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Protein

Coagulation factor VII

Gene

F7

Organism
Homo sapiens (Human)
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)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
  • glycoprotein binding Source: BHF-UCL
  • serine-type endopeptidase activity Source: ProtInc
  • serine-type peptidase activity Source: ProtInc

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

BioCyciZFISH:HS00709-MONOMER.
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-RKP08709.

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:
Gene namesi
Name:F7
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 13

Organism-specific databases

HGNCiHGNC:3544. F7.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

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 rs387906507dbSNPEnsembl.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 rs45572939dbSNPEnsembl.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 rs745374448dbSNPEnsembl.1
Natural variantiVAR_06537284Missing in FA7D. 1 Publication1
Natural variantiVAR_06537385E → K in FA7D. 1 PublicationCorresponds to variant rs121964935dbSNPEnsembl.1
Natural variantiVAR_06537488R → G in FA7D. 1 PublicationCorresponds to variant rs776354144dbSNPEnsembl.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 rs121964932dbSNPEnsembl.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 rs150525536dbSNPEnsembl.1
Natural variantiVAR_006499139R → W in FA7D. 2 PublicationsCorresponds to variant rs776796178dbSNPEnsembl.1
Natural variantiVAR_014410151C → S in FA7D. 1 Publication1
Natural variantiVAR_015137154E → K in FA7D. 2 PublicationsCorresponds to variant rs146795869dbSNPEnsembl.1
Natural variantiVAR_065378156G → S in FA7D. 1 PublicationCorresponds to variant rs563972504dbSNPEnsembl.1
Natural variantiVAR_006501157G → C in FA7D. 1
Natural variantiVAR_006500157G → S in FA7D. 2 PublicationsCorresponds to variant rs763458490dbSNPEnsembl.1
Natural variantiVAR_014411157G → V in FA7D. 1 PublicationCorresponds to variant rs771335282dbSNPEnsembl.1
Natural variantiVAR_006502160Q → R in FA7D. 4 PublicationsCorresponds to variant rs200016360dbSNPEnsembl.1
Natural variantiVAR_065379171S → F in FA7D. 1 PublicationCorresponds to variant rs143855920dbSNPEnsembl.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 rs764971156dbSNPEnsembl.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 rs372577568dbSNPEnsembl.1
Natural variantiVAR_006504197K → E in FA7D. 1 Publication1
Natural variantiVAR_065386198I → T in FA7D. 1 PublicationCorresponds to variant rs762621913dbSNPEnsembl.1
Natural variantiVAR_006505212R → Q in FA7D; Charlotte. 4 Publications1
Natural variantiVAR_015138216G → D in FA7D. 2 Publications1
Natural variantiVAR_006506238C → Y in FA7D. 1 PublicationCorresponds to variant rs121964928dbSNPEnsembl.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 rs753266903dbSNPEnsembl.1
Natural variantiVAR_015140266A → T in FA7D. 2 PublicationsCorresponds to variant rs764807079dbSNPEnsembl.1
Natural variantiVAR_065393272D → N in FA7D. 1 PublicationCorresponds to variant rs751028917dbSNPEnsembl.1
Natural variantiVAR_065394277D → N in FA7D. 1 PublicationCorresponds to variant rs550074221dbSNPEnsembl.1
Natural variantiVAR_006507283R → W in FA7D. 2 PublicationsCorresponds to variant rs779589651dbSNPEnsembl.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 rs770328850dbSNPEnsembl.1
Natural variantiVAR_014416304A → T in FA7D. 2 PublicationsCorresponds to variant rs773627551dbSNPEnsembl.1
Natural variantiVAR_006508304A → V in FA7D; Malta-II. 5 PublicationsCorresponds to variant rs121964931dbSNPEnsembl.1
Natural variantiVAR_014417307R → C in FA7D. 3 PublicationsCorresponds to variant rs147680958dbSNPEnsembl.1
Natural variantiVAR_006509307R → H in FA7D; Mie. 2 PublicationsCorresponds to variant rs121964929dbSNPEnsembl.1
Natural variantiVAR_015141312V → M in FA7D. 2 PublicationsCorresponds to variant rs201991361dbSNPEnsembl.1
Natural variantiVAR_065397314L → V in FA7D. 1 Publication1
Natural variantiVAR_065398321L → F in FA7D. 1 PublicationCorresponds to variant rs778138366dbSNPEnsembl.1
Natural variantiVAR_065399323L → R in FA7D. 1 Publication1
Natural variantiVAR_006510325E → K in FA7D. 3 PublicationsCorresponds to variant rs749760143dbSNPEnsembl.1
Natural variantiVAR_065400326R → Q in FA7D. 1 PublicationCorresponds to variant rs146698837dbSNPEnsembl.1
Natural variantiVAR_014418332T → M in FA7D. 1 PublicationCorresponds to variant rs200212201dbSNPEnsembl.1
Natural variantiVAR_065401337R → C in FA7D. 1 PublicationCorresponds to variant rs139372641dbSNPEnsembl.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 rs747876824dbSNPEnsembl.1
Natural variantiVAR_006511354A → V in FA7D. 5 PublicationsCorresponds to variant rs36209567dbSNPEnsembl.1
Natural variantiVAR_006512358M → I in FA7D. 4 PublicationsCorresponds to variant rs149283257dbSNPEnsembl.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 Publications1
Natural variantiVAR_006514364R → Q in FA7D; Harrow/Padua. 6 PublicationsCorresponds to variant rs121964926dbSNPEnsembl.1
Natural variantiVAR_065408364R → W in FA7D. 1 PublicationCorresponds to variant rs750980786dbSNPEnsembl.1
Natural variantiVAR_006515370C → F in FA7D. 6 PublicationsCorresponds to variant rs121964927dbSNPEnsembl.1
Natural variantiVAR_065409375R → W in FA7D. 1 PublicationCorresponds to variant rs137919286dbSNPEnsembl.1
Natural variantiVAR_065410384T → M in FA7D. 2 PublicationsCorresponds to variant rs531225271dbSNPEnsembl.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 rs121964938dbSNPEnsembl.1
Natural variantiVAR_014392389C → G in FA7D. 3 PublicationsCorresponds to variant rs121964934dbSNPEnsembl.1
Natural variantiVAR_065414391G → C in FA7D. 1 Publication1
Natural variantiVAR_014419391G → S in FA7D. 2 PublicationsCorresponds to variant rs190485816dbSNPEnsembl.1
Natural variantiVAR_065415398D → E in FA7D. 1 Publication1
Natural variantiVAR_065416401K → E in FA7D. 1 PublicationCorresponds to variant rs748979195dbSNPEnsembl.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 rs121964936dbSNPEnsembl.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 rs121964937dbSNPEnsembl.1
Natural variantiVAR_006519419T → M in FA7D. 3 PublicationsCorresponds to variant rs121964930dbSNPEnsembl.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 rs755377592dbSNPEnsembl.1
Natural variantiVAR_065426432G → D in FA7D. 1 Publication1
Natural variantiVAR_014420435G → E in FA7D. 2 PublicationsCorresponds to variant rs756956471dbSNPEnsembl.1
Natural variantiVAR_065427437Y → F in FA7D. 1 PublicationCorresponds to variant rs758213652dbSNPEnsembl.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.
DrugBankiDB00100. Coagulation Factor IX.
DB00036. Coagulation factor VIIa.
DB00170. Menadione.
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...)2 Publications1
Glycosylationi112O-linked (Glc...); alternate2 Publications1
Glycosylationi112O-linked (Xyl...); alternate2 Publications1
Disulfide bondi115 ↔ 130
GlycosylationiCAR_000180120O-linked (Fuc)2 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...)2 Publications1
Disulfide bondi219 ↔ 224
Disulfide bondi238 ↔ 254
Disulfide bondi370 ↔ 389
Glycosylationi382N-linked (GlcNAc...)2 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.

