CP2DQ_MOUSE
ID CP2DQ_MOUSE Reviewed; 500 AA.
AC Q8CIM7; Q9DBJ5;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Cytochrome P450 2D26;
DE EC=1.14.14.1;
DE AltName: Full=CYPIID26;
GN Name=Cyp2d26 {ECO:0000312|EMBL:AAH23241.1, ECO:0000312|MGI:MGI:1923529};
GN Synonyms=Cyp2d-26 {ECO:0000250|UniProtKB:P10634};
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].
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAB23666.1};
RC TISSUE=Liver {ECO:0000312|EMBL:BAB23666.1};
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 MRNA].
RC STRAIN=FVB/N {ECO:0000312|EMBL:AAH23241.1};
RC TISSUE=Kidney {ECO:0000312|EMBL:AAH23241.1};
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, and 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 {ECO:0000250|UniProtKB:P10634}.
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 {ECO:0000250};
CC Peripheral membrane protein {ECO:0000250}. Microsome membrane
CC {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
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. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000255}.
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DR EMBL; AK004915; BAB23666.1; -; mRNA.
DR EMBL; BC023241; AAH23241.1; -; mRNA.
DR CCDS; CCDS37163.1; -.
DR RefSeq; NP_083838.1; NM_029562.2.
DR AlphaFoldDB; Q8CIM7; -.
DR SMR; Q8CIM7; -.
DR IntAct; Q8CIM7; 1.
DR STRING; 10090.ENSMUSP00000006094; -.
DR iPTMnet; Q8CIM7; -.
DR PhosphoSitePlus; Q8CIM7; -.
DR SwissPalm; Q8CIM7; -.
DR jPOST; Q8CIM7; -.
DR MaxQB; Q8CIM7; -.
DR PaxDb; Q8CIM7; -.
DR PeptideAtlas; Q8CIM7; -.
DR PRIDE; Q8CIM7; -.
DR ProteomicsDB; 283442; -.
DR DNASU; 76279; -.
DR GeneID; 76279; -.
DR KEGG; mmu:76279; -.
DR UCSC; uc007wzn.1; mouse.
DR CTD; 76279; -.
DR MGI; MGI:1923529; Cyp2d26.
DR eggNOG; KOG0156; Eukaryota.
DR InParanoid; Q8CIM7; -.
DR OrthoDB; 702827at2759; -.
DR PhylomeDB; Q8CIM7; -.
DR TreeFam; TF352043; -.
DR BioGRID-ORCS; 76279; 2 hits in 71 CRISPR screens.
DR PRO; PR:Q8CIM7; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q8CIM7; protein.
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: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:0009410; P:response to xenobiotic stimulus; 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..500
FT /note="Cytochrome P450 2D26"
FT /id="PRO_0000051746"
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|UniProtKB:P10634"
FT MOD_RES 249
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10634"
FT CONFLICT 263
FT /note="L -> S (in Ref. 1; BAB23666)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 500 AA; 56976 MW; B3DDCD88DFA3F265 CRC64;
MGLLVGDDLW AVVIFTAIFL LLVDLVHRRQ RWTACYPPGP VPFPGLGNLL QVDFENIPYS
FYKLQNRYGN VFSLQMAWKP VVVVNGLKAV RELLVTYGED TSDRPLMPIY NHIGYGHKSK
GVILAPYGPE WREQRRFSVS TLRDFGLGKK SLEQWVTEEA GHLCDAFTKE AEHPFNPSPL
LSKAVSNVIA SLIYARRFEY EDPFFNRMLK TLKESLGEDT GFVGEVLNAI PMLLHIPGLP
DKAFPKLNSF IALVNKMLIE HDLTWDPAQP PRDLTDAFLA EVEKAKGNPE SSFNDKNLRI
VVIDLFMAGM VTTSTTLSWA LLLMILHPDV QRRVHQEIDE VIGHVRHPEM ADQARMPYTN
AVIHEVQRFA DIVPTNLPHM TSRDIKFQDF FIPKGTTLIP NLSSVLKDET VWEKPLRFYP
EHFLDAQGHF VKHEAFMPFS AGRRSCLGEP LARMELFLFF TCLLQRFSFS VPDGQPRPSD
YGIYTMPVTP EPYQLCAVAR
