Reviewed, UniProtKB/Swiss-Prot P08709 (FA7_HUMAN)

Names and origin

Protein names

Recommended name:
    Coagulation factor VII
    EC=3.4.21.21
Alternative name(s):
    Serum prothrombin conversion accelerator
      Short name=SPCA
    Proconvertin
    INN=Eptacog alfa
Cleaved into the following 2 chains:
    1- Recommended name:
            Factor VII light chain
    2- Recommended name:
            Factor VII heavy chain

Gene names

Name:

F7

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › 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.
Polymorphism	Individuals with the Q allele (Gln-413) seems to have a decreased susceptibility to myocardial infarction.
Involvement in disease	Defects in F7 are the cause of F7 deficiency [MIM:227500]; also known as factor VII deficiency. F7 deficiency is a rare hereditary hemorrhagic disease. The clinical picture can be very severe, with the early occurrence of intracerebral hemorrhages or hemarthroses, or, in contrast, moderate with cutaneous-mucosal hemorrhages (epistaxis, menorrhagia) or hemorrhages provoked by a surgical intervention. Numerous subjects are completely asymptomatic despite a very low F7 level.
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
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
Gene Ontology (GO)
Biological process	anti-apoptosis Traceable author statement. Source: UniProtKB blood coagulation, extrinsic pathway Inferred from Experiment. Source: Reactome positive regulation of leukocyte chemotaxis Inferred from direct assay. Source: UniProtKB positive regulation of platelet-derived growth factor receptor signaling pathway Inferred from direct assay. Source: UniProtKB positive regulation of positive chemotaxis Inferred from direct assay. Source: UniProtKB positive regulation of protein kinase B signaling cascade Inferred from direct assay. Source: UniProtKB proteolysis Inferred from electronic annotation. Source: InterPro
Cellular component	extracellular region Ref.2 Ref.15 Inferred from Experiment. Source: Reactome plasma membrane Ref.15 Inferred from Experiment. Source: Reactome
Molecular function	calcium ion binding Inferred from electronic annotation. Source: UniProtKB-KW glycoprotein binding Inferred from physical interaction. Source: UniProtKB serine-type endopeptidase activity Ref.2 Traceable author statement. Source: ProtInc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
PII	P04133	1	EBI-355972,EBI-1646019	From a different organism.

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

CAR_000180

Glycosylation

205

1

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

Glycosylation

382

1

N-linked (GlcNAc...)

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 Morioka; FVII deficiency. Ref.29

VAR_014391

Natural variant

64

1

F → L in FVII deficiency. Ref.35

VAR_015135

Natural variant

73

1

L → Q in FVII deficiency. dbSNP rs45572939. Ref.34

VAR_014405

Natural variant

79

1

E → Q in FVII deficiency. Ref.34

VAR_014406

Natural variant

120

1

S → P in FVII deficiency. Ref.35

VAR_015136

Natural variant

121

1

C → F in FVII deficiency. Ref.34

VAR_014407

Natural variant

125

1

L → P in FVII deficiency. Ref.34

VAR_014408

Natural variant

128

1

Y → C in FVII deficiency. Ref.35 Ref.34

VAR_014409

Natural variant

139

1

R → K in FVII deficiency.

VAR_006497

Natural variant

139

1

R → Q in Charlotte; FVII deficiency. Ref.22

VAR_006498

Natural variant

139

1

R → W in FVII deficiency. Ref.34

VAR_006499

Natural variant

151

1

C → S in FVII deficiency. Ref.34

VAR_014410

Natural variant

154

1

E → K in FVII deficiency. Ref.35

VAR_015137

Natural variant

157

1

G → C in FVII deficiency.

VAR_006501

Natural variant

157

1

G → S in FVII deficiency. Ref.35

VAR_006500

Natural variant

157

1

G → V in FVII deficiency. Ref.34

VAR_014411

Natural variant

160

1

Q → R in FVII deficiency. Ref.35 Ref.34

VAR_006502

Natural variant

194

1

P → T in Malta-I; FVII deficiency. Ref.30

VAR_006503

Natural variant

195

1

C → R in FVII deficiency. Ref.35 Ref.34

VAR_014412

Natural variant

197

1

K → E in FVII deficiency.

