GenomeNet

Database: UniProt
Entry: D3ZTE0
LinkDB: D3ZTE0
Original site: D3ZTE0 
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   16-JAN-2019, entry version 66.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; 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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
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). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Selective cleavage of Arg-|-Ile bonds in factor VII to
CC         form factor VIIa and factor XI to form factor XIa.;
CC         EC=3.4.21.38;
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. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- PTM: O- and N-glycosylated. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00274}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EDL93987.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
DR   EMBL; CH474032; EDL93987.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; BC088187; AAH88187.1; -; mRNA.
DR   RefSeq; NP_001014028.1; NM_001014006.1.
DR   UniGene; Rn.53943; -.
DR   ProteinModelPortal; D3ZTE0; -.
DR   STRING; 10116.ENSRNOP00000061983; -.
DR   MEROPS; S01.211; -.
DR   PaxDb; D3ZTE0; -.
DR   PeptideAtlas; D3ZTE0; -.
DR   PRIDE; D3ZTE0; -.
DR   Ensembl; ENSRNOT00000081920; ENSRNOP00000074115; ENSRNOG00000015139.
DR   GeneID; 306761; -.
DR   KEGG; rno:306761; -.
DR   UCSC; RGD:1359175; rat.
DR   CTD; 2161; -.
DR   RGD; 1359175; F12.
DR   eggNOG; KOG1217; Eukaryota.
DR   eggNOG; KOG3627; Eukaryota.
DR   eggNOG; COG5640; LUCA.
DR   GeneTree; ENSGT00940000161657; -.
DR   HOGENOM; HOG000237314; -.
DR   HOVERGEN; HBG004345; -.
DR   InParanoid; D3ZTE0; -.
DR   KO; K01328; -.
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   Bgee; ENSRNOG00000015139; Expressed in 5 organ(s), highest expression level in liver.
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:0004252; F:serine-type endopeptidase activity; IBA:GO_Central.
DR   GO; GO:0007596; P:blood coagulation; IDA:RGD.
DR   GO; GO:0042730; P:fibrinolysis; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IBA:GO_Central.
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; 2.40.20.10; -; 1.
DR   InterPro; IPR014394; Coagulation_fac_XII/HGFA.
DR   InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR   InterPro; IPR013032; EGF-like_CS.
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; 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; Complete proteome; Disulfide bond; EGF-like domain;
KW   Fibrinolysis; Glycoprotein; Hemostasis; Hydrolase; Kringle; Protease;
KW   Reference proteome; Repeat; Secreted; Serine protease; Signal;
KW   Zymogen.
FT   SIGNAL        1     19       {ECO:0000250}.
FT   CHAIN        20    353       Coagulation factor XIIa heavy chain.
FT                                /FTId=PRO_0000394557.
FT   CHAIN       354    595       Coagulation factor XIIa light chain.
FT                                /FTId=PRO_0000394558.
FT   DOMAIN       41     89       Fibronectin type-II.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00478,
FT                                ECO:0000255|PROSITE-ProRule:PRU00479}.
FT   DOMAIN       93    130       EGF-like 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      132    172       Fibronectin type-I. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00478}.
FT   DOMAIN      173    209       EGF-like 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      215    294       Kringle. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00121}.
FT   DOMAIN      354    594       Peptidase S1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00274}.
FT   COMPBIAS    297    322       Pro-rich.
FT   ACT_SITE    393    393       Charge relay system. {ECO:0000250}.
FT   ACT_SITE    442    442       Charge relay system. {ECO:0000250}.
FT   ACT_SITE    543    543       Charge relay system. {ECO:0000250}.
FT   CARBOHYD    108    108       O-linked (Fuc) threonine. {ECO:0000250}.
FT   CARBOHYD    248    248       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000250}.
FT   CARBOHYD    298    298       O-linked (GalNAc...) threonine.
FT                                {ECO:0000250}.
FT   CARBOHYD    307    307       O-linked (GalNAc...) serine.
FT                                {ECO:0000250}.
FT   CARBOHYD    326    326       O-linked (GalNAc...) threonine.
FT                                {ECO:0000250}.
FT   CARBOHYD    414    414       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000250}.
FT   DISULFID     46     72       {ECO:0000250}.
FT   DISULFID     60     87       {ECO:0000250}.
FT   DISULFID     97    109       {ECO:0000250}.
FT   DISULFID    103    118       {ECO:0000250}.
FT   DISULFID    120    129       {ECO:0000250}.
FT   DISULFID    134    162       {ECO:0000250}.
FT   DISULFID    160    169       {ECO:0000250}.
FT   DISULFID    177    188       {ECO:0000250}.
FT   DISULFID    182    197       {ECO:0000250}.
FT   DISULFID    199    208       {ECO:0000250}.
FT   DISULFID    216    294       {ECO:0000250}.
FT   DISULFID    237    276       {ECO:0000250}.
FT   DISULFID    265    289       {ECO:0000250}.
FT   DISULFID    340    466       {ECO:0000250}.
FT   DISULFID    378    394       {ECO:0000250}.
FT   DISULFID    386    455       {ECO:0000250}.
FT   DISULFID    417    420       {ECO:0000250}.
FT   DISULFID    480    549       {ECO:0000250}.
FT   DISULFID    512    528       {ECO:0000250}.
FT   DISULFID    539    570       {ECO:0000250}.
FT   CONFLICT    320    324       SSPRD -> MPQFPSLSDALDN (in Ref. 2;
FT                                AAH88187). {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
//
DBGET integrated database retrieval system