO:0000250}.
FT   ACT_SITE    282    282       Charge relay system. {ECO:0000250}.
FT   ACT_SITE    384    384       Charge relay system. {ECO:0000250}.
FT   BINDING     378    378       Substrate. {ECO:0000250}.
FT   SITE         93     93       Important for S-92 for O-xylosylation.
FT                                {ECO:0000250}.
FT   SITE        192    193       Cleavage; by factor Xa, factor XIIa,
FT                                factor IXa, or thrombin.
FT   MOD_RES      46     46       4-carboxyglutamate. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00463,
FT                                ECO:0000269|PubMed:3049594}.
FT   MOD_RES      47     47       4-carboxyglutamate. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00463,
FT                                ECO:0000269|PubMed:3049594}.
FT   MOD_RES      54     54       4-carboxyglutamate. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00463,
FT                                ECO:0000269|PubMed:3049594}.
FT   MOD_RES      56     56       4-carboxyglutamate. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00463,
FT                                ECO:0000269|PubMed:3049594}.
FT   MOD_RES      59     59       4-carboxyglutamate. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00463,
FT                                ECO:0000269|PubMed:3049594}.
FT   MOD_RES      60     60       4-carboxyglutamate. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00463,
FT                                ECO:0000269|PubMed:3049594}.
FT   MOD_RES      65     65       4-carboxyglutamate. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00463,
FT                                ECO:0000269|PubMed:3049594}.
FT   MOD_RES      66     66       4-carboxyglutamate. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00463,
FT                                ECO:0000269|PubMed:3049594}.
FT   MOD_RES      69     69       4-carboxyglutamate. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00463,
FT                                ECO:0000269|PubMed:3049594}.
FT   MOD_RES      74     74       4-carboxyglutamate. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00463,
FT                                ECO:0000269|PubMed:3049594}.
FT   MOD_RES      75     75       4-carboxyglutamate. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00463,
FT                                ECO:0000269|PubMed:3049594}.
FT   CARBOHYD     92     92       O-linked (Glc...) serine.
FT                                {ECO:0000269|PubMed:2129367,
FT                                ECO:0000269|PubMed:3149637}.
FT   CARBOHYD     92     92       O-linked (Glc...) serine; alternate.
FT                                {ECO:0000250, ECO:0000269|PubMed:2129367,
FT                                ECO:0000269|PubMed:3149637}.
FT   CARBOHYD     92     92       O-linked (Xyl...) serine; alternate.
FT                                {ECO:0000250, ECO:0000269|PubMed:2129367,
FT                                ECO:0000269|PubMed:3149637}.
FT   CARBOHYD    100    100       O-linked (Fuc) serine. {ECO:0000250}.
FT   CARBOHYD    185    185       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000269|PubMed:3049594}.
FT   CARBOHYD    243    243       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000269|PubMed:3049594}.
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    131    142       {ECO:0000250}.
FT   DISULFID    138    152       {ECO:0000250}.
FT   DISULFID    154    167       {ECO:0000250}.
FT   DISULFID    175    302       {ECO:0000250}.
FT   DISULFID    199    204       {ECO:0000250}.
FT   DISULFID    218    234       {ECO:0000250}.
FT   DISULFID    350    369       {ECO:0000250}.
FT   DISULFID    380    408       {ECO:0000250}.
SQ   SEQUENCE   447 AA;  48961 MW;  6FE6CA805E84B871 CRC64;
     MLSQAWALAL LCFLLSLWGS LPAVFLPQEQ ALSILHRPRR ANGFLEELLP GSLERECREE
     LCSFEEAHEI FRNEERTRQF WVSYNDGDQC ASSPCQNGGS CEDQLRSYIC FCPDGFEGRN
     CETDKQSQLI CANDNGGCEQ YCGADPGAGR FCWCHEGYAL QADGVSCAPT VEYPCGKIPV
     LEKRNGSKPQ GRIVGGHVCP KGECPWQAML KLNGALLCGG TLVGPAWVVS AAHCFERLRS
     RGNLTAVLGE HDLSRVEGPE QERRVAQIIV PKQYVPGQTD HDVALLQLAQ PVALGDHVAP
     LCLPDPDFAD QTLAFVRFSA VSGWGQLLER GVTARKLMVV LVPRLLTQDC LQQSRQRPGG
     PVVTDNMFCA GYSDGSKDAC KGDSGGPHAT RFRGTWFLTG VVSWGEGCAA AGHFGIYTRV
     SRYTAWLRQL MGHPPSRQGF FQVPLLP
//
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