[1]	NUCLEOTIDE SEQUENCE [MRNA]. STRAIN=Sprague-Dawley; Murphy K., Ramaker M.; "Nucleotide sequence of the cDNA encoding rat coagulation factor VII."; Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.

Comments

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).
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 (By similarity).
SUBCELLULAR LOCATION: Secreted (By similarity).
TISSUE SPECIFICITY: Plasma.
PTM: The vitamin K-dependent, enzymatic carboxylation of some glutamate residues allows the modified protein to bind calcium (By similarity).
SIMILARITY: Belongs to the peptidase S1 family [view classification].
SIMILARITY: Contains 2 EGF-like domains.
SIMILARITY: Contains 1 Gla (gamma-carboxy-glutamate) domain.
SIMILARITY: Contains 1 peptidase S1 domain [view classification].

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AF532184; AAM95967.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_690059.1; -.

UniGene

Rn.86416

3D structure databases

HSSP

P08709; 1KLJ. [HSSP ENTRY / PDB]

ModBase

Q8K3U6.

Protein family/group databases

MEROPS

S01.215; -.

Organism-specific databases

RGD

628678; F7.

Ontologies

GO:0005576;	Cellular component: extracellular region (inferred from electronic annotation from InterPro).
GO:0005509;	Molecular function: calcium ion binding (inferred from electronic annotation from InterPro).
GO:0004252;	Molecular function: serine-type endopeptidase activity (inferred from electronic annotation from InterPro).
GO:0007596;	Biological process: blood coagulation (inferred from electronic annotation from InterPro).
GO:0006508;	Biological process: proteolysis (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

InterPro

IPR017857; Coagulation_fac_subset_Gla.
IPR002383; Coagulation_factor_Gla.
IPR006210; EGF.
IPR000152; EGF-type_Asp/Asn_hydroxyl_CS.
IPR001438; EGF_2.
IPR000742; EGF_3.
IPR001881; EGF_Ca_bd.
IPR006209; EGF_like.
IPR013032; EGF_like_reg_CS.
IPR012224; Pept_S1A_FX.
IPR001254; Peptidase_S1_S6.
IPR001314; Peptidase_S1A.
IPR000294; VitK_dep_GLA.
Graphical view of domain structure.

Gene3D

G3DSA:4.10.740.10; Coagulation_factor_Gla; 1.

Pfam

PF00008; EGF; 1.
PF00594; Gla; 1.
PF00089; Trypsin; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF001143; Factor_X; 1.

PRINTS

PR00722; CHYMOTRYPSIN.
PR00010; EGFBLOOD.
PR00001; GLABLOOD.

SMART

SM00181; EGF; 1.
SM00179; EGF_CA; 1.
SM00069; GLA; 1.
SM00020; Tryp_SPc; 1.
SMART graphical view of domain structure.

PROSITE

PS00010; ASX_HYDROXYL; 1.
PS00022; EGF_1; 1.
PS01186; EGF_2; FALSE_NEG.
PS50026; EGF_3; 1.
PS01187; EGF_CA; 1.
PS00011; GLA_1; 1.
PS50998; GLA_2; 1.
PS50240; TRYPSIN_DOM; 1.
PS00134; TRYPSIN_HIS; 1.
PS00135; TRYPSIN_SER; 1.
PROSITE graphical view of domain structure (profiles).

Genome annotation databases

Ensembl

ENSRNOG00000032737; Rattus norvegicus. [Contig view]

GeneID

260320; -.

KEGG

rno:260320; -.

NMPDR

fig|10116.3.peg.12777; -.

Phylogenomic databases

HOVERGEN

Q8K3U6; -.