PTM databases

iPTMnetiP08709.
PhosphoSitePlusiP08709.
UniCarbKBiP08709.

Miscellaneous databases

PMAP-CutDBP08709.

Expressioni

Tissue specificityi

Plasma.

Gene expression databases

BgeeiENSG00000057593.
CleanExiHS_F7.
ExpressionAtlasiP08709. baseline and differential.
GenevisibleiP08709. HS.

Organism-specific databases

HPAiCAB034432.
CAB037309.

Interactioni

Subunit structurei

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

Binary interactionsi

WithEntry#Exp.IntActNotes
F3P137266EBI-355972,EBI-1040727

Protein-protein interaction databases

BioGridi108453. 15 interactors.
DIPiDIP-6135N.
IntActiP08709. 10 interactors.
MINTiMINT-1155299.
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
Beta strandi168 – 173Combined sources6
Beta strandi178 – 180Combined sources3
Beta strandi187 – 193Combined sources7
Turni199 – 201Combined sources3
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 strandi337 – 348Combined sources12
Turni352 – 355Combined sources4
Beta strandi358 – 365Combined sources8
Helixi367 – 370Combined sources4
Helixi372 – 374Combined sources3
Turni376 – 378Combined sources3
Turni380 – 382Combined sources3
Helixi383 – 386Combined sources4
Beta strandi387 – 391Combined sources5
Beta strandi393 – 396Combined sources4
Helixi401 – 403Combined sources3
Beta strandi407 – 412Combined sources6
Beta strandi415 – 424Combined sources10
Beta strandi426 – 429Combined sources4
Beta strandi435 – 439Combined sources5
Helixi440 – 443Combined sources4
Helixi444 – 452Combined sources9
Beta strandi459 – 463Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1BF9NMR-A105-145[»]
1CVWX-ray2.28H213-466[»]
L150-204[»]
1DANX-ray2.00H213-466[»]
L61-212[»]
1DVAX-ray3.00H/I213-466[»]
L/M102-202[»]
1F7ENMR-A105-147[»]
1F7MNMR-A105-147[»]
1FAKX-ray2.10H213-466[»]
L61-212[»]
1FF7NMR-A105-147[»]
1FFMNMR-A105-147[»]
1J9CX-ray2.90H213-466[»]
L108-202[»]
1JBUX-ray2.00H213-466[»]
L150-212[»]
1KLIX-ray1.69H213-466[»]
L144-212[»]
1KLJX-ray2.44H213-466[»]
L144-212[»]
1NL8model-H213-466[»]
M61-202[»]
1O5DX-ray2.05H213-466[»]
L61-212[»]
1QFKX-ray2.80H213-466[»]
L109-212[»]
1W0YX-ray2.50H213-466[»]
L61-202[»]
1W2KX-ray3.00H213-466[»]
L61-202[»]
1W7XX-ray1.80H213-466[»]
L150-204[»]
1W8BX-ray3.00H213-466[»]
L148-204[»]
1WQVX-ray2.50H213-466[»]
L61-212[»]
1WSSX-ray2.60H213-466[»]
L61-212[»]
1WTGX-ray2.20H213-466[»]
L61-212[»]
1WUNX-ray2.40H213-466[»]
L61-212[»]
1WV7X-ray2.70H213-466[»]
L61-212[»]
1YGCX-ray2.00H213-466[»]
L150-212[»]
1Z6JX-ray2.00H213-466[»]
L61-202[»]
2A2QX-ray1.80H213-466[»]
L61-212[»]
2AEIX-ray2.52H213-466[»]
L61-212[»]
2AERX-ray1.87H213-466[»]
L61-202[»]
2B7DX-ray2.24H213-466[»]
L61-212[»]
2B8OX-ray2.80H213-466[»]
L61-202[»]
2BZ6X-ray1.60H213-466[»]
L150-202[»]
2C4FX-ray1.72H213-466[»]
L61-202[»]
2EC9X-ray2.00H213-466[»]
L61-202[»]
2F9BX-ray2.54H213-466[»]
L61-212[»]
2FIRX-ray2.00H213-466[»]
L61-202[»]
2FLBX-ray1.95H213-466[»]
L61-212[»]
2FLRX-ray2.35H213-466[»]
L61-212[»]
2PUQX-ray2.05H213-466[»]
L109-202[»]
2ZP0X-ray2.70H213-466[»]
L61-212[»]
2ZWLX-ray2.20H213-466[»]
L61-212[»]
2ZZUX-ray2.50H213-466[»]
L61-212[»]
3ELAX-ray2.20H213-466[»]
L61-212[»]
3TH2X-ray1.72H213-466[»]
L61-202[»]
3TH3X-ray2.70H213-466[»]
L61-202[»]
3TH4X-ray1.80H213-466[»]
L61-202[»]
4IBLX-ray1.80H213-466[»]
L61-212[»]
4ISHX-ray1.82H213-466[»]
L150-204[»]
4ISIX-ray1.94H213-466[»]
L150-204[»]
4JYUX-ray1.80H213-466[»]
L150-204[»]
4JYVX-ray2.19H213-466[»]
L150-204[»]
4JZDX-ray2.20H213-466[»]
L150-204[»]
4JZEX-ray1.52H213-466[»]
L150-204[»]
4JZFX-ray1.84H213-466[»]
L150-204[»]
4NA9X-ray2.24H213-466[»]
L150-204[»]
4NG9X-ray2.20H213-466[»]
L150-204[»]
4NGAX-ray2.15H213-466[»]
L150-204[»]
4X8SX-ray2.10H213-466[»]
L150-204[»]
4X8TX-ray2.20H213-466[»]
L150-204[»]
4X8UX-ray2.10H213-466[»]
L150-204[»]
4X8VX-ray2.50H213-466[»]
L150-204[»]
4YLQX-ray1.40H213-466[»]
L61-212[»]
4YT6X-ray2.07H213-466[»]
L148-204[»]
4YT7X-ray2.30H213-466[»]
L148-204[»]
4Z6AX-ray2.25H213-466[»]
L108-203[»]
4ZMAX-ray2.30H213-466[»]
L61-212[»]
4ZXXX-ray2.60H213-466[»]
L150-204[»]
4ZXYX-ray2.06H213-466[»]
L150-204[»]
5I46X-ray2.06H213-466[»]
L150-204[»]
5L2YX-ray1.82H213-466[»]
L150-204[»]
5L2ZX-ray1.79H213-466[»]
L147-204[»]
5L30X-ray1.73H213-466[»]
L147-204[»]
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
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.
HOVERGENiHBG013304.
InParanoidiP08709.
KOiK01320.
OMAiCEQYCSD.
OrthoDBiEOG091G0AH5.
PhylomeDBiP08709.
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. 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]

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.

« Hide

        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.

Show »
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 rs387906507dbSNPEnsembl.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 rs45572939dbSNPEnsembl.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 rs745374448dbSNPEnsembl.1
Natural variantiVAR_06537284Missing in FA7D. 1 Publication1