FA12_PIG
ID FA12_PIG Reviewed; 616 AA.
AC O97507;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 25-MAY-2022, entry version 113.
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 Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RA Takahashi T., Kihara T.;
RT "Porcine liver factor XII.";
RL Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases.
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.
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; AB022426; BAA37148.1; -; mRNA.
DR RefSeq; NP_999407.1; NM_214242.1.
DR AlphaFoldDB; O97507; -.
DR SMR; O97507; -.
DR STRING; 9823.ENSSSCP00000024170; -.
DR MEROPS; S01.211; -.
DR PaxDb; O97507; -.
DR PeptideAtlas; O97507; -.
DR GeneID; 397474; -.
DR KEGG; ssc:397474; -.
DR CTD; 2161; -.
DR eggNOG; KOG1217; Eukaryota.
DR eggNOG; KOG3627; Eukaryota.
DR HOGENOM; CLU_057870_0_0_1; -.
DR InParanoid; O97507; -.
DR OrthoDB; 1314811at2759; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; 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; 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 2: Evidence at transcript 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..371
FT /note="Coagulation factor XIIa heavy chain"
FT /id="PRO_0000232379"
FT CHAIN 372..616
FT /note="Coagulation factor XIIa light chain"
FT /id="PRO_0000232382"
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 372..615
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT REGION 303..342
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 306..341
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 411
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 460
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 564
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:0000255"
FT CARBOHYD 271
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 335
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 432
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..295
FT /evidence="ECO:0000250"
FT DISULFID 238..277
FT /evidence="ECO:0000250"
FT DISULFID 266..290
FT /evidence="ECO:0000250"
FT DISULFID 358..485
FT /evidence="ECO:0000250"
FT DISULFID 396..412
FT /evidence="ECO:0000250"
FT DISULFID 404..474
FT /evidence="ECO:0000250"
FT DISULFID 435..438
FT /evidence="ECO:0000250"
FT DISULFID 501..570
FT /evidence="ECO:0000250"
FT DISULFID 533..549
FT /evidence="ECO:0000250"
FT DISULFID 560..591
FT /evidence="ECO:0000250"
SQ SEQUENCE 616 AA; 68012 MW; 4C5FE3D71EBBD1A9 CRC64;
MRALLLLGIL LVSLESALLI PPWKDPRKHK VMASEHTVVL TVTGEPCHFP FQYYRQLYYK
CIQRGQRGPR PWCATTPNFE KDQRWAYCLE PMKVKDHCNK GNPCQKGGTC VNMPNGPHCI
CPDHFTGKHC QKEKCFEPQF LQFFQENEIW HRFEPAGVSK CQCKGPKAQC KPVASQVCST
NPCLNGGSCL QTEGHRLCRC PTGYAGRLCD VDLKERCYSD RGLSYRGMAQ TTLSGAPCQP
WASEATYWNM TAEQALNWGL GDHAFCRNPD NDTRPWCFVW RGDQLSWQYC RLARCQAPIG
EAPPILTPTQ SPSEHQDSPL LSREPQPTTQ TPSQNLTSAW CAPPEQRGPL PSAGLVGCGQ
RLRKRLSSLN RIVGGLVALP GAHPYIAALY WGQNFCAGSL IAPCWVLTAA HCLQNRPAPE
ELTVVLGQDR HNQSCEQCQT LAVRSYRLHE SYSPKTYQHD LALVRLKETA DGCCAHPSPF
VQPVCLPRSV ASSAEPEGAL CEVAGWGHQF EGAEEYSSFL QEAQVPLISP ERCSAADVHG
AAFTPGMLCA GFLEGGTDAC QGDSGGPLVC EDETAERQLV LRGIVSWGSG CGDRLKPGVY
TDVANYLAWI QEHTTS
