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Q8K3U6 (FA7_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 83. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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
OrganismRattus norvegicus (Rat)
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length446 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript 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 By similarity.

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2424 Potential
Propeptide25 – 4117 Potential
PRO_0000027738
Chain42 – 193152Factor VII light chain By similarity
PRO_0000027739
Chain194 – 446253Factor VII heavy chain By similarity
PRO_0000027740

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 By similarity
Modified residue4814-carboxyglutamate By similarity
Modified residue5514-carboxyglutamate By similarity
Modified residue5714-carboxyglutamate By similarity
Modified residue6014-carboxyglutamate By similarity
Modified residue6114-carboxyglutamate By similarity
Modified residue6614-carboxyglutamate By similarity
Modified residue6714-carboxyglutamate By similarity
Modified residue7014-carboxyglutamate By similarity
Modified residue7614-carboxyglutamate By similarity
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

Sequences

Sequence LengthMass (Da)Tools
Q8K3U6 [UniParc].

Last modified October 1, 2002. Version 1.
Checksum: 292985EBF119C0AA

FASTA44650,399
        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

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References

[1]"Nucleotide sequence of the cDNA encoding rat coagulation factor VII."
Murphy K., Ramaker M.
Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Sprague-Dawley.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF532184 mRNA. Translation: AAM95967.1.
IPIIPI00202610.
RefSeqNP_690059.1. NM_152846.1.
UniGeneRn.86416.

3D structure databases

ProteinModelPortalQ8K3U6.
SMRQ8K3U6. Positions 61-183, 194-440.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ8K3U6.

Protein family/group databases

MEROPSS01.215.

Proteomic databases

PRIDEQ8K3U6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000037806; ENSRNOP00000038466; ENSRNOG00000032737.
GeneID260320.
KEGGrno:260320.
NMPDRfig|10116.3.peg.12777.
UCSCNM_152846. rat.

Organism-specific databases

CTD2155.
RGD628678. F7.

Phylogenomic databases

eggNOGroNOG14960.
GeneTreeENSGT00560000076714.
HOVERGENHBG013304.
InParanoidQ8K3U6.
OMAGHFGVYT.
OrthoDBEOG4HX51H.
PhylomeDBQ8K3U6.

Gene expression databases

GenevestigatorQ8K3U6.

Family and domain databases

InterProIPR017857. Coagulation_fac_subgr_Gla_dom.
IPR006209. EGF.
IPR006210. EGF-like.
IPR001881. EGF-like_Ca-bd.
IPR013032. EGF-like_reg_CS.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR000742. EGF_3.
IPR018097. EGF_Ca-bd_CS.
IPR000294. GLA_domain.
IPR009003. Pept_cys/ser_Trypsin-like.
IPR012224. Pept_S1A_FX.
IPR018114. Peptidase_S1/S6_AS.
IPR001254. Peptidase_S1_S6.
IPR001314. Peptidase_S1A.
[Graphical view]
Gene3DG3DSA:4.10.740.10. Coagulation_factor_Gla. 1 hit.
KOK01320.
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. Pept_Ser_Cys. 1 hit.
SSF57630. VitK_dep_GLA. 1 hit.
PROSITEPS00010. 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]
ProtoNetSearch...

Other

NextBio624347.

Entry information

Entry nameFA7_RAT
AccessionPrimary (citable) accession number: Q8K3U6
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2004
Last sequence update: October 1, 2002
Last modified: November 16, 2011
This is version 83 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

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