CP2DB_MOUSE
ID CP2DB_MOUSE Reviewed; 504 AA.
AC P24457; E9Q750;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 18-SEP-2013, sequence version 2.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Cytochrome P450 2D11;
DE EC=1.14.14.1;
DE AltName: Full=CYPIID11;
DE AltName: Full=Cytochrome P450-16-alpha;
DE AltName: Full=Cytochrome P450CC;
DE AltName: Full=Testosterone 16-alpha hydroxylase;
GN Name=Cyp2d11; Synonyms=Cyp2d-11;
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 [GENOMIC DNA].
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 [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).
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; M24264; AAA37514.1; -; Genomic_DNA.
DR EMBL; AC113593; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS49680.1; -.
DR PIR; S19169; S19169.
DR RefSeq; NP_001098001.1; NM_001104531.1.
DR AlphaFoldDB; P24457; -.
DR SMR; P24457; -.
DR STRING; 10090.ENSMUSP00000130338; -.
DR iPTMnet; P24457; -.
DR PhosphoSitePlus; P24457; -.
DR SwissPalm; P24457; -.
DR jPOST; P24457; -.
DR MaxQB; P24457; -.
DR PaxDb; P24457; -.
DR PeptideAtlas; P24457; -.
DR PRIDE; P24457; -.
DR Ensembl; ENSMUST00000170255; ENSMUSP00000130338; ENSMUSG00000068085.
DR GeneID; 545123; -.
DR KEGG; mmu:545123; -.
DR UCSC; uc009vas.1; mouse.
DR CTD; 545123; -.
DR MGI; MGI:88603; Cyp2d11.
DR VEuPathDB; HostDB:ENSMUSG00000068085; -.
DR eggNOG; KOG0156; Eukaryota.
DR GeneTree; ENSGT00940000153331; -.
DR HOGENOM; CLU_001570_22_0_1; -.
DR InParanoid; P24457; -.
DR OMA; DSIFCTR; -.
DR OrthoDB; 702827at2759; -.
DR PhylomeDB; P24457; -.
DR TreeFam; TF352043; -.
DR BioGRID-ORCS; 545123; 0 hits in 70 CRISPR screens.
DR ChiTaRS; Cyp2d11; mouse.
DR PRO; PR:P24457; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; P24457; protein.
DR Bgee; ENSMUSG00000068085; Expressed in liver and 3 other tissues.
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 2: Evidence at transcript level;
KW Endoplasmic reticulum; Heme; Iron; Membrane; Metal-binding; Microsome;
KW Monooxygenase; Oxidoreductase; Reference proteome.
FT CHAIN 1..504
FT /note="Cytochrome P450 2D11"
FT /id="PRO_0000051737"
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 /evidence="ECO:0000250"
FT CONFLICT 55
FT /note="G -> D (in Ref. 1; AAA37514)"
FT /evidence="ECO:0000305"
FT CONFLICT 77
FT /note="G -> A (in Ref. 1; AAA37514)"
FT /evidence="ECO:0000305"
FT CONFLICT 93
FT /note="V -> M (in Ref. 1; AAA37514)"
FT /evidence="ECO:0000305"
FT CONFLICT 106
FT /note="Q -> P (in Ref. 1; AAA37514)"
FT /evidence="ECO:0000305"
FT CONFLICT 132
FT /note="Q -> R (in Ref. 1; AAA37514)"
FT /evidence="ECO:0000305"
FT CONFLICT 154
FT /note="D -> E (in Ref. 1; AAA37514)"
FT /evidence="ECO:0000305"
FT CONFLICT 174
FT /note="S -> P (in Ref. 1; AAA37514)"
FT /evidence="ECO:0000305"
FT CONFLICT 179
FT /note="T -> P (in Ref. 1; AAA37514)"
FT /evidence="ECO:0000305"
FT CONFLICT 183..185
FT /note="NAV -> KST (in Ref. 1; AAA37514)"
FT /evidence="ECO:0000305"
FT CONFLICT 204
FT /note="Y -> F (in Ref. 1; AAA37514)"
FT /evidence="ECO:0000305"
FT CONFLICT 289
FT /note="P -> A (in Ref. 1; AAA37514)"
FT /evidence="ECO:0000305"
FT CONFLICT 303
FT /note="G -> L (in Ref. 1; AAA37514)"
FT /evidence="ECO:0000305"
FT CONFLICT 371..386
FT /note="DIAPLPLPRITSRDIE -> TLLHCLCHASQVVTFTQ (in Ref. 1;
FT AAA37514)"
FT /evidence="ECO:0000305"
FT CONFLICT 402
FT /note="M -> L (in Ref. 1; AAA37514)"
FT /evidence="ECO:0000305"
FT CONFLICT 408
FT /note="D -> G (in Ref. 1; AAA37514)"
FT /evidence="ECO:0000305"
FT CONFLICT 500
FT /note="R -> H (in Ref. 1; AAA37514)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 504 AA; 56988 MW; 2C432A8B5848E946 CRC64;
MELLTGAGLW SVAIFTVIFI LLVDLMHRHQ HWTSRCPPGP VPWPVLGNLL QVDLGNMPYS
LYKLQNRYGD VFSLQMGWKP MVVINGLKAM KEVLLTCGED TADRPQVPIF EYLGVKPGSQ
GVVLAPYGPE WQEQRRFSVS TLRNFGLGKK SLEDWVTKEA RHLCDAFTAQ AGQSINPNTM
LNNAVCNVIA SLIFARRFEY EDPYLIRMLK MLKECFTEIS GFIPGVLNEF PIFLRIPGLA
DMVFQGQKSF MAILDNLLTE NRTTWDPDQP PRNLTDAFLA EIEKAKGNPE SSFNDENLRM
VVGDLFTAGM VTTSTTLSWA LLLMILHPDV QRRVQQEIDA VIGQVQHPEM ADQARMPYTN
AVIHEVQRFG DIAPLPLPRI TSRDIEVQDF LVTKGSTLIP NMSSVLKDET VWEKPLRFHP
EHFLDAQGHF VKPEAFMPFS AGHRSCLGEA LARMELFLFF TCLLQRFSIS VPDGQPQPSN
YRVHAIPVAP FPYQLCAVMR EQGH
