CP237_MOUSE
ID CP237_MOUSE Reviewed; 490 AA.
AC P56654; E9QKN4;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Cytochrome P450 2C37;
DE EC=1.14.14.1 {ECO:0000269|PubMed:9721182};
DE AltName: Full=CYPIIC37;
DE Flags: Precursor;
GN Name=Cyp2c37 {ECO:0000303|PubMed:9721182, ECO:0000312|MGI:MGI:1306806};
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], FUNCTION, CATALYTIC ACTIVITY, TISSUE
RP SPECIFICITY, AND PATHWAY.
RC STRAIN=CD-1;
RX PubMed=9721182; DOI=10.1006/abbi.1998.0806;
RA Luo G., Zeldin D.C., Blaisdell J.A., Hodgson E., Goldstein J.A.;
RT "Cloning and expression of murine CYP2Cs and their ability to metabolize
RT arachidonic acid.";
RL Arch. Biochem. Biophys. 357:45-57(1998).
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 MRNA].
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 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 that metabolizes
CC (5Z,8Z,11Z,14Z)-eicosatetraenoic acid (arachidonate) to primarily
CC produce 12-hydroxyeicosatetraenoic acid (12-HETE). Mechanistically,
CC uses 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--hemoprotein
CC reductase). {ECO:0000269|PubMed:9721182}.
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:9721182};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17150;
CC Evidence={ECO:0000305|PubMed:9721182};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 + reduced [NADPH--
CC hemoprotein reductase] = 12-hydroxy-(5Z,8Z,10E,14Z)-eicosatetraenoate
CC + H(+) + H2O + oxidized [NADPH--hemoprotein reductase];
CC Xref=Rhea:RHEA:51484, 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:90718; Evidence={ECO:0000269|PubMed:9721182};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:51485;
CC Evidence={ECO:0000305|PubMed:9721182};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC -!- PATHWAY: Lipid metabolism; arachidonate metabolism.
CC {ECO:0000305|PubMed:9721182}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral
CC membrane protein. Microsome membrane; Peripheral membrane protein.
CC -!- TISSUE SPECIFICITY: Liver. {ECO:0000269|PubMed:9721182}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; AF047542; AAD13719.1; -; mRNA.
DR EMBL; AC148014; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC057912; AAH57912.1; -; mRNA.
DR CCDS; CCDS29799.1; -.
DR RefSeq; NP_034131.2; NM_010001.2.
DR AlphaFoldDB; P56654; -.
DR SMR; P56654; -.
DR STRING; 10090.ENSMUSP00000045362; -.
DR SwissLipids; SLP:000001671; -.
DR iPTMnet; P56654; -.
DR PhosphoSitePlus; P56654; -.
DR jPOST; P56654; -.
DR MaxQB; P56654; -.
DR PaxDb; P56654; -.
DR PeptideAtlas; P56654; -.
DR PRIDE; P56654; -.
DR ProteomicsDB; 278002; -.
DR DNASU; 13096; -.
DR Ensembl; ENSMUST00000049178; ENSMUSP00000045362; ENSMUSG00000042248.
DR GeneID; 13096; -.
DR KEGG; mmu:13096; -.
DR UCSC; uc008hkf.2; mouse.
DR CTD; 13096; -.
DR MGI; MGI:1306806; Cyp2c37.
DR VEuPathDB; HostDB:ENSMUSG00000042248; -.
DR eggNOG; KOG0156; Eukaryota.
DR GeneTree; ENSGT00940000155736; -.
DR HOGENOM; CLU_001570_22_3_1; -.
DR InParanoid; P56654; -.
DR OMA; SVPPVYQ; -.
DR OrthoDB; 702827at2759; -.
DR PhylomeDB; P56654; -.
DR TreeFam; TF352043; -.
DR UniPathway; UPA00383; -.
DR BioGRID-ORCS; 13096; 0 hits in 72 CRISPR screens.
DR ChiTaRS; Cyp2c37; mouse.
DR PRO; PR:P56654; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; P56654; protein.
DR Bgee; ENSMUSG00000042248; Expressed in left lobe of liver and 10 other tissues.
