Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Coagulation factor XII

Gene

F12

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: -Experimental evidence at protein 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)DescriptionActionsGraphical viewLength
Active sitei394Charge relay systemBy similarity1
Active sitei443Charge relay systemBy similarity1
Active sitei545Charge relay systemBy similarity1

GO - Molecular functioni

  • calcium ion binding Source: InterPro
  • peptidase activity Source: MGI
  • serine-type endopeptidase activity Source: MGI

GO - Biological processi

Keywordsi

Molecular functionHydrolase, Protease, Serine protease
Biological processBlood coagulation, Fibrinolysis, Hemostasis

Enzyme and pathway databases

ReactomeiR-MMU-140837 Intrinsic Pathway of Fibrin Clot Formation

Protein family/group databases

MEROPSiS01.211

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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 13

Organism-specific databases

MGIiMGI:1891012 F12

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 19By similarityAdd BLAST19
ChainiPRO_000039455520 – 354Coagulation factor XIIa heavy chainAdd BLAST335
ChainiPRO_0000394556355 – 597Coagulation factor XIIa light chainAdd BLAST243

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi47 ↔ 73By similarity
Disulfide bondi61 ↔ 88By similarity
Disulfide bondi98 ↔ 110By similarity
Disulfide bondi104 ↔ 119By similarity
Glycosylationi109O-linked (Fuc) threonineBy similarity1
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
Glycosylationi249N-linked (GlcNAc...) asparagineBy similarity1
Disulfide bondi266 ↔ 290By similarity
Glycosylationi299O-linked (GalNAc...) threonineBy similarity1
Glycosylationi308O-linked (GalNAc...) serineBy similarity1
Glycosylationi327O-linked (GalNAc...) threonineBy similarity1
Disulfide bondi341 ↔ 468By similarity
Disulfide bondi379 ↔ 395By similarity
Disulfide bondi387 ↔ 457By similarity
Glycosylationi415N-linked (GlcNAc...) asparagineBy similarity1
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
PeptideAtlasiQ80YC5
PRIDEiQ80YC5

PTM databases

PhosphoSitePlusiQ80YC5

Expressioni

Gene expression databases

BgeeiENSMUSG00000021492
ExpressionAtlasiQ80YC5 baseline and differential
GenevisibleiQ80YC5 MM

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 interactors
MINTiQ80YC5
STRINGi10090.ENSMUSP00000021948

Structurei

3D structure databases

ProteinModelPortaliQ80YC5
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini42 – 90Fibronectin type-IIPROSITE-ProRule annotationAdd BLAST49
Domaini94 – 131EGF-like 1PROSITE-ProRule annotationAdd BLAST38
Domaini133 – 173Fibronectin type-IPROSITE-ProRule annotationAdd BLAST41
Domaini174 – 210EGF-like 2PROSITE-ProRule annotationAdd BLAST37
Domaini216 – 295KringlePROSITE-ProRule annotationAdd BLAST80
Domaini355 – 596Peptidase S1PROSITE-ProRule annotationAdd BLAST242

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi296 – 331Pro-richAdd BLAST36

Sequence similaritiesi

Belongs to the peptidase S1 family.PROSITE-ProRule annotation

Keywords - Domaini

EGF-like domain, Kringle, Repeat, Signal

Phylogenomic databases

eggNOGiKOG1217 Eukaryota
KOG3627 Eukaryota
COG5640 LUCA
GeneTreeiENSGT00760000119133
HOGENOMiHOG000237314
HOVERGENiHBG004345
InParanoidiQ80YC5
KOiK01328
OMAiEKCFEPQ
OrthoDBiEOG091G0AH5
PhylomeDBiQ80YC5
TreeFamiTF329901

Family and domain databases

CDDicd00061 FN1, 1 hit
cd00062 FN2, 1 hit
cd00190 Tryp_SPc, 1 hit
Gene3Di2.10.10.10, 1 hit
2.40.20.10, 1 hit
InterProiView protein in InterPro
IPR014394 Coagulation_fac_XII/HGFA
IPR001881 EGF-like_Ca-bd_dom
IPR013032 EGF-like_CS
IPR000742 EGF-like_dom
IPR000083 Fibronectin_type1
IPR000562 FN_type2_dom
IPR036943 FN_type2_sf
IPR000001 Kringle
IPR013806 Kringle-like
IPR018056 Kringle_CS
IPR038178 Kringle_sf
IPR009003 Peptidase_S1_PA
IPR001314 Peptidase_S1A
IPR001254 Trypsin_dom
IPR018114 TRYPSIN_HIS
IPR033116 TRYPSIN_SER
PfamiView protein in Pfam
PF00008 EGF, 2 hits
PF00039 fn1, 1 hit
PF00040 fn2, 1 hit
PF00051 Kringle, 1 hit
PF00089 Trypsin, 1 hit
PIRSFiPIRSF001146 Factor_XII_HGFA, 1 hit
PRINTSiPR00722 CHYMOTRYPSIN
SMARTiView protein in SMART
SM00181 EGF, 2 hits
SM00179 EGF_CA, 2 hits
SM00058 FN1, 1 hit
SM00059 FN2, 1 hit
SM00130 KR, 1 hit
SM00020 Tryp_SPc, 1 hit
SUPFAMiSSF50494 SSF50494, 1 hit
SSF57440 SSF57440, 2 hits
PROSITEiView protein in PROSITE
PS00022 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

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 15, 2010 - v2
Checksum:i342FB7E764957E03
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti82D → N in CAA67891 (Ref. 1) Curated1
Sequence conflicti152R → K in CAA67891 (Ref. 1) Curated1
Sequence conflicti491F → L in CAA67891 (Ref. 1) Curated1

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_021489.3
UniGeneiMm.42224

Genome annotation databases

EnsembliENSMUST00000021948; ENSMUSP00000021948; ENSMUSG00000021492
GeneIDi58992
KEGGimmu:58992
UCSCiuc007qqv.3 mouse

Similar proteinsi

Entry informationi

Entry nameiFA12_MOUSE
AccessioniPrimary (citable) accession number: Q80YC5
Secondary accession number(s): O35727, Q6PER0
Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 15, 2010
Last sequence update: June 15, 2010
Last modified: July 18, 2018
This is version 136 of the entry and version 2 of the sequence. See 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

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health