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Database: UniProt
Entry: P98140
LinkDB: P98140
Original site: P98140 
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   16-JAN-2019, entry version 145.
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;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
OC   Pecora; Bovidae; 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
RT   XII): 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
RT   factor).";
RL   Biochemistry 16:2270-2278(1977).
CC   -!- FUNCTION: Factor XII is a serum glycoprotein that participates in
CC       the initiation of blood coagulation, fibrinolysis, and the
CC       generation of bradykinin and angiotensin. Prekallikrein is cleaved
CC       by factor XII to form kallikrein, which then cleaves factor XII
CC       first to alpha-factor XIIa and then to beta-factor XIIa. Alpha-
CC       factor XIIa activates factor XI to factor XIa (By similarity).
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Selective cleavage of Arg-|-Ile bonds in factor VII to
CC         form factor VIIa and factor XI to form factor XIa.;
CC         EC=3.4.21.38;
CC   -!- SUBUNIT: Interacts with HRG; the interaction, which is enhanced in
CC       the presence of zinc ions and inhibited by heparin-binding,
CC       inhibits factor XII autoactivation and contact-initiated
CC       coagulation. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- PTM: O- and N-glycosylated. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00274}.
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   UniGene; Bt.89433; -.
DR   ProteinModelPortal; P98140; -.
DR   STRING; 9913.ENSBTAP00000025122; -.
DR   ChEMBL; CHEMBL3533; -.
DR   MEROPS; S01.211; -.
DR   PaxDb; P98140; -.
DR   PRIDE; P98140; -.
DR   GeneID; 280789; -.
DR   KEGG; bta:280789; -.
DR   CTD; 2161; -.
DR   eggNOG; KOG1217; Eukaryota.
DR   eggNOG; KOG3627; Eukaryota.
DR   eggNOG; COG5640; LUCA.
DR   HOGENOM; HOG000237314; -.
DR   HOVERGEN; HBG004345; -.
DR   InParanoid; P98140; -.
DR   KO; K01328; -.
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; IEA:UniProtKB-KW.
DR   GO; GO:0042730; P:fibrinolysis; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; 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; 2.40.20.10; -; 1.
DR   InterPro; IPR014394; Coagulation_fac_XII/HGFA.
DR   InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR   InterPro; IPR013032; EGF-like_CS.
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; 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; Complete proteome; Direct protein sequencing;
KW   Disulfide bond; EGF-like domain; Fibrinolysis; Glycoprotein;
KW   Hemostasis; Hydrolase; Kringle; Protease; Reference proteome; Repeat;
KW   Secreted; Serine protease; Signal; Zymogen.
FT   SIGNAL        1     19       {ECO:0000269|PubMed:861210}.
FT   CHAIN        20    368       Coagulation factor XIIa heavy chain.
FT                                /FTId=PRO_0000027829.
FT   CHAIN       369    612       Coagulation factor XIIa light chain.
FT                                /FTId=PRO_0000027830.
FT   DOMAIN       42     90       Fibronectin type-II.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00478,
FT                                ECO:0000255|PROSITE-ProRule:PRU00479}.
FT   DOMAIN       94    131       EGF-like 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      133    173       Fibronectin type-I. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00478}.
FT   DOMAIN      174    210       EGF-like 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      217    306       Kringle. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00121}.
FT   DOMAIN      369    611       Peptidase S1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00274}.
FT   COMPBIAS    316    352       Pro-rich.
FT   ACT_SITE    408    408       Charge relay system. {ECO:0000250}.
FT   ACT_SITE    457    457       Charge relay system. {ECO:0000250}.
FT   ACT_SITE    560    560       Charge relay system. {ECO:0000250}.
FT   CARBOHYD    109    109       O-linked (Fuc) threonine. {ECO:0000250}.
FT   CARBOHYD    251    251       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    282    282       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    429    429       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID     47     73       {ECO:0000250}.
FT   DISULFID     61     88       {ECO:0000250}.
FT   DISULFID     98    110       {ECO:0000250}.
FT   DISULFID    104    119       {ECO:0000250}.
FT   DISULFID    121    130       {ECO:0000250}.
FT   DISULFID    135    163       {ECO:0000250}.
FT   DISULFID    161    170       {ECO:0000250}.
FT   DISULFID    178    189       {ECO:0000250}.
FT   DISULFID    183    198       {ECO:0000250}.
FT   DISULFID    200    209       {ECO:0000250}.
FT   DISULFID    217    306       {ECO:0000250}.
FT   DISULFID    240    288       {ECO:0000250}.
FT   DISULFID    268    301       {ECO:0000250}.
FT   DISULFID    355    482       {ECO:0000250}.
FT   DISULFID    393    409       {ECO:0000250}.
FT   DISULFID    401    471       {ECO:0000250}.
FT   DISULFID    432    435       {ECO:0000250}.
FT   DISULFID    498    566       {ECO:0000250}.
FT   DISULFID    529    545       {ECO:0000250}.
FT   DISULFID    556    587       {ECO:0000250}.
FT   CONFLICT     11     18       LVSLESTV -> GRVGGRVG (in Ref. 2;
FT                                AAB30804). {ECO:0000305}.
FT   CONFLICT     33     33       D -> E (in Ref. 2; AAB30804).
FT                                {ECO:0000305}.
FT   CONFLICT     70     70       R -> Q (in Ref. 2; AAB30804).
FT                                {ECO:0000305}.
FT   CONFLICT    187    187       G -> D (in Ref. 2; AAB30804).
FT                                {ECO:0000305}.
FT   CONFLICT    270    278       Missing (in Ref. 2; AAB30804).
FT                                {ECO:0000305}.
FT   CONFLICT    287    287       L -> W (in Ref. 2; AAB30804).
FT                                {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
//
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