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Database: UniProt
Entry: Q04962
LinkDB: Q04962
Original site: Q04962 
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   19-MAR-2014, entry version 112.
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   STRING; 10141.ENSCPOP00000018858; -.
DR   MEROPS; S01.211; -.
DR   eggNOG; COG5640; -.
DR   HOGENOM; HOG000237314; -.
DR   HOVERGEN; HBG004345; -.
DR   InParanoid; Q04962; -.
DR   GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
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; IEA:UniProtKB-KW.
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; 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   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
//
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