ID H0V1L7_CAVPO Unreviewed; 592 AA.
AC H0V1L7;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 2.
DT 27-MAR-2024, entry version 82.
DE RecName: Full=Coagulation factor XII {ECO:0000256|ARBA:ARBA00039367};
DE EC=3.4.21.38 {ECO:0000256|ARBA:ARBA00039013};
DE AltName: Full=Hageman factor {ECO:0000256|ARBA:ARBA00042651};
GN Name=F12 {ECO:0000313|Ensembl:ENSCPOP00000003389.3};
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 {ECO:0000313|Ensembl:ENSCPOP00000003389.3, ECO:0000313|Proteomes:UP000005447};
RN [1] {ECO:0000313|Proteomes:UP000005447}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2N {ECO:0000313|Proteomes:UP000005447};
RX PubMed=21993624; DOI=10.1038/nature10530;
RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL Nature 478:476-482(2011).
RN [2] {ECO:0000313|Ensembl:ENSCPOP00000003389.3}
RP IDENTIFICATION.
RC STRAIN=2N {ECO:0000313|Ensembl:ENSCPOP00000003389.3};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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. {ECO:0000256|ARBA:ARBA00037517}.
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 Evidence={ECO:0000256|ARBA:ARBA00036304};
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.
CC {ECO:0000256|ARBA:ARBA00038551}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR EMBL; AAKN02022926; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; H0V1L7; -.
DR Ensembl; ENSCPOT00000003796.3; ENSCPOP00000003389.3; ENSCPOG00000003752.4.
DR VEuPathDB; HostDB:ENSCPOG00000003752; -.
DR GeneTree; ENSGT00940000161657; -.
DR HOGENOM; CLU_006842_18_1_1; -.
DR Proteomes; UP000005447; Unassembled WGS sequence.
DR Bgee; ENSCPOG00000003752; Expressed in liver and 3 other cell types or tissues.
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:InterPro.
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 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00479};
KW EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW ProRule:PRU00076}; Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU363034};
KW Kringle {ECO:0000256|ARBA:ARBA00022572, ECO:0000256|PROSITE-
KW ProRule:PRU00121};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU363034};
KW Reference proteome {ECO:0000313|Proteomes:UP000005447};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW ECO:0000256|RuleBase:RU363034}.
FT DOMAIN 30..78
FT /note="Fibronectin type-II"
FT /evidence="ECO:0000259|PROSITE:PS51092"
FT DOMAIN 82..119
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 121..161
FT /note="Fibronectin type-I"
FT /evidence="ECO:0000259|PROSITE:PS51091"
FT DOMAIN 162..198
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 204..283
FT /note="Kringle"
FT /evidence="ECO:0000259|PROSITE:PS50070"
FT DOMAIN 348..591
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT ACT_SITE 387
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR001146-1"
FT ACT_SITE 436
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR001146-1"
FT ACT_SITE 540
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR001146-1"
FT DISULFID 35..61
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00479"
FT DISULFID 49..76
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00479"
FT DISULFID 109..118
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 188..197
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 226..265
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
SQ SEQUENCE 592 AA; 65697 MW; 74E5FD3FF0ED3374 CRC64;
VLGKSLAPPP WKAPKERRHR AEEFTVGLTV TGEPCYFPFQ YNRQLYHHCI HKGRPGPRPW
CATTPNFDQD QQWAYCLEPK KVKDHCSKHN PCQRGGICVN TLSSPHCLCP DHLTGKHCQR
EKCFEPQLHR FFHENEIWFR TGPAGVAKCH CKGPDAHCKQ MHSQECQTNP CLNGGRCLEV
EGHHLCDCPM GYTGPFCDLD TTASCYEGRG LSYRGMARTT VSGAKCQRWA SEATYRNMTA
EQALRRGLGH HTFCRNPDND TRPWCFVWMG NRLSWEYCDL AQCQYPPQPT ATPHDRFEHP
KLPSSRLSIL QTPQPTTQNQ ALANELPETS SLLCGQRLRK RLSSLSRIVG GLVALPGAHP
YIAALYWGSN FCSGSLIAPC WVLTAAHCLQ NRPAPEELKV VLGQDRHNQS CEHCQTLAVH
SYRLHEAFSP SSYLNDLALL RLQKSADGSC AQLSPYVQTV CLPSGPAPPS ESETTCCEVA
GWGHQFEGAE EYSSFLQEAQ VPLISSERCS SPEVHGDAFL SGMLCAGFLE GGTDACQGDS
GGPLVCEDEA AEHRLILRGI VSWGSGCGDR NKPGVYTDVA SYLTWIQKHT AS
//