VAR_006504

Natural variant

212

1

R → Q in Charlotte; FVII deficiency. Ref.35 Ref.22

VAR_006505

Natural variant

216

1

G → D in FVII deficiency. Ref.35

VAR_015138

Natural variant

238

1

C → Y in FVII deficiency. Ref.20

VAR_006506

Natural variant

241

1

T → N in FVII deficiency. Ref.34

VAR_014413

Natural variant

254

1

C → Y in FVII deficiency. Ref.35

VAR_015139

Natural variant

266

1

A → T in FVII deficiency. Ref.35

VAR_015140

Natural variant

283

1

R → W in FVII deficiency. Ref.27

VAR_006507

Natural variant

295

1

V → D: dbSNP rs6045. Ref.31

VAR_013936

Natural variant

302

1

D → H in FVII deficiency. Ref.35 Ref.34

VAR_014414

Natural variant

302

1

D → N in FVII deficiency. Ref.34

VAR_014415

Natural variant

304

1

A → T in FVII deficiency. Ref.34

VAR_014416

Natural variant

304

1

A → V in Malta-II; FVII deficiency. Ref.35 Ref.34 Ref.30 Ref.28

VAR_006508

Natural variant

307

1

R → C in FVII deficiency. Ref.35 Ref.34

VAR_014417

Natural variant

307

1

R → H in Mie; FVII deficiency. Ref.25

VAR_006509

Natural variant

312

1

V → M in FVII deficiency. Ref.35

VAR_015141

Natural variant

325

1

E → K in FVII deficiency. Ref.35 Ref.27

VAR_006510

Natural variant

332

1

T → M in FVII deficiency. Ref.34

VAR_014418

Natural variant

341

1

V → F in FVII deficiency. Ref.35

VAR_015142

Natural variant

352

1

A → T: dbSNP rs3093267. Ref.6

VAR_013122

Natural variant

354

1

A → V in FVII deficiency. dbSNP rs36209567. Ref.35 Ref.34 Ref.3 Ref.24

VAR_006511

Natural variant

358

1

M → I in FVII deficiency. Ref.35 Ref.34 Ref.11

VAR_006512

Natural variant

358

1

M → V in FVII deficiency. Ref.27

VAR_006513

Natural variant

363

1

P → R in FVII deficiency. Ref.35

VAR_015143

Natural variant

364

1

R → Q in Harrow/Padua; FVII deficiency. Ref.27 Ref.11 Ref.18 Ref.19

VAR_006514

Natural variant

367

1

T → S

VAR_018671

Natural variant

370

1

C → F in FVII deficiency. Ref.35 Ref.34 Ref.11 Ref.19

VAR_006515

Natural variant

389

1

C → G in FVII deficiency. Ref.34 Ref.33

VAR_014392

Natural variant

391

1

G → S in FVII deficiency. Ref.34

VAR_014419

Natural variant

402

1

G → E in FVII deficiency. Ref.27

VAR_006517

Natural variant

402

1

G → R in FVII deficiency. Ref.11

VAR_006516

Natural variant

403

1

D → H in FVII deficiency. Ref.35

VAR_015144

Natural variant

413

1

R → Q in allele Q. dbSNP rs6046. Ref.27 Ref.31 Ref.6 Ref.3 Ref.11 Ref.36

VAR_006518

Natural variant

419

1

T → M in FVII deficiency. Ref.35 Ref.26

VAR_006519

Natural variant

435

1

G → E in FVII deficiency. Ref.34

VAR_014420

Natural variant

445

1

E → K: dbSNP rs3093248. Ref.6

VAR_013123

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

466

Helix Strand Turn

Details...

