FA12_MOUSE
ID FA12_MOUSE Reviewed; 597 AA.
AC Q80YC5; O35727; Q6PER0;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 15-JUN-2010, sequence version 2.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Coagulation factor XII;
DE EC=3.4.21.38;
DE AltName: Full=Hageman factor;
DE Short=HAF;
DE Contains:
DE RecName: Full=Coagulation factor XIIa heavy chain;
DE Contains:
DE RecName: Full=Coagulation factor XIIa light chain;
DE Flags: Precursor;
GN Name=F12;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RA Schloesser M., Schwager S., Engel W.;
RL Submitted (JUL-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Liver;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Lung, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Factor XII is a serum glycoprotein that participates in the
CC initiation of blood coagulation, fibrinolysis, and the generation of
CC bradykinin and angiotensin. Prekallikrein is cleaved by factor XII to
CC form kallikrein, which then cleaves factor XII first to alpha-factor
CC XIIa and then trypsin cleaves it to beta-factor XIIa. Alpha-factor XIIa
CC activates factor XI to factor XIa (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Selective cleavage of Arg-|-Ile bonds in factor VII to form
CC factor VIIa and factor XI to form factor XIa.; EC=3.4.21.38;
CC -!- SUBUNIT: Interacts with HRG; the interaction, which is enhanced in the
CC presence of zinc ions and inhibited by heparin-binding, inhibits factor
CC XII autoactivation and contact-initiated coagulation. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- PTM: O- and N-glycosylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00274}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH49867.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; X99571; CAA67891.1; -; mRNA.
DR EMBL; BC057921; AAH57921.1; -; mRNA.
DR EMBL; BC049867; AAH49867.1; ALT_INIT; mRNA.
DR CCDS; CCDS36675.1; -.
DR RefSeq; NP_067464.2; NM_021489.3.
DR AlphaFoldDB; Q80YC5; -.
DR SMR; Q80YC5; -.
DR STRING; 10090.ENSMUSP00000021948; -.
DR MEROPS; S01.211; -.
DR GlyGen; Q80YC5; 6 sites.
DR PhosphoSitePlus; Q80YC5; -.
DR CPTAC; non-CPTAC-3541; -.
DR CPTAC; non-CPTAC-3707; -.
DR MaxQB; Q80YC5; -.
DR PaxDb; Q80YC5; -.
DR PeptideAtlas; Q80YC5; -.
DR PRIDE; Q80YC5; -.
DR ProteomicsDB; 277024; -.
DR ABCD; Q80YC5; 2 sequenced antibodies.
DR Antibodypedia; 864; 759 antibodies from 37 providers.
DR DNASU; 58992; -.
DR Ensembl; ENSMUST00000021948; ENSMUSP00000021948; ENSMUSG00000021492.
DR GeneID; 58992; -.
DR KEGG; mmu:58992; -.
DR UCSC; uc007qqv.3; mouse.
DR CTD; 2161; -.
DR MGI; MGI:1891012; F12.
DR VEuPathDB; HostDB:ENSMUSG00000021492; -.
DR eggNOG; KOG1217; Eukaryota.
DR eggNOG; KOG3627; Eukaryota.
DR GeneTree; ENSGT00940000161657; -.
DR HOGENOM; CLU_006842_18_1_1; -.
DR InParanoid; Q80YC5; -.
DR OMA; SWEYCDL; -.
DR OrthoDB; 1314811at2759; -.
DR PhylomeDB; Q80YC5; -.
DR TreeFam; TF329901; -.
DR Reactome; R-MMU-140837; Intrinsic Pathway of Fibrin Clot Formation.
DR BioGRID-ORCS; 58992; 2 hits in 60 CRISPR screens.
DR PRO; PR:Q80YC5; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q80YC5; protein.
DR Bgee; ENSMUSG00000021492; Expressed in lobe of liver and 32 other tissues.
DR ExpressionAtlas; Q80YC5; baseline and differential.
DR Genevisible; Q80YC5; MM.
DR GO; GO:0005615; C:extracellular space; IMP:MGI.
DR GO; GO:0005791; C:rough endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0008233; F:peptidase activity; IMP:MGI.
DR GO; GO:0004252; F:serine-type endopeptidase activity; ISO:MGI.
DR GO; GO:0007596; P:blood coagulation; IMP:MGI.
DR GO; GO:0002542; P:Factor XII activation; ISO:MGI.
DR GO; GO:0042730; P:fibrinolysis; IEA:UniProtKB-KW.
DR GO; GO:0002353; P:plasma kallikrein-kinin cascade; ISO:MGI.
DR GO; GO:0030194; P:positive regulation of blood coagulation; ISO:MGI.
DR GO; GO:0051919; P:positive regulation of fibrinolysis; ISO:MGI.
DR GO; GO:0010756; P:positive regulation of plasminogen activation; ISO:MGI.
DR GO; GO:0016540; P:protein autoprocessing; ISO:MGI.
DR GO; GO:0016485; P:protein processing; ISO:MGI.
DR GO; GO:0006508; P:proteolysis; ISO:MGI.
DR GO; GO:0051788; P:response to misfolded protein; ISO:MGI.
DR GO; GO:0031638; P:zymogen activation; ISO:MGI.
DR CDD; cd00061; FN1; 1.
DR CDD; cd00062; FN2; 1.
DR CDD; cd00108; KR; 1.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 2.10.10.10; -; 1.
DR Gene3D; 2.40.10.10; -; 2.
DR Gene3D; 2.40.20.10; -; 1.
DR InterPro; IPR014394; Coagulation_fac_XII/HGFA.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000083; Fibronectin_type1.
DR InterPro; IPR000562; FN_type2_dom.
DR InterPro; IPR036943; FN_type2_sf.
DR InterPro; IPR000001; Kringle.
DR InterPro; IPR013806; Kringle-like.
DR InterPro; IPR018056; Kringle_CS.
DR InterPro; IPR038178; Kringle_sf.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001314; Peptidase_S1A.
DR InterPro; IPR001254; Trypsin_dom.
DR InterPro; IPR018114; TRYPSIN_HIS.
DR InterPro; IPR033116; TRYPSIN_SER.
DR Pfam; PF00008; EGF; 2.
DR Pfam; PF00039; fn1; 1.
DR Pfam; PF00040; fn2; 1.
DR Pfam; PF00051; Kringle; 1.
DR Pfam; PF00089; Trypsin; 1.
DR PIRSF; PIRSF001146; Factor_XII_HGFA; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00181; EGF; 2.
DR SMART; SM00179; EGF_CA; 2.
DR SMART; SM00058; FN1; 1.
DR SMART; SM00059; FN2; 1.
DR SMART; SM00130; KR; 1.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF50494; SSF50494; 1.
DR SUPFAM; SSF57440; SSF57440; 2.
DR PROSITE; PS00022; EGF_1; 2.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 2.
DR PROSITE; PS01253; FN1_1; 1.
DR PROSITE; PS51091; FN1_2; 1.
DR PROSITE; PS00023; FN2_1; 1.
DR PROSITE; PS51092; FN2_2; 1.
DR PROSITE; PS00021; KRINGLE_1; 1.
DR PROSITE; PS50070; KRINGLE_2; 1.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
DR PROSITE; PS00134; TRYPSIN_HIS; 1.
DR PROSITE; PS00135; TRYPSIN_SER; 1.
PE 1: Evidence at protein level;
KW Blood coagulation; Disulfide bond; EGF-like domain; Fibrinolysis;
KW Glycoprotein; Hemostasis; Hydrolase; Kringle; Protease; Reference proteome;
KW Repeat; Secreted; Serine protease; Signal; Zymogen.
FT SIGNAL 1..19
FT /evidence="ECO:0000250"
FT CHAIN 20..354
FT /note="Coagulation factor XIIa heavy chain"
FT /id="PRO_0000394555"
FT CHAIN 355..597
FT /note="Coagulation factor XIIa light chain"
FT /id="PRO_0000394556"
FT DOMAIN 42..90
FT /note="Fibronectin type-II"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478,
FT ECO:0000255|PROSITE-ProRule:PRU00479"
FT DOMAIN 94..131
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 133..173
FT /note="Fibronectin type-I"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DOMAIN 174..210
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 216..295
FT /note="Kringle"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00121"
FT DOMAIN 355..596
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT REGION 306..338
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 308..338
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 394
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 443
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 545
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT CARBOHYD 109
FT /note="O-linked (Fuc) threonine"
FT /evidence="ECO:0000250"
FT CARBOHYD 249
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250"
FT CARBOHYD 299
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250"
FT CARBOHYD 308
FT /note="O-linked (GalNAc...) serine"
FT /evidence="ECO:0000250"
FT CARBOHYD 327
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250"
FT CARBOHYD 415
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250"
FT DISULFID 47..73
FT /evidence="ECO:0000250"
FT DISULFID 61..88
FT /evidence="ECO:0000250"
FT DISULFID 98..110
FT /evidence="ECO:0000250"
FT DISULFID 104..119
FT /evidence="ECO:0000250"
FT DISULFID 121..130
FT /evidence="ECO:0000250"
FT DISULFID 135..163
FT /evidence="ECO:0000250"
FT DISULFID 161..170
FT /evidence="ECO:0000250"
FT DISULFID 178..189
FT /evidence="ECO:0000250"
FT DISULFID 183..198
FT /evidence="ECO:0000250"
FT DISULFID 200..209
FT /evidence="ECO:0000250"
FT DISULFID 217..295
FT /evidence="ECO:0000250"
FT DISULFID 238..277
FT /evidence="ECO:0000250"
FT DISULFID 266..290
FT /evidence="ECO:0000250"
FT DISULFID 341..468
FT /evidence="ECO:0000250"
FT DISULFID 379..395
FT /evidence="ECO:0000250"
FT DISULFID 387..457
FT /evidence="ECO:0000250"
FT DISULFID 418..421
FT /evidence="ECO:0000250"
FT DISULFID 482..551
FT /evidence="ECO:0000250"
FT DISULFID 514..530
FT /evidence="ECO:0000250"
FT DISULFID 541..572
FT /evidence="ECO:0000250"
FT CONFLICT 82
FT /note="D -> N (in Ref. 1; CAA67891)"
FT /evidence="ECO:0000305"
FT CONFLICT 152
FT /note="R -> K (in Ref. 1; CAA67891)"
FT /evidence="ECO:0000305"
FT CONFLICT 491
FT /note="F -> L (in Ref. 1; CAA67891)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 597 AA; 65701 MW; 342FB7E764957E03 CRC64;
MTALLFLGSL LMSLDLTLSA PPWKDSKKFK DAPDGPTVVL TVDGRLCHFP FQYHRQLHHK
CIHKRRPGSR PWCATTPNFD EDQQWGYCLE PKKVKDHCSK HNPCHKGGTC INTPNGPHCL
CPEHLTGKHC QKEKCFEPQL LKFFHENELW FRTGPGGVAR CECKGSEAHC KPVASQACSI
NPCLNGGSCL LVEDHPLCRC PTGYTGYFCD LDLWATCYEG RGLSYRGQAG TTQSGAPCQR
WTVEATYRNM TEKQALSWGL GHHAFCRNPD NDTRPWCFVW SGDRLSWDYC GLEQCQTPTF
APLVVPESQE ESPSQAPSLS HAPNDSTDHQ TSLSKTNTMG CGQRFRKGLS SFMRVVGGLV
ALPGSHPYIA ALYWGNNFCA GSLIAPCWVL TAAHCLQNRP APEELTVVLG QDRHNQSCEW
CQTLAVRSYR LHEGFSSITY QHDLALLRLQ ESKTNSCAIL SPHVQPVCLP SGAAPPSETV
LCEVAGWGHQ FEGAEEYSTF LQEAQVPFIA LDRCSNSNVH GDAILPGMLC AGFLEGGTDA
CQGDSGGPLV CEEGTAEHQL TLRGVISWGS GCGDRNKPGV YTDVANYLAW IQKHIAS
