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   27-MAR-2024, entry version 166.
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   GlyCosmos; Q80YC5; 6 sites, No reported glycans.
DR   GlyGen; Q80YC5; 6 sites.
DR   PhosphoSitePlus; Q80YC5; -.
DR   SwissPalm; Q80YC5; -.
DR   CPTAC; non-CPTAC-3541; -.
DR   CPTAC; non-CPTAC-3707; -.
DR   MaxQB; Q80YC5; -.
DR   PaxDb; 10090-ENSMUSP00000021948; -.
DR   PeptideAtlas; Q80YC5; -.
DR   ProteomicsDB; 277024; -.
DR   ABCD; Q80YC5; 2 sequenced antibodies.
DR   Antibodypedia; 864; 940 antibodies from 37 providers.
DR   DNASU; 58992; -.
DR   Ensembl; ENSMUST00000021948.15; ENSMUSP00000021948.9; ENSMUSG00000021492.16.
DR   GeneID; 58992; -.
DR   KEGG; mmu:58992; -.
DR   UCSC; uc007qqv.3; mouse.
DR   AGR; MGI:1891012; -.
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; GPQPWCA; -.
DR   OrthoDB; 4629979at2759; -.
DR   PhylomeDB; Q80YC5; -.
DR   TreeFam; TF329901; -.
DR   Reactome; R-MMU-140837; Intrinsic Pathway of Fibrin Clot Formation.
DR   BioGRID-ORCS; 58992; 2 hits in 63 CRISPR screens.
DR   PRO; PR:Q80YC5; -.
DR   Proteomes; UP000000589; Chromosome 13.
DR   RNAct; Q80YC5; Protein.
DR   Bgee; ENSMUSG00000021492; Expressed in lobe of liver and 33 other cell types or tissues.
DR   ExpressionAtlas; Q80YC5; baseline and differential.
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:0051788; P:response to misfolded protein; ISO:MGI.
DR   GO; GO:0031638; P:zymogen activation; ISO:MGI.
DR   CDD; cd00054; EGF_CA; 2.
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; Fibronectin, type II, collagen-binding; 1.
DR   Gene3D; 2.10.25.10; Laminin; 2.
DR   Gene3D; 2.40.20.10; Plasminogen Kringle 4; 1.
DR   Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
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   PANTHER; PTHR24264:SF46; COAGULATION FACTOR XII; 1.
DR   PANTHER; PTHR24264; TRYPSIN-RELATED; 1.
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   PRINTS; PR00013; FNTYPEII.
DR   PRINTS; PR00018; KRINGLE.
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; SSF57196; EGF/Laminin; 1.
DR   SUPFAM; SSF57440; Kringle-like; 2.
DR   SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
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.
DR   Genevisible; Q80YC5; MM.
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
//