CP2CN_MOUSE
ID CP2CN_MOUSE Reviewed; 494 AA.
AC E9Q5K4; Q6IEF7; Q8BWN7; Q8QZW4;
DT 26-FEB-2020, integrated into UniProtKB/Swiss-Prot.
DT 05-APR-2011, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Cytochrome P450 2C44;
DE EC=1.14.14.- {ECO:0000269|PubMed:15084647};
DE AltName: Full=Arachidonic acid epoxygenase;
DE Flags: Precursor;
GN Name=Cyp2c23 {ECO:0000312|MGI:MGI:1888897};
GN Synonyms=Cyp2c44 {ECO:0000303|PubMed:15084647};
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] (ISOFORM 2).
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] (ISOFORMS 1 AND 2).
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 MRNA] (ISOFORM 1).
RC STRAIN=FVB/N; 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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP IDENTIFICATION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, FUNCTION,
RP CATALYTIC ACTIVITY, AND PATHWAY.
RC STRAIN=C57B16/J;
RX PubMed=15084647; DOI=10.1124/jpet.104.067819;
RA DeLozier T.C., Tsao C.C., Coulter S.J., Foley J., Bradbury J.A.,
RA Zeldin D.C., Goldstein J.A.;
RT "CYP2C44, a new murine CYP2C that metabolizes arachidonic acid to unique
RT stereospecific products.";
RL J. Pharmacol. Exp. Ther. 310:845-854(2004).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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).
RN [6]
RP DISRUPTION PHENOTYPE, FUNCTION, TISSUE SPECIFICITY, AND INDUCTION BY HIGH
RP SODIUM AND POTASSIUM INTAKE.
RX PubMed=24966089; DOI=10.1152/ajprenal.00123.2014;
RA Wang W.H., Zhang C., Lin D.H., Wang L., Graves J.P., Zeldin D.C.,
RA Capdevila J.H.;
RT "Cyp2c44 epoxygenase in the collecting duct is essential for the high K+
RT intake-induced antihypertensive effect.";
RL Am. J. Physiol. 307:F453-F460(2014).
RN [7]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=24368771; DOI=10.1074/jbc.m113.508416;
RA Capdevila J.H., Pidkovka N., Mei S., Gong Y., Falck J.R., Imig J.D.,
RA Harris R.C., Wang W.;
RT "The Cyp2c44 epoxygenase regulates epithelial sodium channel activity and
RT the blood pressure responses to increased dietary salt.";
RL J. Biol. Chem. 289:4377-4386(2014).
CC -!- FUNCTION: A cytochrome P450 monooxygenase involved in polyunsaturated
CC fatty acids (PUFAs) metabolism and signaling (PubMed:15084647).
CC Catalyzes preferentially the epoxidation of double bonds of PUFAs
CC (PubMed:15084647). Converts arachidonic acid (ARA, C20:4(n-6))
CC primarily to stereospecific products 8R,9S-epoxyeicosatrienoate (EET)
CC and 11R,12S-EET (PubMed:15084647). Plays a major role in the formation
CC of EETs and hydroxy-EETs (HEETs) in kidney. Via EETs may inhibit the
CC epithelial sodium channels (ENaCs) in nephron segments, preventing
CC excessive sodium absorption during high dietary salt intake
CC (PubMed:24966089, PubMed:24368771). Participates in the formation of
CC anti-inflammatory hydroxyepoxyeicosatrienoic acids (HEETs) by
CC converting 20-hydroxyeicosatetraenoic acid (20-HETE) to 20,8,9-HEET, an
CC activator of PPARA (By similarity). Metabolizes eicosapentaenoic acid
CC (EPA, C20:5(n-3)) to epoxyeicosatetraenoic acid (EETeTr) regioisomers,
CC 8,9-, 11,12-, 14,15-, and 17,18- EETeTr, preferentially producing
CC 17R,18S enantiomer (By similarity). Mechanistically, uses molecular
CC oxygen inserting one oxygen atom into a substrate, and reducing the
CC second into a water molecule, with two electrons provided by NADPH via
CC cytochrome P450 reductase (CPR; NADPH-ferrihemoprotein reductase)
CC (PubMed:15084647). {ECO:0000250|UniProtKB:P24470,
CC ECO:0000269|PubMed:15084647, ECO:0000269|PubMed:24368771,
CC ECO:0000269|PubMed:24966089}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 + reduced [NADPH--
CC hemoprotein reductase] = (8R,9S)-epoxy-(5Z,11Z,14Z)-eicosatrienoate +
CC H(+) + H2O + oxidized [NADPH--hemoprotein reductase];
CC Xref=Rhea:RHEA:49884, 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:131975; Evidence={ECO:0000269|PubMed:15084647};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49885;
CC Evidence={ECO:0000305|PubMed:15084647};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 + reduced [NADPH--
CC hemoprotein reductase] = (11R,12S)-epoxy-(5Z,8Z,14Z)-eicosatrienoate
CC + H(+) + H2O + oxidized [NADPH--hemoprotein reductase];
CC Xref=Rhea:RHEA:49880, 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:131970; Evidence={ECO:0000269|PubMed:15084647};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:49881;
CC Evidence={ECO:0000305|PubMed:15084647};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 + reduced [NADPH--
CC hemoprotein reductase] = 14,15-epoxy-(5Z,8Z,11Z)-eicosatrienoate +
CC H(+) + H2O + oxidized [NADPH--hemoprotein reductase];
CC Xref=Rhea:RHEA:51472, 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:84024; Evidence={ECO:0000269|PubMed:15084647};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51473;
CC Evidence={ECO:0000305|PubMed:15084647};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,14Z,17Z)-eicosapentaenoate + O2 + reduced [NADPH--
CC hemoprotein reductase] = 8,9-epoxy-(5Z,11Z,14Z,17Z)-eicosatetraenoate
CC + H(+) + H2O + oxidized [NADPH--hemoprotein reductase];
CC Xref=Rhea:RHEA:52168, 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:58562,
CC ChEBI:CHEBI:136439; Evidence={ECO:0000250|UniProtKB:P24470};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52169;
CC Evidence={ECO:0000250|UniProtKB:P24470};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,14Z,17Z)-eicosapentaenoate + O2 + reduced [NADPH--
CC hemoprotein reductase] = 11,12-epoxy-(5Z,8Z,14Z,17Z)-
CC eicosatetraenoate + H(+) + H2O + oxidized [NADPH--hemoprotein
CC reductase]; Xref=Rhea:RHEA:52172, 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:136441; Evidence={ECO:0000250|UniProtKB:P24470};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52173;
CC Evidence={ECO:0000250|UniProtKB:P24470};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,14Z,17Z)-eicosapentaenoate + O2 + reduced [NADPH--
CC hemoprotein reductase] = 14,15-epoxy-(5Z,8Z,11Z,17Z)-
CC eicosatetraenoate + H(+) + H2O + oxidized [NADPH--hemoprotein
CC reductase]; Xref=Rhea:RHEA:52176, 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:136443; Evidence={ECO:0000250|UniProtKB:P24470};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52177;
CC Evidence={ECO:0000250|UniProtKB:P24470};
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:0000250|UniProtKB:P24470};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39780;
CC Evidence={ECO:0000250|UniProtKB:P24470};
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:0000250|UniProtKB:P24470};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39784;
CC Evidence={ECO:0000250|UniProtKB:P24470};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=20-hydroxy-(5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 + reduced
CC [NADPH--hemoprotein reductase] = 20-hydroxy-8,9-epoxy-(5Z,11Z,14Z)-
CC eicosatrienoate + H(+) + H2O + oxidized [NADPH--hemoprotein
CC reductase]; Xref=Rhea:RHEA:64980, 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:137474; Evidence={ECO:0000250|UniProtKB:P24470};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64981;
CC Evidence={ECO:0000250|UniProtKB:P24470};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:P33261};
CC -!- PATHWAY: Lipid metabolism; arachidonate metabolism.
CC {ECO:0000305|PubMed:15084647}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:15084647}. Microsome membrane
CC {ECO:0000269|PubMed:15084647}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=E9Q5K4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=E9Q5K4-2; Sequence=VSP_060520, VSP_060521;
CC -!- TISSUE SPECIFICITY: Highly expressed in liver, particularly in
CC hepatocytes and bile duct epithelial cells (at protein level)
CC (PubMed:24966089). Expressed in nephron segments (PubMed:24966089,
CC PubMed:15084647). Prominent expression is detected in proximal tubules
CC at the corticomedullary junction (at protein level) (PubMed:15084647).
CC Also expressed in renal cortical collecting duct (PubMed:15084647).
CC Lower expression levels are detected in adrenal glands
CC (PubMed:15084647). {ECO:0000269|PubMed:15084647,
CC ECO:0000269|PubMed:24966089}.
CC -!- INDUCTION: Up-regulated by high sodium or high potassium diets. High
CC sodium intake increases expression in thick ascending limb and distal
CC convoluted tubule. An increase in dietary potassium intake induces
CC expression in distal convoluted tubule and cortical collecting duct.
CC {ECO:0000269|PubMed:24966089}.
CC -!- DISRUPTION PHENOTYPE: Mutant mice have normal development and lack
CC symptoms of disease or organ malformation (PubMed:24368771). Become
CC hypertensive in response to high sodium or high potassium diets
CC (PubMed:24368771, PubMed:24966089). {ECO:0000269|PubMed:24368771,
CC ECO:0000269|PubMed:24966089}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; AK050436; BAC34255.1; -; mRNA.
DR EMBL; AC124693; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC025819; AAH25819.1; -; mRNA.
DR EMBL; BC026766; AAH26766.1; -; mRNA.
DR EMBL; BC034834; AAH34834.1; -; mRNA.
DR EMBL; BK005218; DAA05332.1; -; mRNA.
DR CCDS; CCDS29841.1; -. [E9Q5K4-1]
DR CCDS; CCDS84445.1; -. [E9Q5K4-2]
DR RefSeq; NP_001001446.3; NM_001001446.3. [E9Q5K4-1]
DR RefSeq; NP_001161377.1; NM_001167905.1. [E9Q5K4-2]
DR AlphaFoldDB; E9Q5K4; -.
DR SMR; E9Q5K4; -.
DR STRING; 10090.ENSMUSP00000026211; -.
DR SwissLipids; SLP:000001667; -.
DR iPTMnet; E9Q5K4; -.
DR PhosphoSitePlus; E9Q5K4; -.
DR jPOST; E9Q5K4; -.
DR MaxQB; E9Q5K4; -.
DR PaxDb; E9Q5K4; -.
DR PeptideAtlas; E9Q5K4; -.
DR PRIDE; E9Q5K4; -.
DR ProteomicsDB; 305707; -. [E9Q5K4-1]
DR DNASU; 226143; -.
DR Ensembl; ENSMUST00000026211; ENSMUSP00000026211; ENSMUSG00000025197. [E9Q5K4-1]
DR Ensembl; ENSMUST00000211830; ENSMUSP00000148377; ENSMUSG00000025197. [E9Q5K4-2]
DR GeneID; 226143; -.
DR KEGG; mmu:226143; -.
DR UCSC; uc008hpc.2; mouse. [E9Q5K4-1]
DR CTD; 226143; -.
DR MGI; MGI:1888897; Cyp2c23.
DR VEuPathDB; HostDB:ENSMUSG00000025197; -.
DR eggNOG; KOG0156; Eukaryota.
DR GeneTree; ENSGT00940000163402; -.
DR HOGENOM; CLU_001570_22_3_1; -.
DR InParanoid; E9Q5K4; -.
DR OMA; FVWKKSH; -.
DR OrthoDB; 702827at2759; -.
DR PhylomeDB; E9Q5K4; -.
DR TreeFam; TF352043; -.
DR UniPathway; UPA00383; -.
DR BioGRID-ORCS; 226143; 2 hits in 74 CRISPR screens.
DR ChiTaRS; Cyp2c23; mouse.
DR PRO; PR:E9Q5K4; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; E9Q5K4; protein.
DR Bgee; ENSMUSG00000025197; Expressed in left lobe of liver and 46 other tissues.
DR Genevisible; E9Q5K4; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0008405; F:arachidonic acid 11,12-epoxygenase activity; ISO:MGI.
DR GO; GO:0008404; F:arachidonic acid 14,15-epoxygenase activity; ISO:MGI.
DR GO; GO:0008392; F:arachidonic acid epoxygenase activity; ISO:MGI.
DR GO; GO:0020037; F:heme binding; IBA:GO_Central.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0004497; F:monooxygenase activity; ISO:MGI.
DR GO; GO:0016712; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen; IBA:GO_Central.
DR GO; GO:0008395; F:steroid hydroxylase activity; IBA:GO_Central.
DR GO; GO:0019373; P:epoxygenase P450 pathway; ISO:MGI.
DR GO; GO:0046456; P:icosanoid biosynthetic process; ISO:MGI.
DR GO; GO:0006082; P:organic acid metabolic process; IBA:GO_Central.
DR GO; GO:0006805; P:xenobiotic metabolic process; IBA:GO_Central.
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; IPR008067; Cyt_P450_E_grp-I_CYP2A-like.
DR InterPro; IPR036396; Cyt_P450_sf.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00463; EP450I.
DR PRINTS; PR01684; EP450ICYP2A.
DR PRINTS; PR00385; P450.
DR SUPFAM; SSF48264; SSF48264; 1.
DR PROSITE; PS00086; CYTOCHROME_P450; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Endoplasmic reticulum;
KW Fatty acid metabolism; Heme; Iron; Lipid metabolism; Membrane;
KW Metal-binding; Microsome; Monooxygenase; Oxidoreductase; Phosphoprotein;
KW Reference proteome; Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..494
FT /note="Cytochrome P450 2C44"
FT /id="PRO_5003244448"
FT BINDING 439
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:P33261"
FT MOD_RES 131
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P00176"
FT MOD_RES 253
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q64458"
FT MOD_RES 379
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q64458"
FT VAR_SEQ 437..456
FT /note="RSCVGEGLARMELFLFFTTI -> YTRFGQLLASLNYVLRDPLM (in
FT isoform 2)"
FT /id="VSP_060520"
FT VAR_SEQ 457..494
FT /note="Missing (in isoform 2)"
FT /id="VSP_060521"
FT CONFLICT 51
FT /note="L -> F (in Ref. 3; AAH25819/AAH26766/AAH34834)"
FT /evidence="ECO:0000305"
FT CONFLICT 420
FT /note="N -> S (in Ref. 1; BAC34255)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 494 AA; 56422 MW; 6B3B2429685D1FFE CRC64;
MELLGLPTLA LLVLVMSLSL LSVWTKMRTG GRLPPGPTPL PIIGNILQLD LKDIPASLSK
LAKEYGPVYT LYFGSWPTVV LHGYDVVKEA LLNQGDEFLG RGPLPIIEDS QKGHGIVFSE
GERWKLLRRF SLMTLKNFGM GKRSLEERVQ EEARCLVEEL HKTEAQPFDP TFILACAPCN
VICSILFNER FPYNDKTFLN LMDLLNKNFY QLNSIWIQMY NLWPTIMKYI PGKHREFSKR
LGGVKNFILE KVKEHQESLD PANPRDYIDC FLSKIEEEKH NLKSDFNLEN LAICGSNLFT
AGTETTSTTL RFGLLLLVKH PEVQAKVHEE LDRVIGRHQP PSMKDKMKLP YTDAVLHEIQ
RYITLLPSSL PHAVVQDTKF RHYVIPKGTA VFPFLSSILL DQKEFPNPEK FDPGHFLDKN
GCFKKTDYFV PFSLGKRSCV GEGLARMELF LFFTTILQKF SLKALVEPKD LDIKPVTTGL
FNLPPPYKLR LVPR
