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Protein

Coagulation factor VII

Gene

F7

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: -Experimental evidence at protein 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

GO - Biological processi

Keywordsi

Molecular functionHydrolase, Protease, Serine protease
Biological processBlood coagulation, Hemostasis
LigandCalcium

Enzyme and pathway databases

ReactomeiR-MMU-1368110 Bmal1:Clock,Npas2 activates circadian gene expression
R-MMU-140834 Extrinsic Pathway of Fibrin Clot Formation
R-MMU-159740 Gamma-carboxylation of protein precursors
R-MMU-159763 Transport of gamma-carboxylated protein precursors from the endoplasmic reticulum to the Golgi apparatus
R-MMU-159782 Removal of aminoterminal propeptides from gamma-carboxylated proteins

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
Synonyms:Cf7
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 8

Organism-specific databases

MGIiMGI:109325 F7

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 24Sequence analysisAdd BLAST24
PropeptideiPRO_000002773225 – 41Sequence analysisAdd BLAST17
ChainiPRO_000002773342 – 193Factor VII light chainAdd BLAST152
ChainiPRO_0000027734194 – 446Factor VII heavy chainAdd 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...) serine; alternateBy similarity1
Glycosylationi93O-linked (Xyl...) serine; alternateBy similarity1
Disulfide bondi96 ↔ 111By similarity
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...) asparagineSequence analysis1
Disulfide bondi200 ↔ 205By similarity
Disulfide bondi219 ↔ 235By similarity
Glycosylationi244N-linked (GlcNAc...) asparagineSequence 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

PaxDbiP70375
PeptideAtlasiP70375
PRIDEiP70375

PTM databases

PhosphoSitePlusiP70375
SwissPalmiP70375

Expressioni

Tissue specificityi

Plasma and liver.

Inductioni

Expression in the liver and plasma oscillates in a circadian manner.1 Publication

Gene expression databases

BgeeiENSMUSG00000031443
CleanExiMM_F7
ExpressionAtlasiP70375 baseline and differential
GenevisibleiP70375 MM

Interactioni

Subunit structurei

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

GO - Molecular functioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000033820

Structurei

Secondary structure

1446
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi91 – 93Combined sources3
Beta strandi101 – 105Combined sources5
Beta strandi108 – 112Combined sources5
Beta strandi117 – 119Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5KXHX-ray1.33B87-126[»]
5KY2X-ray1.47B87-126[»]
5KY3X-ray1.53B87-126[»]
ProteinModelPortaliP70375
SMRiP70375
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

Keywords - Domaini

EGF-like domain, Repeat, Signal

Phylogenomic databases

eggNOGiENOG410IIMB Eukaryota
COG5640 LUCA
GeneTreeiENSGT00760000118890
HOGENOMiHOG000251821
HOVERGENiHBG013304
InParanoidiP70375
KOiK01320
OMAiCEQYCSD
OrthoDBiEOG091G0AH5
PhylomeDBiP70375
TreeFamiTF327329

Family and domain databases

CDDicd00190 Tryp_SPc, 1 hit
Gene3Di4.10.740.101 hit
InterProiView protein in InterPro
IPR017857 Coagulation_fac-like_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
IPR035972 GLA-like_dom_SF
IPR000294 GLA_domain
IPR012224 Pept_S1A_FX
IPR009003 Peptidase_S1_PA
IPR001314 Peptidase_S1A
IPR001254 Trypsin_dom
IPR018114 TRYPSIN_HIS
IPR033116 TRYPSIN_SER
PANTHERiPTHR44064:SF1 PTHR44064:SF1, 1 hit
PfamiView protein in Pfam
PF00008 EGF, 1 hit
PF00594 Gla, 1 hit
PF00089 Trypsin, 1 hit
PIRSFiPIRSF001143 Factor_X, 1 hit
PRINTSiPR00722 CHYMOTRYPSIN
PR00001 GLABLOOD
SMARTiView protein in SMART
SM00181 EGF, 2 hits
SM00179 EGF_CA, 1 hit
SM00069 GLA, 1 hit
SM00020 Tryp_SPc, 1 hit
SUPFAMiSSF50494 SSF50494, 1 hit
SSF57630 SSF57630, 1 hit
PROSITEiView protein in PROSITE
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

Sequencei

Sequence statusi: Complete.

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

P70375-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVPQAHGLLL LCFLLQLQGP LGTAVFITQE EAHGVLHRQR RANSLLEELW
60 70 80 90 100
PGSLERECNE EQCSFEEARE IFKSPERTKQ FWIVYSDGDQ CASNPCQNGG
110 120 130 140 150
TCQDHLKSYV CFCLLDFEGR NCEKSKNEQL ICANENGDCD QYCRDHVGTK
160 170 180 190 200
RTCSCHEDYT LQPDEVSCKP KVEYPCGRIP VVEKRNSSSR QGRIVGGNVC
210 220 230 240 250
PKGECPWQAV LKINGLLLCG AVLLDARWIV TAAHCFDNIR YWGNITVVMG
260 270 280 290 300
EHDFSEKDGD EQVRRVTQVI MPDKYIRGKI NHDIALLRLH RPVTFTDYVV
310 320 330 340 350
PLCLPEKSFS ENTLARIRFS RVSGWGQLLD RGATALELMS IEVPRLMTQD
360 370 380 390 400
CLEHAKHSSN TPKITENMFC AGYMDGTKDA CKGDSGGPHA THYHGTWYLT
410 420 430 440
GVVSWGEGCA AIGHIGVYTR VSQYIDWLVR HMDSKLQVGV FRLPLL
Length:446
Mass (Da):50,276
Last modified:February 1, 1997 - v1
Checksum:i2512E44A45CBC96E
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti99G → V in AAC52570 (PubMed:8972017).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U44795 mRNA Translation: AAC52570.1
U66079 Genomic DNA Translation: AAC33796.1
BC061149 mRNA Translation: AAH61149.1
CCDSiCCDS22104.1
RefSeqiNP_034302.2, NM_010172.4
UniGeneiMm.4827

Genome annotation databases

EnsembliENSMUST00000033820; ENSMUSP00000033820; ENSMUSG00000031443
GeneIDi14068
KEGGimmu:14068
UCSCiuc009kwr.2 mouse

Similar proteinsi

Entry informationi

Entry nameiFA7_MOUSE
AccessioniPrimary (citable) accession number: P70375
Secondary accession number(s): Q61109
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: February 1, 1997
Last modified: March 28, 2018
This is version 183 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome