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Protein

Coagulation factor XII

Gene

F12

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

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).By similarity

Catalytic activityi

Selective cleavage of Arg-|-Ile bonds in factor VII to form factor VIIa and factor XI to form factor XIa.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei394 – 3941Charge relay systemBy similarity
Active sitei443 – 4431Charge relay systemBy similarity
Active sitei545 – 5451Charge relay systemBy similarity

GO - Molecular functioni

  1. peptidase activity Source: MGI
  2. serine-type aminopeptidase activity Source: Ensembl
  3. serine-type endopeptidase activity Source: MGI

GO - Biological processi

  1. blood coagulation Source: MGI
  2. Factor XII activation Source: MGI
  3. fibrinolysis Source: UniProtKB-KW
  4. plasma kallikrein-kinin cascade Source: MGI
  5. positive regulation of blood coagulation Source: MGI
  6. positive regulation of fibrinolysis Source: MGI
  7. positive regulation of plasminogen activation Source: MGI
  8. protein autoprocessing Source: MGI
  9. protein processing Source: MGI
  10. regulation of blood coagulation Source: MGI
  11. response to misfolded protein Source: MGI
  12. zymogen activation Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Serine protease

Keywords - Biological processi

Blood coagulation, Fibrinolysis, Hemostasis

Enzyme and pathway databases

ReactomeiREACT_340184. Intrinsic Pathway.

Names & Taxonomyi

Protein namesi
Recommended name:
Coagulation factor XII (EC:3.4.21.38)
Alternative name(s):
Hageman factor
Short name:
HAF
Cleaved into the following 2 chains:
Gene namesi
Name:F12
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 13

Organism-specific databases

MGIiMGI:1891012. F12.

Subcellular locationi

Secreted By similarity

GO - Cellular componenti

  1. extracellular space Source: MGI
  2. extracellular vesicular exosome Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1919By similarityAdd
BLAST
Chaini20 – 354335Coagulation factor XIIa heavy chainPRO_0000394555Add
BLAST
Chaini355 – 597243Coagulation factor XIIa light chainPRO_0000394556Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi47 ↔ 73By similarity
Disulfide bondi61 ↔ 88By similarity
Disulfide bondi98 ↔ 110By similarity
Disulfide bondi104 ↔ 119By similarity
Glycosylationi109 – 1091O-linked (Fuc)By similarity
Disulfide bondi121 ↔ 130By similarity
Disulfide bondi135 ↔ 163By similarity
Disulfide bondi161 ↔ 170By similarity
Disulfide bondi178 ↔ 189By similarity
Disulfide bondi183 ↔ 198By similarity
Disulfide bondi200 ↔ 209By similarity
Disulfide bondi217 ↔ 295By similarity
Disulfide bondi238 ↔ 277By similarity
Glycosylationi249 – 2491N-linked (GlcNAc...)By similarity
Disulfide bondi266 ↔ 290By similarity
Glycosylationi299 – 2991O-linked (GalNAc...)By similarity
Glycosylationi308 – 3081O-linked (GalNAc...)By similarity
Glycosylationi327 – 3271O-linked (GalNAc...)By similarity
Disulfide bondi341 ↔ 468By similarity
Disulfide bondi379 ↔ 395By similarity
Disulfide bondi387 ↔ 457By similarity
Glycosylationi415 – 4151N-linked (GlcNAc...)By similarity
Disulfide bondi418 ↔ 421By similarity
Disulfide bondi482 ↔ 551By similarity
Disulfide bondi514 ↔ 530By similarity
Disulfide bondi541 ↔ 572By similarity

Post-translational modificationi

O- and N-glycosylated.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein, Zymogen

Proteomic databases

MaxQBiQ80YC5.
PaxDbiQ80YC5.
PRIDEiQ80YC5.

Expressioni

Gene expression databases

BgeeiQ80YC5.
ExpressionAtlasiQ80YC5. baseline and differential.
GenevestigatoriQ80YC5.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

IntActiQ80YC5. 2 interactions.
MINTiMINT-4104823.
STRINGi10090.ENSMUSP00000021948.

Structurei

3D structure databases

ProteinModelPortaliQ80YC5.
SMRiQ80YC5. Positions 44-88, 96-597.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini42 – 9049Fibronectin type-IIPROSITE-ProRule annotationAdd
BLAST
Domaini94 – 13138EGF-like 1PROSITE-ProRule annotationAdd
BLAST
Domaini133 – 17341Fibronectin type-IPROSITE-ProRule annotationAdd
BLAST
Domaini174 – 21037EGF-like 2PROSITE-ProRule annotationAdd
BLAST
Domaini216 – 29580KringlePROSITE-ProRule annotationAdd
BLAST
Domaini355 – 596242Peptidase S1PROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi296 – 33136Pro-richAdd
BLAST

Sequence similaritiesi

Belongs to the peptidase S1 family.PROSITE-ProRule annotation
Contains 2 EGF-like domains.PROSITE-ProRule annotation
Contains 1 fibronectin type-I domain.PROSITE-ProRule annotation
Contains 1 fibronectin type-II domain.PROSITE-ProRule annotation
Contains 1 kringle domain.PROSITE-ProRule annotation
Contains 1 peptidase S1 domain.PROSITE-ProRule annotation

Keywords - Domaini

EGF-like domain, Kringle, Repeat, Signal

Phylogenomic databases

eggNOGiCOG5640.
GeneTreeiENSGT00760000119133.
HOGENOMiHOG000237314.
HOVERGENiHBG004345.
InParanoidiQ80YC5.
KOiK01328.
OMAiPKKVKDH.
OrthoDBiEOG75B84T.
PhylomeDBiQ80YC5.
TreeFamiTF329901.

Family and domain databases

Gene3Di2.10.10.10. 1 hit.
InterProiIPR014394. 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]
PfamiPF00008. EGF. 2 hits.
PF00039. fn1. 1 hit.
PF00040. fn2. 1 hit.
PF00051. Kringle. 1 hit.
PF00089. Trypsin. 1 hit.
[Graphical view]
PIRSFiPIRSF001146. Factor_XII_HGFA. 1 hit.
PRINTSiPR00722. CHYMOTRYPSIN.
SMARTiSM00181. EGF. 2 hits.
SM00058. FN1. 1 hit.
SM00059. FN2. 1 hit.
SM00130. KR. 1 hit.
SM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMiSSF50494. SSF50494. 1 hit.
SSF57440. SSF57440. 2 hits.
PROSITEiPS00022. 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]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q80YC5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTALLFLGSL LMSLDLTLSA PPWKDSKKFK DAPDGPTVVL TVDGRLCHFP
60 70 80 90 100
FQYHRQLHHK CIHKRRPGSR PWCATTPNFD EDQQWGYCLE PKKVKDHCSK
110 120 130 140 150
HNPCHKGGTC INTPNGPHCL CPEHLTGKHC QKEKCFEPQL LKFFHENELW
160 170 180 190 200
FRTGPGGVAR CECKGSEAHC KPVASQACSI NPCLNGGSCL LVEDHPLCRC
210 220 230 240 250
PTGYTGYFCD LDLWATCYEG RGLSYRGQAG TTQSGAPCQR WTVEATYRNM
260 270 280 290 300
TEKQALSWGL GHHAFCRNPD NDTRPWCFVW SGDRLSWDYC GLEQCQTPTF
310 320 330 340 350
APLVVPESQE ESPSQAPSLS HAPNDSTDHQ TSLSKTNTMG CGQRFRKGLS
360 370 380 390 400
SFMRVVGGLV ALPGSHPYIA ALYWGNNFCA GSLIAPCWVL TAAHCLQNRP
410 420 430 440 450
APEELTVVLG QDRHNQSCEW CQTLAVRSYR LHEGFSSITY QHDLALLRLQ
460 470 480 490 500
ESKTNSCAIL SPHVQPVCLP SGAAPPSETV LCEVAGWGHQ FEGAEEYSTF
510 520 530 540 550
LQEAQVPFIA LDRCSNSNVH GDAILPGMLC AGFLEGGTDA CQGDSGGPLV
560 570 580 590
CEEGTAEHQL TLRGVISWGS GCGDRNKPGV YTDVANYLAW IQKHIAS
Length:597
Mass (Da):65,701
Last modified:June 14, 2010 - v2
Checksum:i342FB7E764957E03
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti82 – 821D → N in CAA67891 (Ref. 1) Curated
Sequence conflicti152 – 1521R → K in CAA67891 (Ref. 1) Curated
Sequence conflicti491 – 4911F → L in CAA67891 (Ref. 1) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X99571 mRNA. Translation: CAA67891.1.
BC057921 mRNA. Translation: AAH57921.1.
BC049867 mRNA. Translation: AAH49867.1. Different initiation.
CCDSiCCDS36675.1.
RefSeqiNP_067464.2. NM_021489.2.
UniGeneiMm.42224.

