CP4CA_MOUSE
ID CP4CA_MOUSE Reviewed; 508 AA.
AC Q91WL5; A2A973; Q3UNE4; Q6P931; Q8N7N3;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Cytochrome P450 4A12A {ECO:0000303|PubMed:17112342};
DE EC=1.14.14.1 {ECO:0000269|PubMed:17112342};
DE AltName: Full=CYPIVA12;
DE Flags: Precursor;
GN Name=Cyp4a12a {ECO:0000303|PubMed:17112342, ECO:0000312|MGI:MGI:88612};
GN Synonyms=Cyp4a12;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Gall bladder;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Kidney, and 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).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY
RP REGULATION, TISSUE SPECIFICITY, INDUCTION BY 5ALPHA-DIHYDROTESTOSTERONE,
RP SUBCELLULAR LOCATION, AND PATHWAY.
RX PubMed=17112342; DOI=10.1042/bj20061328;
RA Muller D.N., Schmidt C., Barbosa-Sicard E., Wellner M., Gross V.,
RA Hercule H., Markovic M., Honeck H., Luft F.C., Schunck W.H.;
RT "Mouse Cyp4a isoforms: enzymatic properties, gender- and strain-specific
RT expression, and role in renal 20-hydroxyeicosatetraenoic acid formation.";
RL Biochem. J. 403:109-118(2007).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: A cytochrome P450 monooxygenase involved in the metabolism of
CC fatty acids and their oxygenated derivatives (oxylipins)
CC (PubMed:17112342). Mechanistically, uses molecular oxygen inserting one
CC oxygen atom into a substrate, and reducing the second into a water
CC molecule, with two electrons provided by NADPH via cytochrome P450
CC reductase (CPR; NADPH-ferrihemoprotein reductase) (PubMed:17112342).
CC Catalyzes predominantly the oxidation of the terminal carbon (omega-
CC oxidation) of saturated and unsaturated fatty acids (PubMed:17112342).
CC May act as a major omega-hydroxylase for dodecanoic (lauric) acid in
CC kidney (PubMed:17112342). Participates in omega-hydroxylation of
CC (5Z,8Z,11Z,14Z)-eicosatetraenoic acid (arachidonate) to 20-
CC hydroxyeicosatetraenoic acid (20-HETE), a signaling molecule acting
CC both as vasoconstrictive and natriuretic with overall effect on
CC arterial blood pressure. Further catalyzes successive omega-oxidations
CC of 20-HETE to the corresponding dicarboxylic acid, and may contribute
CC to the degradation of PUFA by chain shortening (PubMed:17112342). Acts
CC as an omega-hydroxylase and epoxidase toward (5Z,8Z,11Z,14Z,17Z)-
CC eicosapentaenoc acid (EPA). Catalyzes stereoselective epoxidation of
CC the last double bond of EPA, displaying a strong preference for the
CC (R,S) stereoisomer (PubMed:17112342). Can also catalyze the oxidation
CC of the penultimate carbon (omega-1 oxidation) of fatty acids with lower
CC efficiency (PubMed:17112342). {ECO:0000269|PubMed:17112342}.
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 PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17150;
CC Evidence={ECO:0000305};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dodecanoate + O2 + reduced [NADPH--hemoprotein reductase] =
CC 11-hydroxydodecanoate + H(+) + H2O + oxidized [NADPH--hemoprotein
CC reductase]; Xref=Rhea:RHEA:39751, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:18262, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210,
CC ChEBI:CHEBI:76628; Evidence={ECO:0000269|PubMed:17112342};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39752;
CC Evidence={ECO:0000305|PubMed:17112342};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dodecanoate + O2 + reduced [NADPH--hemoprotein reductase] =
CC 12-hydroxydodecanoate + H(+) + H2O + oxidized [NADPH--hemoprotein
CC reductase]; Xref=Rhea:RHEA:38947, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:18262, ChEBI:CHEBI:36204, ChEBI:CHEBI:57618,
CC ChEBI:CHEBI:58210; Evidence={ECO:0000269|PubMed:17112342};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38948;
CC Evidence={ECO:0000305|PubMed:17112342};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 + reduced [NADPH--
CC hemoprotein reductase] = 19-hydroxy-(5Z,8Z,11Z,14Z)-eicosatetraenoate
CC + H(+) + H2O + oxidized [NADPH--hemoprotein reductase];
CC Xref=Rhea:RHEA:39759, 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:76627; Evidence={ECO:0000269|PubMed:17112342};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39760;
CC Evidence={ECO:0000305|PubMed:17112342};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 + reduced [NADPH--
CC hemoprotein reductase] = 20-hydroxy-(5Z,8Z,11Z,14Z)-eicosatetraenoate
CC + H(+) + H2O + oxidized [NADPH--hemoprotein reductase];
CC Xref=Rhea:RHEA:39755, 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:76624; Evidence={ECO:0000269|PubMed:17112342};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39756;
CC Evidence={ECO:0000305|PubMed:17112342};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=20-hydroxy-(5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 + reduced
CC [NADPH--hemoprotein reductase] = 20-oxo-(5Z,8Z,11Z,14Z)-
CC eicosatetraenoate + H(+) + 2 H2O + oxidized [NADPH--hemoprotein
CC reductase]; Xref=Rhea:RHEA:39767, 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:76624,
CC ChEBI:CHEBI:76645; Evidence={ECO:0000269|PubMed:17112342};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39768;
CC Evidence={ECO:0000305|PubMed:17112342};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=20-oxo-(5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 + reduced
CC [NADPH--hemoprotein reductase] = (5Z,8Z,11Z,14Z)-eicosatetraenedioate
CC + 2 H(+) + H2O + oxidized [NADPH--hemoprotein reductase];
CC Xref=Rhea:RHEA:39771, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:76645,
CC ChEBI:CHEBI:76647; Evidence={ECO:0000269|PubMed:17112342};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39772;
CC Evidence={ECO:0000305|PubMed:17112342};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,14Z,17Z)-eicosapentaenoate + O2 + reduced [NADPH--
CC hemoprotein reductase] = 19-hydroxy-(5Z,8Z,11Z,14Z,17Z)-
CC eicosapentaenoate + H(+) + H2O + oxidized [NADPH--hemoprotein
CC reductase]; Xref=Rhea:RHEA:39787, 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:58562,
CC ChEBI:CHEBI:76636; Evidence={ECO:0000269|PubMed:17112342};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39788;
CC Evidence={ECO:0000305|PubMed:17112342};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,14Z,17Z)-eicosapentaenoate + O2 + reduced [NADPH--
CC hemoprotein reductase] = 20-hydroxy-(5Z,8Z,11Z,14Z,17Z)-
CC eicosapentaenoate + H(+) + H2O + oxidized [NADPH--hemoprotein
CC reductase]; Xref=Rhea:RHEA:39791, 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:58562,
CC ChEBI:CHEBI:76639; Evidence={ECO:0000269|PubMed:17112342};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39792;
CC Evidence={ECO:0000305|PubMed:17112342};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,14Z,17Z)-eicosapentaenoate + O2 + reduced [NADPH--
CC hemoprotein reductase] = (17S,18R)-epoxy-(5Z,8Z,11Z,14Z)-
CC eicosatetraenoate + H(+) + H2O + oxidized [NADPH--hemoprotein
CC reductase]; Xref=Rhea:RHEA:39783, 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:58562,
CC ChEBI:CHEBI:76635; Evidence={ECO:0000269|PubMed:17112342};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39784;
CC Evidence={ECO:0000305|PubMed:17112342};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,14Z,17Z)-eicosapentaenoate + O2 + reduced [NADPH--
CC hemoprotein reductase] = (17R,18S)-epoxy-(5Z,8Z,11Z,14Z)-
CC eicosatetraenoate + H(+) + H2O + oxidized [NADPH--hemoprotein
CC reductase]; Xref=Rhea:RHEA:39779, 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:58562,
CC ChEBI:CHEBI:76634; Evidence={ECO:0000269|PubMed:17112342};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39780;
CC Evidence={ECO:0000305|PubMed:17112342};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:P20817};
CC -!- ACTIVITY REGULATION: Activated by cytochrome b5. The Vmax almost
CC doubles in the presence of cytochrome b5.
CC {ECO:0000269|PubMed:17112342}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=16 uM for dodecanoic acid {ECO:0000269|PubMed:17112342};
CC KM=25 uM for (5Z,8Z,11Z,14Z)-eicosatetraenoic acid (without
CC cytochrome b5) {ECO:0000269|PubMed:17112342};
CC KM=34 uM for (5Z,8Z,11Z,14Z)-eicosatetraenoic acid (with cytochrome
CC b5) {ECO:0000269|PubMed:17112342};
CC KM=29 uM for (5Z,8Z,11Z,14Z,17Z)-eicosapentaenoic acid (without
CC cytochrome b5) {ECO:0000269|PubMed:17112342};
CC KM=33 uM for (5Z,8Z,11Z,14Z,17Z)-eicosapentaenoic acid (with
CC cytochrome b5) {ECO:0000269|PubMed:17112342};
CC Vmax=76 nmol/min/nmol enzyme toward dodecanoic acid
CC {ECO:0000269|PubMed:17112342};
CC Vmax=8 nmol/min/nmol enzyme toward (5Z,8Z,11Z,14Z)-eicosatetraenoic
CC acid (without cytochrome b5) {ECO:0000269|PubMed:17112342};
CC Vmax=16 nmol/min/nmol enzyme toward (5Z,8Z,11Z,14Z)-eicosatetraenoic
CC acid (with cytochrome b5) {ECO:0000269|PubMed:17112342};
CC Vmax=14 nmol/min/nmol enzyme toward (5Z,8Z,11Z,14Z,17Z)-
CC eicosapentaenoic acid (without cytochrome b5)
CC {ECO:0000269|PubMed:17112342};
CC Vmax=29 nmol/min/nmol enzyme toward (5Z,8Z,11Z,14Z,17Z)-
CC eicosapentaenoic acid (with cytochrome b5)
CC {ECO:0000269|PubMed:17112342};
CC -!- PATHWAY: Lipid metabolism; fatty acid metabolism.
CC {ECO:0000305|PubMed:17112342}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:17112342}; Peripheral membrane protein. Microsome
CC membrane {ECO:0000269|PubMed:17112342}; Peripheral membrane protein.
CC -!- TISSUE SPECIFICITY: Gender- and strain-specific expression in kidney
CC (at protein level). Predominantly expressed in males, the expression
CC among strains decreasing in the following order: NMRI > FVB/N > 129
CC Sv/J > Balb/c > C57BL/6. Expressed in renal arterioles.
CC {ECO:0000269|PubMed:17112342}.
CC -!- INDUCTION: Up-regulated by 5alpha-dihydrotestosterone.
CC {ECO:0000269|PubMed:17112342}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000255}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAE25803.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK144260; BAE25803.1; ALT_FRAME; mRNA.
DR EMBL; AL627182; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL627227; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466552; EDL30651.1; -; Genomic_DNA.
DR EMBL; BC014721; AAH14721.1; -; mRNA.
DR EMBL; BC025936; AAH25936.1; -; mRNA.
DR EMBL; BC026582; AAH26582.1; -; mRNA.
DR EMBL; BC031141; AAH31141.1; -; mRNA.
DR EMBL; BC033924; AAH33924.1; -; mRNA.
DR CCDS; CCDS18489.1; -.
DR RefSeq; NP_803125.2; NM_177406.3.
DR AlphaFoldDB; Q91WL5; -.
DR SMR; Q91WL5; -.
DR STRING; 10090.ENSMUSP00000081370; -.
DR SwissLipids; SLP:000000482; -.
DR iPTMnet; Q91WL5; -.
DR PhosphoSitePlus; Q91WL5; -.
DR SwissPalm; Q91WL5; -.
DR jPOST; Q91WL5; -.
DR MaxQB; Q91WL5; -.
DR PaxDb; Q91WL5; -.
DR PeptideAtlas; Q91WL5; -.
DR PRIDE; Q91WL5; -.
DR ProteomicsDB; 284154; -.
DR Ensembl; ENSMUST00000084343; ENSMUSP00000081370; ENSMUSG00000066071.
DR GeneID; 277753; -.
DR KEGG; mmu:277753; -.
DR UCSC; uc008uer.1; mouse.
DR CTD; 277753; -.
DR MGI; MGI:88612; Cyp4a12a.
DR VEuPathDB; HostDB:ENSMUSG00000066071; -.
DR eggNOG; KOG0157; Eukaryota.
DR GeneTree; ENSGT00940000155173; -.
DR HOGENOM; CLU_001570_5_1_1; -.
DR InParanoid; Q91WL5; -.
DR OMA; MESILHY; -.
DR OrthoDB; 1247045at2759; -.
DR PhylomeDB; Q91WL5; -.
DR TreeFam; TF105088; -.
DR Reactome; R-MMU-211935; Fatty acids.
DR Reactome; R-MMU-211958; Miscellaneous substrates.
DR Reactome; R-MMU-211979; Eicosanoids.
DR Reactome; R-MMU-2142691; Synthesis of Leukotrienes (LT) and Eoxins (EX).
DR UniPathway; UPA00199; -.
DR BioGRID-ORCS; 277753; 4 hits in 55 CRISPR screens.
DR PRO; PR:Q91WL5; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q91WL5; protein.
DR Bgee; ENSMUSG00000066071; Expressed in left lobe of liver and 38 other tissues.
DR Genevisible; Q91WL5; MM.
DR GO; GO:0016324; C:apical plasma membrane; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISO:MGI.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0103002; F:16-hydroxypalmitate dehydrogenase activity; ISO:MGI.
DR GO; GO:0018685; F:alkane 1-monooxygenase activity; IDA:MGI.
DR GO; GO:0008392; F:arachidonic acid epoxygenase activity; ISO:MGI.
DR GO; GO:0008391; F:arachidonic acid monooxygenase activity; IBA:GO_Central.
DR GO; GO:0052869; F:arachidonic acid omega-hydroxylase activity; IDA:UniProtKB.
DR GO; GO:0070330; F:aromatase activity; IEA:UniProtKB-EC.
DR GO; GO:0120250; F:fatty acid omega-hydroxylase activity; ISO:MGI.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0102116; F:laurate hydroxylase activity; ISO:MGI.
DR GO; GO:0050051; F:leukotriene-B4 20-monooxygenase activity; ISO:MGI.
DR GO; GO:0102033; F:long-chain fatty acid omega-hydroxylase activity; ISO:MGI.
DR GO; GO:0004497; F:monooxygenase activity; ISS:UniProtKB.
DR GO; GO:0019369; P:arachidonic acid metabolic process; ISO:MGI.
DR GO; GO:0006631; P:fatty acid metabolic process; ISS:UniProtKB.
DR GO; GO:0046456; P:icosanoid biosynthetic process; IBA:GO_Central.
DR GO; GO:0001822; P:kidney development; IBA:GO_Central.
DR GO; GO:0048252; P:lauric acid metabolic process; ISO:MGI.
DR GO; GO:0043651; P:linoleic acid metabolic process; IBA:GO_Central.
DR GO; GO:0097267; P:omega-hydroxylase P450 pathway; IDA: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 Endoplasmic reticulum; Heme; Iron; Membrane; Metal-binding; Microsome;
KW Monooxygenase; Oxidoreductase; Reference proteome; Signal.
FT SIGNAL 1..37
FT /evidence="ECO:0000255"
FT CHAIN 38..508
FT /note="Cytochrome P450 4A12A"
FT /evidence="ECO:0000255"
FT /id="PRO_0000051817"
FT BINDING 319
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:P51869"
FT BINDING 455
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:P24464"
FT CONFLICT 58
FT /note="W -> C (in Ref. 1; BAE25803)"
FT /evidence="ECO:0000305"
FT CONFLICT 131
FT /note="M -> L (in Ref. 4; AAH14721/AAH25936/AAH26582/
FT AAH31141/AAH33924)"
FT /evidence="ECO:0000305"
FT CONFLICT 288
FT /note="D -> G (in Ref. 1; BAE25803)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 508 AA; 58350 MW; 0F6C78665E78DF4F CRC64;
MSASALSSIR FPGSISEYLQ VASVLSLLLL LFKTAQLYLH RQWLLSSTQQ FPSPPSHWLF
GHKILKDQDL QDILTRIKNF PSACPQWLWG SKVRIQVYDP DYMKLILGRS DPKANGSYRF
LAPWIGRGLL MLDGQTWFQH RRMLTPAFHY DILKPYTEIM ADSVRVMLDK WEQIVGQDST
LEIFRHITLM TLDTIMKCAF SHEGSVQLDR KYKSYIQAVE DLNDLVFSRV RNIFHQNDII
YRVSSNGCKA NSACKLAHDH TDQVIKSRRI QLQDEEELEK LKKKRRLDFL DILLFARMEN
GKSLSDKDLR AEVDTFMFEG HDTTASGISW IFYALATNPE HQQRCRKEIQ SLLGDGTSIT
WNDLDKMPYT TMCIKEALRI YPPVPSVSRE LSSPVTFPDG RSLPKGIHVM LSFYGLHHNP
TVWPNPEVFD PSRFAPGSSR HSHSFLPFSG GARNCIGKQF AMNELKVAVA LTLLRFELLP
DPTRVPIPIP RIVLKSKNGI HLHLKKLQ
