FA12_CAVPO
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-AUG-2022, 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; Fragment;
GN Name=F12;
OS Cavia porcellus (Guinea pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC 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 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; X68615; CAA48600.1; -; mRNA.
DR PIR; S28941; S28941.
DR AlphaFoldDB; Q04962; -.
DR SMR; Q04962; -.
DR STRING; 10141.ENSCPOP00000018858; -.
DR MEROPS; S01.211; -.
DR PRIDE; Q04962; -.
DR eggNOG; KOG1217; Eukaryota.
DR eggNOG; KOG3627; Eukaryota.
DR InParanoid; Q04962; -.
DR Proteomes; UP000005447; Unassembled WGS sequence.
DR GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC.
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 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 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..18
FT /evidence="ECO:0000269|PubMed:1390917"
FT CHAIN 19..358
FT /note="Coagulation factor XIIa heavy chain"
FT /id="PRO_0000027831"
FT CHAIN 359..603
FT /note="Coagulation factor XIIa light chain"
FT /id="PRO_0000027832"
FT DOMAIN 41..89
FT /note="Fibronectin type-II"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478,
FT ECO:0000255|PROSITE-ProRule:PRU00479"
FT DOMAIN 93..130
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 132..172
FT /note="Fibronectin type-I"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00478"
FT DOMAIN 173..209
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 216..294
FT /note="Kringle"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00121"
FT DOMAIN 359..602
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 398
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 447
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 551
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT CARBOHYD 248
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 270
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 419
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 46..72
FT /evidence="ECO:0000250"
FT DISULFID 60..87
FT /evidence="ECO:0000250"
FT DISULFID 97..109
FT /evidence="ECO:0000250"
FT DISULFID 103..118
FT /evidence="ECO:0000250"
FT DISULFID 120..129
FT /evidence="ECO:0000250"
FT DISULFID 134..162
FT /evidence="ECO:0000250"
FT DISULFID 160..169
FT /evidence="ECO:0000250"
FT DISULFID 177..188
FT /evidence="ECO:0000250"
FT DISULFID 182..197
FT /evidence="ECO:0000250"
FT DISULFID 199..208
FT /evidence="ECO:0000250"
FT DISULFID 216..294
FT /evidence="ECO:0000250"
FT DISULFID 237..276
FT /evidence="ECO:0000250"
FT DISULFID 265..289
FT /evidence="ECO:0000250"
FT DISULFID 345..472
FT /evidence="ECO:0000250"
FT DISULFID 383..399
FT /evidence="ECO:0000250"
FT DISULFID 391..461
FT /evidence="ECO:0000250"
FT DISULFID 422..425
FT /evidence="ECO:0000250"
FT DISULFID 488..557
FT /evidence="ECO:0000250"
FT DISULFID 520..536
FT /evidence="ECO:0000250"
FT DISULFID 547..578
FT /evidence="ECO:0000250"
FT NON_TER 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