DR Genevisible; P56654; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0008392; F:arachidonic acid epoxygenase activity; ISO:MGI.
DR GO; GO:0008391; F:arachidonic acid monooxygenase activity; IDA:UniProtKB.
DR GO; GO:0070330; F:aromatase activity; IEA:UniProtKB-EC.
DR GO; GO:0034875; F:caffeine oxidase activity; ISO:MGI.
DR GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR GO; GO:0020037; F:heme binding; ISO:MGI.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0120319; F:long-chain fatty acid omega-1 hydroxylase activity; ISO:MGI.
DR GO; GO:0004497; F:monooxygenase activity; ISO:MGI.
DR GO; GO:0016491; F:oxidoreductase 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; ISO:MGI.
DR GO; GO:0019369; P:arachidonic acid metabolic process; IDA:UniProtKB.
DR GO; GO:0019373; P:epoxygenase P450 pathway; IBA:GO_Central.
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; 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 Acetylation; Endoplasmic reticulum; Heme; Iron; Lipid metabolism; Membrane;
KW Metal-binding; Microsome; Monooxygenase; Oxidoreductase; Phosphoprotein;
KW Reference proteome; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..490
FT /note="Cytochrome P450 2C37"
FT /evidence="ECO:0000255"
FT /id="PRO_0000051720"
FT BINDING 435
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"
FT MOD_RES 127
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P00176"
FT MOD_RES 249
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q64458"
FT MOD_RES 375
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q64458"
FT CONFLICT 239
FT /note="S -> C (in Ref. 1; AAD13719 and 3; AAH57912)"
FT /evidence="ECO:0000305"
FT CONFLICT 310
FT /note="I -> L (in Ref. 1; AAD13719 and 3; AAH57912)"
FT /evidence="ECO:0000305"
FT CONFLICT 325
FT /note="E -> K (in Ref. 1; AAD13719 and 3; AAH57912)"
FT /evidence="ECO:0000305"
FT CONFLICT 372
FT /note="S -> C (in Ref. 1; AAD13719 and 3; AAH57912)"
FT /evidence="ECO:0000305"
FT CONFLICT 406
FT /note="K -> V (in Ref. 1; AAD13719 and 3; AAH57912)"
FT /evidence="ECO:0000305"
FT CONFLICT 415
FT /note="E -> G (in Ref. 1; AAD13719 and 3; AAH57912)"
FT /evidence="ECO:0000305"
FT CONFLICT 426
FT /note="I -> M (in Ref. 1; AAD13719 and 3; AAH57912)"
FT /evidence="ECO:0000305"
FT CONFLICT 455
FT /note="N -> S (in Ref. 1; AAD13719 and 3; AAH57912)"
FT /evidence="ECO:0000305"
FT CONFLICT 477
FT /note="A -> G (in Ref. 1; AAD13719 and 3; AAH57912)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 490 AA; 55606 MW; 9623AACA4B5E5DBD CRC64;
MDPILVLVLT LSCLFLLSLW RQSSERGKLP PGPTPLPIIG NILQIDVKDI CQSFTNLSKV
YGPVYTLYLG RKPTVVLHGY EAVKEALVDH GEEFAGRGRF PVFDKATNGM GLAFSKGNVW
KNTRRFSLMT LRNLGMGKRS IEDRVQEEAR CLVEELRKTN GSPCDPTFIL GCAPCNVICS
IIFQDRFDYK DRDFLNLMEK LNEITKILSS PWLQICNTYP ALLDYCPGSH KQFFKNYASI
KNFLLEKIKE HEESLDVTIP RDFIDYFLIN GGQEDGNQPL QNRLEHLAIT VTDLFSAGTE
TTSTTLRYAI LLLLKYPHVT AKVQEEIEHV IGKHRSPCMQ DRSRMPYTDA MIHEVQRFID
LIPNSLPHEV TSDIKFRNYF IPKGTTVITS LSSVLHDSTE FPNPEKFDPG HFLDENGKFK
KSDYFIPFST GKRICAGEGL ARMELFLFLT SILQNFNLKP LVHPKDIDVT PMLIGLASVP
PAFQLCFIPS