Beta strand

66 – 69

4

Helix

73 – 76

4

Turn

77 – 79

3

Helix

84 – 91

8

Helix

94 – 104

11

Turn

109 – 112

4

Beta strand

120 – 124

5

Beta strand

127 – 131

5

Beta strand

136 – 138

3

Helix

145 – 147

3

Turn

151 – 153

3

Helix

154 – 157

4

Beta strand

159 – 163

5

Beta strand

171 – 173

3

Beta strand

178 – 180

3

Beta strand

187 – 193

7

Turn

199 – 201

3

Beta strand

227 – 232

6

Beta strand

235 – 242

8

Beta strand

244 – 250

7

Helix

252 – 255

4

Beta strand

264 – 269

6

Beta strand

281 – 291

11

Beta strand

304 – 310

7

Helix

326 – 331

6

Helix

333 – 335

3

Beta strand

337 – 344

8

Beta strand

346 – 348

3

Beta strand

358 – 365

8

Helix

367 – 373

7

Beta strand

387 – 391

5

Turn

401 – 405

5

Beta strand

407 – 412

6

Beta strand

415 – 424

10

Beta strand

426 – 429

4

Beta strand

435 – 439

5

Helix

440 – 443

4

Helix

444 – 451

8

Beta strand

457 – 463

7

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. 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: 3486420] [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: 3037537] [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: 16292673] [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: 15057823] [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: 15489334] [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: 3264725] [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: 8043443] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 354-412, VARIANTS ILE-358; GLN-364; PHE-370; ARG-402 AND 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: 2511201] [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: 2129367] [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: 1904059] [Abstract] Cited for: GLYCOSYLATION AT SER-112 AND SER-120.
[15]	"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: 8598903] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF FVIIA IN COMPLEX WITH TF.
[16]	"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: 9925787] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF FVIIA IN COMPLEX WITH TF.
[17]	"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: 9692950] [Abstract] Cited for: STRUCTURE BY NMR OF 105-145.
[18]	"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: 2070047] [Abstract] Cited for: VARIANT GLN-364.
[19]	"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: 1634227] [Abstract] Cited for: VARIANTS GLN-364 AND PHE-370.
[20]	"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: 8364544] [Abstract] Cited for: VARIANT TYR-238.
[21]	"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: 8242057] [Abstract] Cited for: VARIANTS.
[22]	"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: 8204879] [Abstract] Cited for: VARIANTS CHARLOTTE GLN-139 AND GLN-212.
[23]	"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: 7860081] [Abstract] Cited for: VARIANT SER-367.
[24]	"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: 7981691] [Abstract] Cited for: VARIANT VAL-354.
[25]	"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: 7974346] [Abstract] Cited for: VARIANT MIE HIS-307.
[26]	"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: 8652821] [Abstract] Cited for: VARIANT MET-419.
[27]	"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: 8844208] [Abstract] Cited for: VARIANTS TRP-283; LYS-325; VAL-358; GLN-364; GLU-402 AND GLN-413.
[28]	"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: 8883260] [Abstract] Cited for: VARIANT VAL-304.
[29]	"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: 9576180] [Abstract] Cited for: VARIANT MORIOKA PRO-13.
[30]	"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: 9452082] [Abstract] Cited for: VARIANTS MALTA THR-194 AND VAL-304.
[31]	"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: 10391209] [Abstract] Cited for: VARIANTS ASP-295 AND GLN-413.
[32]	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)
[33]	"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: 11091194] [Abstract] Cited for: VARIANT GLY-389.
[34]	"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: 11129332] [Abstract] Cited for: VARIANTS 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.
[35]	"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: 10862079] [Abstract] Cited for: VARIANTS 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.
[36]	"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: 10984565] [Abstract] Cited for: VARIANT GLN-413.
+	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.
NP_062562.1.

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	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-6135N.

IntAct

P08709. 6 interactions.

STRING

P08709.

Protein family/group databases

MEROPS

S01.215.

PTM databases

GlycoSuiteDB

P08709.

Proteomic databases

PRIDE

P08709.

Genome annotation databases

Ensembl

ENST00000346342; ENSP00000329546; ENSG00000057593; Homo sapiens. [Genome view]
ENST00000375581; ENSP00000364731; ENSG00000057593; Homo sapiens. [Genome view]

GeneID

2155.

KEGG

hsa:2155.

NMPDR

fig|9606.3.peg.9116.

UCSC

uc001vsv.1. human.

Organism-specific databases

CTD

2155.

GeneCards

GC13P112808.

H-InvDB

HIX0037323.

HGNC

HGNC:3544. F7.

MIM

227500. gene+phenotype.

Orphanet

327. Congenital factor VII deficiency.

PharmGKB

PA24977.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

HBG715028.

HOVERGEN

P08709.

InParanoid

P08709.

OMA

VCPKGEC.

OrthoDB

EOG9QRKPC.

PhylomeDB

P08709.

Enzyme and pathway databases

BRENDA

3.4.21.21. 247.

Reactome

REACT_17015. Metabolism of proteins.
REACT_604. Hemostasis.

Gene expression databases

ArrayExpress

P08709.

Bgee

P08709.

CleanEx

HS_F7.

Genevestigator

P08709.

GermOnline

ENSG00000057593. Homo sapiens.

Family and domain databases

InterPro

IPR002383. Coagulation_factor_Gla_dom.
IPR006210. EGF-like.
IPR013032. EGF-like_reg_CS.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR001438. EGF_2.
IPR000742. EGF_3.
IPR001881. EGF_Ca_bd.
IPR018097. EGF_Ca_bd_CS.
IPR000294. GLA_domain.
IPR012224. Pept_S1A_FX.
IPR018114. Peptidase_S1/S6_AS.
IPR001254. Peptidase_S1_S6.
IPR001314. Peptidase_S1A.
IPR009003. Ser/Cys_Pept_Trypsin-like.
[Graphical view]

Pfam

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

PIRSF

PIRSF001143. Factor_X. 1 hit.

PRINTS

PR00722. CHYMOTRYPSIN.
PR00010. EGFBLOOD.
PR00001. GLABLOOD.

SMART

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

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 Resources

DrugBank

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

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:	February 9, 2010
This is version 158 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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.