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   27-MAR-2024, entry version 171.
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,
GN   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
CC         [NADPH--hemoprotein reductase] = 12-hydroxy-(5Z,8Z,10E,14Z)-
CC         eicosatetraenoate + H(+) + H2O + oxidized [NADPH--hemoprotein
CC         reductase]; Xref=Rhea:RHEA:51484, 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: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   SwissPalm; P56654; -.
DR   jPOST; P56654; -.
DR   MaxQB; P56654; -.
DR   PaxDb; 10090-ENSMUSP00000045362; -.
DR   PeptideAtlas; P56654; -.
DR   ProteomicsDB; 278002; -.
DR   DNASU; 13096; -.
DR   Ensembl; ENSMUST00000049178.3; ENSMUSP00000045362.3; ENSMUSG00000042248.5.
DR   GeneID; 13096; -.
DR   KEGG; mmu:13096; -.
DR   UCSC; uc008hkf.2; mouse.
DR   AGR; MGI:1306806; -.
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; GREWSAT; -.
DR   OrthoDB; 2900138at2759; -.
DR   PhylomeDB; P56654; -.
DR   TreeFam; TF352043; -.
DR   UniPathway; UPA00383; -.
DR   BioGRID-ORCS; 13096; 0 hits in 77 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 cell types or tissues.
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:0101020; F:estrogen 16-alpha-hydroxylase activity; 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:0008401; F:retinoic acid 4-hydroxylase activity; ISO:MGI.
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:0006805; P:xenobiotic metabolic process; IBA:GO_Central.
DR   CDD; cd20665; CYP2C-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; PTHR24300:SF374; CYTOCHROME P450 2C18; 1.
DR   PANTHER; PTHR24300; CYTOCHROME P450 508A4-RELATED; 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; P56654; MM.
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
//