Genome annotation databases

EnsembliENSMUST00000021948; ENSMUSP00000021948; ENSMUSG00000021492.
GeneIDi58992.
KEGGimmu:58992.
UCSCiuc007qqv.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X99571 mRNA. Translation: CAA67891.1.
BC057921 mRNA. Translation: AAH57921.1.
BC049867 mRNA. Translation: AAH49867.1. Different initiation.
CCDSiCCDS36675.1.
RefSeqiNP_067464.2. NM_021489.2.
UniGeneiMm.42224.

3D structure databases

ProteinModelPortaliQ80YC5.
SMRiQ80YC5. Positions 44-88, 96-597.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ80YC5. 2 interactions.
MINTiMINT-4104823.
STRINGi10090.ENSMUSP00000021948.

Proteomic databases

MaxQBiQ80YC5.
PaxDbiQ80YC5.
PRIDEiQ80YC5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000021948; ENSMUSP00000021948; ENSMUSG00000021492.
GeneIDi58992.
KEGGimmu:58992.
UCSCiuc007qqv.2. mouse.

Organism-specific databases

CTDi2161.
MGIiMGI:1891012. F12.

Phylogenomic databases

eggNOGiCOG5640.
GeneTreeiENSGT00760000119133.
HOGENOMiHOG000237314.
HOVERGENiHBG004345.
InParanoidiQ80YC5.
KOiK01328.
OMAiPKKVKDH.
OrthoDBiEOG75B84T.
PhylomeDBiQ80YC5.
TreeFamiTF329901.

Enzyme and pathway databases

ReactomeiREACT_340184. Intrinsic Pathway.

Miscellaneous databases

NextBioi314494.
PROiQ80YC5.
SOURCEiSearch...

Gene expression databases

BgeeiQ80YC5.
ExpressionAtlasiQ80YC5. baseline and differential.
GenevestigatoriQ80YC5.

Family and domain databases

Gene3Di2.10.10.10. 1 hit.
InterProiIPR014394. 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]
PfamiPF00008. EGF. 2 hits.
PF00039. fn1. 1 hit.
PF00040. fn2. 1 hit.
PF00051. Kringle. 1 hit.
PF00089. Trypsin. 1 hit.
[Graphical view]
PIRSFiPIRSF001146. Factor_XII_HGFA. 1 hit.
PRINTSiPR00722. CHYMOTRYPSIN.
SMARTiSM00181. EGF. 2 hits.
SM00058. FN1. 1 hit.
SM00059. FN2. 1 hit.
SM00130. KR. 1 hit.
SM00020. Tryp_SPc. 1 hit.
[Graphical view]
SUPFAMiSSF50494. SSF50494. 1 hit.
SSF57440. SSF57440. 2 hits.
PROSITEiPS00022. 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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Schloesser M., Schwager S., Engel W.
    Submitted (JUN-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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: FVB/N.
    Tissue: Liver.

Entry informationi

Entry nameiFA12_MOUSE
AccessioniPrimary (citable) accession number: Q80YC5
Secondary accession number(s): O35727, Q6PER0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 14, 2010
Last sequence update: June 14, 2010
Last modified: March 31, 2015
This is version 112 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.