[1]	NUCLEOTIDE SEQUENCE [MRNA]. TISSUE=Liver; PubMed=8701412 [NCBI, ExPASy, EBI, Israel, Japan] Idusogie E., Rosen E., Geng J.P., Carmeliet P., Collen D., Castellino F.J.; "Characterization of a cDNA encoding murine coagulation factor VII."; Thromb. Haemost. 75:481-487(1996).
[2]	NUCLEOTIDE SEQUENCE. PubMed=8972017 [NCBI, ExPASy, EBI, Israel, Japan] Idusogie E., Rosen E.D., Carmeliet P., Collen D., Castellino F.J.; "Nucleotide structure and characterization of the murine blood coagulation factor VII gene."; Thromb. Haemost. 76:957-964(1996).
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. TISSUE=Liver; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).

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.
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

U44795; AAC52570.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U66079; AAC33796.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC061149; AAH61149.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_034302.1; -.

UniGene

Mm.4827

3D structure databases

HSSP

P08709; 1BF9. [HSSP ENTRY / PDB]

SMR

P70375; 48-183.

ModBase

P70375.

Protein family/group databases

MEROPS

S01.215; -.

PTM databases

PhosphoSite

P70375; -.

Organism-specific databases

MGI

MGI:109325; F7.

Gene expression databases

ArrayExpress

P70375; -.

CleanEx

MM_F7; -.

GermOnline

ENSMUSG00000031443; Mus musculus.

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 mutant phenotype from MGI).
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).

Proteomics databases

PRIDE

P70375; -.

Genome annotation databases

Ensembl

ENSMUSG00000031443; Mus musculus. [Contig view]

GeneID

14068; -.

KEGG

mmu:14068; -.

Phylogenomic databases

HOGENOM

P70375; -.

HOVERGEN

P70375; -.

Other

285056; -.

F7; Mus musculus.

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_0000027732`
`CHAIN`	`42 193`	`152`	`Factor VII light chain.`	`PRO_0000027733`
`CHAIN`	`194 446`	`253`	`Factor VII heavy chain.`	`PRO_0000027734`
`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.`
`MOD_RES`	`48 48`		`4-carboxyglutamate.`
`MOD_RES`	`55 55`		`4-carboxyglutamate.`
`MOD_RES`	`57 57`		`4-carboxyglutamate.`
`MOD_RES`	`60 60`		`4-carboxyglutamate.`
`MOD_RES`	`61 61`		`4-carboxyglutamate.`
`MOD_RES`	`66 66`		`4-carboxyglutamate.`
`MOD_RES`	`67 67`		`4-carboxyglutamate.`
`MOD_RES`	`70 70`		`4-carboxyglutamate.`
`MOD_RES`	`76 76`		`4-carboxyglutamate.`
`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.`
`CONFLICT`	`99 99`		`G -> V (in Ref. 2; AAC52570).`

Sequence information

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

Molecular weight: 50276 Da [This is the MW of the unprocessed precursor]

CRC64: 2512E44A45CBC96E [This is a checksum on the sequence]

        10         20         30         40         50         60 
MVPQAHGLLL LCFLLQLQGP LGTAVFITQE EAHGVLHRQR RANSLLEELW PGSLERECNE 

        70         80         90        100        110        120 
EQCSFEEARE IFKSPERTKQ FWIVYSDGDQ CASNPCQNGG TCQDHLKSYV CFCLLDFEGR 

       130        140        150        160        170        180 
NCEKSKNEQL ICANENGDCD QYCRDHVGTK RTCSCHEDYT LQPDEVSCKP KVEYPCGRIP 

       190        200        210        220        230        240 
VVEKRNSSSR QGRIVGGNVC PKGECPWQAV LKINGLLLCG AVLLDARWIV TAAHCFDNIR 

       250        260        270        280        290        300 
YWGNITVVMG EHDFSEKDGD EQVRRVTQVI MPDKYIRGKI NHDIALLRLH RPVTFTDYVV 

       310        320        330        340        350        360 
PLCLPEKSFS ENTLARIRFS RVSGWGQLLD RGATALELMS IEVPRLMTQD CLEHAKHSSN 

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

       430        440 
VSQYIDWLVR HMDSKLQVGV FRLPLL

P70375 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	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