Coagulation factor XII precursor - Bos taurus (Bovine)

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P98140 (FA12_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 105. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Coagulation factor XII
EC=3.4.21.38

Alternative name(s):
Hageman factor
Short name=HAF

Gene names

Name:

F12

Organism

Bos taurus (Bovine)

Taxonomic identifier

9913 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Protein attributes

Sequence length	612 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	Factor XII is a serum glycoprotein that participates in the initiation of blood coagulation, fibrinolysis, and the generation of bradykinin and angiotensin. Prekallikrein is cleaved by factor XII to form kallikrein, which then cleaves factor XII first to alpha-factor XIIa and then to beta-factor XIIa. Alpha-factor XIIa activates factor XI to factor XIa By similarity.
Catalytic activity	Selective cleavage of Arg-\|-Ile bonds in factor VII to form factor VIIa and factor XI to form factor XIa.
Subunit structure	Interacts with HRG; the interaction, which is enhanced in the presence of zinc ions and inhibited by heparin-binding, inhibits factor XII autoactivation and contact-initiated coagulation By similarity.
Subcellular location	Secreted.
Post-translational modification	O- and N-glycosylated By similarity.
Sequence similarities	Belongs to the peptidase S1 family. Contains 2 EGF-like domains. Contains 1 fibronectin type-I domain. Contains 1 fibronectin type-II domain. Contains 1 kringle domain. Contains 1 peptidase S1 domain.

Ontologies

Keywords
Biological process	Blood coagulation Fibrinolysis
Cellular component	Secreted
Domain	EGF-like domain Kringle Repeat Signal
Molecular function	Hydrolase Protease Serine protease
PTM	Disulfide bond Glycoprotein Zymogen
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	blood coagulation Inferred from electronic annotation. Source: UniProtKB-KW fibrinolysis Inferred from electronic annotation. Source: UniProtKB-KW proteolysis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	extracellular space Inferred from electronic annotation. Source: InterPro
Molecular function	serine-type endopeptidase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 19

Ref.3

Chain

20 – 368

349

Coagulation factor XIIa heavy chain

PRO_0000027829

Chain

369 – 612

244

Coagulation factor XIIa light chain

PRO_0000027830

Regions

Domain

42 – 90

Fibronectin type-II

Domain

94 – 131

EGF-like 1

Domain

133 – 173

Fibronectin type-I

Domain

174 – 210

EGF-like 2

Domain

217 – 306

Kringle

Domain

369 – 611

243

Peptidase S1

Compositional bias

316 – 352

Pro-rich

Sites

Active site

408

Charge relay system By similarity

Active site

457

Charge relay system By similarity

Active site

560

Charge relay system By similarity

Amino acid modifications

Glycosylation

109

O-linked (Fuc) By similarity

Glycosylation

251

N-linked (GlcNAc...) Potential

Glycosylation

282

N-linked (GlcNAc...) Potential

Glycosylation

429

N-linked (GlcNAc...) Potential

Disulfide bond

47 ↔ 73

By similarity

Disulfide bond

61 ↔ 88

By similarity

Disulfide bond

98 ↔ 110

By similarity

Disulfide bond

104 ↔ 119

By similarity

Disulfide bond

121 ↔ 130

By similarity

Disulfide bond

135 ↔ 163

By similarity

Disulfide bond

161 ↔ 170

By similarity

Disulfide bond

178 ↔ 189

By similarity

Disulfide bond

183 ↔ 198

By similarity

Disulfide bond

200 ↔ 209

By similarity

Disulfide bond

217 ↔ 306

By similarity

Disulfide bond

240 ↔ 288

By similarity

Disulfide bond

268 ↔ 301

By similarity

Disulfide bond

355 ↔ 482

By similarity

Disulfide bond

393 ↔ 409

By similarity

Disulfide bond

401 ↔ 471

By similarity

Disulfide bond

432 ↔ 435

By similarity

Disulfide bond

498 ↔ 566

By similarity

Disulfide bond

529 ↔ 545

By similarity

Disulfide bond

556 ↔ 587

By similarity

Experimental info

Sequence conflict

11 – 18

LVSLESTV → GRVGGRVG in AAB30804. Ref.2

Sequence conflict

D → E in AAB30804. Ref.2

Sequence conflict

R → Q in AAB30804. Ref.2

Sequence conflict

187

G → D in AAB30804. Ref.2

Sequence conflict

270 – 278

Missing in AAB30804. Ref.2

Sequence conflict

287

L → W in AAB30804. Ref.2

Sequences

Sequence

Length

Mass (Da)

Tools

P98140 [UniParc].

