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Protein

Coagulation factor VII

Gene

F7

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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.

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei93 – 931Important for S-92 for O-xylosylationBy similarity
Active sitei233 – 2331Charge relay systemBy similarity
Active sitei282 – 2821Charge relay systemBy similarity
Binding sitei378 – 3781SubstrateBy similarity
Active sitei384 – 3841Charge relay systemBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Serine protease

Keywords - Biological processi

Blood coagulation, Hemostasis

Keywords - Ligandi

Calcium

Enzyme and pathway databases

ReactomeiR-BTA-140834. Extrinsic Pathway of Fibrin Clot Formation.
R-BTA-159740. Gamma-carboxylation of protein precursors.
R-BTA-159763. Transport of gamma-carboxylated protein precursors from the endoplasmic reticulum to the Golgi apparatus.
R-BTA-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
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Chromosome 12

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2323Sequence analysisAdd
BLAST
Propeptidei24 – 40171 PublicationPRO_0000240126Add
BLAST
Chaini41 – 192152Factor VII light chain1 PublicationPRO_0000027727Add
BLAST
Chaini193 – 447255Factor VII heavy chain1 PublicationPRO_0000027728Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei46 – 4614-carboxyglutamatePROSITE-ProRule annotation1 Publication
Modified residuei47 – 4714-carboxyglutamatePROSITE-ProRule annotation1 Publication
Modified residuei54 – 5414-carboxyglutamatePROSITE-ProRule annotation1 Publication
Modified residuei56 – 5614-carboxyglutamatePROSITE-ProRule annotation1 Publication
Disulfide bondi57 ↔ 62By similarity
Modified residuei59 – 5914-carboxyglutamatePROSITE-ProRule annotation1 Publication
Modified residuei60 – 6014-carboxyglutamatePROSITE-ProRule annotation1 Publication
Modified residuei65 – 6514-carboxyglutamatePROSITE-ProRule annotation1 Publication
Modified residuei66 – 6614-carboxyglutamatePROSITE-ProRule annotation1 Publication
Modified residuei69 – 6914-carboxyglutamatePROSITE-ProRule annotation1 Publication
Modified residuei74 – 7414-carboxyglutamatePROSITE-ProRule annotation1 Publication
Modified residuei75 – 7514-carboxyglutamatePROSITE-ProRule annotation1 Publication
Disulfide bondi90 ↔ 101By similarity
Glycosylationi92 – 921O-linked (Glc...)1 Publication
Glycosylationi92 – 921O-linked (Glc...); alternateBy similarity
Glycosylationi92 – 921O-linked (Xyl...); alternateBy similarity
Disulfide bondi95 ↔ 110By similarity
Glycosylationi100 – 1001O-linked (Fuc)By similarity
Disulfide bondi112 ↔ 121By similarity
Disulfide bondi131 ↔ 142By similarity
Disulfide bondi138 ↔ 152By similarity
Disulfide bondi154 ↔ 167By similarity
Disulfide bondi175 ↔ 302By similarity
Glycosylationi185 – 1851N-linked (GlcNAc...)1 Publication
Disulfide bondi199 ↔ 204By similarity
Disulfide bondi218 ↔ 234By similarity
Glycosylationi243 – 2431N-linked (GlcNAc...)1 Publication
Disulfide bondi350 ↔ 369By similarity
Disulfide bondi380 ↔ 408By similarity

Post-translational modificationi

The vitamin K-dependent, enzymatic carboxylation of some glutamate residues allows the modified protein to bind calcium.
O-glycosylated. O-fucosylated by POFUT1 on a conserved serine or threonine residue found in the consensus sequence C2-X(4,5)-[S/T]-C3 of EGF domains, where C2 and C3 are the second and third conserved cysteines.By similarity
Can be either O-glucosylated or O-xylosylated at Ser-92 by POGLUT1.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei192 – 1932Cleavage; by factor Xa, factor XIIa, factor IXa, or thrombin

Keywords - PTMi

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

Proteomic databases

PaxDbiP22457.
PRIDEiP22457.

Expressioni

Tissue specificityi

Plasma.

Gene expression databases

BgeeiENSBTAG00000007411.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000009746.

Structurei

3D structure databases

ProteinModelPortaliP22457.
SMRiP22457. Positions 41-182, 193-445.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini41 – 8545GlaPROSITE-ProRule annotationAdd
BLAST
Domaini86 – 12237EGF-like 1; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini127 – 16842EGF-like 2PROSITE-ProRule annotationAdd
BLAST
Domaini193 – 432240Peptidase S1PROSITE-ProRule annotationAdd
BLAST

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.
InParanoidiP22457.
KOiK01320.
OMAiCEQYCSD.
OrthoDBiEOG091G0AH5.
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.
PS01186. EGF_2. 2 hits.
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.

P22457-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLSQAWALAL LCFLLSLWGS LPAVFLPQEQ ALSILHRPRR ANGFLEELLP
60 70 80 90 100
GSLERECREE LCSFEEAHEI FRNEERTRQF WVSYNDGDQC ASSPCQNGGS
110 120 130 140 150
CEDQLRSYIC FCPDGFEGRN CETDKQSQLI CANDNGGCEQ YCGADPGAGR
160 170 180 190 200
FCWCHEGYAL QADGVSCAPT VEYPCGKIPV LEKRNGSKPQ GRIVGGHVCP
210 220 230 240 250
KGECPWQAML KLNGALLCGG TLVGPAWVVS AAHCFERLRS RGNLTAVLGE
260 270 280 290 300
HDLSRVEGPE QERRVAQIIV PKQYVPGQTD HDVALLQLAQ PVALGDHVAP
310 320 330 340 350
LCLPDPDFAD QTLAFVRFSA VSGWGQLLER GVTARKLMVV LVPRLLTQDC
360 370 380 390 400
LQQSRQRPGG PVVTDNMFCA GYSDGSKDAC KGDSGGPHAT RFRGTWFLTG
410 420 430 440
VVSWGEGCAA AGHFGIYTRV SRYTAWLRQL MGHPPSRQGF FQVPLLP
Length:447
Mass (Da):48,961
Last modified:June 13, 2006 - v2
Checksum:i6FE6CA805E84B871
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BT021584 mRNA. Translation: AAX46431.1.
BC146045 mRNA. Translation: AAI46046.1.
PIRiA31979. KFBO7.
RefSeqiNP_001029978.1. NM_001034806.1.
UniGeneiBt.37397.

Genome annotation databases

EnsembliENSBTAT00000009746; ENSBTAP00000009746; ENSBTAG00000007411.
GeneIDi617960.
KEGGibta:617960.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BT021584 mRNA. Translation: AAX46431.1.
BC146045 mRNA. Translation: AAI46046.1.
PIRiA31979. KFBO7.
RefSeqiNP_001029978.1. NM_001034806.1.
UniGeneiBt.37397.

3D structure databases

ProteinModelPortaliP22457.
SMRiP22457. Positions 41-182, 193-445.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000009746.

Protein family/group databases

MEROPSiS01.215.

Proteomic databases

PaxDbiP22457.
PRIDEiP22457.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000009746; ENSBTAP00000009746; ENSBTAG00000007411.
GeneIDi617960.
KEGGibta:617960.

Organism-specific databases

CTDi2155.

Phylogenomic databases

eggNOGiENOG410IIMB. Eukaryota.
COG5640. LUCA.
GeneTreeiENSGT00760000118890.
HOGENOMiHOG000251821.
HOVERGENiHBG013304.
InParanoidiP22457.
KOiK01320.
OMAiCEQYCSD.
OrthoDBiEOG091G0AH5.
TreeFamiTF327329.

Enzyme and pathway databases

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

Gene expression databases

BgeeiENSBTAG00000007411.

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.
PS01186. EGF_2. 2 hits.
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_BOVIN
AccessioniPrimary (citable) accession number: P22457
Secondary accession number(s): A6H6Y5, Q58DL3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: June 13, 2006
Last modified: September 7, 2016
This is version 160 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, 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.