CP4FC_HUMAN
ID CP4FC_HUMAN Reviewed; 524 AA.
AC Q9HCS2; E7ET51; O60389; Q5JPJ7; Q9HCS1;
DT 10-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 12-SEP-2018, sequence version 3.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=Cytochrome P450 4F12 {ECO:0000303|PubMed:11162645};
DE EC=1.14.14.1 {ECO:0000269|PubMed:11162607, ECO:0000269|PubMed:16112640};
DE AltName: Full=CYPIVF12;
GN Name=CYP4F12 {ECO:0000303|PubMed:16112640, ECO:0000312|HGNC:HGNC:18857};
GN ORFNames=UNQ568/PRO1129;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, FUNCTION,
RP CATALYTIC ACTIVITY, PATHWAY, AND VARIANTS MET-16; ASP-76 AND GLY-522.
RC TISSUE=Liver;
RX PubMed=11162607; DOI=10.1006/bbrc.2000.4191;
RA Bylund J., Bylund M., Oliw E.H.;
RT "cDNA cloning and expression of CYP4F12, a novel human cytochrome P450.";
RL Biochem. Biophys. Res. Commun. 280:892-897(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY,
RP CHARACTERIZATION, AND VARIANTS LEU-13; MET-16; ASP-76 AND GLY-522.
RC TISSUE=Small intestine;
RX PubMed=11162645; DOI=10.1006/bbrc.2000.4238;
RA Hashizume T., Imaoka S., Hiroi T., Terauchi Y., Fujii T., Miyazaki H.,
RA Kamataki T., Funae Y.;
RT "cDNA cloning and expression of a novel cytochrome p450 (cyp4f12) from
RT human small intestine.";
RL Biochem. Biophys. Res. Commun. 280:1135-1141(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS MET-16;
RP ASP-76 AND GLY-522.
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANTS MET-16 AND
RP ASP-76.
RC TISSUE=Placenta;
RX PubMed=16303743; DOI=10.1093/dnares/12.2.117;
RA Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J.,
RA Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S.,
RA Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y.,
RA Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S.,
RA Isogai T.;
RT "Signal sequence and keyword trap in silico for selection of full-length
RT human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA
RT libraries.";
RL DNA Res. 12:117-126(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANTS MET-16 AND
RP ASP-76.
RC TISSUE=Cervix;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANTS ILE-90 AND
RP CYS-188.
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANTS MET-16; ASP-76
RP AND GLY-522.
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=16112640; DOI=10.1016/j.abb.2005.07.003;
RA Stark K., Wongsud B., Burman R., Oliw E.H.;
RT "Oxygenation of polyunsaturated long chain fatty acids by recombinant
RT CYP4F8 and CYP4F12 and catalytic importance of Tyr-125 and Gly-328 of
RT CYP4F8.";
RL Arch. Biochem. Biophys. 441:174-181(2005).
CC -!- FUNCTION: A cytochrome P450 monooxygenase involved in the metabolism of
CC endogenous polyunsaturated fatty acids (PUFAs). Mechanistically, uses
CC molecular oxygen inserting one oxygen atom into a substrate, and
CC reducing the second into a water molecule, with two electrons provided
CC by NADPH via cytochrome P450 reductase (CPR; NADPH-ferrihemoprotein
CC reductase). Catalyzes the hydroxylation of carbon hydrogen bonds, with
CC preference for omega-2 position. Metabolizes (5Z,8Z,11Z,14Z)-
CC eicosatetraenoic acid (arachidonate) toward 18-hydroxy arachidonate
CC (PubMed:11162607). Catalyzes the epoxidation of double bonds of PUFAs
CC such as docosapentaenoic and docosahexaenoic acids (PubMed:16112640).
CC Has low omega-hydroxylase activity toward leukotriene B4 and
CC arachidonate (PubMed:11162645). Involved in the metabolism of
CC xenobiotics. Catalyzes the hydroxylation of the antihistamine drug
CC ebastine (PubMed:11162645). {ECO:0000269|PubMed:11162607,
CC ECO:0000269|PubMed:11162645, ECO:0000269|PubMed:16112640}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an organic molecule + O2 + reduced [NADPH--hemoprotein
CC reductase] = an alcohol + H(+) + H2O + oxidized [NADPH--hemoprotein
CC reductase]; Xref=Rhea:RHEA:17149, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:30879, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210,
CC ChEBI:CHEBI:142491; EC=1.14.14.1;
CC Evidence={ECO:0000269|PubMed:11162607};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17150;
CC Evidence={ECO:0000305|PubMed:11162607};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 + reduced [NADPH--
CC hemoprotein reductase] = 18-hydroxy-(5Z,8Z,11Z,14Z)-eicosatetraenoate
CC + H(+) + H2O + oxidized [NADPH--hemoprotein reductase];
CC Xref=Rhea:RHEA:39811, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:32395, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210,
CC ChEBI:CHEBI:63590; Evidence={ECO:0000269|PubMed:11162607};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39812;
CC Evidence={ECO:0000305|PubMed:11162607};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(7Z,10Z,13Z,16Z,19Z)-docosapentaenoate + O2 + reduced [NADPH--
CC hemoprotein reductase] = 10,11-epoxy-(7Z,13Z,16Z,19Z)-
CC docosatetraenoate + H(+) + H2O + oxidized [NADPH--hemoprotein
CC reductase]; Xref=Rhea:RHEA:51108, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:77224,
CC ChEBI:CHEBI:133938; Evidence={ECO:0000269|PubMed:16112640};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51109;
CC Evidence={ECO:0000305|PubMed:16112640};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(7Z,10Z,13Z,16Z,19Z)-docosapentaenoate + O2 + reduced [NADPH--
CC hemoprotein reductase] = 13,14-epoxy-(7Z,10Z,16Z,19Z)-
CC docosatetraenoate + H(+) + H2O + oxidized [NADPH--hemoprotein
CC reductase]; Xref=Rhea:RHEA:51104, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:77224,
CC ChEBI:CHEBI:133937; Evidence={ECO:0000269|PubMed:16112640};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51105;
CC Evidence={ECO:0000305|PubMed:16112640};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(7Z,10Z,13Z,16Z,19Z)-docosapentaenoate + O2 + reduced [NADPH--
CC hemoprotein reductase] = 16,17-epoxy-(7Z,10Z,13Z,19Z)-
CC docosatetraenoate + H(+) + H2O + oxidized [NADPH--hemoprotein
CC reductase]; Xref=Rhea:RHEA:51100, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:77224,
CC ChEBI:CHEBI:133936; Evidence={ECO:0000269|PubMed:16112640};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51101;
CC Evidence={ECO:0000305|PubMed:16112640};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(7Z,10Z,13Z,16Z,19Z)-docosapentaenoate + O2 + reduced [NADPH--
CC hemoprotein reductase] = 19,20-epoxy-(7Z,10Z,13Z,16Z)-
CC docosatetraenoate + H(+) + H2O + oxidized [NADPH--hemoprotein
CC reductase]; Xref=Rhea:RHEA:51096, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:77224,
CC ChEBI:CHEBI:133935; Evidence={ECO:0000269|PubMed:16112640};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51097;
CC Evidence={ECO:0000305|PubMed:16112640};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(4Z,7Z,10Z,13Z,16Z,19Z)-docosahexaenoate + O2 + reduced
CC [NADPH--hemoprotein reductase] = 10,11-epoxy-(4Z,7Z,13Z,16Z,19Z)-
CC docosapentaenoate + H(+) + H2O + oxidized [NADPH--hemoprotein
CC reductase]; Xref=Rhea:RHEA:51092, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:77016,
CC ChEBI:CHEBI:133934; Evidence={ECO:0000269|PubMed:16112640};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51093;
CC Evidence={ECO:0000305|PubMed:16112640};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(4Z,7Z,10Z,13Z,16Z,19Z)-docosahexaenoate + O2 + reduced
CC [NADPH--hemoprotein reductase] = 13,14-epoxy-(4Z,7Z,10Z,16Z,19Z)-
CC docosapentaenoate + H(+) + H2O + oxidized [NADPH--hemoprotein
CC reductase]; Xref=Rhea:RHEA:51088, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:77016,
CC ChEBI:CHEBI:133933; Evidence={ECO:0000269|PubMed:16112640};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51089;
CC Evidence={ECO:0000305|PubMed:16112640};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(4Z,7Z,10Z,13Z,16Z,19Z)-docosahexaenoate + O2 + reduced
CC [NADPH--hemoprotein reductase] = 16,17-epoxy-(4Z,7Z,10Z,13Z,19Z)-
CC docosapentaenoate + H(+) + H2O + oxidized [NADPH--hemoprotein
CC reductase]; Xref=Rhea:RHEA:51084, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:77016,
CC ChEBI:CHEBI:133932; Evidence={ECO:0000269|PubMed:16112640};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51085;
CC Evidence={ECO:0000305|PubMed:16112640};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(4Z,7Z,10Z,13Z,16Z,19Z)-docosahexaenoate + O2 + reduced
CC [NADPH--hemoprotein reductase] = 19,20-epoxy-(4Z,7Z,10Z,13Z,16Z)-
CC docosapentaenoate + H(+) + H2O + oxidized [NADPH--hemoprotein
CC reductase]; Xref=Rhea:RHEA:51080, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:77016,
CC ChEBI:CHEBI:133931; Evidence={ECO:0000269|PubMed:16112640};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51081;
CC Evidence={ECO:0000305|PubMed:16112640};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:Q02928};
CC -!- PATHWAY: Lipid metabolism; arachidonate metabolism.
CC {ECO:0000269|PubMed:11162607}.
CC -!- INTERACTION:
CC Q9HCS2; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-3918831, EBI-16439278;
CC Q9HCS2; Q9NPL8: TIMMDC1; NbExp=3; IntAct=EBI-3918831, EBI-6268651;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q9HBI6}. Microsome membrane
CC {ECO:0000250|UniProtKB:Q9HBI6}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9HCS2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9HCS2-2; Sequence=VSP_055581, VSP_055582;
CC -!- TISSUE SPECIFICITY: Expressed in small intestine, liver, colon and
CC heart. {ECO:0000269|PubMed:11162607, ECO:0000269|PubMed:11162645}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EAW84492.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AY008841; AAG33247.1; -; mRNA.
DR EMBL; AB035130; BAB18269.1; -; mRNA.
DR EMBL; AB035131; BAB18270.1; -; mRNA.
DR EMBL; AY358977; AAQ89336.1; -; mRNA.
DR EMBL; AK075435; BAG52137.1; -; mRNA.
DR EMBL; AL832171; CAI46131.1; -; mRNA.
DR EMBL; AC004523; AAC11543.1; -; Genomic_DNA.
DR EMBL; KF459712.1; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC122702; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471106; EAW84492.1; ALT_INIT; Genomic_DNA.
DR EMBL; CH471106; EAW84495.1; -; Genomic_DNA.
DR CCDS; CCDS42517.1; -. [Q9HCS2-1]
DR PIR; JC7594; JC7594.
DR PIR; JC7598; JC7598.
DR RefSeq; NP_076433.3; NM_023944.3. [Q9HCS2-1]
DR AlphaFoldDB; Q9HCS2; -.
DR SMR; Q9HCS2; -.
DR BioGRID; 122449; 30.
DR IntAct; Q9HCS2; 10.
DR STRING; 9606.ENSP00000448998; -.
DR BindingDB; Q9HCS2; -.
DR ChEMBL; CHEMBL3509589; -.
DR DrugBank; DB01026; Ketoconazole.
DR DrugBank; DB12016; Ponesimod.
DR GuidetoPHARMACOLOGY; 1348; -.
DR SwissLipids; SLP:000001652; -.
DR iPTMnet; Q9HCS2; -.
DR PhosphoSitePlus; Q9HCS2; -.
DR BioMuta; CYP4F12; -.
DR DMDM; 313104094; -.
DR EPD; Q9HCS2; -.
DR jPOST; Q9HCS2; -.
DR MassIVE; Q9HCS2; -.
DR MaxQB; Q9HCS2; -.
DR PaxDb; Q9HCS2; -.
DR PeptideAtlas; Q9HCS2; -.
DR PRIDE; Q9HCS2; -.
DR ProteomicsDB; 18127; -.
DR ProteomicsDB; 81793; -. [Q9HCS2-1]
DR Antibodypedia; 27141; 138 antibodies from 23 providers.
DR DNASU; 66002; -.
DR Ensembl; ENST00000324632.10; ENSP00000321821.9; ENSG00000186204.15. [Q9HCS2-1]
DR Ensembl; ENST00000517734.5; ENSP00000430849.1; ENSG00000186204.15. [Q9HCS2-2]
DR Ensembl; ENST00000548435.5; ENSP00000449703.1; ENSG00000186204.15. [Q9HCS2-2]
DR Ensembl; ENST00000550308.6; ENSP00000448998.1; ENSG00000186204.15. [Q9HCS2-1]
DR GeneID; 66002; -.
DR KEGG; hsa:66002; -.
DR MANE-Select; ENST00000550308.6; ENSP00000448998.1; NM_023944.4; NP_076433.3.
DR UCSC; uc060uvi.1; human. [Q9HCS2-1]
DR CTD; 66002; -.
DR DisGeNET; 66002; -.
DR GeneCards; CYP4F12; -.
DR HGNC; HGNC:18857; CYP4F12.
DR HPA; ENSG00000186204; Tissue enhanced (intestine, liver).
DR MIM; 611485; gene.
DR neXtProt; NX_Q9HCS2; -.
DR OpenTargets; ENSG00000186204; -.
DR PharmGKB; PA38717; -.
DR VEuPathDB; HostDB:ENSG00000186204; -.
DR eggNOG; KOG0157; Eukaryota.
DR GeneTree; ENSGT00940000163718; -.
DR InParanoid; Q9HCS2; -.
DR OMA; GRSCIGY; -.
DR OrthoDB; 1247045at2759; -.
DR PhylomeDB; Q9HCS2; -.
DR TreeFam; TF105088; -.
DR BRENDA; 1.14.14.B9; 2681.
DR PathwayCommons; Q9HCS2; -.
DR Reactome; R-HSA-211935; Fatty acids.
DR Reactome; R-HSA-211979; Eicosanoids.
DR SignaLink; Q9HCS2; -.
DR UniPathway; UPA00383; -.
DR BioGRID-ORCS; 66002; 7 hits in 1065 CRISPR screens.
DR ChiTaRS; CYP4F12; human.
DR GeneWiki; CYP4F12; -.
DR GenomeRNAi; 66002; -.
DR Pharos; Q9HCS2; Tbio.
DR PRO; PR:Q9HCS2; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q9HCS2; protein.
DR Bgee; ENSG00000186204; Expressed in mucosa of transverse colon and 180 other tissues.
DR ExpressionAtlas; Q9HCS2; baseline and differential.
DR Genevisible; Q9HCS2; HS.
DR GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISS:UniProtKB.
DR GO; GO:0018685; F:alkane 1-monooxygenase activity; ISS:UniProtKB.
DR GO; GO:0008392; F:arachidonic acid epoxygenase activity; ISS:UniProtKB.
DR GO; GO:0008391; F:arachidonic acid monooxygenase activity; IBA:GO_Central.
DR GO; GO:0070330; F:aromatase activity; IEA:UniProtKB-EC.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0050051; F:leukotriene-B4 20-monooxygenase activity; ISS:UniProtKB.
DR GO; GO:0004497; F:monooxygenase activity; TAS:Reactome.
DR GO; GO:0019369; P:arachidonic acid metabolic process; ISS:UniProtKB.
DR GO; GO:0019373; P:epoxygenase P450 pathway; ISS:UniProtKB.
DR GO; GO:0006631; P:fatty acid metabolic process; TAS:Reactome.
DR GO; GO:0036101; P:leukotriene B4 catabolic process; ISS:UniProtKB.
DR GO; GO:0001676; P:long-chain fatty acid metabolic process; ISS:UniProtKB.
DR GO; GO:0042361; P:menaquinone catabolic process; IBA:GO_Central.
DR GO; GO:0042376; P:phylloquinone catabolic process; IBA:GO_Central.
DR GO; GO:0003095; P:pressure natriuresis; ISS:UniProtKB.
DR GO; GO:0003091; P:renal water homeostasis; ISS:UniProtKB.
DR GO; GO:0055078; P:sodium ion homeostasis; ISS:UniProtKB.
DR GO; GO:0000038; P:very long-chain fatty acid metabolic process; ISS:UniProtKB.
DR GO; GO:0042360; P:vitamin E metabolic process; ISS:UniProtKB.
DR GO; GO:0006805; P:xenobiotic metabolic process; ISS:UniProtKB.
