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FA7_PANTR
ID   FA7_PANTR               Reviewed;         466 AA.
AC   Q2F9P2;
DT   16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   03-AUG-2022, entry version 89.
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   Pan troglodytes (Chimpanzee).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pan.
OX   NCBI_TaxID=9598;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=16292673; DOI=10.1007/s00439-005-0045-5;
RA   Sabater-Lleal M., Soria J.M., Bertranpetit J., Almasy L., Blangero J.,
RA   Fontcuberta J., Calafell F.;
RT   "Human F7 sequence is split into three deep clades that are related to FVII
RT   plasma levels.";
RL   Hum. Genet. 118:741-751(2006).
CC   -!- FUNCTION: Initiates the extrinsic pathway of blood coagulation. Serine
CC       protease that circulates in the blood in a zymogen form. Factor VII is
CC       converted to factor VIIa by factor Xa, factor XIIa, factor IXa, or
CC       thrombin by minor proteolysis. In the presence of tissue factor and
CC       calcium ions, factor VIIa then converts factor X to factor Xa by
CC       limited proteolysis. Factor VIIa will also convert factor IX to factor
CC       IXa in the presence of tissue factor and calcium (By similarity).
CC       {ECO:0000250}.
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 a
CC       disulfide bond. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- PTM: The vitamin K-dependent, enzymatic carboxylation of some glutamate
CC       residues allows the modified protein to bind calcium. {ECO:0000250}.
CC   -!- PTM: The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate
CC       and asparagine is (R) stereospecific within EGF domains. {ECO:0000250}.
CC   -!- PTM: O-glycosylated. O-fucosylated by POFUT1 on a conserved serine or
CC       threonine residue found in the consensus sequence C2-X(4,5)-[S/T]-C3 of
CC       EGF domains, where C2 and C3 are the second and third conserved
CC       cysteines. {ECO:0000250}.
CC   -!- PTM: Can be either O-glucosylated or O-xylosylated at Ser-112 by
CC       POGLUT1. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC       ProRule:PRU00274}.
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DR   EMBL; DQ142914; ABD17894.1; -; Genomic_DNA.
DR   EMBL; DQ142915; ABD17895.1; -; Genomic_DNA.
DR   STRING; 9598.ENSPTRP00000010284; -.
DR   MEROPS; S01.215; -.
DR   PaxDb; Q2F9P2; -.
DR   eggNOG; ENOG502QRGI; Eukaryota.
DR   InParanoid; Q2F9P2; -.
DR   Proteomes; UP000002277; Unplaced.
DR   GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProt.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0005796; C:Golgi lumen; IEA:UniProt.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC.
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:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd00190; Tryp_SPc; 1.
DR   Gene3D; 2.40.10.10; -; 2.
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; 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; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR   InterPro; IPR001314; Peptidase_S1A.
DR   InterPro; IPR001254; Trypsin_dom.
DR   InterPro; IPR018114; TRYPSIN_HIS.
DR   InterPro; IPR033116; TRYPSIN_SER.
DR   PANTHER; PTHR24278:SF26; PTHR24278:SF26; 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; 1.
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   3: Inferred from homology;
KW   Blood coagulation; Calcium; Cleavage on pair of basic residues;
KW   Disulfide bond; EGF-like domain; Gamma-carboxyglutamic acid; Glycoprotein;
KW   Hemostasis; Hydrolase; Hydroxylation; Protease; Reference proteome; Repeat;
KW   Secreted; Serine protease; Signal; Zymogen.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   PROPEP          21..60
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000235182"
FT   CHAIN           61..212
FT                   /note="Factor VII light chain"
FT                   /id="PRO_0000235183"
FT   CHAIN           213..466
FT                   /note="Factor VII heavy chain"
FT                   /id="PRO_0000235184"
FT   DOMAIN          61..105
FT                   /note="Gla"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00463"
FT   DOMAIN          106..142
FT                   /note="EGF-like 1; calcium-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          147..188
FT                   /note="EGF-like 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT   DOMAIN          213..452
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT   ACT_SITE        253
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        302
