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UniProtKB - P08709 (FA7_HUMAN)

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Protein

Coagulation factor VII

Gene

F7

Organism
Homo sapiens (Human)
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.

Catalytic activityi

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei113Important for S-112 for O-xylosylation1
Active sitei253Charge relay systemBy similarity1
Active sitei302Charge relay systemBy similarity1
Binding sitei398SubstrateBy similarity1
Active sitei404Charge relay systemBy similarity1

GO - Molecular functioni

  • calcium ion binding Source: InterPro
  • serine-type endopeptidase activity Source: ProtInc
  • serine-type peptidase activity Source: ProtInc
  • signaling receptor binding Source: Ensembl
View the complete GO annotation on QuickGO ...

GO - Biological processi

View the complete GO annotation on QuickGO ...

Keywordsi

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

Enzyme and pathway databases

BRENDAi3.4.21.21 2681
ReactomeiR-HSA-1368108 BMAL1:CLOCK,NPAS2 activates circadian gene expression
R-HSA-140834 Extrinsic Pathway of Fibrin Clot Formation
R-HSA-159740 Gamma-carboxylation of protein precursors
R-HSA-159763 Transport of gamma-carboxylated protein precursors from the endoplasmic reticulum to the Golgi apparatus
R-HSA-159782 Removal of aminoterminal propeptides from gamma-carboxylated proteins
SABIO-RKiP08709

Protein family/group databases

MEROPSiS01.215

Names & Taxonomyi

Protein namesi
Recommended name:
Coagulation factor VII (EC:3.4.21.21)
Alternative name(s):
Proconvertin
Serum prothrombin conversion accelerator
Short name:
SPCA
INN: Eptacog alfa
Cleaved into the following 2 chains:
Factor VII light chain
Factor VII heavy chain
Gene namesi
Name:F7
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
Proteomesi
  • UP000005640 Componenti: Chromosome 13

Organism-specific databases

EuPathDBiHostDB:ENSG00000057593.13
HGNCiHGNC:3544 F7
MIMi613878 gene
neXtProtiNX_P08709