Other

624347; -.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Blood coagulation; Calcium; Cleavage on pair of basic residues; EGF-like domain; Gamma-carboxyglutamic acid; Glycoprotein; Hydrolase; Hydroxylation; Protease; Repeat; Secreted; Serine protease; Signal; Zymogen.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 24`	`24`	`Potential.`
`PROPEP`	`25 41`	`17`	`Potential.`	`PRO_0000027738`
`CHAIN`	`42 193`	`152`	`Factor VII light chain (By similarity).`	`PRO_0000027739`
`CHAIN`	`194 446`	`253`	`Factor VII heavy chain (By similarity).`	`PRO_0000027740`
`DOMAIN`	`42 86`	`45`	`Gla.`
`DOMAIN`	`87 123`	`37`	`EGF-like 1; calcium-binding (Potential).`
`DOMAIN`	`128 169`	`42`	`EGF-like 2.`
`DOMAIN`	`194 433`	`240`	`Peptidase S1.`
`ACT_SITE`	`234 234`		`Charge relay system (By similarity).`
`ACT_SITE`	`283 283`		`Charge relay system (By similarity).`
`ACT_SITE`	`385 385`		`Charge relay system (By similarity).`
`BINDING`	`379 379`		`Substrate (By similarity).`
`SITE`	`193 194`	`2`	`Cleavage; by factor Xa, factor XIIa, factor IXa, or thrombin (By similarity).`
`MOD_RES`	`47 47`		`4-carboxyglutamate (By similarity).`
`MOD_RES`	`48 48`		`4-carboxyglutamate (By similarity).`
`MOD_RES`	`55 55`		`4-carboxyglutamate (By similarity).`
`MOD_RES`	`57 57`		`4-carboxyglutamate (By similarity).`
`MOD_RES`	`60 60`		`4-carboxyglutamate (By similarity).`
`MOD_RES`	`61 61`		`4-carboxyglutamate (By similarity).`
`MOD_RES`	`66 66`		`4-carboxyglutamate (By similarity).`
`MOD_RES`	`67 67`		`4-carboxyglutamate (By similarity).`
`MOD_RES`	`70 70`		`4-carboxyglutamate (By similarity).`
`MOD_RES`	`76 76`		`4-carboxyglutamate (By similarity).`
`MOD_RES`	`104 104`		`3-hydroxyaspartate (By similarity).`
`CARBOHYD`	`186 186`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`244 244`		`N-linked (GlcNAc...) (Potential).`
`DISULFID`	`58 63`		`By similarity.`
`DISULFID`	`91 102`		`By similarity.`
`DISULFID`	`96 111`		`By similarity.`
`DISULFID`	`113 122`		`By similarity.`
`DISULFID`	`132 143`		`By similarity.`
`DISULFID`	`139 153`		`By similarity.`
`DISULFID`	`155 168`		`By similarity.`
`DISULFID`	`176 303`		`By similarity.`
`DISULFID`	`200 205`		`By similarity.`
`DISULFID`	`219 235`		`By similarity.`
`DISULFID`	`351 370`		`By similarity.`
`DISULFID`	`381 409`		`By similarity.`

Sequence information

Length: 446 AA [This is the length of the unprocessed precursor]

Molecular weight: 50399 Da [This is the MW of the unprocessed precursor]

CRC64: 292985EBF119C0AA [This is a checksum on the sequence]

        10         20         30         40         50         60 
MVPQTHGLLL LYFLLQLQGP LGAVVFITQE EAHGVLHRQR RANSLLEELW SSSLERECNE 

        70         80         90        100        110        120 
ERCSFEEARE IFKSPERTKQ FWTIYSDGDQ CASNPCQNGG TCQDHLKSYV CFCPLDFEGR 

       130        140        150        160        170        180 
NCEKNKNEQL ICANENGDCD QYCRDHVGTK RTCSCHEDYV LQPDEVSCKP KVEYPCGRIP 

       190        200        210        220        230        240 
VVEKRNFSRP QGRIVGGYVC PKGECPWQAV LKFNEALLCG AVLLDTRWIV TAAHCFDKFG 

       250        260        270        280        290        300 
KLVNITVVLG EHDFSEKEGT EQVRLVEQVI MPNKYTRGRT DHDIALVRLH RPVTFTDYVV 

       310        320        330        340        350        360 
PLCLPERAFS ENTLASIRFS RVSGWGQLLD RGATALELMV IEVPRLMTQD CLEHAKHSAN 

       370        380        390        400        410        420 
TPRITENMFC AGYMDGTKDA CKGDSGGPHA THYHGTWYLT GVVSWGEGCA AIGHIGVYTR 

       430        440 
VSQYIDWLVK YMDSKLRVGI SRVSLL

Q8K3U6 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools