FA12_BOVIN
ID FA12_BOVIN Reviewed; 612 AA.
AC P98140; Q0P5I3;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 2.
DT 25-MAY-2022, entry version 154.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 11-612.
RC TISSUE=Liver;
RX PubMed=8186251; DOI=10.1016/0167-4838(94)90073-6;
RA Shibuya Y., Semba U., Okabe H., Kambara T., Yamamoto T.;
RT "Primary structure of bovine Hageman factor (blood coagulation factor XII):
RT comparison with human and guinea pig molecules.";
RL Biochim. Biophys. Acta 1206:63-70(1994).
RN [3]
RP PROTEIN SEQUENCE OF 20-31; 369-383 AND 544-569.
RX PubMed=861210; DOI=10.1021/bi00629a036;
RA Fujikawa K., Walsh A.K., Davie W.E.;
RT "Isolation and characterization of bovine factor XII (Hageman factor).";
RL Biochemistry 16:2270-2278(1977).
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 to beta-factor XIIa. Alpha-factor XIIa activates factor
CC 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.
CC -!- PTM: O- and N-glycosylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00274}.
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DR EMBL; BC120000; AAI20001.1; -; mRNA.
DR EMBL; S70164; AAB30804.2; -; mRNA.
DR PIR; S45281; S45281.
DR RefSeq; NP_001068587.1; NM_001075119.2.
DR AlphaFoldDB; P98140; -.
DR SMR; P98140; -.
DR STRING; 9913.ENSBTAP00000025122; -.
DR ChEMBL; CHEMBL3533; -.
DR MEROPS; S01.211; -.
DR PaxDb; P98140; -.
DR GeneID; 280789; -.
DR KEGG; bta:280789; -.
DR CTD; 2161; -.
DR eggNOG; KOG1217; Eukaryota.
DR eggNOG; KOG3627; Eukaryota.
DR InParanoid; P98140; -.
DR OrthoDB; 1314811at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005791; C:rough endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0007596; P:blood coagulation; IBA:GO_Central.
DR GO; GO:0042730; P:fibrinolysis; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR GO; GO:0031638; P:zymogen activation; IBA:GO_Central.
DR CDD; cd00061; FN1; 1.
DR CDD; cd00062; FN2; 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; 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; 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; 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; Direct protein sequencing; Disulfide bond;
KW EGF-like domain; Fibrinolysis; Glycoprotein; Hemostasis; Hydrolase;
KW Kringle; Protease; Reference proteome; Repeat; Secreted; Serine protease;
KW Signal; Zymogen.
FT SIGNAL 1..19
FT /evidence="ECO:0000269|PubMed:861210"
FT CHAIN 20..368
FT /note="Coagulation factor XIIa heavy chain"
FT /id="PRO_0000027829"
FT CHAIN 369..612
FT /note="Coagulation factor XIIa light chain"
FT /id="PRO_0000027830"
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 217..306
FT /note="Kringle"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00121"
FT DOMAIN 369..611
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 408
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 457
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 560
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT CARBOHYD 109
FT /note="O-linked (Fuc) threonine"
FT /evidence="ECO:0000250"
FT CARBOHYD 251
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 282
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 429
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
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..306
FT /evidence="ECO:0000250"
FT DISULFID 240..288
FT /evidence="ECO:0000250"
FT DISULFID 268..301
FT /evidence="ECO:0000250"
FT DISULFID 355..482
FT /evidence="ECO:0000250"
FT DISULFID 393..409
FT /evidence="ECO:0000250"
FT DISULFID 401..471
FT /evidence="ECO:0000250"
FT DISULFID 432..435
FT /evidence="ECO:0000250"
FT DISULFID 498..566
FT /evidence="ECO:0000250"
FT DISULFID 529..545
FT /evidence="ECO:0000250"
FT DISULFID 556..587
FT /evidence="ECO:0000250"
FT CONFLICT 11..18
FT /note="LVSLESTV -> GRVGGRVG (in Ref. 2; AAB30804)"
FT /evidence="ECO:0000305"
FT CONFLICT 33
FT /note="D -> E (in Ref. 2; AAB30804)"
FT /evidence="ECO:0000305"
FT CONFLICT 70
FT /note="R -> Q (in Ref. 2; AAB30804)"
FT /evidence="ECO:0000305"
FT CONFLICT 187
FT /note="G -> D (in Ref. 2; AAB30804)"
FT /evidence="ECO:0000305"
FT CONFLICT 270..278
FT /note="Missing (in Ref. 2; AAB30804)"
FT /evidence="ECO:0000305"
FT CONFLICT 287
FT /note="L -> W (in Ref. 2; AAB30804)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 612 AA; 67160 MW; D5C9292807DD5283 CRC64;
MRALLLLGAL LVSLESTVST PPWKGPKKHK LTDSEHTVVL TVTGEPCHFP FQYHRQLHHK
CIHRGRPGPR PWCATTPNFE KDQRWAYCLE PKKVKDHCSK HNPCQKGGTC VNMPDGPRCI
CADHFTGKHC QKEKCFEPQF FRFFHENEIW HRLEPAGVVK CQCKGPNAQC KPLASQVCRT
NPCLNGGSCL QAEGHRLCRC APSFAGRLCD VDLKASCYDD RDRGLSYRGM AGTTLSGAPC
QSWASEATYW NVTAEQVLNW GLGDHAFCRA STPPRGYRNP DNDTRPLCFI WKGDRLSWNY
CRLAPCQAAA GHEHFPLPSP SALQKPESTT QTPLPSLTSG WCSPTPLASG GPGGCGQRLR
KWLSSLNRVV GGLVALPGAH PYIAALYWDQ HFCAGSLIAP CWVLTAAHCL QNRPAPKELT
VVLGQDRHNQ SCEQCQTLAV RDYRLHEAFS PITYQHDLAL VRLQESADGC CAHPSPFVQP
VCLPSTAARP AESEAAVCEV AGWGHQFEGG EYSSFLQEAQ VPLIDPQRCS APDVHGAAFT
QGMLCAGFLE GGTDACQGDS GGPLVCEDET PERQLILRGI VSWGSGCGNR LKPGVYTDVA
NYLAWIREHT AS