Last modified May 1, 2007. Version 2.
Checksum: D5C9292807DD5283
Show »

FASTA

612

67,160

        10         20         30         40         50         60 
MRALLLLGAL LVSLESTVST PPWKGPKKHK LTDSEHTVVL TVTGEPCHFP FQYHRQLHHK 

        70         80         90        100        110        120 
CIHRGRPGPR PWCATTPNFE KDQRWAYCLE PKKVKDHCSK HNPCQKGGTC VNMPDGPRCI 

       130        140        150        160        170        180 
CADHFTGKHC QKEKCFEPQF FRFFHENEIW HRLEPAGVVK CQCKGPNAQC KPLASQVCRT 

       190        200        210        220        230        240 
NPCLNGGSCL QAEGHRLCRC APSFAGRLCD VDLKASCYDD RDRGLSYRGM AGTTLSGAPC 

       250        260        270        280        290        300 
QSWASEATYW NVTAEQVLNW GLGDHAFCRA STPPRGYRNP DNDTRPLCFI WKGDRLSWNY 

       310        320        330        340        350        360 
CRLAPCQAAA GHEHFPLPSP SALQKPESTT QTPLPSLTSG WCSPTPLASG GPGGCGQRLR 

       370        380        390        400        410        420 
KWLSSLNRVV GGLVALPGAH PYIAALYWDQ HFCAGSLIAP CWVLTAAHCL QNRPAPKELT 

       430        440        450        460        470        480 
VVLGQDRHNQ SCEQCQTLAV RDYRLHEAFS PITYQHDLAL VRLQESADGC CAHPSPFVQP 

       490        500        510        520        530        540 
VCLPSTAARP AESEAAVCEV AGWGHQFEGG EYSSFLQEAQ VPLIDPQRCS APDVHGAAFT 

       550        560        570        580        590        600 
QGMLCAGFLE GGTDACQGDS GGPLVCEDET PERQLILRGI VSWGSGCGNR LKPGVYTDVA 

       610 
NYLAWIREHT AS

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	NIH - Mammalian Gene Collection (MGC) project Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Hereford. Tissue: Fetal liver.
[2]	"Primary structure of bovine Hageman factor (blood coagulation factor XII): comparison with human and guinea pig molecules." Shibuya Y., Semba U., Okabe H., Kambara T., Yamamoto T. Biochim. Biophys. Acta 1206:63-70(1994) [PubMed: 8186251] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 11-612. Tissue: Liver.
[3]	"Isolation and characterization of bovine factor XII (Hageman factor)." Fujikawa K., Walsh A.K., Davie W.E. Biochemistry 16:2270-2278(1977) [PubMed: 861210] [Abstract] Cited for: PROTEIN SEQUENCE OF 20-31; 369-383 AND 544-569.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BC120000 mRNA. Translation: AAI20001.1. S70164 mRNA. Translation: AAB30804.2.
IPI	IPI00825179.
PIR	S45281.
RefSeq	NP_001068587.1. NM_001075119.1.
UniGene	Bt.89433.
3D structure databases
ProteinModelPortal	P98140.
ModBase	Search...
Protein-protein interaction databases
STRING	P98140.
Protein family/group databases
MEROPS	S01.211.
Proteomic databases
PRIDE	P98140.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	280789.
KEGG	bta:280789.
Organism-specific databases
CTD	2161.
Phylogenomic databases
eggNOG	maNOG14534.
GeneTree	ENSGT00570000078945.
HOVERGEN	HBG004345.
InParanoid	P98140.
OrthoDB	EOG41G33Q.
Family and domain databases
InterPro	IPR014394. Coagulation_fac_XIIa/HGFA. IPR006209. EGF. IPR006210. EGF-like. IPR013032. EGF-like_reg_CS. IPR000742. EGF_3. IPR000083. Fibronectin_type1. IPR000562. FN_type2_col-bd. IPR000001. Kringle. IPR013806. Kringle-like. IPR009003. Pept_cys/ser_Trypsin-like. IPR018114. Peptidase_S1/S6_AS. IPR001254. Peptidase_S1_S6. IPR001314. Peptidase_S1A. [Graphical view]
Gene3D	G3DSA:2.10.10.10. FN2. 1 hit. G3DSA:2.40.20.10. Kringle. 1 hit.
KO	K01328.
Pfam	PF00008. EGF. 2 hits. PF00039. fn1. 1 hit. PF00040. fn2. 1 hit. PF00051. Kringle. 1 hit. PF00089. Trypsin. 1 hit. [Graphical view]
PIRSF	PIRSF001146. Factor_XII_HGFA. 1 hit.
PRINTS	PR00722. CHYMOTRYPSIN. PR00018. KRINGLE.
SMART	SM00181. EGF. 2 hits. SM00058. FN1. 1 hit. SM00059. FN2. 1 hit. SM00130. KR. 1 hit. SM00020. Tryp_SPc. 1 hit. [Graphical view]
SUPFAM	SSF57440. Kringle-like. 2 hits. SSF50494. Pept_Ser_Cys. 1 hit.
PROSITE	PS00022. EGF_1. 2 hits. PS01186. EGF_2. False negative. PS50026. EGF_3. 2 hits. PS01253. FN1_1. 1 hit. PS51091. FN1_2. 1 hit. PS00023. FN2_1. 1 hit. PS51092. FN2_2. 1 hit. PS00021. KRINGLE_1. False negative. PS50070. KRINGLE_2. 1 hit. PS50240. TRYPSIN_DOM. 1 hit. PS00134. TRYPSIN_HIS. 1 hit. PS00135. TRYPSIN_SER. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

FA12_BOVIN

Accession

Primary (citable) accession number: P98140
Secondary accession number(s): Q0P5I3

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1996
Last sequence update:	May 1, 2007
Last modified:	November 16, 2011
This is version 105 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Cleaved into the following 2 chains:

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Family and domain databases

Entry information

Relevant documents