ID G7MUG1_MACMU Unreviewed; 615 AA.
AC G7MUG1;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE RecName: Full=Coagulation factor XII {ECO:0000256|ARBA:ARBA00039367};
DE EC=3.4.21.38 {ECO:0000256|ARBA:ARBA00039013};
DE AltName: Full=Hageman factor {ECO:0000256|ARBA:ARBA00042651};
GN ORFNames=EGK_17196 {ECO:0000313|EMBL:EHH27083.1};
OS Macaca mulatta (Rhesus macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9544 {ECO:0000313|EMBL:EHH27083.1};
RN [1] {ECO:0000313|EMBL:EHH27083.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CR-5 {ECO:0000313|EMBL:EHH27083.1};
RX PubMed=22002653; DOI=10.1038/nbt.1992;
RA Yan G., Zhang G., Fang X., Zhang Y., Li C., Ling F., Cooper D.N., Li Q.,
RA Li Y., van Gool A.J., Du H., Chen J., Chen R., Zhang P., Huang Z.,
RA Thompson J.R., Meng Y., Bai Y., Wang J., Zhuo M., Wang T., Huang Y.,
RA Wei L., Li J., Wang Z., Hu H., Yang P., Le L., Stenson P.D., Li B., Liu X.,
RA Ball E.V., An N., Huang Q., Zhang Y., Fan W., Zhang X., Li Y., Wang W.,
RA Katze M.G., Su B., Nielsen R., Yang H., Wang J., Wang X., Wang J.;
RT "Genome sequencing and comparison of two nonhuman primate animal models,
RT the cynomolgus and Chinese rhesus macaques.";
RL Nat. Biotechnol. 29:1019-1023(2011).
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. {ECO:0000256|ARBA:ARBA00037517}.
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 Evidence={ECO:0000256|ARBA:ARBA00036304};
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.
CC {ECO:0000256|ARBA:ARBA00038551}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR EMBL; CM001258; EHH27083.1; -; Genomic_DNA.
DR AlphaFoldDB; G7MUG1; -.
DR MEROPS; S01.211; -.
DR Proteomes; UP000013456; Chromosome 6.
DR GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00479};
KW EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW ProRule:PRU00076}; Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU363034};
KW Kringle {ECO:0000256|ARBA:ARBA00022572, ECO:0000256|PROSITE-
KW ProRule:PRU00121};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU363034};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW ECO:0000256|RuleBase:RU363034}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..615
FT /note="Coagulation factor XII"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003500146"
FT DOMAIN 42..90
FT /note="Fibronectin type-II"
FT /evidence="ECO:0000259|PROSITE:PS51092"
FT DOMAIN 94..131
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 133..173
FT /note="Fibronectin type-I"
FT /evidence="ECO:0000259|PROSITE:PS51091"
FT DOMAIN 174..210
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 216..295
FT /note="Kringle"
FT /evidence="ECO:0000259|PROSITE:PS50070"
FT DOMAIN 373..614
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT REGION 301..357
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 302..329
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 412
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR001146-1"
FT ACT_SITE 461
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR001146-1"
FT ACT_SITE 563
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR001146-1"
FT DISULFID 47..73
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00479"
FT DISULFID 61..88
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00479"
FT DISULFID 121..130
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 200..209
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 238..277
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
SQ SEQUENCE 615 AA; 67698 MW; 1A4C0E256242BFC2 CRC64;
MRALLLLGFL LVSLESTLSI PPWKAPKEHK YKAEEHTVVL TVTGEPCHFP FQYHRRLYHK
CTHKGRPGPQ TWCATTPNFD EDQRWGYCVE PKKVKDHCSK HSPCQKGGTC VNTLSGTHCL
CPQHLTGNHC QREKCFEPQL LRFFHENEIW YRSEQAAVAR CQCKGPDAHC QRLASQACRT
NPCLHGGRCL EVEGHRLCHC PVGYTGPFCD LDTKASCYDG RGLSYRGLAR TTLSGAPCQP
WTSEATYWNV TAEQARNWGL GGHAFCRNPD NDIRPWCFVL IGDRLSWEYC DVAQCQAPTQ
AVPPTPVSPG LHVPLMPPQP APPKLQPTTR TPPQSQTPGA LPVKQEQPPR LTRNGSVSCG
QRLRKSLSSM TRVVGGLVAL RGAHPYIAAL YWGHSFCAGS LIAPCWVLTA AHCLQDRPAP
EDLTVVLGQE RHNHSCEQCQ TLAVRSYRLH EAFSPDSYQH DLALLRLQED ADGSCALLSP
YVQPVCLPSG AARPSEPALC QVAGWGHQFE GAEEYSSFLQ EAQVPFLSLE SCSAPEVHGA
SILPGMLCAG FLEGGTDACQ GDSGGPLVCE DQAAERRLTL QGIISWGSGC GDRNKPGVYT
DVAYYLAWIR EHTAS
//
