Coagulation factor VII precursor - Mus musculus (Mouse)

Contribute

Send feedback

Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot P70375 (FA7_MOUSE)

Last modified June 16, 2009. Version 96. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data |

Customize display

text xml rdf/xml gff fasta

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Hide | Top

Names and origin

Protein names

Recommended name:
    Coagulation factor VII
    EC=3.4.21.21
Alternative name(s):
    Serum prothrombin conversion accelerator
Cleaved into the following 2 chains:
    1- Recommended name:
            Factor VII light chain
    2- Recommended name:
            Factor VII heavy chain

Gene names

Name:	F7
Synonyms:	Cf7

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Hide | Top

Protein attributes

Sequence length	446 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

Hide | Top

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.

Hide | Top

Ontologies

Keywords
Biological process	Blood coagulation
Cellular component	Secreted
Domain	EGF-like domain Repeat Signal
Ligand	Calcium
Molecular function	Hydrolase Protease Serine protease
PTM	Cleavage on pair of basic residues Disulfide bond Gamma-carboxyglutamic acid Glycoprotein Hydroxylation Zymogen
Gene Ontology (GO)
Biological process	blood coagulation Inferred from mutant phenotype. Source: MGI proteolysis Inferred from electronic annotation. Source: InterPro
Cellular component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	calcium ion binding Inferred from electronic annotation. Source: UniProtKB-KW serine-type endopeptidase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Hide | Top

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 24

Potential

Propeptide

25 – 41

Potential

PRO_0000027732

Chain

42 – 193

152

Factor VII light chain

PRO_0000027733

Chain

194 – 446

253

Factor VII heavy chain

PRO_0000027734

Regions

Domain

42 – 86

Gla

Domain

87 – 123

EGF-like 1; calcium-binding Potential

Domain

128 – 169

EGF-like 2

Domain

194 – 433

240

Peptidase S1

Sites

Active site

234

Charge relay system By similarity

Active site

283

Charge relay system By similarity

Active site

385

Charge relay system By similarity

Binding site

379

Substrate By similarity

Site

193 – 194

Cleavage; by factor Xa, factor XIIa, factor IXa, or thrombin By similarity

Amino acid modifications

Modified residue

4-carboxyglutamate

Modified residue

4-carboxyglutamate

Modified residue

4-carboxyglutamate

Modified residue

4-carboxyglutamate

Modified residue

4-carboxyglutamate

Modified residue

4-carboxyglutamate

Modified residue

4-carboxyglutamate

Modified residue

4-carboxyglutamate

Modified residue

4-carboxyglutamate

Modified residue

4-carboxyglutamate

Modified residue

104

(3R)-3-hydroxyaspartate By similarity

Glycosylation

186

N-linked (GlcNAc...) Potential

Glycosylation

244

N-linked (GlcNAc...) Potential

Disulfide bond

58 ↔ 63

By similarity

Disulfide bond

91 ↔ 102

By similarity

Disulfide bond

96 ↔ 111

By similarity

Disulfide bond

113 ↔ 122

By similarity

Disulfide bond

132 ↔ 143

By similarity

Disulfide bond

139 ↔ 153

By similarity

Disulfide bond

155 ↔ 168

By similarity

Disulfide bond

176 ↔ 303

By similarity

Disulfide bond

200 ↔ 205

By similarity

Disulfide bond

219 ↔ 235

By similarity

Disulfide bond

351 ↔ 370

By similarity

Disulfide bond

381 ↔ 409

By similarity

Experimental info

Sequence conflict

G → V in AAC52570. Ref.2

Hide | Top

Sequences

Sequence

Length

Mass (Da)

Tools

P70375-1 [UniParc].

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

FASTA

446

50,276

        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

Hide | Top

References

	« Hide 'large scale' referencesShow '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: 8701412] [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: 8972017] [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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Liver.
+	Additional computationally mapped references.

Hide | Top

Cross-references

Sequence databases
	U44795 mRNA. Translation: AAC52570.1. U66079 Genomic DNA. Translation: AAC33796.1. BC061149 mRNA. Translation: AAH61149.1.
IPI	IPI00307890.
RefSeq	NP_034302.2.
UniGene	Mm.4827
3D structure databases
HSSP	HSSP built from PDB template 1BF9 based on UniProtKB P08709.
SMR	P70375. Positions 48-183.
ModBase	Search...
Protein family/group databases
MEROPS	S01.215.
Proteomic databases
PRIDE	P70375.
Genome annotation databases
Ensembl	ENSMUSG00000031443. Mus musculus. [Contig view]
GeneID	14068.
KEGG	mmu:14068.
Organism-specific databases
MGI	MGI:109325. F7.
Phylogenomic databases
HOGENOM	P70375.
HOVERGEN	P70375.
OMA	P70375. DGDQCAS.
Enzyme and pathway databases
BRENDA	3.4.21.21. 244.
Gene expression databases
ArrayExpress	P70375.
Bgee	P70375.
CleanEx	MM_F7.
GermOnline	ENSMUSG00000031443. Mus musculus.
Family and domain databases
InterPro	IPR017857. Coagulation_fac_subset_Gla. IPR002383. Coagulation_factor_Gla. IPR006209. EGF. IPR006210. EGF-like. IPR013032. EGF-like_reg_CS. IPR000152. EGF-type_Asp/Asn_hydroxyl_CS. IPR001438. EGF_2. IPR000742. EGF_3. IPR001881. EGF_Ca_bd. IPR018097. EGF_Ca_bd_CS. IPR000294. GLA_domain. IPR012224. Pept_S1A_FX. IPR018114. Peptidase_S1/S6_AS. IPR001254. Peptidase_S1_S6. IPR001314. Peptidase_S1A. [Graphical view]
Gene3D	G3DSA:4.10.740.10. Coagulation_factor_Gla. 1 hit.
Pfam	PF00008. EGF. 1 hit. PF00594. Gla. 1 hit. PF00089. Trypsin. 1 hit. [Graphical view]
PIRSF	PIRSF001143. Factor_X. 1 hit.
PRINTS	PR00722. CHYMOTRYPSIN. PR00010. EGFBLOOD. PR00001. GLABLOOD.
SMART	SM00181. EGF. 1 hit. SM00179. EGF_CA. 1 hit. SM00069. GLA. 1 hit. SM00020. Tryp_SPc. 1 hit. [Graphical view]
PROSITE	PS00010. ASX_HYDROXYL. 1 hit. PS00022. EGF_1. 1 hit. PS01186. EGF_2. False negative. 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]
ProtoNet	Search...
Other Resources
NextBio	285056.
SOURCE	Search...

Hide | Top

Entry information

Entry name

FA7_MOUSE

Accession

Primary (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:	June 16, 2009
This is version 96 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Hide | Top

Relevant documents

MGD cross-references

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

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein family/group databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents