P08709 (FA7_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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:

1. Factor VII light chain
2. Factor VII heavy chain

Gene names

Name:

F7

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	466 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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 activity	Selective cleavage of Arg-|-Ile bond in factor X to form factor Xa.
Subunit structure	Heterodimer of a light chain and a heavy chain linked by a disulfide bond.
Subcellular location	Secreted.
Tissue specificity	Plasma.
Post-translational modification	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. 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. Ref.12 Ref.13 Ref.14 Ref.15 Ref.16
Involvement in disease	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. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.11 Ref.20 Ref.21 Ref.22 Ref.24 Ref.26 Ref.27 Ref.28 Ref.29 Ref.30 Ref.31 Ref.32 Ref.33 Ref.34 Ref.37 Ref.38 Ref.39 Ref.41 Ref.42 Ref.43 Ref.44 Ref.45 Ref.46 Ref.47
Pharmaceutical use	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.
Sequence similarities	Belongs to the peptidase S1 family. Contains 2 EGF-like domains. Contains 1 Gla (gamma-carboxy-glutamate) domain. Contains 1 peptidase S1 domain.

Ontologies

Keywords
Biological process	Blood coagulation Hemostasis
Cellular component	Secreted
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Disease mutation
Domain	EGF-like domain Repeat Signal
Ligand	Calcium
Molecular function	Hydrolase Protease Serine protease
PTM	Cleavage on pair of basic residues Disulfide bond Gamma-carboxyglutamic acid Glycoprotein Hydroxylation Zymogen
Technical term	3D-structure Complete proteome Direct protein sequencing Pharmaceutical Reference proteome
Gene Ontology (GO)
Biological_process	blood coagulation, extrinsic pathway Traceable author statement. Source: Reactome circadian rhythm Inferred from electronic annotation. Source: Compara negative regulation of apoptotic process Traceable author statement PubMed 18612547. Source: BHF-UCL organ regeneration Inferred from electronic annotation. Source: Compara peptidyl-glutamic acid carboxylation Traceable author statement. Source: Reactome positive regulation of blood coagulation Inferred from electronic annotation. Source: Compara positive regulation of leukocyte chemotaxis Inferred from direct assay PubMed 17991872. Source: BHF-UCL positive regulation of platelet-derived growth factor receptor signaling pathway Inferred from direct assay PubMed 17991872. Source: BHF-UCL positive regulation of positive chemotaxis Inferred from direct assay PubMed 17991872. Source: BHF-UCL positive regulation of protein kinase B signaling cascade Inferred from direct assay PubMed 18612547. Source: BHF-UCL post-translational protein modification Traceable author statement. Source: Reactome proteolysis Traceable author statement. Source: Reactome response to estrogen stimulus Inferred from electronic annotation. Source: Compara response to growth hormone stimulus Inferred from electronic annotation. Source: Compara response to vitamin K Inferred from electronic annotation. Source: Compara
Cellular_component	Golgi lumen Traceable author statement. Source: Reactome endoplasmic reticulum lumen Traceable author statement. Source: Reactome extracellular region Traceable author statement. Source: Reactome extracellular space Inferred from electronic annotation. Source: Compara plasma membrane Traceable author statement. Source: Reactome vesicle Inferred from electronic annotation. Source: Compara
Molecular_function	calcium ion binding Inferred from electronic annotation. Source: InterPro serine-type endopeptidase activity Traceable author statement Ref.2. Source: ProtInc
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform A (identifier: P08709-1)

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.

Isoform B (identifier: P08709-2)

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

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 20

20

Potential

Propeptide

21 – 60

40

PRO_0000027729

Chain

61 – 212

152

Factor VII light chain

PRO_0000027730

Chain

213 – 466

254

Factor VII heavy chain

PRO_0000027731

Regions

Domain

61 – 105

45

Gla

Domain

106 – 142

37

EGF-like 1; calcium-binding Potential

Domain

147 – 188

42

EGF-like 2

Domain

213 – 452

240

Peptidase S1

Sites

Active site

253

1

Charge relay system By similarity

Active site

302

1

Charge relay system By similarity

Active site

404

1

Charge relay system By similarity

Binding site

398

1

Substrate By similarity

Site

212 – 213

2

Cleavage; by factor Xa, factor XIIa, factor IXa, or thrombin Ref.1

Amino acid modifications

Modified residue

66

1

4-carboxyglutamate Ref.1

Modified residue

67

1

4-carboxyglutamate Ref.1

Modified residue

74

1

4-carboxyglutamate Ref.1

Modified residue

76

1

4-carboxyglutamate Ref.1

Modified residue

79

1

4-carboxyglutamate

Modified residue

80

1

4-carboxyglutamate Ref.1

Modified residue

85

1

4-carboxyglutamate Ref.1

Modified residue

86

1

4-carboxyglutamate Ref.1

Modified residue

89

1

4-carboxyglutamate Ref.1

Modified residue

95

1

4-carboxyglutamate Ref.1

Modified residue

123

1

(3R)-3-hydroxyaspartate

Glycosylation

112

1

O-linked (Glc...) Ref.14

CAR_000007

Glycosylation

120

1

O-linked (Fuc) Ref.14 Ref.15

CAR_000180

Glycosylation

205

1

N-linked (GlcNAc...) Ref.10 Ref.16

Glycosylation

382

1

N-linked (GlcNAc...) Ref.16

Disulfide bond

77 ↔ 82

Disulfide bond

110 ↔ 121

Disulfide bond

115 ↔ 130

Disulfide bond

132 ↔ 141

Disulfide bond

151 ↔ 162

Disulfide bond

158 ↔ 172

Disulfide bond

174 ↔ 187

Disulfide bond

195 ↔ 322

Disulfide bond

219 ↔ 224

Disulfide bond

238 ↔ 254

Disulfide bond

370 ↔ 389

Disulfide bond

400 ↔ 428

Natural variations

Alternative sequence

22 – 43

22

Missing in isoform B.

VSP_005387

Natural variant

13

1

L → P in FA7D; Morioka. Ref.33

VAR_014391

Natural variant

59

1

R → RR in FA7D. Ref.46

VAR_065369

Natural variant

64

1

F → L in FA7D. Ref.39 Ref.44

VAR_015135

Natural variant

73

1

L → Q in FA7D. Ref.38 Ref.44
Corresponds to variant rs45572939 [ dbSNP | Ensembl ].

VAR_014405

Natural variant

79

1

E → Q in FA7D. Ref.38

VAR_014406

Natural variant

82

1

C → F in FA7D. Ref.44

VAR_065370

Natural variant

82

1

C → R in FA7D. Ref.43

VAR_065371

Natural variant

84

1

Missing in FA7D. Ref.44

VAR_065372

Natural variant

85

1

E → K in FA7D. Ref.41

VAR_065373

Natural variant

88

1

R → G in FA7D. Ref.44

VAR_065374

Natural variant

88

1

R → P in FA7D. Ref.44

VAR_065375

Natural variant

117

1

N → D in FA7D; exhibits no procoagulant activity and is unable to bind tissue factor. Ref.32

VAR_065376

Natural variant

120

1

S → P in FA7D. Ref.39 Ref.44

VAR_015136

Natural variant

121

1

C → F in FA7D. Ref.38

VAR_014407

Natural variant

125

1

L → P in FA7D. Ref.38

VAR_014408

Natural variant

128

1

Y → C in FA7D. Ref.38 Ref.39 Ref.44

VAR_014409

Natural variant

138

1

G → D in FA7D. Ref.44

VAR_065377

Natural variant

139

1

R → K in FA7D.

VAR_006497

Natural variant

139

1

R → Q in FA7D; Charlotte. Ref.24 Ref.44

VAR_006498

Natural variant

139

1

R → W in FA7D. Ref.38

VAR_006499

Natural variant

151

1

C → S in FA7D. Ref.38

VAR_014410

Natural variant

154

1

E → K in FA7D. Ref.39 Ref.44

VAR_015137

Natural variant

156

1

G → S in FA7D. Ref.44

VAR_065378

Natural variant

157

1

G → C in FA7D.

VAR_006501

Natural variant

157

1

G → S in FA7D. Ref.39 Ref.44

VAR_006500

Natural variant

157

1

G → V in FA7D. Ref.38

VAR_014411

Natural variant

160

1

Q → R in FA7D. Ref.38 Ref.39 Ref.44

VAR_006502

Natural variant

171

1

S → F in FA7D. Ref.44

VAR_065379

Natural variant

177

1

G → R in FA7D. Ref.43

VAR_065380

Natural variant

181

1

L → P in FA7D. Ref.44

VAR_065381

Natural variant

183

1

D → N in FA7D. Ref.44

VAR_065382

Natural variant

186

1

S → F in FA7D. Ref.44

VAR_065383

Natural variant

189

1

P → S in FA7D. Ref.44

VAR_065384

Natural variant

194

1

P → L in FA7D. Ref.44

VAR_065385

Natural variant

194

1

P → T in FA7D; Malta-I. Ref.34 Ref.44

VAR_006503

Natural variant

195

1

C → R in FA7D. Ref.38 Ref.39 Ref.44

VAR_014412

Natural variant

197

1

K → E in FA7D.

VAR_006504

Natural variant

198

1

I → T in FA7D. Ref.43

VAR_065386

Natural variant

212

1

R → Q in FA7D; Charlotte. Ref.24 Ref.39 Ref.43 Ref.44

VAR_006505

Natural variant

216

1

G → D in FA7D. Ref.39 Ref.44

VAR_015138

Natural variant

238

1

C → Y in FA7D. Ref.22

VAR_006506

Natural variant

240

1

G → R in FA7D. Ref.45

VAR_065387

Natural variant

241

1

T → N in FA7D. Ref.38 Ref.44

VAR_014413

Natural variant

250

1

S → F in FA7D. Ref.47

VAR_065388

Natural variant

251

1

A → P in FA7D. Ref.43

VAR_065389

Natural variant

251

1

A → T in FA7D. Ref.44

VAR_065390

Natural variant

254

1

C → R in FA7D. Ref.44

VAR_065391

Natural variant

254

1

C → Y in FA7D. Ref.39 Ref.44

VAR_015139

Natural variant

264

1

L → P in FA7D. Ref.44

VAR_065392

Natural variant

266

1

A → T in FA7D. Ref.39 Ref.44

VAR_015140

Natural variant

272

1

D → N in FA7D. Ref.44

VAR_065393

Natural variant

277

1

D → N in FA7D. Ref.44

VAR_065394

Natural variant

283

1

R → W in FA7D. Ref.29 Ref.44

VAR_006507

Natural variant

295

1

V → D. Ref.35
Corresponds to variant rs6045 [ dbSNP | Ensembl ].

VAR_013936

Natural variant

298

1

T → I in FA7D. Ref.44

VAR_065395

Natural variant

301

1

H → Q in FA7D. Ref.44

VAR_065396

Natural variant

302

1

D → H in FA7D. Ref.38 Ref.39 Ref.44

VAR_014414

Natural variant

302

1

D → N in FA7D. Ref.38 Ref.44

VAR_014415

Natural variant

304

1

A → T in FA7D. Ref.38 Ref.44

VAR_014416

Natural variant

304

1

A → V in FA7D; Malta-II. Ref.31 Ref.34 Ref.38 Ref.39 Ref.44

VAR_006508

Natural variant

307

1

R → C in FA7D. Ref.38 Ref.39 Ref.44

VAR_014417

Natural variant

307

1

R → H in FA7D; Mie. Ref.27 Ref.44

VAR_006509

Natural variant

312

1

V → M in FA7D. Ref.39 Ref.44

VAR_015141

Natural variant

314

1

L → V in FA7D. Ref.46

VAR_065397

Natural variant

321

1

L → F in FA7D. Ref.44

VAR_065398

Natural variant

323

1

L → R in FA7D. Ref.43

VAR_065399

Natural variant

325

1

E → K in FA7D. Ref.29 Ref.39 Ref.44

VAR_006510

Natural variant

326

1

R → Q in FA7D. Ref.44

VAR_065400

Natural variant

332

1

T → M in FA7D. Ref.38

VAR_014418

Natural variant

337

1

R → C in FA7D. Ref.44

VAR_065401

Natural variant

341

1

V → F in FA7D. Ref.39 Ref.44

VAR_015142

Natural variant

343

1

G → S in FA7D. Ref.44 Ref.46

VAR_065402

Natural variant

344

1

W → R in FA7D. Ref.43

VAR_065403

Natural variant

345

1

G → S in FA7D. Ref.44

VAR_065404

Natural variant

350

1

R → C in FA7D. Ref.44

VAR_065405

Natural variant

352

1

A → T. Ref.6
Corresponds to variant rs3093267 [ dbSNP | Ensembl ].

VAR_013122

Natural variant

354

1

A → V in FA7D. Ref.3 Ref.26 Ref.38 Ref.39 Ref.44
Corresponds to variant rs36209567 [ dbSNP | Ensembl ].

VAR_006511

Natural variant

358

1

M → I in FA7D. Ref.11 Ref.38 Ref.39 Ref.44

VAR_006512

Natural variant

358

1

M → V in FA7D. Ref.29

VAR_006513

Natural variant

360

1

L → P in FA7D. Ref.44

VAR_065406

Natural variant

363

1

P → H in FA7D. Ref.44

VAR_065407

Natural variant

363

1

P → R in FA7D. Ref.39 Ref.44

VAR_015143

Natural variant

364

1

R → Q in FA7D; Harrow/Padua. Ref.11 Ref.20 Ref.21 Ref.29 Ref.44

VAR_006514

Natural variant

364

1

R → W in FA7D. Ref.44

VAR_065408

Natural variant

367

1

T → S. Ref.25

VAR_018671

Natural variant

370

1

C → F in FA7D. Ref.11 Ref.21 Ref.38 Ref.39 Ref.43 Ref.44

VAR_006515

Natural variant

375

1

R → W in FA7D. Ref.44

VAR_065409

Natural variant

384

1

T → M in FA7D. Ref.43 Ref.44

VAR_065410

Natural variant

387

1

M → T in FA7D. Ref.44

VAR_065411

Natural variant

387

1

M → V in FA7D. Ref.44

VAR_065412

Natural variant

388

1

F → S in FA7D; reduces tissue factor binding; impairs activation by factor Xa; abolishes amidolytic and coagulant activities. Ref.30 Ref.44

VAR_065413

Natural variant

389

1

C → G in FA7D. Ref.37 Ref.38 Ref.46

VAR_014392

Natural variant

391

1

G → C in FA7D. Ref.44

VAR_065414

Natural variant

391

1

G → S in FA7D. Ref.38 Ref.44

VAR_014419

Natural variant

398

1

D → E in FA7D. Ref.43

VAR_065415

Natural variant

401

1

K → E in FA7D. Ref.44

VAR_065416

Natural variant

402

1

G → E in FA7D. Ref.29

VAR_006517

Natural variant

402

1

G → R in FA7D. Ref.11

VAR_006516

Natural variant

403

1

D → H in FA7D. Ref.39 Ref.44

VAR_015144

Natural variant

404

1

S → N in FA7D. Ref.44

VAR_065417

Natural variant

408

1

H → Q in FA7D. Ref.41

VAR_065418

Natural variant

408

1

H → R in FA7D. Ref.43

VAR_065419

Natural variant

413

1

R → G in FA7D. Ref.44

VAR_065420

Natural variant

413

1

R → Q May be associated with decreased susceptibility to myocardial infarction. Ref.3 Ref.6 Ref.11 Ref.29 Ref.35 Ref.40
Corresponds to variant rs6046 [ dbSNP | Ensembl ].

VAR_006518

Natural variant

414

1

G → C in FA7D; results in severely impaired protein secretion. Ref.42

VAR_065421

Natural variant

419

1

T → M in FA7D. Ref.28 Ref.39 Ref.44

VAR_006519

Natural variant

422

1

V → F in FA7D. Ref.44

VAR_065422

Natural variant

425

1

G → A in FA7D. Ref.44

VAR_065423

Natural variant

425

1

G → C in FA7D. Ref.44

VAR_065424

Natural variant

429

1

A → T in FA7D. Ref.44

VAR_065425

Natural variant

432

1

G → D in FA7D. Ref.44

VAR_065426

Natural variant

435

1

G → E in FA7D. Ref.38 Ref.44

VAR_014420

Natural variant

437

1

Y → F in FA7D. Ref.44

VAR_065427

Natural variant

445

1

E → K. Ref.6
Corresponds to variant rs3093248 [ dbSNP | Ensembl ].

VAR_013123

Secondary structure

1

.

.

.

.

.

.

.

.

.

466

Helix Strand Turn

Details...

Helix

109 – 111

3

Beta strand

120 – 123

4

Beta strand

125 – 129

5

Beta strand

136 – 138

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform A [UniParc]. Last modified January 1, 1988. Version 1. Checksum: 9B5D501669D67B06	FASTA	466	51,594
	10 20 30 40 50 60 MVSQALRLLC LLLGLQGCLA AGGVAKASGG ETRDMPWKPG PHRVFVTQEE AHGVLHRRRR 70 80 90 100 110 120 ANAFLEELRP GSLERECKEE QCSFEEAREI FKDAERTKLF WISYSDGDQC ASSPCQNGGS 130 140 150 160 170 180 CKDQLQSYIC FCLPAFEGRN CETHKDDQLI CVNENGGCEQ YCSDHTGTKR SCRCHEGYSL 190 200 210 220 230 240 LADGVSCTPT VEYPCGKIPI LEKRNASKPQ GRIVGGKVCP KGECPWQVLL LVNGAQLCGG 250 260 270 280 290 300 TLINTIWVVS AAHCFDKIKN WRNLIAVLGE HDLSEHDGDE QSRRVAQVII PSTYVPGTTN 310 320 330 340 350 360 HDIALLRLHQ PVVLTDHVVP LCLPERTFSE RTLAFVRFSL VSGWGQLLDR GATALELMVL 370 380 390 400 410 420 NVPRLMTQDC LQQSRKVGDS PNITEYMFCA GYSDGSKDSC KGDSGGPHAT HYRGTWYLTG 430 440 450 460 IVSWGQGCAT VGHFGVYTRV SQYIEWLQKL MRSEPRPGVL LRAPFP
	Isoform B [UniParc]. Checksum: 2E74EAFD2FADF2A4	FASTA	444	49,320
	10 20 30 40 50 60 MVSQALRLLC LLLGLQGCLA AVFVTQEEAH GVLHRRRRAN AFLEELRPGS LERECKEEQC 70 80 90 100 110 120 SFEEAREIFK DAERTKLFWI SYSDGDQCAS SPCQNGGSCK DQLQSYICFC LPAFEGRNCE 130 140 150 160 170 180 THKDDQLICV NENGGCEQYC SDHTGTKRSC RCHEGYSLLA DGVSCTPTVE YPCGKIPILE 190 200 210 220 230 240 KRNASKPQGR IVGGKVCPKG ECPWQVLLLV NGAQLCGGTL INTIWVVSAA HCFDKIKNWR 250 260 270 280 290 300 NLIAVLGEHD LSEHDGDEQS RRVAQVIIPS TYVPGTTNHD IALLRLHQPV VLTDHVVPLC 310 320 330 340 350 360 LPERTFSERT LAFVRFSLVS GWGQLLDRGA TALELMVLNV PRLMTQDCLQ QSRKVGDSPN 370 380 390 400 410 420 ITEYMFCAGY SDGSKDSCKG DSGGPHATHY RGTWYLTGIV SWGQGCATVG HFGVYTRVSQ 430 440 YIEWLQKLMR SEPRPGVLLR APFP

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Characterization of a cDNA coding for human factor VII." Hagen F.S., Gray C.L., O'Hara P.J., Grant F.J., Saari G.C., Woodbury R.G., Hart C.E., Insley M.Y., Kisiel W., Kurachi K., Davie E.W. Proc. Natl. Acad. Sci. U.S.A. 83:2412-2416(1986) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND B). Tissue: Liver.
[2]	"Nucleotide sequence of the gene coding for human factor VII, a vitamin K-dependent protein participating in blood coagulation." O'Hara P.J., Grant F.J., Haldeman B.A., Gray C.L., Insley M.Y., Hagen F.S., Murray M.J. Proc. Natl. Acad. Sci. U.S.A. 84:5158-5162(1987) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"Human F7 sequence is split into three deep clades that are related to FVII plasma levels." Sabater-Lleal M., Soria J.M., Bertranpetit J., Almasy L., Blangero J., Fontcuberta J., Calafell F. Hum. Genet. 118:741-751(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS VAL-354 AND GLN-413.
[4]	"Complete dissection of a human quantitative trait locus: allelic architecture of F7 and factor VII levels." Soria J.M., Almasy L., Souto J.C., Sabater M., Fontcuberta J., Blangero J. Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]	Masroori N., Habibi Roudkenar M., Halabian R. Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
[6]	SeattleSNPs variation discovery resource Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS THR-352; GLN-413 AND LYS-445.
[7]	NHLBI resequencing and genotyping service (RS&G) Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[8]	"The DNA sequence and analysis of human chromosome 13." Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T. , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L., Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T. Nature 428:522-528(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B).
[10]	"Amino acid sequence and posttranslational modifications of human factor VIIa from plasma and transfected baby hamster kidney cells." Thim L., Bjoern S., Christensen M., Nicolaisen E.M., Lund-Hansen T., Pedersen A.H., Hedner U. Biochemistry 27:7785-7793(1988) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 61-466, POST-TRANSLATIONAL MODIFICATIONS.
[11]	"Molecular defects in CRM+ factor VII deficiencies: modelling of missense mutations in the catalytic domain of FVII." Bernardi F., Liney D.L., Patracchini P., Gemmati D., Legnani C., Arcieri P., Pinotti M., Redaelli R., Ballerini G., Pemberton S., Wacey A.I., Mariani G., Tuddenham E.G.D., Marchetti G. Br. J. Haematol. 86:610-618(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 354-412, VARIANTS FA7D ILE-358; GLN-364; PHE-370 AND ARG-402, VARIANT GLN-413.
[12]	"Identification of a disaccharide (Xyl-Glc) and a trisaccharide (Xyl2-Glc) O-glycosidically linked to a serine residue in the first epidermal growth factor-like domain of human factors VII and IX and protein Z and bovine protein Z." Nishimura H., Kawabata S., Kisiel W., Hase S., Ikenaka T., Takao T., Shimonishi Y., Iwanaga S. J. Biol. Chem. 264:20320-20325(1989) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE OF CARBOHYDRATE ON SER-112.
[13]	"A new trisaccharide sugar chain linked to a serine residue in the first EGF-like domain of clotting factors VII and IX and protein Z." Iwanaga S., Nishimura H., Kawabata S., Kisiel W., Hase S., Ikenaka T. Adv. Exp. Med. Biol. 281:121-131(1990) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE OF CARBOHYDRATE ON SER-112.
[14]	"Human plasma and recombinant factor VII. Characterization of O-glycosylations at serine residues 52 and 60 and effects of site-directed mutagenesis of serine 52 to alanine." Bjoern S., Foster D.C., Thim L., Wiberg F.C., Christensen M., Komiyama Y., Pedersen A.H., Kisiel W. J. Biol. Chem. 266:11051-11057(1991) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION AT SER-112 AND SER-120.
[15]	"Identification of a GDP-L-fucose:polypeptide fucosyltransferase and enzymatic addition of O-linked fucose to EGF domains." Wang Y., Lee G.F., Kelley R.F., Spellman M.W. Glycobiology 6:837-842(1996) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION AT SER-120, MASS SPECTROMETRY.
[16]	"Cotranslational and posttranslational N-glycosylation of polypeptides by distinct mammalian OST isoforms." Ruiz-Canada C., Kelleher D.J., Gilmore R. Cell 136:272-283(2009) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION AT ASN-205 AND ASN-382.
[17]	"The crystal structure of the complex of blood coagulation factor VIIa with soluble tissue factor." Banner D.W., D'Arcy A., Chene C., Winkler F.K., Guha A., Konigsberg W.H., Nemreson Y., Kirchhofer D. Nature 380:41-46(1996) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF FVIIA IN COMPLEX WITH TF.
[18]	"Structure of extracellular tissue factor complexed with factor VIIa inhibited with a BPTI mutant." Zhang E., St Charles R., Tulinsky A. J. Mol. Biol. 285:2089-2104(1999) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF FVIIA IN COMPLEX WITH TF.
[19]	"Solution structure of the N-terminal EGF-like domain from human factor VII." Muranyi A., Finn B.E., Gippert G.P., Forsen S., Stenflo J., Drakenberg T. Biochemistry 37:10605-10615(1998) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 105-145.
