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Q80YC5 (FA12_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 105. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Coagulation factor XII

EC=3.4.21.38
Alternative name(s):
Hageman factor
Short name=HAF
Gene names
Name:F12
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length597 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript 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 trypsin cleaves it 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 By similarity.

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.

Sequence caution

The sequence AAH49867.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
   Biological processBlood coagulation
Fibrinolysis
Hemostasis
   Cellular componentSecreted
   DomainEGF-like domain
Kringle
Repeat
Signal
   Molecular functionHydrolase
Protease
Serine protease
   PTMDisulfide bond
Glycoprotein
Zymogen
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processFactor XII activation

Inferred from electronic annotation. Source: Ensembl

blood coagulation

Inferred from mutant phenotype PubMed 15351846. Source: MGI

fibrinolysis

Inferred from electronic annotation. Source: UniProtKB-KW

positive regulation of blood coagulation

Inferred from electronic annotation. Source: Ensembl

positive regulation of fibrinolysis

Inferred from electronic annotation. Source: Ensembl

positive regulation of plasminogen activation

Inferred from electronic annotation. Source: Ensembl

protein autoprocessing

Inferred from electronic annotation. Source: Ensembl

regulation of blood coagulation

Inferred from mutant phenotype PubMed 16533887. Source: MGI

response to misfolded protein

Inferred from electronic annotation. Source: Ensembl

zymogen activation

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentextracellular space

Inferred from mutant phenotype PubMed 15351846. Source: MGI

   Molecular_functionpeptidase activity

Inferred from mutant phenotype PubMed 15351846. Source: MGI

serine-type aminopeptidase activity

Inferred from electronic annotation. Source: Ensembl

serine-type endopeptidase activity

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 By similarity
Chain20 – 354335Coagulation factor XIIa heavy chain
PRO_0000394555
Chain355 – 597243Coagulation factor XIIa light chain
PRO_0000394556

Regions

Domain42 – 9049Fibronectin type-II
Domain94 – 13138EGF-like 1
Domain133 – 17341Fibronectin type-I
Domain174 – 21037EGF-like 2
Domain216 – 29580Kringle
Domain355 – 596242Peptidase S1
Compositional bias296 – 33136Pro-rich

Sites

Active site3941Charge relay system By similarity
Active site4431Charge relay system By similarity
Active site5451Charge relay system By similarity

Amino acid modifications

Glycosylation1091O-linked (Fuc) By similarity
Glycosylation2491N-linked (GlcNAc...) By similarity
Glycosylation2991O-linked (GalNAc...) By similarity
Glycosylation3081O-linked (GalNAc...) By similarity
Glycosylation3271O-linked (GalNAc...) By similarity
Glycosylation4151N-linked (GlcNAc...) By similarity
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 bond341 ↔ 468 By similarity
Disulfide bond379 ↔ 395 By similarity
Disulfide bond387 ↔ 457 By similarity
Disulfide bond418 ↔ 421 By similarity
Disulfide bond482 ↔ 551 By similarity
Disulfide bond514 ↔ 530 By similarity
Disulfide bond541 ↔ 572 By similarity

Experimental info

Sequence conflict821D → N in CAA67891. Ref.1
Sequence conflict1521R → K in CAA67891. Ref.1
Sequence conflict4911F → L in CAA67891. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q80YC5 [UniParc].

Last modified June 15, 2010. Version 2.
Checksum: 342FB7E764957E03

FASTA59765,701
        10         20         30         40         50         60 
MTALLFLGSL LMSLDLTLSA PPWKDSKKFK DAPDGPTVVL TVDGRLCHFP FQYHRQLHHK 

        70         80         90        100        110        120 
CIHKRRPGSR PWCATTPNFD EDQQWGYCLE PKKVKDHCSK HNPCHKGGTC INTPNGPHCL 

       130        140        150        160        170        180 
CPEHLTGKHC QKEKCFEPQL LKFFHENELW FRTGPGGVAR CECKGSEAHC KPVASQACSI 

       190        200        210        220        230        240 
NPCLNGGSCL LVEDHPLCRC PTGYTGYFCD LDLWATCYEG RGLSYRGQAG TTQSGAPCQR 

       250        260        270        280        290        300 
WTVEATYRNM TEKQALSWGL GHHAFCRNPD NDTRPWCFVW SGDRLSWDYC GLEQCQTPTF 

       310        320        330        340        350        360 
APLVVPESQE ESPSQAPSLS HAPNDSTDHQ TSLSKTNTMG CGQRFRKGLS SFMRVVGGLV 

       370        380        390        400        410        420 
ALPGSHPYIA ALYWGNNFCA GSLIAPCWVL TAAHCLQNRP APEELTVVLG QDRHNQSCEW 

       430        440        450        460        470        480 
CQTLAVRSYR LHEGFSSITY QHDLALLRLQ ESKTNSCAIL SPHVQPVCLP SGAAPPSETV 

       490        500        510        520        530        540 
LCEVAGWGHQ FEGAEEYSTF LQEAQVPFIA LDRCSNSNVH GDAILPGMLC AGFLEGGTDA 

       550        560        570        580        590 
CQGDSGGPLV CEEGTAEHQL TLRGVISWGS GCGDRNKPGV YTDVANYLAW IQKHIAS 

« Hide

References

« Hide 'large scale' references
[1]Schloesser M., Schwager S., Engel W.
Submitted (JUL-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Liver.
[2]"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].
Strain: FVB/N.
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X99571 mRNA. Translation: CAA67891.1.
BC057921 mRNA. Translation: AAH57921.1.
BC049867 mRNA. Translation: AAH49867.1. Different initiation.
CCDSCCDS36675.1.
RefSeqNP_067464.2. NM_021489.2.
UniGeneMm.42224.

3D structure databases

ProteinModelPortalQ80YC5.
SMRQ80YC5. Positions 44-88, 96-597.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ80YC5. 2 interactions.
MINTMINT-4104823.
STRING10090.ENSMUSP00000021948.

Protein family/group databases

MEROPSS01.211.

Proteomic databases

PaxDbQ80YC5.
PRIDEQ80YC5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000021948; ENSMUSP00000021948; ENSMUSG00000021492.
GeneID58992.
KEGGmmu:58992.
UCSCuc007qqv.2. mouse.

Organism-specific databases

CTD2161.
MGIMGI:1891012. F12.

Phylogenomic databases

eggNOGCOG5640.
GeneTreeENSGT00740000115235.
HOGENOMHOG000237314.
HOVERGENHBG004345.
InParanoidQ6PER0.
KOK01328.
OMAPKKVKDH.
OrthoDBEOG75B84T.
PhylomeDBQ80YC5.
TreeFamTF329901.

Gene expression databases

BgeeQ80YC5.
GenevestigatorQ80YC5.

Family and domain databases

Gene3D2.10.10.10. 1 hit.
2.40.20.10. 1 hit.
InterProIPR014394. Coagulation_fac_XIIa/HGFA.
IPR000742. EG-like_dom.
IPR013032. EGF-like_CS.
IPR000083. Fibronectin_type1.
IPR000562. FN_type2_col-bd.
IPR000001. Kringle.
IPR013806. Kringle-like.
IPR018056. Kringle_CS.
IPR001254. Peptidase_S1.
IPR018114. Peptidase_S1_AS.
IPR001314. Peptidase_S1A.
IPR009003. Trypsin-like_Pept_dom.
[Graphical view]
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.
SMARTSM00181. EGF. 2 hits.
SM00058. FN1. 1 hit.
SM00059. FN2. 1 hit.
SM00130. KR. 1 hit.
SM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMSSF50494. SSF50494. 1 hit.
SSF57440. SSF57440. 2 hits.
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...

Other

NextBio314494.
PROQ80YC5.
SOURCESearch...

Entry information

Entry nameFA12_MOUSE
AccessionPrimary (citable) accession number: Q80YC5
Secondary accession number(s): O35727, Q6PER0
Entry history
Integrated into UniProtKB/Swiss-Prot: June 15, 2010
Last sequence update: June 15, 2010
Last modified: July 9, 2014
This is version 105 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot