FA7_RABIT
ID FA7_RABIT Reviewed; 444 AA.
AC P98139; P79224;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 2.
DT 03-AUG-2022, entry version 155.
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 Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=8383365; DOI=10.1016/0049-3848(93)90048-s;
RA Brothers A.B., Clarke B.J., Sheffield W.P., Blajchman M.A.;
RT "Complete nucleotide sequence of the cDNA encoding rabbit coagulation
RT factor VII.";
RL Thromb. Res. Suppl. 69:231-238(1993).
RN [2]
RP SEQUENCE REVISION TO 395.
RC TISSUE=Liver;
RA Ruiz S.R., Blajchman M.A., Clarke B.J.;
RL Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases.
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 -!- TISSUE SPECIFICITY: Plasma.
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-91 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; U77477; AAB37326.1; -; mRNA.
DR PIR; I46932; I46932.
DR RefSeq; NP_001076148.1; NM_001082679.1.
DR AlphaFoldDB; P98139; -.
DR SMR; P98139; -.
DR STRING; 9986.ENSOCUP00000024648; -.
DR BindingDB; P98139; -.
DR ChEMBL; CHEMBL3351187; -.
DR GeneID; 100009399; -.
DR KEGG; ocu:100009399; -.
DR CTD; 2155; -.
DR eggNOG; ENOG502QRGI; Eukaryota.
DR InParanoid; P98139; -.
DR OrthoDB; 1314811at2759; -.
DR Proteomes; UP000001811; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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; IEA:UniProtKB-KW.
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 2: Evidence at transcript level;
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..21
FT /evidence="ECO:0000255"
FT PROPEP 22..39
FT /evidence="ECO:0000255"
FT /id="PRO_0000027735"
FT CHAIN 40..191
FT /note="Factor VII light chain"
FT /id="PRO_0000027736"
FT CHAIN 192..444
FT /note="Factor VII heavy chain"
FT /id="PRO_0000027737"
FT DOMAIN 40..84
FT /note="Gla"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00463"
FT DOMAIN 85..121
FT /note="EGF-like 1; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 126..167
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 192..431
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 232
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 281
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 383
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT BINDING 377
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 191..192
FT /note="Cleavage; by factor Xa, factor XIIa, factor IXa, or
FT thrombin"
FT /evidence="ECO:0000250"
FT MOD_RES 45
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000250|UniProtKB:P22457,
FT ECO:0000255|PROSITE-ProRule:PRU00463"
FT MOD_RES 46
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000250|UniProtKB:P22457,
FT ECO:0000255|PROSITE-ProRule:PRU00463"
FT MOD_RES 53
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000250|UniProtKB:P22457,
FT ECO:0000255|PROSITE-ProRule:PRU00463"
FT MOD_RES 55
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000250|UniProtKB:P22457,
FT ECO:0000255|PROSITE-ProRule:PRU00463"
FT MOD_RES 58
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000250|UniProtKB:P22457,
FT ECO:0000255|PROSITE-ProRule:PRU00463"
FT MOD_RES 59
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000250|UniProtKB:P22457,
FT ECO:0000255|PROSITE-ProRule:PRU00463"
FT MOD_RES 64
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000250|UniProtKB:P22457,
FT ECO:0000255|PROSITE-ProRule:PRU00463"
FT MOD_RES 65
FT /note="4-carboxyglutamate"
FT /evidence="ECO:0000250|UniProtKB:P22457,
FT ECO:0000255|PROSITE-ProRule:PRU00463"
FT MOD_RES 68
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 102
FT /note="(3R)-3-hydroxyaspartate"
FT /evidence="ECO:0000250"
FT CARBOHYD 91
FT /note="O-linked (Glc...) serine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P08709"
FT CARBOHYD 91
FT /note="O-linked (Xyl...) serine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P08709"
FT CARBOHYD 99
FT /note="O-linked (Fuc) serine"
FT /evidence="ECO:0000250"
FT CARBOHYD 211
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 242
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 306
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 56..61
FT /evidence="ECO:0000250"
FT DISULFID 89..100
FT /evidence="ECO:0000250"
FT DISULFID 94..109
FT /evidence="ECO:0000250"
FT DISULFID 111..120
FT /evidence="ECO:0000250"
FT DISULFID 130..141
FT /evidence="ECO:0000250"
FT DISULFID 137..151
FT /evidence="ECO:0000250"
FT DISULFID 153..166
FT /evidence="ECO:0000250"
FT DISULFID 174..301
FT /evidence="ECO:0000250"
FT DISULFID 198..203
FT /evidence="ECO:0000250"
FT DISULFID 217..233
FT /evidence="ECO:0000250"
FT DISULFID 349..368
FT /evidence="ECO:0000250"
FT DISULFID 379..407
FT /evidence="ECO:0000250"
SQ SEQUENCE 444 AA; 49011 MW; 0481ABC4FE5427F8 CRC64;
MAPQARGLGL CSLLALQASL AAVFITQEEA HSVLRRQRRA NSFLEELRPG SLERECKEEL
CSFEEAREVF QSTERTKQFW ITYNDGDQCA SNPCQNGGSC EDQIQSYICF CLADFEGRNC
EKNKNDQLIC MYENGGCEQY CSDHVGSQRS CRCHEGYTLL PNGVSCTPTV DYPCGKVPAL
EKRGASNPQG RIVGGKVCPK GECPWQAALM NGSTLLCGGS LLDTHWVVSA AHCFDKLSSL
RNLTIVLGEH DLSEHEGDEQ VRHVAQLIMP DKYVPGKTDH DIALLRLLQP AALTNNVVPL
CLPERNFSES TLATIRFSRV SGWGQLLYRG ALARELMAID VPRLMTQDCV EQSEHKPGSP
EVTGNMFCAG YLDGSKDACK GDSGGPHATS YHGTWYLTGV VSWGEGCAAV GHVGVYTRVS
RYTEWLSRLM RSKLHHGIQR HPFP
