CP2DA_MOUSE
ID CP2DA_MOUSE Reviewed; 504 AA.
AC P24456; Q64490;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 2.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Cytochrome P450 2D10;
DE EC=1.14.14.1;
DE AltName: Full=CYPIID10;
DE AltName: Full=Cytochrome P450-16-alpha;
DE AltName: Full=Cytochrome P450CB;
DE AltName: Full=Testosterone 16-alpha hydroxylase;
GN Name=Cyp2d10; Synonyms=Cyp2d-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.
RX PubMed=2914938; DOI=10.1016/s0021-9258(19)81700-3;
RA Wong G., Itakura T., Kawajiri K., Skow L., Negishi M.;
RT "Gene family of male-specific testosterone 16 alpha-hydroxylase (C-P-450(16
RT alpha)) in mice. Organization, differential regulation, and chromosome
RT localization.";
RL J. Biol. Chem. 264:2920-2927(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=129/J; TISSUE=Liver;
RX PubMed=2788458; DOI=10.1021/bi00437a039;
RA Ichikawa T., Itakura T., Negishi M.;
RT "Functional characterization of two cytochrome P-450s within the mouse,
RT male-specific steroid 16 alpha-hydroxylase gene family: expression in
RT mammalian cells and chimeric proteins.";
RL Biochemistry 28:4779-4784(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Liver, and Salivary gland;
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: Cytochromes P450 are a group of heme-thiolate monooxygenases.
CC In liver microsomes, this enzyme is involved in an NADPH-dependent
CC electron transport pathway. It oxidizes a variety of structurally
CC unrelated compounds, including steroids, fatty acids, and xenobiotics.
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 -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral
CC membrane protein. Microsome membrane; Peripheral membrane protein.
CC -!- INDUCTION: P450 can be induced to high levels in liver and other
CC tissues by various foreign compounds, including drugs, pesticides, and
CC carcinogens.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; M24263; AAA79023.1; -; Genomic_DNA.
DR EMBL; M27167; AAA39878.1; -; mRNA.
DR EMBL; BC010989; AAH10989.1; -; mRNA.
DR EMBL; BC057924; AAH57924.1; -; mRNA.
DR CCDS; CCDS27690.1; -.
DR PIR; A30247; A30247.
DR RefSeq; NP_034135.2; NM_010005.3.
DR AlphaFoldDB; P24456; -.
DR SMR; P24456; -.
DR IntAct; P24456; 4.
DR STRING; 10090.ENSMUSP00000072555; -.
DR iPTMnet; P24456; -.
DR PhosphoSitePlus; P24456; -.
DR SwissPalm; P24456; -.
DR jPOST; P24456; -.
DR MaxQB; P24456; -.
DR PaxDb; P24456; -.
DR PeptideAtlas; P24456; -.
DR PRIDE; P24456; -.
DR ProteomicsDB; 283617; -.
DR DNASU; 13101; -.
DR Ensembl; ENSMUST00000072776; ENSMUSP00000072555; ENSMUSG00000094806.
DR GeneID; 13101; -.
DR KEGG; mmu:13101; -.
DR UCSC; uc007wzf.2; mouse.
DR CTD; 13101; -.
DR MGI; MGI:88602; Cyp2d10.
DR VEuPathDB; HostDB:ENSMUSG00000094806; -.
DR eggNOG; KOG0156; Eukaryota.
DR GeneTree; ENSGT00940000153331; -.
DR HOGENOM; CLU_001570_22_0_1; -.
DR InParanoid; P24456; -.
DR OMA; DFENMAY; -.
DR OrthoDB; 702827at2759; -.
DR PhylomeDB; P24456; -.
DR TreeFam; TF352043; -.
DR BioGRID-ORCS; 13101; 2 hits in 74 CRISPR screens.
DR ChiTaRS; Cyp2d10; mouse.
DR PRO; PR:P24456; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; P24456; protein.
DR Bgee; ENSMUSG00000094806; Expressed in left lobe of liver and 65 other tissues.
DR ExpressionAtlas; P24456; baseline and differential.
DR Genevisible; P24456; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; ISO:MGI.
DR GO; GO:0062188; F:anandamide 11,12 epoxidase activity; ISO:MGI.
DR GO; GO:0062189; F:anandamide 14,15 epoxidase activity; ISO:MGI.
DR GO; GO:0062187; F:anandamide 8,9 epoxidase activity; ISO:MGI.
DR GO; GO:0070330; F:aromatase activity; IEA:UniProtKB-EC.
DR GO; GO:0020037; F:heme binding; ISO:MGI.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
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; IBA:GO_Central.
DR GO; GO:0009822; P:alkaloid catabolic process; ISO:MGI.
DR GO; GO:0009820; P:alkaloid metabolic process; ISO:MGI.
DR GO; GO:0019369; P:arachidonic acid metabolic process; IBA:GO_Central.
DR GO; GO:0009804; P:coumarin metabolic process; ISO:MGI.
DR GO; GO:0008210; P:estrogen metabolic process; ISO:MGI.
DR GO; GO:0046483; P:heterocycle metabolic process; ISO:MGI.
DR GO; GO:0033076; P:isoquinoline alkaloid metabolic process; ISO:MGI.
DR GO; GO:0016098; P:monoterpenoid metabolic process; ISO:MGI.
DR GO; GO:0051100; P:negative regulation of binding; ISO:MGI.
DR GO; GO:0090350; P:negative regulation of cellular organofluorine metabolic process; ISO:MGI.
DR GO; GO:0006082; P:organic acid metabolic process; IBA:GO_Central.
DR GO; GO:0070989; P:oxidative demethylation; ISO:MGI.
DR GO; GO:0042572; P:retinol metabolic process; ISO:MGI.
DR GO; GO:0008202; P:steroid metabolic process; ISO:MGI.
DR GO; GO:0042178; P:xenobiotic catabolic process; ISO:MGI.
DR GO; GO:0006805; P:xenobiotic 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; IPR008069; Cyt_P450_E_grp-I_CYP2D-like.
DR InterPro; IPR036396; Cyt_P450_sf.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00463; EP450I.
DR PRINTS; PR01686; EP450ICYP2D.
DR PRINTS; PR00385; P450.
DR SUPFAM; SSF48264; SSF48264; 1.
DR PROSITE; PS00086; CYTOCHROME_P450; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Heme; Iron; Membrane; Metal-binding; Microsome;
KW Monooxygenase; Oxidoreductase; Phosphoprotein; Reference proteome.
FT CHAIN 1..504
FT /note="Cytochrome P450 2D10"
FT /id="PRO_0000051735"
FT BINDING 446
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 MOD_RES 249
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10634"
FT CONFLICT 46
FT /note="L -> Q (in Ref. 2; AAA39878)"
FT /evidence="ECO:0000305"
FT CONFLICT 221..224
FT /note="GLIP -> LAYS (in Ref. 1; AAA79023)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 504 AA; 57233 MW; 41375F9834489401 CRC64;
MELLTGAGLW SVAIFTVIFI LLVDLMHRHQ RWTSRYPPGP VPWPVLGNLL QVDLDNMPYS
LYKLQNRYGD VFSLQMGWKP MVVINGLKAM KEVLLTCGED TADRPQVPIF EYLGVKPGSQ
GVVLAPYGPE WREQRRFSVS TLRNFGLGKK SLEDWVTKEA RHLCDAFTAQ AGQPINPNTM
LNNAVCNVIA SLIFARRFEY EDPYLIRMQK VLEDSLTEIS GLIPEVLNMF PILLRIPGLP
GKVFQGQKSL LAIVENLLTE NRNTWDPDQP PRNLTDAFLA EIEKVKGNAE SSFNDENLRM
VVLDLFTAGM VTTSTTLSWA LLLMILHPDV QRRVQQEIDA VIGQVRHPEM ADQARMPYTN
AVIHEVQRFG DIAPLNLPRI TSRDIEVQDF LIPKGSILIP NMSSVLKDET VWEKPLRFHP
EHFLDAQGHF VKPEAFMPFS AGRRSCLGEP LARMELFLFF TCLLQHFSFS VPNGQPRPRN
LGVFPFPVAP YPYQLCAVMR EQGH