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P08709

- FA7_HUMAN

UniProt

P08709 - FA7_HUMAN

Protein

Coagulation factor VII

Gene

F7

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 208 (01 Oct 2014)
      Sequence version 1 (01 Jan 1988)
      Previous versions | rss
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    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. protein binding Source: IntAct
    4. serine-type endopeptidase activity Source: ProtInc
    5. 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

    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

    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

    ArrayExpressiP08709.
    BgeeiP08709.
    CleanExiHS_F7.
    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. 7 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 – 684
    Helixi73 – 764
    Turni77 – 793
    Helixi84 – 918
    Helixi94 – 10411
    Helixi109 – 1124
    Turni116 – 1183
    Beta strandi120 – 1245
    Beta strandi127 – 1315
    Beta strandi136 – 1383
    Helixi145 – 1473
    Beta strandi148 – 1503
    Turni151 – 1533
    Helixi154 – 1574
    Beta strandi159 – 1646
    Beta strandi166 – 1683
    Beta strandi170 – 1734
    Beta strandi178 – 1803
    Beta strandi187 – 1893
    Beta strandi191 – 1933
    Helixi199 – 2024
    Helixi220 – 2223
    Beta strandi227 – 2326
    Beta strandi235 – 2428
    Beta strandi244 – 2507
    Helixi252 – 2554
    Helixi261 – 2633
    Beta strandi264 – 2696
    Beta strandi272 – 2743
    Beta strandi281 – 29111
    Beta strandi298 – 3014
    Beta strandi304 – 3107
    Helixi326 – 3316
    Helixi333 – 3353
    Beta strandi338 – 3447
    Beta strandi346 – 3483
    Turni352 – 3554
    Beta strandi358 – 3658
    Helixi367 – 3726
    Beta strandi378 – 3803
    Helixi383 – 3864
    Beta strandi387 – 3915
    Beta strandi393 – 3964
    Helixi401 – 4033
    Beta strandi407 – 4126
    Beta strandi415 – 42410
    Turni427 – 4293
    Beta strandi435 – 4395
    Helixi440 – 4434
    Helixi444 – 4518
    Beta strandi457 – 4637

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    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

    MVSQALRLLC LLLGLQGCLA AGGVAKASGG ETRDMPWKPG PHRVFVTQEE    50
    AHGVLHRRRR ANAFLEELRP GSLERECKEE QCSFEEAREI FKDAERTKLF 100
    WISYSDGDQC ASSPCQNGGS CKDQLQSYIC FCLPAFEGRN CETHKDDQLI 150
    CVNENGGCEQ YCSDHTGTKR SCRCHEGYSL LADGVSCTPT VEYPCGKIPI 200
    LEKRNASKPQ GRIVGGKVCP KGECPWQVLL LVNGAQLCGG TLINTIWVVS 250
    AAHCFDKIKN WRNLIAVLGE HDLSEHDGDE QSRRVAQVII PSTYVPGTTN 300
    HDIALLRLHQ PVVLTDHVVP LCLPERTFSE RTLAFVRFSL VSGWGQLLDR 350
    GATALELMVL NVPRLMTQDC LQQSRKVGDS PNITEYMFCA GYSDGSKDSC 400
    KGDSGGPHAT HYRGTWYLTG IVSWGQGCAT VGHFGVYTRV SQYIEWLQKL 450
    MRSEPRPGVL LRAPFP 466
    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
    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