[20]	"Purification and characterization of factor VII 304-Gln: a variant molecule with reduced activity isolated from a clinically unaffected male." O'Brien D.P., Gale K.M., Anderson J.S., McVey J.H., Miller G.J., Meade T.W., Tuddenham E.G.D. Blood 78:132-140(1991) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT FA7D GLN-364.
[21]	"Detection of two missense mutations and characterization of a repeat polymorphism in the factor VII gene (F7)." Marchetti G., Patracchini P., Gemmati D., Derosa V., Pinotti M., Rodorigo G., Casonato A., Girolami A., Bernardi F. Hum. Genet. 89:497-502(1992) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS FA7D GLN-364 AND PHE-370.
[22]	"A missense mutation (178Cys-->Tyr) and two neutral dimorphisms (115His and 333Ser) in the human coagulation factor VII gene." Marchetti G., Ferrati M., Patracchini P., Redaelli R., Bernardi F. Hum. Mol. Genet. 2:1055-1056(1993) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT FA7D TYR-238.
[23]	"Detection of missense mutations by single-strand conformational polymorphism (SSCP) analysis in five dysfunctional variants of coagulation factor VII." Takamiya O., Kemball-Cook G., Martin D.M.A., Cooper D.N., von Felten A., Meili E., Hahn I., Prangnell D.R., Lumley H., Tuddenham E.G.D., McVey J.H. Hum. Mol. Genet. 2:1355-1359(1993) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS.
[24]	"Severe factor VII deficiency caused by mutations abolishing the cleavage site for activation and altering binding to tissue factor." Chaing S., Clarke B., Sridhara S., Chu K., Friedman P., Vandusen W., Roberts H.R., Blajchman M., Monroe D.M., High K.A. Blood 83:3524-3535(1994) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS FA7D GLN-139 AND GLN-212.
[25]	"A common Ser/Thr polymorphism in the perforin-homologous region of human complement component C7." Dewald G., Noethen M.M., Ruther K. Hum. Hered. 44:301-304(1994) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT SER-367.
[26]	"Topologically equivalent mutations causing dysfunctional coagulation factors VII (294Ala-->Val) and X (334Ser-->Pro)." Bernardi F., Castaman G., Redaelli R., Pinotti M., Lunghi B., Rodeghiero F., Marchetti G. Hum. Mol. Genet. 3:1175-1177(1994) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT FA7D VAL-354.
[27]	"Factor VII Mie: homozygous asymptomatic type I deficiency caused by an amino acid substitution of His (CAC) for Arg(247) (CGC) in the catalytic domain." Ohiwa M., Hayashi T., Wada H., Minamikawa K., Shirakawa S., Suzuki K. Thromb. Haemost. 71:773-777(1994) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT FA7D HIS-307.
[28]	"A Thr359Met mutation in factor VII of a patient with a hereditary deficiency causes defective secretion of the molecule." Arbini A.A., Mannucci P.M., Bauer K.A. Blood 87:5085-5094(1996) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT FA7D MET-419.
[29]	"Mutation pattern in clinically asymptomatic coagulation factor VII deficiency." Bernardi F., Castaman G., Pinotti M., Ferraresi P., di Iasio M.G., Lunghi B., Rodeghiero F., Marchetti G. Hum. Mutat. 8:108-115(1996) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS FA7D TRP-283; LYS-325; VAL-358; GLN-364 AND GLU-402, VARIANT GLN-413.
[30]	"Factor VII central. A novel mutation in the catalytic domain that reduces tissue factor binding, impairs activation by factor Xa, and abolishes amidolytic and coagulant activity." Bharadwaj D., Iino M., Kontoyianni M., Smith K.J., Foster D.C., Kisiel W. J. Biol. Chem. 271:30685-30691(1996) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT FA7D SER-388, CHARACTERIZATION OF VARIANT FA7D SER-388.
[31]	"Ala244Val is a common, probably ancient mutation causing factor VII deficiency in Moroccan and Iranian Jews." Tamary H., Fromovich Y., Shalmon L., Reich Z., Dym O., Lanir N., Brenner B., Paz M., Luder A.S., Blau O., Korostishevsky M., Zaizov R., Seligsohn U. Thromb. Haemost. 76:283-291(1996) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT FA7D VAL-304.
[32]	"Factor VII deficiency caused by a structural variant N57D of the first epidermal growth factor domain." Leonard B.J., Chen Q., Blajchman M.A., Ofosu F.A., Sridhara S., Yang D., Clarke B.J. Blood 91:142-148(1998) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT FA7D ASP-117, CHARACTERIZATION OF VARIANT FA7D ASP-117.
[33]	"Factor VII Morioka (FVII L-26P): a homozygous missense mutation in the signal sequence identified in a patient with factor VII deficiency." Ozawa T., Takikawa Y., Niiya K., Ejiri N., Suzuki K., Sato S., Sakuragawa N. Br. J. Haematol. 101:47-49(1998) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT FA7D PRO-13.
[34]	"Two new missense mutations (P134T and A244V) in the coagulation factor VII gene." Alshinawi C., Scerri C., Galdies R., Aquilina A., Felice A.E. Hum. Mutat. Suppl. 1:S189-S191(1998) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS FA7D THR-194 AND VAL-304.
[35]	"Characterization of single-nucleotide polymorphisms in coding regions of human genes." Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N., Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L., Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q., Lander E.S. Nat. Genet. 22:231-238(1999) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS ASP-295 AND GLN-413.
[36]	Erratum Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N., Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L., Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q., Lander E.S. Nat. Genet. 23:373-373(1999)
[37]	"Two novel factor VII gene mutations in a Chinese family with factor VII deficiency." Au W.Y., Lam C.C.K., Chan E.C., Kwong Y.L. Br. J. Haematol. 111:143-145(2000) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT FA7D GLY-389.
[38]	"Molecular analysis of the genotype-phenotype relationship in factor VII deficiency." Millar D.S., Kemball-Cook G., McVey J.H., Tuddenham E.G.D., Mumford A.D., Attock G.B., Reverter J.C., Lanir N., Parapia L.A., Reynaud J., Meili E., von Felton A., Martinowitz U., Prangnell D.R., Krawczak M., Cooper D.N. Hum. Genet. 107:327-342(2000) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS FA7D GLN-73; GLN-79; PHE-121; PRO-125; CYS-128; TRP-139; SER-151; VAL-157; ARG-160; ARG-195; ASN-241; HIS-302; ASN-302; THR-304; VAL-304; CYS-307; MET-332; VAL-354; ILE-358; PHE-370; GLY-389; SER-391 AND GLU-435.
[39]	"Twenty two novel mutations of the factor VII gene in factor VII deficiency." Wulff K., Herrmann F.H. Hum. Mutat. 15:489-496(2000) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS FA7D LEU-64; PRO-120; CYS-128; LYS-154; SER-157; ARG-160; ARG-195; GLN-212; ASP-216; TYR-254; THR-266; HIS-302; VAL-304; CYS-307; MET-312; LYS-325; PHE-341; VAL-354; ILE-358; ARG-363; PHE-370; HIS-403 AND MET-419.
[40]	"Polymorphisms in the factor VII gene and the risk of myocardial infarction in patients with coronary artery disease." Girelli D., Russo C., Ferraresi P., Olivieri O., Pinotti M., Friso S., Manzato F., Mazzucco A., Bernardi F., Corrocher R. N. Engl. J. Med. 343:774-780(2000) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT GLN-413.
[41]	"Two double heterozygous mutations in the F7 gene show different manifestations." Nagaizumi K., Inaba H., Suzuki T., Hatta Y., Hagiwara T., Amano K., Arai M., Fukutake K. Br. J. Haematol. 119:1052-1058(2002) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS FA7D LYS-85 AND GLN-408.
[42]	"A patient homozygous for a Gly354Cys mutation in factor VII that results in severely impaired secretion of the molecule, but not complete deficiency." Takamiya O., Hino K. Br. J. Haematol. 124:336-342(2004) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT FA7D CYS-414, CHARACTERIZATION OF VARIANT FA7D CYS-414.
[43]	"Phenotypic and genotypic characterization of Factor VII deficiency patients from Western India." Mota L., Shetty S., Idicula-Thomas S., Ghosh K. Clin. Chim. Acta 409:106-111(2009) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS FA7D ARG-82; ARG-177; THR-198; GLN-212; PRO-251; ARG-323; ARG-344; PHE-370; MET-384; GLU-398 AND ARG-408.
[44]	"Factor VII deficiency: clinical manifestation of 717 subjects from Europe and Latin America with mutations in the factor 7 gene." Herrmann F.H., Wulff K., Auerswald G., Schulman S., Astermark J., Batorova A., Kreuz W., Pollmann H., Ruiz-Saez A., De Bosch N., Salazar-Sanchez L. Haemophilia 15:267-280(2009) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS FA7D LEU-64; GLN-73; PHE-82; PHE-84 DEL; GLY-88; PRO-88; PRO-120; CYS-128; ASP-138; GLN-139; LYS-154; SER-156; SER-157; ARG-160; PHE-171; PRO-181; ASN-183; PHE-186; SER-189; LEU-194; THR-194; ARG-195; GLN-212; ASP-216; ASN-241; THR-251; ARG-254; TYR-254; PRO-264; THR-266; ASN-272; ASN-277; TRP-283; ILE-298; GLN-301; ASN-302; HIS-302; THR-304; VAL-304; CYS-307; HIS-307; MET-312; PHE-321; LYS-325; GLN-326; CYS-337; PHE-341; SER-343; SER-345; CYS-350; VAL-354; ILE-358; PRO-360; ARG-363; HIS-363; GLN-364; TRP-364; PHE-370; TRP-375; MET-384; THR-387; VAL-387; SER-388; CYS-391; SER-391; GLU-401; HIS-403; ASN-404; GLY-413; MET-419; PHE-422; ALA-425; CYS-425; THR-429; ASP-432; GLU-435 AND PHE-437.
[45]	"Familial factor VII deficiency with foetal and neonatal fatal cerebral haemorrhage associated with homozygosis to Gly180Arg mutation." Landau D., Rosenberg N., Zivelin A., Staretz-Chacham O., Kapelushnik J. Haemophilia 15:774-778(2009) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT FA7D ARG-240.
[46]	"Recurrent mutations and genotype-phenotype correlations in hereditary factor VII deficiency in Korea." Kwon M.J., Yoo K.Y., Lee K.O., Kim S.H., Kim H.J. Blood Coagul. Fibrinolysis 22:102-105(2011) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS FA7D ARG-59 INS; VAL-314; SER-343 AND GLY-389.
[47]	"A novel missense mutation close to the charge-stabilizing system in a patient with congenital factor VII deficiency." Jiang M., Wang Z., Yu Z., Bai X., Su J., Cao L., Zhang W., Ruan C. Blood Coagul. Fibrinolysis 22:264-270(2011) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT FA7D PHE-250.
+	Additional computationally mapped references.

