CP4AA_MOUSE
ID CP4AA_MOUSE Reviewed; 509 AA.
AC O88833; A2A976; Q9DCS5;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Cytochrome P450 4A10;
DE AltName: Full=CYPIVA10;
DE AltName: Full=Cytochrome P450-LA-omega 1;
DE AltName: Full=Cytochrome P452;
DE AltName: Full=Lauric acid omega-hydroxylase;
DE AltName: Full=Long-chain fatty acid omega-monooxygenase;
DE EC=1.14.14.80 {ECO:0000250|UniProtKB:P08516};
GN Name=Cyp4a10 {ECO:0000303|PubMed:16691295, ECO:0000312|MGI:MGI:88611};
GN Synonyms=Cyp4a-10;
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 [MRNA].
RC STRAIN=C57BL/6J; TISSUE=Liver;
RX PubMed=8031839; DOI=10.1016/0304-4165(94)90134-1;
RA Henderson C.J., Bammler T., Wolf C.R.;
RT "Deduced amino acid sequence of a murine cytochrome P-450 Cyp4a protein:
RT developmental and hormonal regulation in liver and kidney.";
RL Biochim. Biophys. Acta 1200:182-190(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=ddY; TISSUE=Liver;
RA Yasumura N., Ikeda T.;
RT "Polymorphism of cyp 4A10 sequence between C57BL/6 and ddY mouse.";
RL Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Kidney;
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Kidney;
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 [6]
RP DISRUPTION PHENOTYPE.
RX PubMed=16691295; DOI=10.1172/jci27546;
RA Nakagawa K., Holla V.R., Wei Y., Wang W.H., Gatica A., Wei S., Mei S.,
RA Miller C.M., Cha D.R., Price E. Jr., Zent R., Pozzi A., Breyer M.D.,
RA Guan Y., Falck J.R., Waterman M.R., Capdevila J.H.;
RT "Salt-sensitive hypertension is associated with dysfunctional Cyp4a10 gene
RT and kidney epithelial sodium channel.";
RL J. Clin. Invest. 116:1696-1702(2006).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE
RP SPECIFICITY.
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).
CC -!- FUNCTION: A cytochrome P450 monooxygenase involved in the metabolism of
CC fatty acids. Catalyzes predominantly the oxidation of the terminal
CC carbon (omega-oxidation) of long-chain fatty acids (By similarity).
CC Acts as a major omega-hydroxylase for dodecanoic (lauric) acid in liver
CC (PubMed:17112342) (By similarity). In kidney, may play an important
CC role in omega-hydroxylation of (5Z,8Z,11Z,14Z)-eicosatetraenoic acid
CC (arachidonate) to 20-hydroxyeicosatetraenoic acid (20-HETE), a
CC signaling molecule acting both as vasoconstrictive and natriuretic with
CC overall effect on arterial blood pressure (By similarity). Also
CC participates in the formation of anti-inflammatory
CC hydroxyepoxyeicosatrienoic acids (HEETs) in kidney by converting 8,9-
CC epoxyeicosatrienoic acid (EET) to 20,8,9-HEET, an activator of PPARA.
CC Displays substantially lower fatty acid omega-1 hydroxylase activity
CC (By similarity). 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).
CC {ECO:0000250|UniProtKB:P08516, ECO:0000269|PubMed:17112342}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an omega-methyl-long-chain fatty acid + O2 + reduced [NADPH--
CC hemoprotein reductase] = an omega-hydroxy-long-chain fatty acid +
CC H(+) + H2O + oxidized [NADPH--hemoprotein reductase];
CC Xref=Rhea:RHEA:56748, 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:140991,
CC ChEBI:CHEBI:140992; EC=1.14.14.80;
CC Evidence={ECO:0000250|UniProtKB:P08516};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56749;
CC Evidence={ECO:0000250|UniProtKB:P08516};
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=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=O2 + reduced [NADPH--hemoprotein reductase] + tetradecanoate =
CC 14-hydroxytetradecanoate + H(+) + H2O + oxidized [NADPH--hemoprotein
CC reductase]; Xref=Rhea:RHEA:40203, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:30807, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210,
CC ChEBI:CHEBI:77033; Evidence={ECO:0000250|UniProtKB:P08516};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40204;
CC Evidence={ECO:0000250|UniProtKB:P08516};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=hexadecanoate + O2 + reduced [NADPH--hemoprotein reductase] =
CC 16-hydroxyhexadecanoate + H(+) + H2O + oxidized [NADPH--hemoprotein
CC reductase]; Xref=Rhea:RHEA:40199, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC COMP:11965, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:55329, ChEBI:CHEBI:57618,
CC ChEBI:CHEBI:58210; EC=1.14.14.80;
CC Evidence={ECO:0000250|UniProtKB:P08516};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40200;
CC Evidence={ECO:0000250|UniProtKB:P08516};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoate + O2 + reduced [NADPH--hemoprotein
CC reductase] = 18-hydroxy-(9Z)-octadecenoate + H(+) + H2O + oxidized
CC [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:41728, Rhea:RHEA-
CC COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:30823,
CC ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:78424;
CC EC=1.14.14.80; Evidence={ECO:0000250|UniProtKB:P08516};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41729;
CC Evidence={ECO:0000250|UniProtKB:P08516};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z)-octadecadienoate + O2 + reduced [NADPH--hemoprotein
CC reductase] = 18-hydroxy-(9Z,12Z)-octadecadienoate + H(+) + H2O +
CC oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:60580,
CC Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:30245,
CC ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:132029;
CC Evidence={ECO:0000250|UniProtKB:P08516};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60581;
CC Evidence={ECO:0000250|UniProtKB:P08516};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z,12Z)-octadecadienoate + O2 + reduced [NADPH--hemoprotein
CC reductase] = 17-hydroxy-(9Z,12Z)-octadecadienoate + H(+) + H2O +
CC oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:60932,
CC Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:30245,
CC ChEBI:CHEBI:57618, ChEBI:CHEBI:58210, ChEBI:CHEBI:144041;
CC Evidence={ECO:0000250|UniProtKB:P08516};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60933;
CC Evidence={ECO:0000250|UniProtKB:P08516};
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:0000250|UniProtKB:P08516};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39756;
CC Evidence={ECO:0000250|UniProtKB:P08516};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=8,9-epoxy-(5Z,11Z,14Z)-eicosatrienoate + O2 + reduced [NADPH--
CC hemoprotein reductase] = 20-hydroxy-8,9-epoxy-(5Z,11Z,14Z)-
CC eicosatrienoate + H(+) + H2O + oxidized [NADPH--hemoprotein
CC reductase]; Xref=Rhea:RHEA:53572, 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:84025,
CC ChEBI:CHEBI:137474; Evidence={ECO:0000250|UniProtKB:P08516};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53573;
CC Evidence={ECO:0000250|UniProtKB:P08516};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:P08516};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2 uM for dodecanoate {ECO:0000269|PubMed:17112342};
CC Vmax=55 nmol/min/nmol enzyme toward dodecanoate
CC {ECO:0000269|PubMed:17112342};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:P08516}; Multi-pass membrane protein
CC {ECO:0000255}. Microsome membrane {ECO:0000250|UniProtKB:P08516};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Highly expressed in the kidneys of both genders.
CC {ECO:0000269|PubMed:17112342}.
CC -!- DISRUPTION PHENOTYPE: Mutant mice are hypertensive due to constitutive
CC activation of renal epithelial sodium channels and increased sodium
CC reabsorption. {ECO:0000269|PubMed:16691295}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000255}.
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DR EMBL; X69296; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AB018421; BAA33804.1; -; mRNA.
DR EMBL; AK002528; BAB22165.1; -; mRNA.
DR EMBL; AL627182; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC010747; AAH10747.1; -; mRNA.
DR EMBL; BC051049; AAH51049.1; -; mRNA.
DR CCDS; CCDS18492.1; -.
DR PIR; S47553; S47553.
DR RefSeq; NP_034141.3; NM_010011.3.
DR AlphaFoldDB; O88833; -.
DR SMR; O88833; -.
DR STRING; 10090.ENSMUSP00000061126; -.
DR SwissLipids; SLP:000000399; -.
DR iPTMnet; O88833; -.
DR PhosphoSitePlus; O88833; -.
DR jPOST; O88833; -.
DR MaxQB; O88833; -.
DR PaxDb; O88833; -.
DR PRIDE; O88833; -.
DR ProteomicsDB; 284152; -.
DR DNASU; 13117; -.
DR Ensembl; ENSMUST00000058785; ENSMUSP00000061126; ENSMUSG00000066072.
DR GeneID; 13117; -.
DR KEGG; mmu:13117; -.
DR UCSC; uc008uex.2; mouse.
DR CTD; 13117; -.
DR MGI; MGI:88611; Cyp4a10.
DR VEuPathDB; HostDB:ENSMUSG00000066072; -.
DR eggNOG; KOG0157; Eukaryota.
DR GeneTree; ENSGT00940000163570; -.
DR HOGENOM; CLU_001570_5_1_1; -.
DR InParanoid; O88833; -.
DR OMA; YGVQVCM; -.
DR OrthoDB; 1247045at2759; -.
DR PhylomeDB; O88833; -.
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 BioGRID-ORCS; 13117; 5 hits in 43 CRISPR screens.
DR PRO; PR:O88833; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; O88833; protein.
DR Bgee; ENSMUSG00000066072; Expressed in left lobe of liver and 53 other tissues.
DR ExpressionAtlas; O88833; baseline and differential.
DR Genevisible; O88833; 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; IEA:UniProtKB-SubCell.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:UniProtKB.
DR GO; GO:0103002; F:16-hydroxypalmitate dehydrogenase activity; ISO:MGI.
DR GO; GO:0018685; F:alkane 1-monooxygenase activity; ISO:MGI.
DR GO; GO:0008392; F:arachidonic acid epoxygenase activity; ISO:MGI.
DR GO; GO:0008391; F:arachidonic acid monooxygenase 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; TAS:UniProtKB.
DR GO; GO:0019369; P:arachidonic acid metabolic process; ISO:MGI.
DR GO; GO:0006631; P:fatty acid metabolic process; TAS:UniProtKB.
DR GO; GO:0046456; P:icosanoid biosynthetic process; ISO:MGI.
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; ISO:MGI.
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; Fatty acid metabolism; Heme; Iron; Lipid metabolism;
KW Membrane; Metal-binding; Microsome; Monooxygenase; NADP; Oxidoreductase;
KW Phosphoprotein; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..509
FT /note="Cytochrome P450 4A10"
FT /id="PRO_0000051815"
FT TRANSMEM 15..35
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 121..141
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 320
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:P51869"
FT BINDING 456
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:P08516"
FT MOD_RES 439
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P20816"
FT CONFLICT 62
FT /note="H -> L (in Ref. 1; X69296)"
FT /evidence="ECO:0000305"
FT CONFLICT 64
FT /note="K -> Q (in Ref. 2; BAA33804 and 5; AAH10747/
FT AAH51049)"
FT /evidence="ECO:0000305"
FT CONFLICT 69
FT /note="Q -> H (in Ref. 2; BAA33804 and 5; AAH10747/
FT AAH51049)"
FT /evidence="ECO:0000305"
FT CONFLICT 234
FT /note="I -> N (in Ref. 1; X69296)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 509 AA; 58330 MW; 94F22CE77BD3EDC0 CRC64;
MSVSALSPTR FADSLSGFLQ VASVLGLLLL LVKAVQFYLH RQWLLKAFQQ FPSPPFHWFF
GHEKFKGDQE LQEIVSCIEN FPSAFPRWFW GSKAYLTVYD PDYMKVILGR SDPKANGAYR
LLAPWIGYGL LLLNGQPWFQ HRRMLTPAFH YDILKPYVKN MADSIRLMLD KWERLADQDS
SIEIFQHISL MTLDTVMKCA FSHKGSVQVD GNYRTYLQAI GDLNNLFHSR VRNIFHQNDT
IYKLSSNGRL AKQACQLAHD HTDGVIKLRK DQLQDEGELE KIKKKRRLDF LDILLFARME
NGDSMSDKDL RAEVDTFMFE GHDTTASGVS WIFYALATHP DHQQRCREEV QSLLGDGSSI
TWDHLDQIPY TTMCIKEALR LYPPVPGIVR ELSTSVTFPD GRSLPKGVQV TLSIYGLHHN
PKVWPNPEVF DPSRFAPDSP RHSHSFLPFS GGARNCIGKQ FAMSELKVIV ALTLLRFELL
PDPTRVPMPL ARLVLKSKNG IYLHLKKLH
