FA12_RAT
ID FA12_RAT Reviewed; 595 AA.
AC D3ZTE0; Q5M879;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 1.
DT 03-AUG-2022, entry version 78.
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;
GN Name=F12;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Liver;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
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 {ECO:0000250}.
CC -!- PTM: O- and N-glycosylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00274}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EDL93987.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; CH474032; EDL93987.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BC088187; AAH88187.1; -; mRNA.
DR RefSeq; NP_001014028.1; NM_001014006.1.
DR AlphaFoldDB; D3ZTE0; -.
DR SMR; D3ZTE0; -.
DR IntAct; D3ZTE0; 1.
DR STRING; 10116.ENSRNOP00000061983; -.
DR MEROPS; S01.211; -.
DR GlyGen; D3ZTE0; 6 sites.
DR PaxDb; D3ZTE0; -.
DR PeptideAtlas; D3ZTE0; -.
DR PRIDE; D3ZTE0; -.
DR GeneID; 306761; -.
DR KEGG; rno:306761; -.
DR UCSC; RGD:1359175; rat.
DR CTD; 2161; -.
DR RGD; 1359175; F12.
DR VEuPathDB; HostDB:ENSRNOG00000015139; -.
DR eggNOG; KOG1217; Eukaryota.
DR eggNOG; KOG3627; Eukaryota.
DR InParanoid; D3ZTE0; -.
DR OrthoDB; 1314811at2759; -.
DR PhylomeDB; D3ZTE0; -.
DR TreeFam; TF329901; -.
DR BRENDA; 3.4.21.38; 5301.
DR Reactome; R-RNO-140837; Intrinsic Pathway of Fibrin Clot Formation.
DR PRO; PR:D3ZTE0; -.
DR Proteomes; UP000002494; Chromosome 17.
DR Proteomes; UP000234681; Chromosome 17.
DR Bgee; ENSRNOG00000015139; Expressed in liver and 6 other tissues.
DR ExpressionAtlas; D3ZTE0; baseline and differential.
DR Genevisible; D3ZTE0; RN.
DR GO; GO:0005615; C:extracellular space; IDA:RGD.
DR GO; GO:0005791; C:rough endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0008233; F:peptidase activity; ISO:RGD.
DR GO; GO:0004252; F:serine-type endopeptidase activity; ISO:RGD.
DR GO; GO:0007596; P:blood coagulation; IDA:RGD.
DR GO; GO:0002542; P:Factor XII activation; ISO:RGD.
DR GO; GO:0042730; P:fibrinolysis; IEA:UniProtKB-KW.
DR GO; GO:0002353; P:plasma kallikrein-kinin cascade; ISO:RGD.
DR GO; GO:0030194; P:positive regulation of blood coagulation; ISO:RGD.
DR GO; GO:0051919; P:positive regulation of fibrinolysis; ISO:RGD.
DR GO; GO:0010756; P:positive regulation of plasminogen activation; ISO:RGD.
DR GO; GO:0016540; P:protein autoprocessing; ISO:RGD.
DR GO; GO:0016485; P:protein processing; ISO:RGD.
DR GO; GO:0006508; P:proteolysis; ISO:RGD.
DR GO; GO:0051788; P:response to misfolded protein; ISO:RGD.
DR GO; GO:0031638; P:zymogen activation; ISO:RGD.
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 2: Evidence at transcript level;
KW Blood coagulation; Disulfide bond; EGF-like domain; Fibrinolysis;
KW Glycoprotein; Hemostasis; Hydrolase; Kringle; Protease; Reference proteome;
KW Repeat; Secreted; Serine protease; Signal; Zymogen.
FT SIGNAL 1..19
FT /evidence="ECO:0000250"
FT CHAIN 20..353
FT /note="Coagulation factor XIIa heavy chain"
FT /id="PRO_0000394557"
FT CHAIN 354..595
FT /note="Coagulation factor XIIa light chain"
FT /id="PRO_0000394558"
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 215..294
FT /note="Kringle"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00121"
FT DOMAIN 354..594
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT REGION 302..332
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 393
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 442
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 543
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT CARBOHYD 108
FT /note="O-linked (Fuc) threonine"
FT /evidence="ECO:0000250"
FT CARBOHYD 248
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250"
FT CARBOHYD 298
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250"
FT CARBOHYD 307
FT /note="O-linked (GalNAc...) serine"
FT /evidence="ECO:0000250"
FT CARBOHYD 326
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250"
FT CARBOHYD 414
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250"
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 340..466
FT /evidence="ECO:0000250"
FT DISULFID 378..394
FT /evidence="ECO:0000250"
FT DISULFID 386..455
FT /evidence="ECO:0000250"
FT DISULFID 417..420
FT /evidence="ECO:0000250"
FT DISULFID 480..549
FT /evidence="ECO:0000250"
FT DISULFID 512..528
FT /evidence="ECO:0000250"
FT DISULFID 539..570
FT /evidence="ECO:0000250"
FT CONFLICT 320..324
FT /note="SSPRD -> MPQFPSLSDALDN (in Ref. 2; AAH88187)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 595 AA; 65844 MW; 6CCDA05AB136178A CRC64;
MTALLFLGSL LMSLDLTLSA PPWKSKEFKD GAGDPSVVLT VDGKLCHFPF QYHRRLYHKC
IHKGQPGSRP WCATTPNFDE DQQWGYCLEP KKVKDHCSKH SPCHKGGTCV NTPNGPHCLC
PEHLTGKHCQ REKCFESQLL KFFHENEIWF RTGPGGVARC QCKGPQAVCK LLTSQVCRVN
PCLNGGTCLL VEDHRLCHCP AGYAGPFCDL DLKATCYEDR GLSYRGQAKT TLSGAPCQRW
ASEATYRNMT ETQALSWGLG HHAFCRNPDN DTRPWCYVWS GDRLSWDYCD LEQCQMPTLT
SPVSPESHDM LKPRPPILQS SPRDSTRNQN VVSRTSTVVC GQRFRKRLSS LRRVVGGLVA
LPGSHPYIAA LYWGDSFCAG SLIDPCWVLT AAHCLQKRPA PEELTVVLGQ DRHNQSCERC
QTLAVHSYRL HEGFSSKTYQ HDLALLRLRG RKNSCAILSP HVQPVCLPSS AAPPSETVLC
EVAGWGHQFE GAEEYATFLQ EAQVPFISLD RCSSSNVHGD AILPGMLCAG FLEGGADACQ
GDSGGPLVCD EGVTERQLTL RGVISWGSGC GDRNKPGVYT DVANYLDWIQ EHTAF
