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P70375 (FA7_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 143. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Coagulation factor VII

EC=3.4.21.21
Alternative name(s):
Serum prothrombin conversion accelerator

Cleaved into the following 2 chains:

  1. Factor VII light chain
  2. Factor VII heavy chain
Gene names
Name:F7
Synonyms:Cf7
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length446 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (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 structure

Heterodimer of a light chain and a heavy chain linked by a disulfide bond By similarity.

Subcellular location

Secreted.

Tissue specificity

Plasma.

Post-translational modification

The vitamin K-dependent, enzymatic carboxylation of some glutamate residues allows the modified protein to bind calcium By similarity.

The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate and asparagine is (R) stereospecific within EGF domains By similarity.

Sequence similarities

Belongs to the peptidase S1 family.

Contains 2 EGF-like domains.

Contains 1 Gla (gamma-carboxy-glutamate) domain.

Contains 1 peptidase S1 domain.

Ontologies

Keywords
   Biological processBlood coagulation
Hemostasis
   Cellular componentSecreted
   DomainEGF-like domain
Repeat
Signal
   LigandCalcium
   Molecular functionHydrolase
Protease
Serine protease
   PTMCleavage on pair of basic residues
Disulfide bond
Gamma-carboxyglutamic acid
Glycoprotein
Hydroxylation
Zymogen
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processblood coagulation

Inferred from mutant phenotype PubMed 9384381. Source: MGI

circadian rhythm

Inferred from electronic annotation. Source: Ensembl

organ regeneration

Inferred from electronic annotation. Source: Ensembl

positive regulation of blood coagulation

Inferred from electronic annotation. Source: Ensembl

positive regulation of leukocyte chemotaxis

Inferred from electronic annotation. Source: Ensembl

positive regulation of platelet-derived growth factor receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

positive regulation of positive chemotaxis

Inferred from electronic annotation. Source: Ensembl

positive regulation of protein kinase B signaling

Inferred from electronic annotation. Source: Ensembl

proteolysis

Inferred from electronic annotation. Source: UniProtKB-KW

response to estrogen

Inferred from electronic annotation. Source: Ensembl

response to growth hormone

Inferred from electronic annotation. Source: Ensembl

response to vitamin K

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentextracellular region

Traceable author statement. Source: Reactome

extracellular space

Inferred from electronic annotation. Source: Ensembl

vesicle

Inferred from electronic annotation. Source: Ensembl

   Molecular_functioncalcium ion binding

Inferred from electronic annotation. Source: InterPro

serine-type endopeptidase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2424 Potential
Propeptide25 – 4117 Potential
PRO_0000027732
Chain42 – 193152Factor VII light chain
PRO_0000027733
Chain194 – 446253Factor VII heavy chain
PRO_0000027734

Regions

Domain42 – 8645Gla
Domain87 – 12337EGF-like 1; calcium-binding Potential
Domain128 – 16942EGF-like 2
Domain194 – 433240Peptidase S1

Sites

Active site2341Charge relay system By similarity
Active site2831Charge relay system By similarity
Active site3851Charge relay system By similarity
Binding site3791Substrate By similarity
Site193 – 1942Cleavage; by factor Xa, factor XIIa, factor IXa, or thrombin By similarity

Amino acid modifications

Modified residue4714-carboxyglutamate
Modified residue4814-carboxyglutamate
Modified residue5514-carboxyglutamate
Modified residue5714-carboxyglutamate
Modified residue6014-carboxyglutamate
Modified residue6114-carboxyglutamate
Modified residue6614-carboxyglutamate
Modified residue6714-carboxyglutamate
Modified residue7014-carboxyglutamate
Modified residue7614-carboxyglutamate
Modified residue1041(3R)-3-hydroxyaspartate By similarity
Glycosylation1861N-linked (GlcNAc...) Potential
Glycosylation2441N-linked (GlcNAc...) Potential
Disulfide bond58 ↔ 63 By similarity
Disulfide bond91 ↔ 102 By similarity
Disulfide bond96 ↔ 111 By similarity
Disulfide bond113 ↔ 122 By similarity
Disulfide bond132 ↔ 143 By similarity
Disulfide bond139 ↔ 153 By similarity
Disulfide bond155 ↔ 168 By similarity
Disulfide bond176 ↔ 303 By similarity
Disulfide bond200 ↔ 205 By similarity
Disulfide bond219 ↔ 235 By similarity
Disulfide bond351 ↔ 370 By similarity
Disulfide bond381 ↔ 409 By similarity

Experimental info

Sequence conflict991G → V in AAC52570. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P70375 [UniParc].

Last modified February 1, 1997. Version 1.
Checksum: 2512E44A45CBC96E

FASTA44650,276
        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 

« Hide

References

« Hide 'large scale' references
[1]"Characterization of a cDNA encoding murine coagulation factor VII."
Idusogie E., Rosen E., Geng J.P., Carmeliet P., Collen D., Castellino F.J.
Thromb. Haemost. 75:481-487(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Liver.
[2]"Nucleotide structure and characterization of the murine blood coagulation factor VII gene."
Idusogie E., Rosen E.D., Carmeliet P., Collen D., Castellino F.J.
Thromb. Haemost. 76:957-964(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U44795 mRNA. Translation: AAC52570.1.
U66079 Genomic DNA. Translation: AAC33796.1.
BC061149 mRNA. Translation: AAH61149.1.
RefSeqNP_034302.2. NM_010172.3.
UniGeneMm.4827.

3D structure databases

ProteinModelPortalP70375.
SMRP70375. Positions 49-184, 194-445.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

MEROPSS01.215.

Proteomic databases

PaxDbP70375.
PRIDEP70375.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000033820; ENSMUSP00000033820; ENSMUSG00000031443.
GeneID14068.
KEGGmmu:14068.
UCSCuc009kwr.2. mouse.

Organism-specific databases

CTD2155.
MGIMGI:109325. F7.

Phylogenomic databases

eggNOGCOG5640.
HOGENOMHOG000251821.
HOVERGENHBG013304.
InParanoidP70375.
KOK01320.
OMAGCEQYCS.
OrthoDBEOG75B84T.
TreeFamTF327329.

Enzyme and pathway databases

ReactomeREACT_109335. Circadian Clock.
REACT_24972. Circadian Clock.

Gene expression databases

ArrayExpressP70375.
BgeeP70375.
CleanExMM_F7.
GenevestigatorP70375.

Family and domain databases

Gene3D4.10.740.10. 1 hit.
InterProIPR017857. Coagulation_fac_subgr_Gla_dom.
IPR000742. EG-like_dom.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR000294. GLA_domain.
IPR012224. Pept_S1A_FX.
IPR001254. Peptidase_S1.
IPR018114. Peptidase_S1_AS.
IPR001314. Peptidase_S1A.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view]
PfamPF00008. EGF. 1 hit.
PF00594. Gla. 1 hit.
PF00089. Trypsin. 1 hit.
[Graphical view]
PIRSFPIRSF001143. Factor_X. 1 hit.
PRINTSPR00722. CHYMOTRYPSIN.
PR00001. GLABLOOD.
SMARTSM00181. EGF. 1 hit.
SM00179. EGF_CA. 1 hit.
SM00069. GLA. 1 hit.
SM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMSSF50494. SSF50494. 1 hit.
SSF57630. SSF57630. 1 hit.
PROSITEPS00010. ASX_HYDROXYL. 1 hit.
PS00022. EGF_1. 1 hit.
PS50026. EGF_3. 1 hit.
PS01187. EGF_CA. 1 hit.
PS00011. GLA_1. 1 hit.
PS50998. GLA_2. 1 hit.
PS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio285056.
PROP70375.
SOURCESearch...

Entry information

Entry nameFA7_MOUSE
AccessionPrimary (citable) accession number: P70375
Secondary accession number(s): Q61109
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: February 1, 1997
Last modified: February 19, 2014
This is version 143 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot