ID FA12_CAVPO Reviewed; 603 AA.
AC Q04962;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-APR-2013, entry version 108.
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; Fragment;
GN Name=F12;
OS Cavia porcellus (Guinea pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia;
OC Hystricognathi; Caviidae; Cavia.
OX NCBI_TaxID=10141;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 19-37; 318-332 AND
RP 359-373.
RC TISSUE=Liver;
RX PubMed=1390917; DOI=10.1016/0167-4838(92)90014-5;
RA Semba U., Yamamoto T., Kunisada T., Shibuya Y., Tanase S., Kambara T.,
RA Okabe H.;
RT "Primary structure of guinea-pig Hageman factor: sequence around the
RT cleavage site differs from the human molecule.";
RL Biochim. Biophys. Acta 1159:113-121(1992).
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 trypsin cleaves it to beta-
CC factor XIIa. Alpha-factor XIIa activates factor XI to factor XIa
CC (By similarity).
CC -!- CATALYTIC ACTIVITY: Selective cleavage of Arg-|-Ile bonds in
CC factor VII to form factor VIIa and factor XI to form factor XIa.
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 (By similarity).
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- PTM: O- and N-glycosylated (By similarity).
CC -!- SIMILARITY: Belongs to the peptidase S1 family.
CC -!- SIMILARITY: Contains 2 EGF-like domains.
CC -!- SIMILARITY: Contains 1 fibronectin type-I domain.
CC -!- SIMILARITY: Contains 1 fibronectin type-II domain.
CC -!- SIMILARITY: Contains 1 kringle domain.
CC -!- SIMILARITY: Contains 1 peptidase S1 domain.
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DR EMBL; X68615; CAA48600.1; -; mRNA.
DR PIR; S28941; S28941.
DR ProteinModelPortal; Q04962; -.
DR MEROPS; S01.211; -.
DR eggNOG; COG5640; -.
DR HOGENOM; HOG000237314; -.
DR HOVERGEN; HBG004345; -.
DR InParanoid; Q04962; -.
DR OrthoDB; EOG41G33Q; -.
DR GO; GO:0005615; C:extracellular space; IEA:Compara.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:Compara.
DR GO; GO:0007596; P:blood coagulation; IEA:UniProtKB-KW.
DR GO; GO:0002542; P:Factor XII activation; IEA:Compara.
DR GO; GO:0042730; P:fibrinolysis; IEA:UniProtKB-KW.
DR GO; GO:0030194; P:positive regulation of blood coagulation; IEA:Compara.
DR GO; GO:0051919; P:positive regulation of fibrinolysis; IEA:Compara.
DR GO; GO:0010756; P:positive regulation of plasminogen activation; IEA:Compara.
DR GO; GO:0016540; P:protein autoprocessing; IEA:Compara.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0051788; P:response to misfolded protein; IEA:Compara.
DR GO; GO:0031638; P:zymogen activation; IEA:Compara.
DR Gene3D; 2.10.10.10; -; 1.
DR Gene3D; 2.40.20.10; -; 1.
DR InterPro; IPR014394; Coagulation_fac_XIIa/HGFA.
DR InterPro; IPR000742; EG-like_dom.
DR InterPro; IPR013032; EGF-like_CS.
DR InterPro; IPR000083; Fibronectin_type1.
DR InterPro; IPR000562; FN_type2_col-bd.
DR InterPro; IPR000001; Kringle.
DR InterPro; IPR013806; Kringle-like.
DR InterPro; IPR018056; Kringle_CS.
DR InterPro; IPR001254; Peptidase_S1.
DR InterPro; IPR018114; Peptidase_S1_AS.
DR InterPro; IPR001314; Peptidase_S1A.
DR InterPro; IPR009003; Trypsin-like_Pept_dom.
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; SM00058; FN1; 1.
DR SMART; SM00059; FN2; 1.
DR SMART; SM00130; KR; 1.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF57440; Kringle-like; 2.
DR SUPFAM; SSF50494; Pept_Ser_Cys; 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 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 18
FT CHAIN 19 358 Coagulation factor XIIa heavy chain.
FT /FTId=PRO_0000027831.
FT CHAIN 359 603 Coagulation factor XIIa light chain.
FT /FTId=PRO_0000027832.
FT DOMAIN 41 89 Fibronectin type-II.
FT DOMAIN 93 130 EGF-like 1.
FT DOMAIN 132 172 Fibronectin type-I.
FT DOMAIN 173 209 EGF-like 2.
FT DOMAIN 216 294 Kringle.
FT DOMAIN 359 602 Peptidase S1.
FT COMPBIAS 312 342 Pro-rich.
FT ACT_SITE 398 398 Charge relay system (By similarity).
FT ACT_SITE 447 447 Charge relay system (By similarity).
FT ACT_SITE 551 551 Charge relay system (By similarity).
FT CARBOHYD 248 248 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 270 270 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 419 419 N-linked (GlcNAc...) (Potential).
FT DISULFID 46 72 By similarity.
FT DISULFID 60 87 By similarity.
FT DISULFID 97 109 By similarity.
FT DISULFID 103 118 By similarity.
FT DISULFID 120 129 By similarity.
FT DISULFID 134 162 By similarity.
FT DISULFID 160 169 By similarity.
FT DISULFID 177 188 By similarity.
FT DISULFID 182 197 By similarity.
FT DISULFID 199 208 By similarity.
FT DISULFID 216 294 By similarity.
FT DISULFID 237 276 By similarity.
FT DISULFID 265 289 By similarity.
FT DISULFID 345 472 By similarity.
FT DISULFID 383 399 By similarity.
FT DISULFID 391 461 By similarity.
FT DISULFID 422 425 By similarity.
FT DISULFID 488 557 By similarity.
FT DISULFID 520 536 By similarity.
FT DISULFID 547 578 By similarity.
FT NON_TER 1 1
SQ SEQUENCE 603 AA; 66795 MW; 48DC6B946FB9ED59 CRC64;
GRLLLGSLLV SLESALSAPP PWKAPKERRH RAEEFTVGLT VTGEPCYFPF QYNRQLYHHC
IHKGRPGPRP WCATTPNFDQ DQQWAYCLEP KKVKDHCSKH NPCQRGGICV NTLSSPHCLC
PDHLTGKHCQ REKCFEPQLH RFFHENEIWF RTGPAGVAKC HCKGPDAHCK QMHSQECQTN
PCLNGGRCLE VEGHHLCDCP MGYTGPFCDL DTTASCYEGR GVSYRGMART TVSGAKCQRW
ASEATYRNMT AEQALRRGLG HHTFCRNPDN DTRPWCFVWM GNRLSWEYCD LAQCQYPPQP
TATPHDRFEH PKLPSSRLSI LQTPQPTTQN QALANELPET SSLLCGQRLR KRLSSLSRIV
GGLVALPGAH PYIAALYWGS NFCSGSLIAP CWVLTAAHCL QNRPAPEELK VVLGQDRHNQ
SCEHCQTLAV HSYRLHEAFS PSSYLNDLAL LRLQKSADGS CAQLSPYVQT VCLPSGPAPP
SESETTCCEV AGWGHQFEGA EEYSSFLQEA QVPLISSERC SSPEVHGDAF LSGMLCAGFL
EGGTDACQGD SGGPLVCEDE AAEHRLILRG IVSWGSGCGD RNKPGVYTDV ASYLTWIQKH
TAS
//