DR Gene3D; 1.10.630.10; -; 1.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR017972; Cyt_P450_CS.
DR InterPro; IPR002401; Cyt_P450_E_grp-I.
DR InterPro; IPR036396; Cyt_P450_sf.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00463; EP450I.
DR PRINTS; PR00385; P450.
DR SUPFAM; SSF48264; SSF48264; 1.
DR PROSITE; PS00086; CYTOCHROME_P450; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Endoplasmic reticulum; Fatty acid metabolism; Heme;
KW Iron; Lipid metabolism; Membrane; Metal-binding; Microsome; Monooxygenase;
KW Oxidoreductase; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..524
FT /note="Cytochrome P450 4F12"
FT /id="PRO_0000051857"
FT TRANSMEM 19..39
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 87..107
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 468
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:P51869"
FT VAR_SEQ 90..102
FT /note="VWLGPIIPFIVLC -> LPLHPRIISSSGS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16303743,
FT ECO:0000303|PubMed:17974005"
FT /id="VSP_055581"
FT VAR_SEQ 103..524
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16303743,
FT ECO:0000303|PubMed:17974005"
FT /id="VSP_055582"
FT VARIANT 13
FT /note="P -> L (in dbSNP:rs16995376)"
FT /evidence="ECO:0000269|PubMed:11162645"
FT /id="VAR_013244"
FT VARIANT 16
FT /note="T -> M (in dbSNP:rs16995378)"
FT /evidence="ECO:0000269|PubMed:11162607,
FT ECO:0000269|PubMed:11162645, ECO:0000269|PubMed:12975309,
FT ECO:0000269|PubMed:16303743, ECO:0000269|PubMed:17974005,
FT ECO:0000269|Ref.7"
FT /id="VAR_048459"
FT VARIANT 76
FT /note="N -> D (in dbSNP:rs609636)"
FT /evidence="ECO:0000269|PubMed:11162607,
FT ECO:0000269|PubMed:11162645, ECO:0000269|PubMed:12975309,
FT ECO:0000269|PubMed:16303743, ECO:0000269|PubMed:17974005,
FT ECO:0000269|Ref.7"
FT /id="VAR_013245"
FT VARIANT 90
FT /note="V -> I (in dbSNP:rs609290)"
FT /evidence="ECO:0000269|PubMed:15057824"
FT /id="VAR_013246"
FT VARIANT 188
FT /note="R -> C (in dbSNP:rs2285888)"
FT /evidence="ECO:0000269|PubMed:15057824"
FT /id="VAR_013247"
FT VARIANT 522
FT /note="S -> G (in dbSNP:rs593818)"
FT /evidence="ECO:0000269|PubMed:11162607,
FT ECO:0000269|PubMed:11162645, ECO:0000269|PubMed:12975309,
FT ECO:0000269|Ref.7"
FT /id="VAR_048460"
SQ SEQUENCE 524 AA; 60309 MW; 91F80BF82FED6337 CRC64;
MSLLSLPWLG LRPVATSPWL LLLLVVGSWL LARILAWTYA FYNNCRRLQC FPQPPKRNWF
WGHLGLITPT EEGLKNSTQM SATYSQGFTV WLGPIIPFIV LCHPDTIRSI TNASAAIAPK
DNLFIRFLKP WLGEGILLSG GDKWSRHRRM LTPAFHFNIL KSYITIFNKS ANIMLDKWQH
LASEGSSRLD MFEHISLMTL DSLQKCIFSF DSHCQERPSE YIATILELSA LVEKRSQHIL
QHMDFLYYLS HDGRRFHRAC RLVHDFTDAV IRERRRTLPT QGIDDFFKDK AKSKTLDFID
VLLLSKDEDG KALSDEDIRA EADTFMFGGH DTTASGLSWV LYNLARHPEY QERCRQEVQE
LLKDRDPKEI EWDDLAQLPF LTMCVKESLR LHPPAPFISR CCTQDIVLPD GRVIPKGITC
LIDIIGVHHN PTVWPDPEVY DPFRFDPENS KGRSPLAFIP FSAGPRNCIG QAFAMAEMKV
VLALMLLHFR FLPDHTEPRR KLELIMRAEG GLWLRVEPLN VSLQ
