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   24-JAN-2024, entry version 167.
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,
GN   ECO:0000312|MGI:MGI:88612}; 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
CC         [NADPH--hemoprotein reductase] = 19-hydroxy-(5Z,8Z,11Z,14Z)-
CC         eicosatetraenoate + H(+) + H2O + oxidized [NADPH--hemoprotein
CC         reductase]; Xref=Rhea:RHEA:39759, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC         COMP:11965, 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
CC         [NADPH--hemoprotein reductase] = 20-hydroxy-(5Z,8Z,11Z,14Z)-
CC         eicosatetraenoate + H(+) + H2O + oxidized [NADPH--hemoprotein
CC         reductase]; Xref=Rhea:RHEA:39755, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC         COMP:11965, 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
CC         [NADPH--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
CC         [NADPH--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
CC         [NADPH--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
CC         [NADPH--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
CC         (5Z,8Z,11Z,14Z,17Z)-eicosapentaenoic acid (without cytochrome b5)
CC         {ECO:0000269|PubMed:17112342};
CC         Vmax=29 nmol/min/nmol enzyme toward
CC         (5Z,8Z,11Z,14Z,17Z)-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; 10090-ENSMUSP00000081370; -.
DR   PeptideAtlas; Q91WL5; -.
DR   ProteomicsDB; 284154; -.
DR   Ensembl; ENSMUST00000084343.4; ENSMUSP00000081370.4; ENSMUSG00000066071.7.
DR   GeneID; 277753; -.
DR   KEGG; mmu:277753; -.
DR   UCSC; uc008uer.1; mouse.
DR   AGR; MGI:88612; -.
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; NMVFLHV; -.
DR   OrthoDB; 1611592at2759; -.
DR   PhylomeDB; Q91WL5; -.
DR   TreeFam; TF105088; -.
DR   UniPathway; UPA00199; -.
DR   BioGRID-ORCS; 277753; 4 hits in 60 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 cell types or tissues.
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: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:0140981; F:medium-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   CDD; cd20678; CYP4B-like; 1.
DR   Gene3D; 1.10.630.10; Cytochrome P450; 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   PANTHER; PTHR24291:SF39; CYTOCHROME P450 4A11-RELATED; 1.
DR   PANTHER; PTHR24291; CYTOCHROME P450 FAMILY 4; 1.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00463; EP450I.
DR   PRINTS; PR00385; P450.
DR   SUPFAM; SSF48264; Cytochrome P450; 1.
DR   PROSITE; PS00086; CYTOCHROME_P450; 1.
DR   Genevisible; Q91WL5; MM.
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;
FT                   AAH14721/AAH25936/AAH26582/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
//