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Reviewed, UniProtKB/Swiss-Prot O97507 (FA12_PIG)

Last modified June 16, 2009. Version 47. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Coagulation factor XII
    EC=3.4.21.38
Alternative name(s):
    Hageman factor
      Short name=HAF
Cleaved into the following 2 chains:
    1- Recommended name:
            Coagulation factor XIIa heavy chain
    2- Recommended name:
            Coagulation factor XIIa light chain
Gene names
Name: F12
OrganismSus scrofa (Pig)
Taxonomic identifier9823 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Suina › Suidae › Sus

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Protein attributes

Sequence length616 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level.

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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 to alpha-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.

Subcellular location

Secreted.

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.

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Ontologies

Keywords
   Biological processBlood coagulation
Fibrinolysis
   Cellular componentSecreted
   DomainEGF-like domain
Kringle
Repeat
Signal
   Molecular functionHydrolase
Protease
Serine protease
   PTMDisulfide bond
Glycoprotein
Zymogen
Gene Ontology (GO)
   Biological processblood coagulation

Inferred from electronic annotation. Source: UniProtKB-KW

fibrinolysis

Inferred from electronic annotation. Source: UniProtKB-KW

proteolysis

Inferred from electronic annotation. Source: InterPro

   Cellular componentextracellular space

Inferred from electronic annotation. Source: InterPro

   Molecular functionserine-type endopeptidase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 By similarity
Chain20 – 371352Coagulation factor XIIa heavy chain
PRO_0000232379
Chain372 – 616245Coagulation factor XIIa light chain
PRO_0000232382

Regions

Domain42 – 9049Fibronectin type-II
Domain94 – 13138EGF-like 1
Domain133 – 17341Fibronectin type-I
Domain174 – 21037EGF-like 2
Domain216 – 29580Kringle
Domain372 – 615244Peptidase S1
Compositional bias296 – 34853Pro-rich

Sites

Active site4111Charge relay system By similarity
Active site4601Charge relay system By similarity
Active site5641Charge relay system By similarity

Amino acid modifications

Glycosylation1091O-linked (Fuc) By similarity
Glycosylation2491N-linked (GlcNAc...) Potential
Glycosylation2711N-linked (GlcNAc...) Potential
Glycosylation3351N-linked (GlcNAc...) Potential
Glycosylation4321N-linked (GlcNAc...) Potential
Disulfide bond47 ↔ 73 By similarity
Disulfide bond61 ↔ 88 By similarity
Disulfide bond98 ↔ 110 By similarity
Disulfide bond104 ↔ 119 By similarity
Disulfide bond121 ↔ 130 By similarity
Disulfide bond135 ↔ 163 By similarity
Disulfide bond161 ↔ 170 By similarity
Disulfide bond178 ↔ 189 By similarity
Disulfide bond183 ↔ 198 By similarity
Disulfide bond200 ↔ 209 By similarity
Disulfide bond217 ↔ 295 By similarity
Disulfide bond238 ↔ 277 By similarity
Disulfide bond266 ↔ 290 By similarity
Disulfide bond358 ↔ 485 By similarity
Disulfide bond396 ↔ 412 By similarity
Disulfide bond404 ↔ 474 By similarity
Disulfide bond435 ↔ 438 By similarity
Disulfide bond501 ↔ 570 By similarity
Disulfide bond533 ↔ 549 By similarity
Disulfide bond560 ↔ 591 By similarity

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Sequences

Sequence LengthMass (Da)Tools
O97507-1 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: 4C5FE3D71EBBD1A9

FASTA61668,012
        10         20         30         40         50         60 
MRALLLLGIL LVSLESALLI PPWKDPRKHK VMASEHTVVL TVTGEPCHFP FQYYRQLYYK 

        70         80         90        100        110        120 
CIQRGQRGPR PWCATTPNFE KDQRWAYCLE PMKVKDHCNK GNPCQKGGTC VNMPNGPHCI 