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        404
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   BINDING         398
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   SITE            113
FT                   /note="Important for S-112 for O-xylosylation"
FT   SITE            212..213
FT                   /note="Cleavage; by factor Xa, factor XIIa, factor IXa, or
FT                   thrombin"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         66
FT                   /note="4-carboxyglutamate"
FT                   /evidence="ECO:0000250|UniProtKB:P22457,
FT                   ECO:0000255|PROSITE-ProRule:PRU00463"
FT   MOD_RES         67
FT                   /note="4-carboxyglutamate"
FT                   /evidence="ECO:0000250|UniProtKB:P22457,
FT                   ECO:0000255|PROSITE-ProRule:PRU00463"
FT   MOD_RES         74
FT                   /note="4-carboxyglutamate"
FT                   /evidence="ECO:0000250|UniProtKB:P22457,
FT                   ECO:0000255|PROSITE-ProRule:PRU00463"
FT   MOD_RES         76
FT                   /note="4-carboxyglutamate"
FT                   /evidence="ECO:0000250|UniProtKB:P22457,
FT                   ECO:0000255|PROSITE-ProRule:PRU00463"
FT   MOD_RES         79
FT                   /note="4-carboxyglutamate"
FT                   /evidence="ECO:0000250|UniProtKB:P22457,
FT                   ECO:0000255|PROSITE-ProRule:PRU00463"
FT   MOD_RES         80
FT                   /note="4-carboxyglutamate"
FT                   /evidence="ECO:0000250|UniProtKB:P22457,
FT                   ECO:0000255|PROSITE-ProRule:PRU00463"
FT   MOD_RES         85
FT                   /note="4-carboxyglutamate"
FT                   /evidence="ECO:0000250|UniProtKB:P22457,
FT                   ECO:0000255|PROSITE-ProRule:PRU00463"
FT   MOD_RES         86
FT                   /note="4-carboxyglutamate"
FT                   /evidence="ECO:0000250|UniProtKB:P22457,
FT                   ECO:0000255|PROSITE-ProRule:PRU00463"
FT   MOD_RES         89
FT                   /note="4-carboxyglutamate"
FT                   /evidence="ECO:0000250|UniProtKB:P22457,
FT                   ECO:0000255|PROSITE-ProRule:PRU00463"
FT   MOD_RES         95
FT                   /note="4-carboxyglutamate"
FT                   /evidence="ECO:0000250|UniProtKB:P22457,
FT                   ECO:0000255|PROSITE-ProRule:PRU00463"
FT   MOD_RES         123
FT                   /note="(3R)-3-hydroxyaspartate"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        112
FT                   /note="O-linked (Glc...) serine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P08709"
FT   CARBOHYD        112
FT                   /note="O-linked (Xyl...) serine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P08709"
FT   CARBOHYD        120
FT                   /note="O-linked (Fuc) serine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        205
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        382
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        77..82
FT                   /evidence="ECO:0000250"
FT   DISULFID        110..121
FT                   /evidence="ECO:0000250"
FT   DISULFID        115..130
FT                   /evidence="ECO:0000250"
FT   DISULFID        132..141
FT                   /evidence="ECO:0000250"
FT   DISULFID        151..162
FT                   /evidence="ECO:0000250"
FT   DISULFID        158..172
FT                   /evidence="ECO:0000250"
FT   DISULFID        174..187
FT                   /evidence="ECO:0000250"
FT   DISULFID        195..322
FT                   /evidence="ECO:0000250"
FT   DISULFID        219..224
FT                   /evidence="ECO:0000250"
FT   DISULFID        238..254
FT                   /evidence="ECO:0000250"
FT   DISULFID        370..389
FT                   /evidence="ECO:0000250"
FT   DISULFID        400..428
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   466 AA;  51641 MW;  8F5D5B3B22B58C36 CRC64;
     MVSQALRLLC LLLGLQGCLA AGGVAEASGG ETRDXXWKPG PHRVFITQEE AHGVLHRRRR
     ANAFLEELRP GSLERECKEE QCSFEEAREI FKDLERTKLF WISYSDGDQC ASSPCQNGGS
     CKDQLQSYIC FCLPAFEGRN CETYKDDQLI CVNENGGCEQ YCSDHTGTKR SCRCHEGYSL
     LADGVSCTPT VEYPCGKIPI LEKRNASKPQ GRIVGGKVCP KGECPWQVLL LVNGAQLCGG
     TLINTIWVVS AAHCFDKIKN WRNLIAVLGE HDLSEHDGDE QSRRVAQVII PSTYIPGTTN
     HDIALLRLHQ PVVLTDHVVP LCLPERAFSE RTLAFVRFSL VSGWGQLLDR GATALELMVL
     NVPRLMTQDC LQQSRKVGDS PNITEYMFCA GYSDGSKDSC KGDSGGPHAT HYRGTWYLTG
     IVSWGQGCAS VGHFGVYTRV SQYIEWLQKL MRSEPRPGVL LRAPFP
 
 
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