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

Pathology & Biotechi

Involvement in diseasei

Factor VII deficiency (FA7D)26 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA hemorrhagic disease with variable presentation. The clinical picture can be very severe, with the early occurrence of intracerebral hemorrhages or repeated hemarthroses, or, in contrast, moderate with cutaneous-mucosal hemorrhages (epistaxis, menorrhagia) or hemorrhages provoked by a surgical intervention. Finally, numerous subjects are completely asymptomatic despite very low factor VII levels.
See also OMIM:227500
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_01439113L → P in FA7D; Morioka. 1 PublicationCorresponds to variant dbSNP:rs387906507EnsemblClinVar.1
Natural variantiVAR_06536959R → RR in FA7D. 1 Publication1
Natural variantiVAR_01513564F → L in FA7D. 2 Publications1
Natural variantiVAR_01440573L → Q in FA7D. 2 PublicationsCorresponds to variant dbSNP:rs45572939Ensembl.1
Natural variantiVAR_01440679E → Q in FA7D. 1 Publication1
Natural variantiVAR_06537082C → F in FA7D. 1 Publication1
Natural variantiVAR_06537182C → R in FA7D. 1 PublicationCorresponds to variant dbSNP:rs745374448Ensembl.1
Natural variantiVAR_06537284Missing in FA7D. 1 Publication1
Natural variantiVAR_06537385E → K in FA7D. 1 PublicationCorresponds to variant dbSNP:rs121964935Ensembl.1
Natural variantiVAR_06537488R → G in FA7D. 1 PublicationCorresponds to variant dbSNP:rs776354144Ensembl.1
Natural variantiVAR_06537588R → P in FA7D. 1 Publication1
Natural variantiVAR_065376117N → D in FA7D; exhibits no procoagulant activity and is unable to bind tissue factor. 1 PublicationCorresponds to variant dbSNP:rs121964932Ensembl.1
Natural variantiVAR_015136120S → P in FA7D. 2 Publications1
Natural variantiVAR_014407121C → F in FA7D. 1 Publication1
Natural variantiVAR_014408125L → P in FA7D. 1 Publication1
Natural variantiVAR_014409128Y → C in FA7D. 3 Publications1
Natural variantiVAR_065377138G → D in FA7D. 1 Publication1
Natural variantiVAR_006497139R → K in FA7D. 1
Natural variantiVAR_006498139R → Q in FA7D; Charlotte. 3 PublicationsCorresponds to variant dbSNP:rs150525536Ensembl.1
Natural variantiVAR_006499139R → W in FA7D. 2 PublicationsCorresponds to variant dbSNP:rs776796178Ensembl.1
Natural variantiVAR_014410151C → S in FA7D. 1 Publication1
Natural variantiVAR_015137154E → K in FA7D. 2 PublicationsCorresponds to variant dbSNP:rs146795869Ensembl.1
Natural variantiVAR_065378156G → S in FA7D. 1 PublicationCorresponds to variant dbSNP:rs563972504Ensembl.1
Natural variantiVAR_006501157G → C in FA7D. 1
Natural variantiVAR_006500157G → S in FA7D. 2 PublicationsCorresponds to variant dbSNP:rs763458490Ensembl.1
Natural variantiVAR_014411157G → V in FA7D. 1 PublicationCorresponds to variant dbSNP:rs771335282Ensembl.1
Natural variantiVAR_006502160Q → R in FA7D. 4 PublicationsCorresponds to variant dbSNP:rs200016360Ensembl.1
Natural variantiVAR_065379171S → F in FA7D. 1 PublicationCorresponds to variant dbSNP:rs143855920Ensembl.1
Natural variantiVAR_065380177G → R in FA7D. 1 Publication1
Natural variantiVAR_065381181L → P in FA7D. 1 Publication1
Natural variantiVAR_065382183D → N in FA7D. 1 Publication1
Natural variantiVAR_065383186S → F in FA7D. 1 PublicationCorresponds to variant dbSNP:rs764971156Ensembl.1
Natural variantiVAR_065384189P → S in FA7D. 1 Publication1
Natural variantiVAR_065385194P → L in FA7D. 1 Publication1
Natural variantiVAR_006503194P → T in FA7D; Malta-I. 2 Publications1
Natural variantiVAR_014412195C → R in FA7D. 3 PublicationsCorresponds to variant dbSNP:rs372577568Ensembl.1
Natural variantiVAR_006504197K → E in FA7D. 1 Publication1
Natural variantiVAR_065386198I → T in FA7D. 1 PublicationCorresponds to variant dbSNP:rs762621913Ensembl.1
Natural variantiVAR_006505212R → Q in FA7D; Charlotte. 4 PublicationsCorresponds to variant dbSNP:rs868044209Ensembl.1
Natural variantiVAR_015138216G → D in FA7D. 2 Publications1
Natural variantiVAR_006506238C → Y in FA7D. 1 PublicationCorresponds to variant dbSNP:rs121964928Ensembl.1
Natural variantiVAR_065387240G → R in FA7D. 1 Publication1
Natural variantiVAR_014413241T → N in FA7D. 2 Publications1
Natural variantiVAR_065388250S → F in FA7D. 1 Publication1
Natural variantiVAR_065389251A → P in FA7D. 1 Publication1
Natural variantiVAR_065390251A → T in FA7D. 1 Publication1
Natural variantiVAR_065391254C → R in FA7D. 1 Publication1
Natural variantiVAR_015139254C → Y in FA7D. 2 Publications1
Natural variantiVAR_065392264L → P in FA7D. 1 PublicationCorresponds to variant dbSNP:rs753266903Ensembl.1
Natural variantiVAR_015140266A → T in FA7D. 2 PublicationsCorresponds to variant dbSNP:rs764807079Ensembl.1
Natural variantiVAR_065393272D → N in FA7D. 1 PublicationCorresponds to variant dbSNP:rs751028917Ensembl.1
Natural variantiVAR_065394277D → N in FA7D. 1 PublicationCorresponds to variant dbSNP:rs550074221Ensembl.1
Natural variantiVAR_006507283R → W in FA7D. 2 PublicationsCorresponds to variant dbSNP:rs779589651Ensembl.1
Natural variantiVAR_065395298T → I in FA7D. 1 Publication1
Natural variantiVAR_065396301H → Q in FA7D. 1 Publication1
Natural variantiVAR_014414302D → H in FA7D. 3 Publications1
Natural variantiVAR_014415302D → N in FA7D. 2 PublicationsCorresponds to variant dbSNP:rs770328850Ensembl.1
Natural variantiVAR_014416304A → T in FA7D. 2 PublicationsCorresponds to variant dbSNP:rs773627551Ensembl.1
Natural variantiVAR_006508304A → V in FA7D; Malta-II. 5 PublicationsCorresponds to variant dbSNP:rs121964931Ensembl.1
Natural variantiVAR_014417307R → C in FA7D. 3 PublicationsCorresponds to variant dbSNP:rs147680958Ensembl.1
Natural variantiVAR_006509307R → H in FA7D; Mie. 2 PublicationsCorresponds to variant dbSNP:rs121964929Ensembl.1
Natural variantiVAR_015141312V → M in FA7D. 2 PublicationsCorresponds to variant dbSNP:rs201991361Ensembl.1
Natural variantiVAR_065397314L → V in FA7D. 1 Publication1
Natural variantiVAR_065398321L → F in FA7D. 1 PublicationCorresponds to variant dbSNP:rs778138366Ensembl.1
Natural variantiVAR_065399323L → R in FA7D. 1 Publication1
Natural variantiVAR_006510325E → K in FA7D. 3 PublicationsCorresponds to variant dbSNP:rs749760143Ensembl.1
Natural variantiVAR_065400326R → Q in FA7D. 1 PublicationCorresponds to variant dbSNP:rs146698837Ensembl.1
Natural variantiVAR_014418332T → M in FA7D. 1 PublicationCorresponds to variant dbSNP:rs200212201Ensembl.1
Natural variantiVAR_065401337R → C in FA7D. 1 PublicationCorresponds to variant dbSNP:rs139372641Ensembl.1
Natural variantiVAR_015142341V → F in FA7D. 2 Publications1
Natural variantiVAR_065402343G → S in FA7D. 2 Publications1
Natural variantiVAR_076570344W → G in FA7D. 1 Publication1
Natural variantiVAR_065403344W → R in FA7D. 1 Publication1
Natural variantiVAR_065404345G → S in FA7D. 1 Publication1
Natural variantiVAR_065405350R → C in FA7D. 1 PublicationCorresponds to variant dbSNP:rs747876824Ensembl.1
Natural variantiVAR_006511354A → V in FA7D. 5 PublicationsCorresponds to variant dbSNP:rs36209567EnsemblClinVar.1
Natural variantiVAR_006512358M → I in FA7D. 4 PublicationsCorresponds to variant dbSNP:rs149283257Ensembl.1
Natural variantiVAR_006513358M → V in FA7D. 1 Publication1
Natural variantiVAR_065406360L → P in FA7D. 1 Publication1
Natural variantiVAR_065407363P → H in FA7D. 1 Publication1
Natural variantiVAR_015143363P → R in FA7D. 2 PublicationsCorresponds to variant dbSNP:rs963430078Ensembl.1
Natural variantiVAR_006514364R → Q in FA7D; Harrow/Padua. 6 PublicationsCorresponds to variant dbSNP:rs121964926EnsemblClinVar.1
Natural variantiVAR_065408364R → W in FA7D. 1 PublicationCorresponds to variant dbSNP:rs750980786Ensembl.1
Natural variantiVAR_006515370C → F in FA7D. 6 PublicationsCorresponds to variant dbSNP:rs121964927EnsemblClinVar.1
Natural variantiVAR_065409375R → W in FA7D. 1 PublicationCorresponds to variant dbSNP:rs137919286Ensembl.1
Natural variantiVAR_065410384T → M in FA7D. 2 PublicationsCorresponds to variant dbSNP:rs531225271EnsemblClinVar.1
Natural variantiVAR_065411387M → T in FA7D. 1 Publication1
Natural variantiVAR_065412387M → V in FA7D. 1 Publication1
Natural variantiVAR_065413388F → S in FA7D; reduces tissue factor binding; impairs activation by factor Xa; abolishes amidolytic and coagulant activities. 2 PublicationsCorresponds to variant dbSNP:rs121964938Ensembl.1
Natural variantiVAR_014392389C → G in FA7D. 3 PublicationsCorresponds to variant dbSNP:rs121964934EnsemblClinVar.1
Natural variantiVAR_065414391G → C in FA7D. 1 Publication1
Natural variantiVAR_014419391G → S in FA7D. 2 PublicationsCorresponds to variant dbSNP:rs190485816Ensembl.1
Natural variantiVAR_065415398D → E in FA7D. 1 Publication1
Natural variantiVAR_065416401K → E in FA7D. 1 PublicationCorresponds to variant dbSNP:rs748979195Ensembl.1
Natural variantiVAR_006517402G → E in FA7D. 1 Publication1
Natural variantiVAR_006516402G → R in FA7D. 1 Publication1
Natural variantiVAR_015144403D → H in FA7D. 2 Publications1
Natural variantiVAR_065417404S → N in FA7D. 1 Publication1
Natural variantiVAR_065418408H → Q in FA7D. 1 PublicationCorresponds to variant dbSNP:rs121964936EnsemblClinVar.1
Natural variantiVAR_065419408H → R in FA7D. 1 Publication1
Natural variantiVAR_065420413R → G in FA7D. 1 Publication1
Natural variantiVAR_065421414G → C in FA7D; results in severely impaired protein secretion. 1 PublicationCorresponds to variant dbSNP:rs121964937Ensembl.1
Natural variantiVAR_006519419T → M in FA7D. 3 PublicationsCorresponds to variant dbSNP:rs121964930Ensembl.1
Natural variantiVAR_065422422V → F in FA7D. 1 Publication1
Natural variantiVAR_065423425G → A in FA7D. 1 Publication1
Natural variantiVAR_065424425G → C in FA7D. 1 Publication1
Natural variantiVAR_065425429A → T in FA7D. 1 PublicationCorresponds to variant dbSNP:rs755377592EnsemblClinVar.1
Natural variantiVAR_065426432G → D in FA7D. 1 Publication1
Natural variantiVAR_014420435G → E in FA7D. 2 PublicationsCorresponds to variant dbSNP:rs756956471Ensembl.1
Natural variantiVAR_065427437Y → F in FA7D. 1 PublicationCorresponds to variant dbSNP:rs758213652Ensembl.1

Pharmaceutical usei

Available under the names Niastase or Novoseven (Novo Nordisk). Used for the treatment of bleeding episodes in hemophilia A or B patients with antibodies to coagulation factors VIII or IX.

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi112S → A: Complete loss of O-glycosylation and O-xylosylation by POGLUT1. 1 Publication1
Mutagenesisi113S → A: No effect on O-glycosylation by POGLUT1. Drastic decrease in O-xylosylation. 1 Publication1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNETi2155
MalaCardsiF7
MIMi227500 phenotype
OpenTargetsiENSG00000057593
Orphaneti327 Congenital factor VII deficiency
PharmGKBiPA160

Chemistry databases

ChEMBLiCHEMBL3991
DrugBankiDB04590 (2R)-({4-[AMINO(IMINO)METHYL]PHENYL}AMINO){5-ETHOXY-2-FLUORO-3-[(3R)-TETRAHYDROFURAN-3-YLOXY]PHENYL}ACETICACID
DB07207 2-(4-HYDROXY-5-PHENYL-1H-PYRAZOL-3-YL)-1H-BENZOIMIDAZOLE-5-CARBOXAMIDINE
DB04758 2-[2-ETHANESULFONYLAMINO-3-(1H-INDOL-3-YL)-PROPIONYLAMINO]-PENTANEDIOIC ACID 5-AMIDE 1-(4-CARBAMIM IDOYL-BENZYLAMIDE)
DB04606 2-[2-ETHANESULFONYLAMINO-3-(5-PROPOXY-1H-INDOL-3-YL)-PROPIONYLAMINO]-PENTANEDIOIC ACID 5-AMIDE 1-(4-CARBAMIMIDOYL-BENZYLAMIDE)
DB04593 3-({1-[3-CARBAMIMIDOYL-1-(4-CARBAMIMIDOYL-BENZYLCARBAMOYL)-PROPYLCARBAMOYL]-2-METHYL-BUTYLSULFAMOYL}-METHYL)-BENZOIC ACID
DB07376 5-(DIMETHYLAMINO)-1-NAPHTHALENESULFONIC ACID(DANSYL ACID)
DB00100 Coagulation Factor IX (Recombinant)
DB00036 Coagulation factor VIIa Recombinant Human
DB00170 Menadione
DB04767 N-[1-(4-CARBAMIMIDOYL-BENZYLCARBAMOYL)-3-METHYLSULFANYL-PROPYL]-3-HYDROXY-2-PROPOXYAMINO-BUTYRAMID
GuidetoPHARMACOLOGYi2363

Polymorphism and mutation databases

BioMutaiF7
DMDMi119766

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 20Sequence analysisAdd BLAST20
PropeptideiPRO_000002772921 – 601 PublicationAdd BLAST40
ChainiPRO_000002773061 – 212Factor VII light chainAdd BLAST152
ChainiPRO_0000027731213 – 466Factor VII heavy chainAdd BLAST254

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei664-carboxyglutamatePROSITE-ProRule annotation2 Publications1
Modified residuei674-carboxyglutamatePROSITE-ProRule annotation2 Publications1
Modified residuei744-carboxyglutamatePROSITE-ProRule annotation2 Publications1
Modified residuei764-carboxyglutamatePROSITE-ProRule annotation2 Publications1
Disulfide bondi77 ↔ 82
Modified residuei794-carboxyglutamatePROSITE-ProRule annotation1 Publication1
Modified residuei804-carboxyglutamatePROSITE-ProRule annotation2 Publications1
Modified residuei854-carboxyglutamatePROSITE-ProRule annotation2 Publications1
Modified residuei864-carboxyglutamatePROSITE-ProRule annotation2 Publications1
Modified residuei894-carboxyglutamatePROSITE-ProRule annotation2 Publications1
Modified residuei954-carboxyglutamatePROSITE-ProRule annotation2 Publications1
Disulfide bondi110 ↔ 121
GlycosylationiCAR_000007112O-linked (Glc...) serine; alternate4 Publications1
Glycosylationi112O-linked (Xyl...) serine; alternate4 Publications1
Disulfide bondi115 ↔ 130
GlycosylationiCAR_000180120O-linked (Fuc) serine2 Publications1
Modified residuei123(3R)-3-hydroxyaspartate1 Publication1
Disulfide bondi132 ↔ 141
Disulfide bondi151 ↔ 162
Disulfide bondi158 ↔ 172
Disulfide bondi174 ↔ 187
Disulfide bondi195 ↔ 322
Glycosylationi205N-linked (GlcNAc...) asparagine2 Publications1
Disulfide bondi219 ↔ 224
Disulfide bondi238 ↔ 254
Disulfide bondi370 ↔ 389
Glycosylationi382N-linked (GlcNAc...) asparagine2 Publications1
Disulfide bondi400 ↔ 428

Post-translational modificationi

The vitamin K-dependent, enzymatic carboxylation of some glutamate residues allows the modified protein to bind calcium.
The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate and asparagine is (R) stereospecific within EGF domains.1 Publication
O- and N-glycosylated. N-glycosylation at Asn-205 occurs cotranslationally and is mediated by STT3A-containing complexes, while glycosylation at Asn-382 is post-translational and is mediated STT3B-containing complexes before folding. 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.5 Publications
Can be either O-glucosylated or O-xylosylated at Ser-112 by POGLUT1 in vitro.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei212 – 213Cleavage; by factor Xa, factor XIIa, factor IXa, or thrombin2

Keywords - PTMi

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

Proteomic databases

MaxQBiP08709
PaxDbiP08709
PeptideAtlasiP08709
PRIDEiP08709
ProteomicsDBi52160
52161 [P08709-2]

PTM databases

GlyConnecti98
iPTMnetiP08709
PhosphoSitePlusiP08709
UniCarbKBiP08709

Miscellaneous databases

PMAP-CutDBiP08709

Expressioni

Tissue specificityi

Plasma.

Gene expression databases

BgeeiENSG00000057593
CleanExiHS_F7
ExpressionAtlasiP08709 baseline and differential
GenevisibleiP08709 HS

Organism-specific databases

HPAiHPA004826

Interactioni

Subunit structurei

Heterodimer of a light chain and a heavy chain linked by a disulfide bond.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
F3P137267EBI-355972,EBI-1040727

GO - Molecular functioni

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridi108453, 19 interactors
ComplexPortaliCPX-2808 Factor VII - TF complex
CORUMiP08709
DIPiDIP-6135N
ELMiP08709
IntActiP08709, 11 interactors
STRINGi9606.ENSP00000364731

