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Coagulation factor VII (EC 3.4.21.21) (Serum prothrombin conversion accelerator) [Cleaved into: Factor VII light chain; Factor VII heavy chain]

 FA7_RABIT               Reviewed;         444 AA.
P98139; P79224;
01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
15-JUL-1998, sequence version 2.
25-OCT-2017, entry version 141.
RecName: Full=Coagulation factor VII;
EC=3.4.21.21;
AltName: Full=Serum prothrombin conversion accelerator;
Contains:
RecName: Full=Factor VII light chain;
Contains:
RecName: Full=Factor VII heavy chain;
Flags: Precursor;
Name=F7;
Oryctolagus cuniculus (Rabbit).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae;
Oryctolagus.
NCBI_TaxID=9986;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Liver;
PubMed=8383365; DOI=10.1016/0049-3848(93)90048-S;
Brothers A.B., Clarke B.J., Sheffield W.P., Blajchman M.A.;
"Complete nucleotide sequence of the cDNA encoding rabbit coagulation
factor VII.";
Thromb. Res. Suppl. 69:231-238(1993).
[2]
SEQUENCE REVISION TO 395.
TISSUE=Liver;
Ruiz S.R., Blajchman M.A., Clarke B.J.;
Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Initiates the extrinsic pathway of blood coagulation.
Serine protease that circulates in the blood in a zymogen form.
Factor VII is converted to factor VIIa by factor Xa, factor XIIa,
factor IXa, or thrombin by minor proteolysis. In the presence of
tissue factor and calcium ions, factor VIIa then converts factor X
to factor Xa by limited proteolysis. Factor VIIa will also convert
factor IX to factor IXa in the presence of tissue factor and
calcium (By similarity). {ECO:0000250}.
-!- CATALYTIC ACTIVITY: Selective cleavage of Arg-|-Ile bond in factor
X to form factor Xa.
-!- SUBUNIT: Heterodimer of a light chain and a heavy chain linked by
a disulfide bond. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
-!- TISSUE SPECIFICITY: Plasma.
-!- PTM: The vitamin K-dependent, enzymatic carboxylation of some
glutamate residues allows the modified protein to bind calcium.
{ECO:0000250}.
-!- PTM: The iron and 2-oxoglutarate dependent 3-hydroxylation of
aspartate and asparagine is (R) stereospecific within EGF domains.
{ECO:0000250}.
-!- PTM: O-glycosylated. O-fucosylated by POFUT1 on a conserved serine
or threonine residue found in the consensus sequence C2-X(4,5)-
[S/T]-C3 of EGF domains, where C2 and C3 are the second and third
conserved cysteines. {ECO:0000250}.
-!- PTM: Can be either O-glucosylated or O-xylosylated at Ser-91 by
POGLUT1. {ECO:0000250}.
-!- SIMILARITY: Belongs to the peptidase S1 family.
{ECO:0000255|PROSITE-ProRule:PRU00274}.
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EMBL; U77477; AAB37326.1; -; mRNA.
PIR; I46932; I46932.
RefSeq; NP_001076148.1; NM_001082679.1.
UniGene; Ocu.2617; -.
ProteinModelPortal; P98139; -.
SMR; P98139; -.
STRING; 9986.ENSOCUP00000024648; -.
BindingDB; P98139; -.
ChEMBL; CHEMBL3351187; -.
GeneID; 100009399; -.
KEGG; ocu:100009399; -.
CTD; 2155; -.
eggNOG; ENOG410IIMB; Eukaryota.
eggNOG; COG5640; LUCA.
HOGENOM; HOG000251821; -.
HOVERGEN; HBG013304; -.
InParanoid; P98139; -.
KO; K01320; -.
Proteomes; UP000001811; Unplaced.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
GO; GO:0007596; P:blood coagulation; IEA:UniProtKB-KW.
CDD; cd00190; Tryp_SPc; 1.
Gene3D; 4.10.740.10; -; 1.
InterPro; IPR017857; Coagulation_fac_subgr_Gla_dom.
InterPro; IPR001881; EGF-like_Ca-bd_dom.
InterPro; IPR013032; EGF-like_CS.
InterPro; IPR000742; EGF-like_dom.
InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
InterPro; IPR018097; EGF_Ca-bd_CS.
InterPro; IPR033190; F7.
InterPro; IPR035972; GLA-like_dom_SF.
InterPro; IPR000294; GLA_domain.
InterPro; IPR012224; Pept_S1A_FX.
InterPro; IPR009003; Peptidase_S1_PA.
InterPro; IPR001314; Peptidase_S1A.
InterPro; IPR001254; Trypsin_dom.
InterPro; IPR018114; TRYPSIN_HIS.
InterPro; IPR033116; TRYPSIN_SER.
PANTHER; PTHR44064:SF1; PTHR44064:SF1; 1.
Pfam; PF00008; EGF; 1.
Pfam; PF00594; Gla; 1.
Pfam; PF00089; Trypsin; 1.
PIRSF; PIRSF001143; Factor_X; 1.
PRINTS; PR00722; CHYMOTRYPSIN.
PRINTS; PR00001; GLABLOOD.
SMART; SM00181; EGF; 2.
SMART; SM00179; EGF_CA; 1.
SMART; SM00069; GLA; 1.
SMART; SM00020; Tryp_SPc; 1.
SUPFAM; SSF50494; SSF50494; 1.
SUPFAM; SSF57630; SSF57630; 1.
PROSITE; PS00010; ASX_HYDROXYL; 1.
PROSITE; PS00022; EGF_1; 1.
PROSITE; PS01186; EGF_2; 1.
PROSITE; PS50026; EGF_3; 1.
PROSITE; PS01187; EGF_CA; 1.
PROSITE; PS00011; GLA_1; 1.
PROSITE; PS50998; GLA_2; 1.
PROSITE; PS50240; TRYPSIN_DOM; 1.
PROSITE; PS00134; TRYPSIN_HIS; 1.
PROSITE; PS00135; TRYPSIN_SER; 1.
2: Evidence at transcript level;
Blood coagulation; Calcium; Cleavage on pair of basic residues;
Complete proteome; Disulfide bond; EGF-like domain;
Gamma-carboxyglutamic acid; Glycoprotein; Hemostasis; Hydrolase;
Hydroxylation; Protease; Reference proteome; Repeat; Secreted;
Serine protease; Signal; Zymogen.
SIGNAL 1 21 {ECO:0000255}.
PROPEP 22 39 {ECO:0000255}.
/FTId=PRO_0000027735.
CHAIN 40 191 Factor VII light chain.
/FTId=PRO_0000027736.
CHAIN 192 444 Factor VII heavy chain.
/FTId=PRO_0000027737.
DOMAIN 40 84 Gla. {ECO:0000255|PROSITE-
ProRule:PRU00463}.
DOMAIN 85 121 EGF-like 1; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 126 167 EGF-like 2. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 192 431 Peptidase S1. {ECO:0000255|PROSITE-
ProRule:PRU00274}.
ACT_SITE 232 232 Charge relay system. {ECO:0000250}.
ACT_SITE 281 281 Charge relay system. {ECO:0000250}.
ACT_SITE 383 383 Charge relay system. {ECO:0000250}.
BINDING 377 377 Substrate. {ECO:0000250}.
SITE 191 192 Cleavage; by factor Xa, factor XIIa,
factor IXa, or thrombin. {ECO:0000250}.
MOD_RES 45 45 4-carboxyglutamate.
{ECO:0000250|UniProtKB:P22457,
ECO:0000255|PROSITE-ProRule:PRU00463}.
MOD_RES 46 46 4-carboxyglutamate.
{ECO:0000250|UniProtKB:P22457,
ECO:0000255|PROSITE-ProRule:PRU00463}.
MOD_RES 53 53 4-carboxyglutamate.
{ECO:0000250|UniProtKB:P22457,
ECO:0000255|PROSITE-ProRule:PRU00463}.
MOD_RES 55 55 4-carboxyglutamate.
{ECO:0000250|UniProtKB:P22457,
ECO:0000255|PROSITE-ProRule:PRU00463}.
MOD_RES 58 58 4-carboxyglutamate.
{ECO:0000250|UniProtKB:P22457,
ECO:0000255|PROSITE-ProRule:PRU00463}.
MOD_RES 59 59 4-carboxyglutamate.
{ECO:0000250|UniProtKB:P22457,
ECO:0000255|PROSITE-ProRule:PRU00463}.
MOD_RES 64 64 4-carboxyglutamate.
{ECO:0000250|UniProtKB:P22457,
ECO:0000255|PROSITE-ProRule:PRU00463}.
MOD_RES 65 65 4-carboxyglutamate.
{ECO:0000250|UniProtKB:P22457,
ECO:0000255|PROSITE-ProRule:PRU00463}.
MOD_RES 68 68 4-carboxyglutamate.
{ECO:0000250|UniProtKB:P22457,
ECO:0000255|PROSITE-ProRule:PRU00463}.
MOD_RES 74 74 4-carboxyglutamate.
{ECO:0000250|UniProtKB:P22457,
ECO:0000255|PROSITE-ProRule:PRU00463}.
MOD_RES 102 102 (3R)-3-hydroxyaspartate. {ECO:0000250}.
CARBOHYD 91 91 O-linked (Glc...) serine; alternate.
{ECO:0000250}.
CARBOHYD 91 91 O-linked (Xyl...) serine; alternate.
{ECO:0000250}.
CARBOHYD 99 99 O-linked (Fuc) serine. {ECO:0000250}.
CARBOHYD 211 211 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 242 242 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 306 306 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 56 61 {ECO:0000250}.
DISULFID 89 100 {ECO:0000250}.
DISULFID 94 109 {ECO:0000250}.
DISULFID 111 120 {ECO:0000250}.
DISULFID 130 141 {ECO:0000250}.
DISULFID 137 151 {ECO:0000250}.
DISULFID 153 166 {ECO:0000250}.
DISULFID 174 301 {ECO:0000250}.
DISULFID 198 203 {ECO:0000250}.
DISULFID 217 233 {ECO:0000250}.
DISULFID 349 368 {ECO:0000250}.
DISULFID 379 407 {ECO:0000250}.
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


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