       130        140        150        160        170        180 
CPDHFTGKHC QKEKCFEPQF LQFFQENEIW HRFEPAGVSK CQCKGPKAQC KPVASQVCST 

       190        200        210        220        230        240 
NPCLNGGSCL QTEGHRLCRC PTGYAGRLCD VDLKERCYSD RGLSYRGMAQ TTLSGAPCQP 

       250        260        270        280        290        300 
WASEATYWNM TAEQALNWGL GDHAFCRNPD NDTRPWCFVW RGDQLSWQYC RLARCQAPIG 

       310        320        330        340        350        360 
EAPPILTPTQ SPSEHQDSPL LSREPQPTTQ TPSQNLTSAW CAPPEQRGPL PSAGLVGCGQ 

       370        380        390        400        410        420 
RLRKRLSSLN RIVGGLVALP GAHPYIAALY WGQNFCAGSL IAPCWVLTAA HCLQNRPAPE 

       430        440        450        460        470        480 
ELTVVLGQDR HNQSCEQCQT LAVRSYRLHE SYSPKTYQHD LALVRLKETA DGCCAHPSPF 

       490        500        510        520        530        540 
VQPVCLPRSV ASSAEPEGAL CEVAGWGHQF EGAEEYSSFL QEAQVPLISP ERCSAADVHG 

       550        560        570        580        590        600 
AAFTPGMLCA GFLEGGTDAC QGDSGGPLVC EDETAERQLV LRGIVSWGSG CGDRLKPGVY 

       610 
TDVANYLAWI QEHTTS

« Hide

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References

[1]"Porcine liver factor XII."
Takahashi T., Kihara T.
Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Liver.

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Cross-references

Sequence databases

AB022426 mRNA. Translation: BAA37148.1.
RefSeqNP_999407.1.
UniGeneSsc.749

3D structure databases

HSSPHSSP built from PDB template 1FDP based on UniProtKB P00746.
ModBaseSearch...

Protein family/group databases

MEROPSS01.211.

Genome annotation databases

GeneID397474.
KEGGssc:397474.

Phylogenomic databases

HOVERGENO97507.

Enzyme and pathway databases

BRENDA3.4.21.38. 249.

Family and domain databases

InterProIPR014394. Coagulation_fac_XII_Hep-GF-Act.
IPR006209. EGF.
IPR006210. EGF-like.
IPR013032. EGF-like_reg_CS.
IPR000742. EGF_3.
IPR000083. Fibrnctn1.
IPR000562. FN_type2_col_bd.
IPR000001. Kringle.
IPR018056. Kringle_CS.
IPR018059. Kringle_sub.
IPR018114. Peptidase_S1/S6_AS.
IPR001254. Peptidase_S1_S6.
IPR001314. Peptidase_S1A.
[Graphical view]
Gene3DG3DSA:2.40.20.10. Kringle. 1 hit.
PfamPF00008. EGF. 2 hits.
PF00039. fn1. 1 hit.
PF00040. fn2. 1 hit.
PF00051. Kringle. 1 hit.
PF00089. Trypsin. 1 hit.
[Graphical view]
PIRSFPIRSF001146. Factor_XII_HGFA. 1 hit.
PRINTSPR00722. CHYMOTRYPSIN.
PR00013. FNTYPEII.
PR00018. KRINGLE.
ProDomPD000995. FN_Type_II. 1 hit.
PD000395. Kringle. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00181. EGF. 2 hits.
SM00058. FN1. 1 hit.
SM00059. FN2. 1 hit.
SM00130. KR. 1 hit.
SM00020. Tryp_SPc. 1 hit.
[Graphical view]
PROSITEPS00022. EGF_1. 2 hits.
PS01186. EGF_2. 1 hit.
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. 1 hit.
PS50070. KRINGLE_2. 1 hit.
PS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameFA12_PIG
AccessionPrimary (citable) accession number: O97507
Entry history
Integrated into UniProtKB/Swiss-Prot: April 4, 2006
Last sequence update: May 1, 1999
Last modified: June 16, 2009
This is version 47 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents