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   22-FEB-2023, entry version 148.
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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   GlyCosmos; Q04962; 3 sites, No reported glycans.
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; cd00054; EGF_CA; 2.
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; Fibronectin, type II, collagen-binding; 1.
DR   Gene3D; 2.10.25.10; Laminin; 2.
DR   Gene3D; 2.40.20.10; Plasminogen Kringle 4; 1.
DR   Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
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   PANTHER; PTHR24264:SF46; COAGULATION FACTOR XII; 1.
DR   PANTHER; PTHR24264; TRYPSIN-RELATED; 1.
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   PRINTS; PR00013; FNTYPEII.
DR   PRINTS; PR00018; KRINGLE.
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; SSF57196; EGF/Laminin; 1.
DR   SUPFAM; SSF57440; Kringle-like; 2.
DR   SUPFAM; SSF50494; Trypsin-like serine proteases; 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; 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
//