Chemistry databases

BindingDBiP08709

Structurei

Secondary structure

1466
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi66 – 68Combined sources3
Helixi73 – 77Combined sources5
Helixi84 – 91Combined sources8
Helixi94 – 104Combined sources11
Turni109 – 112Combined sources4
Turni116 – 118Combined sources3
Beta strandi120 – 124Combined sources5
Beta strandi127 – 131Combined sources5
Beta strandi136 – 138Combined sources3
Helixi145 – 147Combined sources3
Beta strandi148 – 150Combined sources3
Turni151 – 153Combined sources3
Helixi154 – 157Combined sources4
Beta strandi159 – 165Combined sources7
Turni166 – 168Combined sources3
Beta strandi169 – 173Combined sources5
Beta strandi178 – 180Combined sources3
Beta strandi187 – 189Combined sources3
Beta strandi191 – 193Combined sources3
Helixi199 – 205Combined sources7
Helixi220 – 222Combined sources3
Beta strandi227 – 232Combined sources6
Beta strandi235 – 242Combined sources8
Beta strandi244 – 250Combined sources7
Helixi252 – 255Combined sources4
Helixi261 – 263Combined sources3
Beta strandi264 – 269Combined sources6
Beta strandi272 – 274Combined sources3
Beta strandi281 – 291Combined sources11
Beta strandi298 – 301Combined sources4
Beta strandi304 – 310Combined sources7
Helixi326 – 331Combined sources6
Helixi333 – 335Combined sources3
Beta strandi338 – 344Combined sources7
Beta strandi346 – 348Combined sources3
Turni352 – 355Combined sources4
Beta strandi358 – 365Combined sources8
Helixi367 – 373Combined sources7
Turni376 – 378Combined sources3
Turni380 – 382Combined sources3
Helixi383 – 386Combined sources4
Beta strandi387 – 391Combined sources5
Beta strandi393 – 398Combined sources6
Helixi401 – 403Combined sources3
Beta strandi407 – 412Combined sources6
Beta strandi415 – 422Combined sources8
Turni427 – 429Combined sources3
Beta strandi435 – 439Combined sources5
Helixi440 – 443Combined sources4
Helixi444 – 451Combined sources8
Beta strandi457 – 463Combined sources7

3D structure databases

ProteinModelPortaliP08709
SMRiP08709
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP08709

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini61 – 105GlaPROSITE-ProRule annotationAdd BLAST45
Domaini106 – 142EGF-like 1; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini147 – 188EGF-like 2PROSITE-ProRule annotationAdd BLAST42
Domaini213 – 452Peptidase 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
HOVERGENiHBG013304
InParanoidiP08709
KOiK01320
OMAiCEQYCSD
OrthoDBiEOG091G0AH5
PhylomeDBiP08709
TreeFamiTF327329

Family and domain databases

CDDicd00190 Tryp_SPc, 1 hit
Gene3Di4.10.740.10, 1 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
PS01186 EGF_2, 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

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform A (identifier: P08709-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

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        10         20         30         40         50
MVSQALRLLC LLLGLQGCLA AGGVAKASGG ETRDMPWKPG PHRVFVTQEE 
        60         70         80         90        100
AHGVLHRRRR ANAFLEELRP GSLERECKEE QCSFEEAREI FKDAERTKLF 
       110        120        130        140        150
WISYSDGDQC ASSPCQNGGS CKDQLQSYIC FCLPAFEGRN CETHKDDQLI 
       160        170        180        190        200
CVNENGGCEQ YCSDHTGTKR SCRCHEGYSL LADGVSCTPT VEYPCGKIPI 
       210        220        230        240        250
LEKRNASKPQ GRIVGGKVCP KGECPWQVLL LVNGAQLCGG TLINTIWVVS 
       260        270        280        290        300
AAHCFDKIKN WRNLIAVLGE HDLSEHDGDE QSRRVAQVII PSTYVPGTTN 
       310        320        330        340        350
HDIALLRLHQ PVVLTDHVVP LCLPERTFSE RTLAFVRFSL VSGWGQLLDR 
       360        370        380        390        400
GATALELMVL NVPRLMTQDC LQQSRKVGDS PNITEYMFCA GYSDGSKDSC 
       410        420        430        440        450
KGDSGGPHAT HYRGTWYLTG IVSWGQGCAT VGHFGVYTRV SQYIEWLQKL 
       460 
MRSEPRPGVL LRAPFP
Length:466
Mass (Da):51,594
Last modified:January 1, 1988 - v1
Checksum:i9B5D501669D67B06
GO
Isoform B (identifier: P08709-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     22-43: Missing.

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Length:444
Mass (Da):49,320
Checksum:i2E74EAFD2FADF2A4
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_01439113L → P in FA7D; Morioka. 1 PublicationCorresponds to variant dbSNP:rs387906507EnsemblClinVar.1
Natural variantiVAR_06536959R → RR in FA7D. 1 Publication1
Natural variantiVAR_01513564F → L in FA7D. 2 Publications1
Natural variantiVAR_01440573L → Q in FA7D. 2 Publications