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Protein

Coagulation factor VII

Gene

F7

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

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).By similarity

Catalytic activityi

Selective cleavage of Arg-|-Ile bond in factor X to form factor Xa.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei234Charge relay systemBy similarity1
Active sitei283Charge relay systemBy similarity1
Binding sitei379SubstrateBy similarity1
Active sitei385Charge relay systemBy similarity1

GO - Molecular functioni

  • calcium ion binding Source: InterPro
  • endopeptidase activity Source: RGD
  • glycoprotein binding Source: Ensembl
  • receptor binding Source: RGD
  • serine-type endopeptidase activity Source: Ensembl
  • serine-type peptidase activity Source: RGD

GO - Biological processi

  • animal organ regeneration Source: RGD
  • blood coagulation Source: RGD
  • circadian rhythm Source: RGD
  • positive regulation of blood coagulation Source: RGD
  • positive regulation of leukocyte chemotaxis Source: Ensembl
  • positive regulation of platelet-derived growth factor receptor signaling pathway Source: Ensembl
  • positive regulation of positive chemotaxis Source: Ensembl
  • positive regulation of protein kinase B signaling Source: Ensembl
  • protein processing Source: Ensembl
  • response to 2,3,7,8-tetrachlorodibenzodioxine Source: RGD
  • response to anticoagulant Source: RGD
  • response to astaxanthin Source: RGD
  • response to carbon dioxide Source: RGD
  • response to cholesterol Source: RGD
  • response to estradiol Source: RGD
  • response to estrogen Source: RGD
  • response to genistein Source: RGD
  • response to growth hormone Source: RGD
  • response to hormone Source: RGD
  • response to hypoxia Source: RGD
  • response to nutrient levels Source: RGD
  • response to organic cyclic compound Source: RGD
  • response to thyroid hormone Source: RGD
  • response to Thyroid stimulating hormone Source: RGD
  • response to thyrotropin-releasing hormone Source: RGD
  • response to thyroxine Source: RGD
  • response to vitamin K Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Serine protease

Keywords - Biological processi

Blood coagulation, Hemostasis

Keywords - Ligandi

Calcium

Enzyme and pathway databases

ReactomeiR-RNO-140834. Extrinsic Pathway of Fibrin Clot Formation.
R-RNO-159740. Gamma-carboxylation of protein precursors.
R-RNO-159763. Transport of gamma-carboxylated protein precursors from the endoplasmic reticulum to the Golgi apparatus.
R-RNO-159782. Removal of aminoterminal propeptides from gamma-carboxylated proteins.

Protein family/group databases

MEROPSiS01.215.

Names & Taxonomyi

Protein namesi
Recommended name:
Coagulation factor VII (EC:3.4.21.21)
Alternative name(s):
Serum prothrombin conversion accelerator
Cleaved into the following 2 chains:
Gene namesi
Name:F7
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 16

Organism-specific databases

RGDi628678. F7.

Subcellular locationi

GO - Cellular componenti

  • extracellular space Source: RGD
  • vesicle Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 24Sequence analysisAdd BLAST24
PropeptideiPRO_000002773825 – 41Sequence analysisAdd BLAST17
ChainiPRO_000002773942 – 193Factor VII light chainBy similarityAdd BLAST152
ChainiPRO_0000027740194 – 446Factor VII heavy chainBy similarityAdd BLAST253

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei474-carboxyglutamatePROSITE-ProRule annotationBy similarity1
Modified residuei484-carboxyglutamatePROSITE-ProRule annotationBy similarity1
Modified residuei554-carboxyglutamatePROSITE-ProRule annotationBy similarity1
Modified residuei574-carboxyglutamatePROSITE-ProRule annotationBy similarity1
Disulfide bondi58 ↔ 63By similarity
Modified residuei604-carboxyglutamatePROSITE-ProRule annotationBy similarity1
Modified residuei614-carboxyglutamatePROSITE-ProRule annotationBy similarity1
Modified residuei664-carboxyglutamatePROSITE-ProRule annotationBy similarity1
Modified residuei674-carboxyglutamatePROSITE-ProRule annotationBy similarity1
Modified residuei704-carboxyglutamatePROSITE-ProRule annotationBy similarity1
Modified residuei764-carboxyglutamatePROSITE-ProRule annotationBy similarity1
Disulfide bondi91 ↔ 102By similarity
Glycosylationi93O-linked (Glc...); alternateBy similarity1
Glycosylationi93O-linked (Xyl...); alternateBy similarity1
Disulfide bondi96 ↔ 111By similarity
Glycosylationi101O-linked (Fuc)By similarity1
Modified residuei104(3R)-3-hydroxyaspartateBy similarity1
Disulfide bondi113 ↔ 122By similarity
Disulfide bondi132 ↔ 143By similarity
Disulfide bondi139 ↔ 153By similarity
Disulfide bondi155 ↔ 168By similarity
Disulfide bondi176 ↔ 303By similarity
Glycosylationi186N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi200 ↔ 205By similarity
Disulfide bondi219 ↔ 235By similarity
Glycosylationi244N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi351 ↔ 370By similarity
Disulfide bondi381 ↔ 409By similarity

Post-translational modificationi

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
Can be either O-glucosylated or O-xylosylated at Ser-93 by POGLUT1.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei193 – 194Cleavage; by factor Xa, factor XIIa, factor IXa, or thrombinBy similarity2

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Gamma-carboxyglutamic acid, Glycoprotein, Hydroxylation, Zymogen

Proteomic databases

PaxDbiQ8K3U6.
PRIDEiQ8K3U6.

Expressioni

Tissue specificityi

Plasma.

Gene expression databases

BgeeiENSRNOG00000032737.

Interactioni

Subunit structurei

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

GO - Molecular functioni

  • receptor binding Source: RGD

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000038466.

Structurei

3D structure databases

ProteinModelPortaliQ8K3U6.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini42 – 86GlaPROSITE-ProRule annotationAdd BLAST45
Domaini87 – 123EGF-like 1; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini128 – 169EGF-like 2PROSITE-ProRule annotationAdd BLAST42
Domaini194 – 433Peptidase S1PROSITE-ProRule annotationAdd BLAST240

Sequence similaritiesi

Belongs to the peptidase S1 family.PROSITE-ProRule annotation
Contains 2 EGF-like domains.PROSITE-ProRule annotation
Contains 1 Gla (gamma-carboxy-glutamate) domain.PROSITE-ProRule annotation
Contains 1 peptidase S1 domain.PROSITE-ProRule annotation

Keywords - Domaini

EGF-like domain, Repeat, Signal

Phylogenomic databases

eggNOGiENOG410IIMB. Eukaryota.
COG5640. LUCA.
GeneTreeiENSGT00760000118890.
HOGENOMiHOG000251821.
HOVERGENiHBG013304.
InParanoidiQ8K3U6.
KOiK01320.
OMAiCEQYCSD.
OrthoDBiEOG091G0AH5.
PhylomeDBiQ8K3U6.
TreeFamiTF327329.

Family and domain databases

CDDicd00190. Tryp_SPc. 1 hit.
Gene3Di4.10.740.10. 1 hit.
InterProiIPR017857. Coagulation_fac_subgr_Gla_dom.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR033190. F7.
IPR000294. GLA_domain.
IPR012224. Pept_S1A_FX.
IPR009003. Peptidase_S1_PA.
IPR001314. Peptidase_S1A.
IPR001254. Trypsin_dom.
IPR018114. TRYPSIN_HIS.
IPR033116. TRYPSIN_SER.
[Graphical view]
PANTHERiPTHR24256:SF212. PTHR24256:SF212. 1 hit.
PfamiPF00008. EGF. 1 hit.
PF00594. Gla. 1 hit.
PF00089. Trypsin. 1 hit.
[Graphical view]
PIRSFiPIRSF001143. Factor_X. 1 hit.
PRINTSiPR00722. CHYMOTRYPSIN.
PR00001. GLABLOOD.
SMARTiSM00181. EGF. 2 hits.
SM00179. EGF_CA. 1 hit.
SM00069. GLA. 1 hit.
SM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMiSSF50494. SSF50494. 1 hit.
SSF57630. SSF57630. 1 hit.
PROSITEiPS00010. 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]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q8K3U6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVPQTHGLLL LYFLLQLQGP LGAVVFITQE EAHGVLHRQR RANSLLEELW
60 70 80 90 100
SSSLERECNE ERCSFEEARE IFKSPERTKQ FWTIYSDGDQ CASNPCQNGG
110 120 130 140 150
TCQDHLKSYV CFCPLDFEGR NCEKNKNEQL ICANENGDCD QYCRDHVGTK
160 170 180 190 200
RTCSCHEDYV LQPDEVSCKP KVEYPCGRIP VVEKRNFSRP QGRIVGGYVC
210 220 230 240 250
PKGECPWQAV LKFNEALLCG AVLLDTRWIV TAAHCFDKFG KLVNITVVLG
260 270 280 290 300
EHDFSEKEGT EQVRLVEQVI MPNKYTRGRT DHDIALVRLH RPVTFTDYVV
310 320 330 340 350
PLCLPERAFS ENTLASIRFS RVSGWGQLLD RGATALELMV IEVPRLMTQD
360 370 380 390 400
CLEHAKHSAN TPRITENMFC AGYMDGTKDA CKGDSGGPHA THYHGTWYLT
410 420 430 440
GVVSWGEGCA AIGHIGVYTR VSQYIDWLVK YMDSKLRVGI SRVSLL
Length:446
Mass (Da):50,399
Last modified:October 1, 2002 - v1
Checksum:i292985EBF119C0AA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF532184 mRNA. Translation: AAM95967.1.
RefSeqiNP_690059.1. NM_152846.1.
UniGeneiRn.86416.