Web resources

Wikipedia

Factor VII entry

GeneReviews

SeattleSNPs

SHMPD

The Singapore human mutation and polymorphism database

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M13232 mRNA. Translation: AAA88040.1.
M13232 mRNA. Translation: AAA88041.1.
J02933 Genomic DNA. Translation: AAA51983.1.
DQ142911 Genomic DNA. Translation: ABD17891.1.
AY212252 Genomic DNA. Translation: AAP33841.1.
EU557239 mRNA. Translation: ACB87203.1.
AF466933 Genomic DNA. Translation: AAL66184.1.
EF445049 Genomic DNA. Translation: ACA06107.1.
EF445049 Genomic DNA. Translation: ACA06108.1.
AL137002 Genomic DNA. Translation: CAI41381.1.
AL137002 Genomic DNA. Translation: CAI41382.1.
BC130468 mRNA. Translation: AAI30469.1.

IPI

IPI00329555.
IPI00798065.

PIR

KFHU7. A28322.

RefSeq

NP_000122.1. NM_000131.4.
NP_062562.1. NM_019616.3.

UniGene

Hs.36989.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1BF9	NMR	-	A	105-145	[»]
1CVW	X-ray	2.28	H	213-466	[»]
			L	150-204	[»]
1DAN	X-ray	2.00	H	213-466	[»]
			L	61-212	[»]
1DVA	X-ray	3.00	H/I	213-466	[»]
			L/M	102-202	[»]
1F7E	NMR	-	A	105-147	[»]
1F7M	NMR	-	A	105-147	[»]
1FAK	X-ray	2.10	H	213-466	[»]
			L	61-212	[»]
1FF7	NMR	-	A	105-147	[»]
1FFM	NMR	-	A	105-147	[»]
1J9C	X-ray	2.90	H	213-466	[»]
			L	108-202	[»]
1JBU	X-ray	2.00	H	213-466	[»]
			L	150-212	[»]
1KLI	X-ray	1.69	H	213-466	[»]
			L	144-212	[»]
1KLJ	X-ray	2.44	H	213-466	[»]
			L	144-212	[»]
1NL8	model	-	H	213-466	[»]
			M	61-202	[»]
1O5D	X-ray	2.05	H	213-466	[»]
			L	61-212	[»]
1QFK	X-ray	2.80	H	213-466	[»]
			L	109-212	[»]
1W0Y	X-ray	2.50	H	213-466	[»]
			L	61-202	[»]
1W2K	X-ray	3.00	H	213-466	[»]
			L	61-202	[»]
1W7X	X-ray	1.80	H	213-466	[»]
			L	150-204	[»]
1W8B	X-ray	3.00	H	213-466	[»]
			L	148-204	[»]
1WQV	X-ray	2.50	H	213-466	[»]
			L	61-212	[»]
1WSS	X-ray	2.60	H	213-466	[»]
			L	61-212	[»]
1WTG	X-ray	2.20	H	213-466	[»]
			L	61-212	[»]
1WUN	X-ray	2.40	H	213-466	[»]
			L	61-212	[»]
1WV7	X-ray	2.70	H	213-466	[»]
			L	61-212	[»]
1YGC	X-ray	2.00	H	213-466	[»]
			L	150-212	[»]
1Z6J	X-ray	2.00	H	213-466	[»]
			L	61-202	[»]
2A2Q	X-ray	1.80	H	213-466	[»]
			L	61-212	[»]
2AEI	X-ray	2.52	H	213-466	[»]
			L	61-212	[»]
2AER	X-ray	1.87	H	213-466	[»]
			L	61-202	[»]
2B7D	X-ray	2.24	H	213-466	[»]
			L	61-212	[»]
2B8O	X-ray	2.80	H	213-466	[»]
			L	61-202	[»]
2BZ6	X-ray	1.60	H	213-466	[»]
			L	150-202	[»]
2C4F	X-ray	1.72	H	213-466	[»]
			L	61-202	[»]
2EC9	X-ray	2.00	H	213-466	[»]
			L	61-202	[»]
2F9B	X-ray	2.54	H	213-466	[»]
			L	61-212	[»]
2FIR	X-ray	2.00	H	213-466	[»]
			L	61-202	[»]
2FLB	X-ray	1.95	H	213-466	[»]
			L	61-212	[»]
2FLR	X-ray	2.35	H	213-466	[»]
			L	61-212	[»]
2PUQ	X-ray	2.05	H	213-466	[»]
			L	109-202	[»]
2ZP0	X-ray	2.70	H	213-466	[»]
			L	61-212	[»]
2ZWL	X-ray	2.20	H	213-466	[»]
			L	61-212	[»]
2ZZU	X-ray	2.50	H	213-466	[»]
			L	61-212	[»]
3ELA	X-ray	2.20	H	213-466	[»]
			L	61-212	[»]
3TH2	X-ray	1.72	H	213-466	[»]
			L	61-202	[»]
3TH3	X-ray	2.70	H	213-466	[»]
			L	61-202	[»]
3TH4	X-ray	1.80	H	213-466	[»]
			L	61-202	[»]
4ISI	X-ray	1.94	H	213-466	[»]
			L	150-204	[»]

ProteinModelPortal

P08709.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-6135N.

IntAct

P08709. 10 interactions.

MINT

MINT-1155299.

STRING

9606.ENSP00000364731.

Protein family/group databases

MEROPS

S01.215.

PTM databases

GlycoSuiteDB

P08709.

Polymorphism databases

DMDM

119766.

Proteomic databases

PaxDb

P08709.

PRIDE

P08709.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000346342; ENSP00000329546; ENSG00000057593.
ENST00000375581; ENSP00000364731; ENSG00000057593.

GeneID

2155.

KEGG

hsa:2155.

UCSC

uc001vsv.3. human.
uc001vsw.3. human.

Organism-specific databases

CTD

2155.

GeneCards

GC13P113760.

HGNC

HGNC:3544. F7.

HPA

HPA004826.

MIM

227500. phenotype.
613878. gene.

neXtProt

NX_P08709.

Orphanet

327. Congenital factor VII deficiency.

PharmGKB

PA160.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG5640.

HOVERGEN

HBG013304.

InParanoid

P08709.

KO

K01320.

OMA

GCEQYCS.

OrthoDB

EOG4HX51H.

PhylomeDB

P08709.

Enzyme and pathway databases

Reactome

REACT_17015. Metabolism of proteins.
REACT_24941. Circadian Clock.
REACT_604. Hemostasis.

SABIO-RK

P08709.

Gene expression databases

ArrayExpress

P08709.

Bgee

P08709.

CleanEx

HS_F7.

Genevestigator

P08709.

GermOnline

ENSG00000057593. Homo sapiens.

Family and domain databases

Gene3D

4.10.740.10. 1 hit.

InterPro

IPR017857. Coagulation_fac_subgr_Gla_dom.
IPR000742. EG-like_dom.
IPR001881. EGF-like_Ca-bd.
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]

Pfam

PF00008. EGF. 1 hit.
PF00594. Gla. 1 hit.
PF00089. Trypsin. 1 hit.
[Graphical view]

PIRSF

PIRSF001143. Factor_X. 1 hit.

PRINTS

PR00722. CHYMOTRYPSIN.
PR00001. GLABLOOD.

SMART

SM00181. EGF. 1 hit.
SM00179. EGF_CA. 1 hit.
SM00069. GLA. 1 hit.
SM00020. Tryp_SPc. 1 hit.
[Graphical view]

SUPFAM

SSF50494. Pept_Ser_Cys. 1 hit.
SSF57630. VitK_dep_GLA. 1 hit.

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.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P08709.

ChEMBL

CHEMBL3991.

DrugBank

DB00100. Coagulation Factor IX.
DB00036. Coagulation factor VIIa.
DB00170. Menadione.

EvolutionaryTrace

P08709.

GenomeRNAi

2155.

NextBio

8705.

PMAP-CutDB

P08709.

SOURCE

Search...

Entry information

Entry name

FA7_HUMAN

Accession

Primary (citable) accession number: P08709
Secondary accession number(s): B0YJC8 , Q14339, Q5JVF1, Q5JVF2, Q9UD52, Q9UD53, Q9UD54

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1988
Last sequence update:	January 1, 1988
Last modified:	May 1, 2013
This is version 192 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.