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Q8K3U6

- FA7_RAT

UniProt

Q8K3U6 - FA7_RAT

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Protein

Coagulation factor VII

Gene
F7
Organism
Rattus norvegicus (Rat)
Status
Reviewed - 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.

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei193 – 1942Cleavage; by factor Xa, factor XIIa, factor IXa, or thrombin By similarity
Active sitei234 – 2341Charge relay system By similarity
Active sitei283 – 2831Charge relay system By similarity
Binding sitei379 – 3791Substrate By similarity
Active sitei385 – 3851Charge relay system By similarity

GO - Molecular functioni

  1. calcium ion binding Source: InterPro
  2. endopeptidase activity Source: RGD
  3. receptor binding Source: RGD
  4. serine-type endopeptidase activity Source: InterPro
  5. serine-type peptidase activity Source: RGD

GO - Biological processi

  1. blood coagulation Source: RGD
  2. circadian rhythm Source: RGD
  3. organ regeneration Source: RGD
  4. positive regulation of blood coagulation Source: RGD
  5. positive regulation of leukocyte chemotaxis Source: Ensembl
  6. positive regulation of platelet-derived growth factor receptor signaling pathway Source: Ensembl
  7. positive regulation of positive chemotaxis Source: Ensembl
  8. positive regulation of protein kinase B signaling Source: Ensembl
  9. response to estrogen Source: RGD
  10. response to growth hormone Source: RGD
  11. response to hormone Source: RGD
  12. response to nutrient levels Source: RGD
  13. response to organic cyclic compound Source: RGD
  14. 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

ReactomeiREACT_196405. BMAL1:CLOCK,NPAS2 activates circadian gene expression.

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
ProteomesiUP000002494: Chromosome 16

Organism-specific databases

RGDi628678. F7.

Subcellular locationi

Secreted By similarity

GO - Cellular componenti

  1. extracellular space Source: RGD
  2. vesicle Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2424 Reviewed predictionAdd
BLAST
Propeptidei25 – 4117 Reviewed predictionPRO_0000027738Add
BLAST
Chaini42 – 193152Factor VII light chain By similarityPRO_0000027739Add
BLAST
Chaini194 – 446253Factor VII heavy chain By similarityPRO_0000027740Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei47 – 4714-carboxyglutamate By similarity
Modified residuei48 – 4814-carboxyglutamate By similarity
Modified residuei55 – 5514-carboxyglutamate By similarity
Modified residuei57 – 5714-carboxyglutamate By similarity
Disulfide bondi58 ↔ 63 By similarity
Modified residuei60 – 6014-carboxyglutamate By similarity
Modified residuei61 – 6114-carboxyglutamate By similarity
Modified residuei66 – 6614-carboxyglutamate By similarity
Modified residuei67 – 6714-carboxyglutamate By similarity
Modified residuei70 – 7014-carboxyglutamate By similarity
Modified residuei76 – 7614-carboxyglutamate By similarity
Disulfide bondi91 ↔ 102 By similarity
Glycosylationi93 – 931O-linked (Glc...); alternate By similarity
Glycosylationi93 – 931O-linked (Xyl...); alternate By similarity
Disulfide bondi96 ↔ 111 By similarity
Glycosylationi101 – 1011O-linked (Fuc) By similarity
Modified residuei104 – 1041(3R)-3-hydroxyaspartate By similarity
Disulfide bondi113 ↔ 122 By similarity
Disulfide bondi132 ↔ 143 By similarity
Disulfide bondi139 ↔ 153 By similarity
Disulfide bondi155 ↔ 168 By similarity
Disulfide bondi176 ↔ 303 By similarity
Glycosylationi186 – 1861N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi200 ↔ 205 By similarity
Disulfide bondi219 ↔ 235 By similarity
Glycosylationi244 – 2441N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi351 ↔ 370 By similarity
Disulfide bondi381 ↔ 409 By 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.

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

GenevestigatoriQ8K3U6.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000038466.

Structurei

3D structure databases

ProteinModelPortaliQ8K3U6.
SMRiQ8K3U6. Positions 61-183, 194-440.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini42 – 8645GlaAdd
BLAST
Domaini87 – 12337EGF-like 1; calcium-binding Reviewed predictionAdd
BLAST
Domaini128 – 16942EGF-like 2Add
BLAST
Domaini194 – 433240Peptidase S1Add
BLAST

Sequence similaritiesi

Belongs to the peptidase S1 family.
Contains 2 EGF-like domains.

Keywords - Domaini

EGF-like domain, Repeat, Signal

Phylogenomic databases

eggNOGiCOG5640.
GeneTreeiENSGT00750000117249.
HOGENOMiHOG000251821.
HOVERGENiHBG013304.
InParanoidiQ8K3U6.
KOiK01320.
OMAiGCEQYCS.
OrthoDBiEOG75B84T.
PhylomeDBiQ8K3U6.
TreeFamiTF327329.

Family and domain databases

Gene3Di4.10.740.10. 1 hit.
InterProiIPR017857. 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]
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. 1 hit.
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

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MVPQTHGLLL LYFLLQLQGP LGAVVFITQE EAHGVLHRQR RANSLLEELW    50
SSSLERECNE ERCSFEEARE IFKSPERTKQ FWTIYSDGDQ CASNPCQNGG 100
TCQDHLKSYV CFCPLDFEGR NCEKNKNEQL ICANENGDCD QYCRDHVGTK 150
RTCSCHEDYV LQPDEVSCKP KVEYPCGRIP VVEKRNFSRP QGRIVGGYVC 200
PKGECPWQAV LKFNEALLCG AVLLDTRWIV TAAHCFDKFG KLVNITVVLG 250
EHDFSEKEGT EQVRLVEQVI MPNKYTRGRT DHDIALVRLH RPVTFTDYVV 300
PLCLPERAFS ENTLASIRFS RVSGWGQLLD RGATALELMV IEVPRLMTQD 350
CLEHAKHSAN TPRITENMFC AGYMDGTKDA CKGDSGGPHA THYHGTWYLT 400
GVVSWGEGCA AIGHIGVYTR VSQYIDWLVK YMDSKLRVGI SRVSLL 446
Length:446
Mass (Da):50,399
Last modified:October 1, 2002 - v1
Checksum:i292985EBF119C0AA
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
AF532184 mRNA. Translation: AAM95967.1 .
RefSeqi NP_690059.1. NM_152846.1.
UniGenei Rn.86416.

3D structure databases

ProteinModelPortali Q8K3U6.
SMRi Q8K3U6. Positions 61-183, 194-440.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 10116.ENSRNOP00000038466.

Protein family/group databases

MEROPSi S01.215.

Proteomic databases

PaxDbi Q8K3U6.
PRIDEi Q8K3U6.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSRNOT00000037806 ; ENSRNOP00000038466 ; ENSRNOG00000032737 .
GeneIDi 260320.
KEGGi rno:260320.
UCSCi RGD:628678. rat.

Organism-specific databases

CTDi 2155.
RGDi 628678. F7.

Phylogenomic databases

eggNOGi COG5640.
GeneTreei ENSGT00750000117249.
HOGENOMi HOG000251821.
HOVERGENi HBG013304.
InParanoidi Q8K3U6.
KOi K01320.
OMAi GCEQYCS.
OrthoDBi EOG75B84T.
PhylomeDBi Q8K3U6.
TreeFami TF327329.

Enzyme and pathway databases

Reactomei REACT_196405. BMAL1:CLOCK,NPAS2 activates circadian gene expression.

Miscellaneous databases

NextBioi 624347.
PROi Q8K3U6.

Gene expression databases

Genevestigatori Q8K3U6.

Family and domain databases

Gene3Di 4.10.740.10. 1 hit.
InterProi IPR017857. 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 ]
Pfami PF00008. EGF. 1 hit.
PF00594. Gla. 1 hit.
PF00089. Trypsin. 1 hit.
[Graphical view ]
PIRSFi PIRSF001143. Factor_X. 1 hit.
PRINTSi PR00722. CHYMOTRYPSIN.
PR00001. GLABLOOD.
SMARTi SM00181. EGF. 1 hit.
SM00179. EGF_CA. 1 hit.
SM00069. GLA. 1 hit.
SM00020. Tryp_SPc. 1 hit.
[Graphical view ]
SUPFAMi SSF50494. SSF50494. 1 hit.
SSF57630. SSF57630. 1 hit.
PROSITEi PS00010. 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 ]
ProtoNeti Search...

Publicationsi

  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.

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: September 3, 2014
This is version 104 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

External Data

Dasty 3

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