Genome annotation databases

EnsembliENSRNOT00000037806; ENSRNOP00000038466; ENSRNOG00000032737.
GeneIDi260320.
KEGGirno:260320.
UCSCiRGD:628678. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF532184 mRNA. Translation: AAM95967.1.
RefSeqiNP_690059.1. NM_152846.1.
UniGeneiRn.86416.

3D structure databases

ProteinModelPortaliQ8K3U6.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000038466.

Protein family/group databases

MEROPSiS01.215.

Proteomic databases

PaxDbiQ8K3U6.
PRIDEiQ8K3U6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000037806; ENSRNOP00000038466; ENSRNOG00000032737.
GeneIDi260320.
KEGGirno:260320.
UCSCiRGD:628678. rat.

Organism-specific databases

CTDi2155.
RGDi628678. F7.

Phylogenomic databases

eggNOGiENOG410IIMB. Eukaryota.
COG5640. LUCA.
GeneTreeiENSGT00760000118890.
HOGENOMiHOG000251821.
HOVERGENiHBG013304.
InParanoidiQ8K3U6.
KOiK01320.
OMAiCEQYCSD.
OrthoDBiEOG091G0AH5.
PhylomeDBiQ8K3U6.
TreeFamiTF327329.

Enzyme and pathway databases

ReactomeiR-RNO-140834. Extrinsic Pathway of Fibrin Clot Formation.
R-RNO-159740. Gamma-carboxylation of protein precursors.
R-RNO-159763. Transport of gamma-carboxylated protein precursors from the endoplasmic reticulum to the Golgi apparatus.
R-RNO-159782. Removal of aminoterminal propeptides from gamma-carboxylated proteins.

Miscellaneous databases

PROiQ8K3U6.

Gene expression databases

BgeeiENSRNOG00000032737.

Family and domain databases

CDDicd00190. Tryp_SPc. 1 hit.
Gene3Di4.10.740.10. 1 hit.
InterProiIPR017857. Coagulation_fac_subgr_Gla_dom.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR033190. F7.
IPR000294. GLA_domain.
IPR012224. Pept_S1A_FX.
IPR009003. Peptidase_S1_PA.
IPR001314. Peptidase_S1A.
IPR001254. Trypsin_dom.
IPR018114. TRYPSIN_HIS.
IPR033116. TRYPSIN_SER.
[Graphical view]
PANTHERiPTHR24256:SF212. PTHR24256:SF212. 1 hit.
PfamiPF00008. EGF. 1 hit.
PF00594. Gla. 1 hit.
PF00089. Trypsin. 1 hit.
[Graphical view]
PIRSFiPIRSF001143. Factor_X. 1 hit.
PRINTSiPR00722. CHYMOTRYPSIN.
PR00001. GLABLOOD.
SMARTiSM00181. EGF. 2 hits.
SM00179. EGF_CA. 1 hit.
SM00069. GLA. 1 hit.
SM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMiSSF50494. SSF50494. 1 hit.
SSF57630. SSF57630. 1 hit.
PROSITEiPS00010. 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]
ProtoNetiSearch...

Entry informationi

Entry nameiFA7_RAT
AccessioniPrimary (citable) accession number: Q8K3U6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 7, 2004
Last sequence update: October 1, 2002
Last modified: November 30, 2016
This is version 123 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.