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P08709

- FA7_HUMAN

UniProt

P08709 - FA7_HUMAN

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Protein

Coagulation factor VII

Gene

F7

Organism
Homo sapiens (Human)
Status
Reviewed - 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
Sitei113 – 1131Important for S-112 for O-xylosylation
Sitei212 – 2132Cleavage; by factor Xa, factor XIIa, factor IXa, or thrombin
Active sitei253 – 2531Charge relay systemBy similarity
Active sitei302 – 3021Charge relay systemBy similarity
Binding sitei398 – 3981SubstrateBy similarity
Active sitei404 – 4041Charge relay systemBy similarity

GO - Molecular functioni

  1. calcium ion binding Source: InterPro
  2. glycoprotein binding Source: BHF-UCL
  3. serine-type endopeptidase activity Source: ProtInc
  4. serine-type peptidase activity Source: ProtInc

GO - Biological processi

  1. blood coagulation Source: Reactome
  2. blood coagulation, extrinsic pathway Source: Reactome
  3. cellular protein metabolic process Source: Reactome
  4. circadian rhythm Source: Ensembl
  5. organ regeneration Source: Ensembl
  6. peptidyl-glutamic acid carboxylation Source: Reactome
  7. positive regulation of blood coagulation Source: Ensembl
  8. positive regulation of cell migration Source: BHF-UCL
  9. positive regulation of leukocyte chemotaxis Source: BHF-UCL
  10. positive regulation of platelet-derived growth factor receptor signaling pathway Source: BHF-UCL
  11. positive regulation of positive chemotaxis Source: BHF-UCL
  12. positive regulation of protein kinase B signaling Source: BHF-UCL
  13. post-translational protein modification Source: Reactome
  14. proteolysis Source: Reactome
  15. response to estrogen Source: Ensembl
  16. response to growth hormone Source: Ensembl
  17. response to vitamin K Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Serine protease

Keywords - Biological processi

Blood coagulation, Hemostasis

Keywords - Ligandi

Calcium

Enzyme and pathway databases

ReactomeiREACT_1050. Gamma-carboxylation of protein precursors.
REACT_111118. BMAL1:CLOCK,NPAS2 activates circadian gene expression.
REACT_1573. Extrinsic Pathway.
REACT_1906. Transport of gamma-carboxylated protein precursors from the endoplasmic reticulum to the Golgi apparatus.
REACT_733. 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
ProteomesiUP000005640: Chromosome 13

Organism-specific databases

HGNCiHGNC:3544. F7.

Subcellular locationi

GO - Cellular componenti

  1. endoplasmic reticulum lumen Source: Reactome
  2. extracellular region Source: Reactome
  3. extracellular space Source: Ensembl
  4. Golgi lumen Source: Reactome
  5. plasma membrane Source: Reactome
  6. vesicle Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Involvement in diseasei

Factor VII deficiency (FA7D) [MIM:227500]: A 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.24 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti13 – 131L → P in FA7D; Morioka. 1 Publication
VAR_014391
Natural varianti59 – 591R → RR in FA7D. 1 Publication
VAR_065369
Natural varianti64 – 641F → L in FA7D. 2 Publications
VAR_015135
Natural varianti73 – 731L → Q in FA7D. 2 Publications
Corresponds to variant rs45572939 [ dbSNP | Ensembl ].
VAR_014405
Natural varianti79 – 791E → Q in FA7D. 1 Publication
VAR_014406
Natural varianti82 – 821C → F in FA7D. 1 Publication
VAR_065370
Natural varianti82 – 821C → R in FA7D. 1 Publication
VAR_065371
Natural varianti84 – 841Missing in FA7D. 1 Publication
VAR_065372
Natural varianti85 – 851E → K in FA7D. 1 Publication
VAR_065373
Natural varianti88 – 881R → G in FA7D. 1 Publication
VAR_065374
Natural varianti88 – 881R → P in FA7D. 1 Publication
VAR_065375
Natural varianti117 – 1171N → D in FA7D; exhibits no procoagulant activity and is unable to bind tissue factor. 1 Publication
VAR_065376
Natural varianti120 – 1201S → P in FA7D. 2 Publications
VAR_015136
Natural varianti121 – 1211C → F in FA7D. 1 Publication
VAR_014407
Natural varianti125 – 1251L → P in FA7D. 1 Publication
VAR_014408
Natural varianti128 – 1281Y → C in FA7D. 3 Publications
VAR_014409
Natural varianti138 – 1381G → D in FA7D. 1 Publication
VAR_065377
Natural varianti139 – 1391R → K in FA7D.
VAR_006497
Natural varianti139 – 1391R → Q in FA7D; Charlotte. 2 Publications
Corresponds to variant rs150525536 [ dbSNP | Ensembl ].
VAR_006498
Natural varianti139 – 1391R → W in FA7D. 1 Publication
VAR_006499
Natural varianti151 – 1511C → S in FA7D. 1 Publication
VAR_014410
Natural varianti154 – 1541E → K in FA7D. 2 Publications
Corresponds to variant rs146795869 [ dbSNP | Ensembl ].
VAR_015137
Natural varianti156 – 1561G → S in FA7D. 1 Publication
VAR_065378
Natural varianti157 – 1571G → C in FA7D.
VAR_006501
Natural varianti157 – 1571G → S in FA7D. 2 Publications
VAR_006500
Natural varianti157 – 1571G → V in FA7D. 1 Publication
VAR_014411
Natural varianti160 – 1601Q → R in FA7D. 3 Publications
VAR_006502
Natural varianti171 – 1711S → F in FA7D. 1 Publication
VAR_065379
Natural varianti177 – 1771G → R in FA7D. 1 Publication
VAR_065380
Natural varianti181 – 1811L → P in FA7D. 1 Publication
VAR_065381
Natural varianti183 – 1831D → N in FA7D. 1 Publication
VAR_065382
Natural varianti186 – 1861S → F in FA7D. 1 Publication
VAR_065383
Natural varianti189 – 1891P → S in FA7D. 1 Publication
VAR_065384
Natural varianti194 – 1941P → L in FA7D. 1 Publication
VAR_065385
Natural varianti194 – 1941P → T in FA7D; Malta-I. 2 Publications
VAR_006503
Natural varianti195 – 1951C → R in FA7D. 3 Publications
VAR_014412
Natural varianti197 – 1971K → E in FA7D.
VAR_006504
Natural varianti198 – 1981I → T in FA7D. 1 Publication
VAR_065386
Natural varianti212 – 2121R → Q in FA7D; Charlotte. 4 Publications
VAR_006505
Natural varianti216 – 2161G → D in FA7D. 2 Publications
VAR_015138
Natural varianti238 – 2381C → Y in FA7D. 1 Publication
VAR_006506
Natural varianti240 – 2401G → R in FA7D. 1 Publication
VAR_065387
Natural varianti241 – 2411T → N in FA7D. 2 Publications
VAR_014413
Natural varianti250 – 2501S → F in FA7D. 1 Publication
VAR_065388
Natural varianti251 – 2511A → P in FA7D. 1 Publication
VAR_065389
Natural varianti251 – 2511A → T in FA7D. 1 Publication
VAR_065390
Natural varianti254 – 2541C → R in FA7D. 1 Publication
VAR_065391
Natural varianti254 – 2541C → Y in FA7D. 2 Publications
VAR_015139
Natural varianti264 – 2641L → P in FA7D. 1 Publication
VAR_065392
Natural varianti266 – 2661A → T in FA7D. 2 Publications
VAR_015140
Natural varianti272 – 2721D → N in FA7D. 1 Publication
VAR_065393
Natural varianti277 – 2771D → N in FA7D. 1 Publication
VAR_065394
Natural varianti283 – 2831R → W in FA7D. 2 Publications
VAR_006507
Natural varianti298 – 2981T → I in FA7D. 1 Publication
VAR_065395
Natural varianti301 – 3011H → Q in FA7D. 1 Publication
VAR_065396
Natural varianti302 – 3021D → H in FA7D. 3 Publications
VAR_014414
Natural varianti302 – 3021D → N in FA7D. 2 Publications
VAR_014415
Natural varianti304 – 3041A → T in FA7D. 2 Publications
VAR_014416
Natural varianti304 – 3041A → V in FA7D; Malta-II. 5 Publications
VAR_006508
Natural varianti307 – 3071R → C in FA7D. 3 Publications
VAR_014417
Natural varianti307 – 3071R → H in FA7D; Mie. 2 Publications
VAR_006509
Natural varianti312 – 3121V → M in FA7D. 2 Publications
VAR_015141
Natural varianti314 – 3141L → V in FA7D. 1 Publication
VAR_065397
Natural varianti321 – 3211L → F in FA7D. 1 Publication
VAR_065398
Natural varianti323 – 3231L → R in FA7D. 1 Publication
VAR_065399
Natural varianti325 – 3251E → K in FA7D. 3 Publications
VAR_006510
Natural varianti326 – 3261R → Q in FA7D. 1 Publication
VAR_065400
Natural varianti332 – 3321T → M in FA7D. 1 Publication
VAR_014418
Natural varianti337 – 3371R → C in FA7D. 1 Publication
VAR_065401
Natural varianti341 – 3411V → F in FA7D. 2 Publications
VAR_015142
Natural varianti343 – 3431G → S in FA7D. 2 Publications
VAR_065402
Natural varianti344 – 3441W → R in FA7D. 1 Publication
VAR_065403
Natural varianti345 – 3451G → S in FA7D. 1 Publication
VAR_065404
Natural varianti350 – 3501R → C in FA7D. 1 Publication
VAR_065405
Natural varianti354 – 3541A → V in FA7D. 5 Publications
Corresponds to variant rs36209567 [ dbSNP | Ensembl ].
VAR_006511
Natural varianti358 – 3581M → I in FA7D. 4 Publications
VAR_006512
Natural varianti358 – 3581M → V in FA7D. 1 Publication
VAR_006513
Natural varianti360 – 3601L → P in FA7D. 1 Publication
VAR_065406
Natural varianti363 – 3631P → H in FA7D. 1 Publication
VAR_065407
Natural varianti363 – 3631P → R in FA7D. 2 Publications
VAR_015143
Natural varianti364 – 3641R → Q in FA7D; Harrow/Padua. 5 Publications
Corresponds to variant rs121964926 [ dbSNP | Ensembl ].
VAR_006514
Natural varianti364 – 3641R → W in FA7D. 1 Publication
VAR_065408
Natural varianti370 – 3701C → F in FA7D. 6 Publications
VAR_006515
Natural varianti375 – 3751R → W in FA7D. 1 Publication
Corresponds to variant rs137919286 [ dbSNP | Ensembl ].
VAR_065409
Natural varianti384 – 3841T → M in FA7D. 2 Publications
VAR_065410
Natural varianti387 – 3871M → T in FA7D. 1 Publication
VAR_065411
Natural varianti387 – 3871M → V in FA7D. 1 Publication
VAR_065412
Natural varianti388 – 3881F → S in FA7D; reduces tissue factor binding; impairs activation by factor Xa; abolishes amidolytic and coagulant activities. 2 Publications
VAR_065413
Natural varianti389 – 3891C → G in FA7D. 3 Publications
VAR_014392
Natural varianti391 – 3911G → C in FA7D. 1 Publication
VAR_065414
Natural varianti391 – 3911G → S in FA7D. 2 Publications
Corresponds to variant rs190485816 [ dbSNP | Ensembl ].
VAR_014419
Natural varianti398 – 3981D → E in FA7D. 1 Publication
VAR_065415
Natural varianti401 – 4011K → E in FA7D. 1 Publication
VAR_065416
Natural varianti402 – 4021G → E in FA7D. 1 Publication
VAR_006517
Natural varianti402 – 4021G → R in FA7D. 1 Publication
VAR_006516
Natural varianti403 – 4031D → H in FA7D. 2 Publications
VAR_015144
Natural varianti404 – 4041S → N in FA7D. 1 Publication
VAR_065417
Natural varianti408 – 4081H → Q in FA7D. 1 Publication
Corresponds to variant rs121964936 [ dbSNP | Ensembl ].
VAR_065418
Natural varianti408 – 4081H → R in FA7D. 1 Publication
VAR_065419
Natural varianti413 – 4131R → G in FA7D. 1 Publication
VAR_065420
Natural varianti414 – 4141G → C in FA7D; results in severely impaired protein secretion. 1 Publication
VAR_065421
Natural varianti419 – 4191T → M in FA7D. 3 Publications
VAR_006519
Natural varianti422 – 4221V → F in FA7D. 1 Publication
VAR_065422
Natural varianti425 – 4251G → A in FA7D. 1 Publication
VAR_065423
Natural varianti425 – 4251G → C in FA7D. 1 Publication
VAR_065424
Natural varianti429 – 4291A → T in FA7D. 1 Publication
VAR_065425
Natural varianti432 – 4321G → D in FA7D. 1 Publication
VAR_065426
Natural varianti435 – 4351G → E in FA7D. 2 Publications
VAR_014420
Natural varianti437 – 4371Y → F in FA7D. 1 Publication
VAR_065427

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)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi112 – 1121S → A: Complete loss of O-glycosylation and O-xylosylation by POGLUT1. 1 Publication
Mutagenesisi113 – 1131S → A: No effect on O-glycosylation by POGLUT1. Drastic decrease in O-xylosylation. 1 Publication

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi227500. phenotype.
Orphaneti327. Congenital factor VII deficiency.
PharmGKBiPA160.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2020Sequence AnalysisAdd
BLAST
Propeptidei21 – 60401 PublicationPRO_0000027729Add
BLAST
Chaini61 – 212152Factor VII light chainPRO_0000027730Add
BLAST
Chaini213 – 466254Factor VII heavy chainPRO_0000027731Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei66 – 6614-carboxyglutamate2 PublicationsPROSITE-ProRule annotation
Modified residuei67 – 6714-carboxyglutamate2 PublicationsPROSITE-ProRule annotation
Modified residuei74 – 7414-carboxyglutamate2 PublicationsPROSITE-ProRule annotation
Modified residuei76 – 7614-carboxyglutamate2 PublicationsPROSITE-ProRule annotation
Disulfide bondi77 ↔ 82
Modified residuei79 – 7914-carboxyglutamate1 PublicationPROSITE-ProRule annotation
Modified residuei80 – 8014-carboxyglutamate2 PublicationsPROSITE-ProRule annotation
Modified residuei85 – 8514-carboxyglutamate2 PublicationsPROSITE-ProRule annotation
Modified residuei86 – 8614-carboxyglutamate2 PublicationsPROSITE-ProRule annotation
Modified residuei89 – 8914-carboxyglutamate2 PublicationsPROSITE-ProRule annotation
Modified residuei95 – 9514-carboxyglutamate2 PublicationsPROSITE-ProRule annotation
Disulfide bondi110 ↔ 121
Glycosylationi112 – 1121O-linked (Glc...)2 PublicationsCAR_000007
Glycosylationi112 – 1121O-linked (Glc...); alternate2 Publications
Glycosylationi112 – 1121O-linked (Xyl...); alternate2 Publications
Disulfide bondi115 ↔ 130
Glycosylationi120 – 1201O-linked (Fuc)2 PublicationsCAR_000180
Modified residuei123 – 1231(3R)-3-hydroxyaspartate1 Publication
Disulfide bondi132 ↔ 141
Disulfide bondi151 ↔ 162
Disulfide bondi158 ↔ 172
Disulfide bondi174 ↔ 187
Disulfide bondi195 ↔ 322
Glycosylationi205 – 2051N-linked (GlcNAc...)2 Publications
Disulfide bondi219 ↔ 224
Disulfide bondi238 ↔ 254
Disulfide bondi370 ↔ 389
Glycosylationi382 – 3821N-linked (GlcNAc...)2 Publications
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.

Keywords - PTMi

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

Proteomic databases

MaxQBiP08709.
PaxDbiP08709.
PRIDEiP08709.

PTM databases

UniCarbKBiP08709.

Miscellaneous databases

PMAP-CutDBP08709.

Expressioni

Tissue specificityi

Plasma.

Gene expression databases

BgeeiP08709.
CleanExiHS_F7.
ExpressionAtlasiP08709. baseline and differential.
GenevestigatoriP08709.

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
F3P137266EBI-355972,EBI-1040727

Protein-protein interaction databases

BioGridi108453. 10 interactions.
DIPiDIP-6135N.
IntActiP08709. 10 interactions.
MINTiMINT-1155299.
STRINGi9606.ENSP00000364731.

Structurei

Secondary structure

1
466
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi65 – 684Combined sources
Helixi73 – 764Combined sources
Turni77 – 793Combined sources
Helixi84 – 918Combined sources
Helixi94 – 10411Combined sources
Helixi109 – 1124Combined sources
Turni116 – 1183Combined sources
Beta strandi120 – 1245Combined sources
Beta strandi127 – 1315Combined sources
Beta strandi136 – 1383Combined sources
Helixi145 – 1473Combined sources
Beta strandi148 – 1503Combined sources
Turni151 – 1533Combined sources
Helixi154 – 1574Combined sources
Beta strandi159 – 1646Combined sources
Beta strandi166 – 1683Combined sources
Beta strandi170 – 1734Combined sources
Beta strandi178 – 1803Combined sources
Beta strandi187 – 1893Combined sources
Beta strandi191 – 1933Combined sources
Helixi199 – 2024Combined sources
Helixi220 – 2223Combined sources
Beta strandi227 – 2326Combined sources
Beta strandi235 – 2428Combined sources
Beta strandi244 – 2507Combined sources
Helixi252 – 2554Combined sources
Helixi261 – 2633Combined sources
Beta strandi264 – 2696Combined sources
Beta strandi272 – 2743Combined sources
Beta strandi281 – 29111Combined sources
Beta strandi298 – 3014Combined sources
Beta strandi304 – 3107Combined sources
Helixi326 – 3316Combined sources
Helixi333 – 3353Combined sources
Beta strandi338 – 3447Combined sources
Beta strandi346 – 3483Combined sources
Turni352 – 3554Combined sources
Beta strandi358 – 3658Combined sources
Helixi367 – 3726Combined sources
Beta strandi378 – 3803Combined sources
Helixi383 – 3864Combined sources
Beta strandi387 – 3915Combined sources
Beta strandi393 – 3964Combined sources
Helixi401 – 4033Combined sources
Beta strandi407 – 4126Combined sources
Beta strandi415 – 42410Combined sources
Turni427 – 4293Combined sources
Beta strandi435 – 4395Combined sources
Helixi440 – 4434Combined sources
Helixi444 – 4518Combined sources
Beta strandi457 – 4637Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP08709.
SMRiP08709. Positions 68-466.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP08709.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini61 – 10545GlaPROSITE-ProRule annotationAdd
BLAST
Domaini106 – 14237EGF-like 1; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini147 – 18842EGF-like 2PROSITE-ProRule annotationAdd
BLAST
Domaini213 – 452240Peptidase 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

eggNOGiCOG5640.
GeneTreeiENSGT00760000118890.
HOVERGENiHBG013304.
InParanoidiP08709.
KOiK01320.
OMAiGCEQYCS.
OrthoDBiEOG75B84T.
PhylomeDBiP08709.
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.
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. Align

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)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti13 – 131L → P in FA7D; Morioka. 1 Publication
VAR_014391
Natural varianti59 – 591R → RR in FA7D. 1 Publication
VAR_065369
Natural varianti64 – 641F → L in FA7D. 2 Publications
VAR_015135
Natural varianti73 – 731L → Q in FA7D. 2 Publications
Corresponds to variant rs45572939 [ dbSNP | Ensembl ].
VAR_014405
Natural varianti79 – 791E → Q in FA7D. 1 Publication
VAR_014406
Natural varianti82 – 821C → F in FA7D. 1 Publication
VAR_065370
Natural varianti82 – 821C → R in FA7D. 1 Publication
VAR_065371
Natural varianti84 – 841Missing in FA7D. 1 Publication
VAR_065372
Natural varianti85 – 851E → K in FA7D. 1 Publication
VAR_065373
Natural varianti88 – 881R → G in FA7D. 1 Publication
VAR_065374
Natural varianti88 – 881R → P in FA7D. 1 Publication
VAR_065375
Natural varianti117 – 1171N → D in FA7D; exhibits no procoagulant activity and is unable to bind tissue factor. 1 Publication
VAR_065376
Natural varianti120 – 1201S → P in FA7D. 2 Publications
VAR_015136
Natural varianti121 – 1211C → F in FA7D. 1 Publication
VAR_014407
Natural varianti125 – 1251L → P in FA7D. 1 Publication
VAR_014408
Natural varianti128 – 1281Y → C in FA7D. 3 Publications
VAR_014409
Natural varianti138 – 1381G → D in FA7D. 1 Publication
VAR_065377
Natural varianti139 – 1391R → K in FA7D.
VAR_006497
Natural varianti139 – 1391R → Q in FA7D; Charlotte. 2 Publications
Corresponds to variant rs150525536 [ dbSNP | Ensembl ].
VAR_006498
Natural varianti139 – 1391R → W in FA7D. 1 Publication
VAR_006499
Natural varianti151 – 1511C → S in FA7D. 1 Publication
VAR_014410
Natural varianti154 – 1541E → K in FA7D. 2 Publications
Corresponds to variant rs146795869 [ dbSNP | Ensembl ].
VAR_015137
Natural varianti156 – 1561G → S in FA7D. 1 Publication
VAR_065378
Natural varianti157 – 1571G → C in FA7D.
VAR_006501
Natural varianti157 – 1571G → S in FA7D. 2 Publications