ID Q2XND2_HUMAN Unreviewed; 497 AA.
AC Q2XND2;
DT 20-DEC-2005, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2005, sequence version 1.
DT 08-NOV-2023, entry version 90.
DE RecName: Full=Cytochrome P450 {ECO:0000256|RuleBase:RU368047};
DE EC=1.14.14.- {ECO:0000256|RuleBase:RU368047};
GN Name=CYP2D6 {ECO:0000313|EMBL:ABB77907.1};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606 {ECO:0000313|EMBL:ABB77907.1};
RN [1] {ECO:0000313|EMBL:ABB77907.1}
RP NUCLEOTIDE SEQUENCE.
RA Koch W.H., Nikoloff D.M., Lu W., Pan R.M., deLeon J., Wedlund P.J.;
RT "CYP2D6 Evolution and Allele Diversity Among Human Races.";
RL Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ADR66993.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=21833166;
RA Gaedigk A., Jaime L.K., Bertino J.S.Jr., Berard A., Pratt V.M.,
RA Bradfordand L.D., Leeder J.S.;
RT "Identification of Novel CYP2D7-2D6 Hybrids: Non-Functional and Functional
RT Variants.";
RL Front. Pharmacol. 1:121-121(2010).
RN [3] {ECO:0000313|EMBL:ADF36329.1}
RP NUCLEOTIDE SEQUENCE.
RA Fuselli S., de Filippo C., Mona S., Sistonen J., Fariselli P.,
RA Destro-Bisol G., Barbujani G., Bertorelle G., Sajantila A.;
RT "Evolution of Detoxifying Systems: The Role of Environment and Population
RT History in Shaping Genetic Diversity at Human CYP2D6 Locus.";
RL Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EMBL:ANW61983.1}
RP NUCLEOTIDE SEQUENCE.
RA Simona D., Francesca M., Mauro M., Serafina M., Maria B.;
RT "Evaluation of CYP2D6, CYP2C9 and CYP2C19 polymorphisms in patients with
RT Self-reported Chemical Sensitivity from Southern Italy.";
RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
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:0000256|RuleBase:RU368047}.
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000256|ARBA:ARBA00001971,
CC ECO:0000256|RuleBase:RU368047};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|RuleBase:RU368047}. Microsome membrane
CC {ECO:0000256|RuleBase:RU368047}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family.
CC {ECO:0000256|ARBA:ARBA00010617, ECO:0000256|RuleBase:RU000461}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; DQ282159; ABB77907.1; -; Genomic_DNA.
DR EMBL; GU587100; ADF36329.1; -; Genomic_DNA.
DR EMBL; GU587124; ADF36352.1; -; Genomic_DNA.
DR EMBL; GU587130; ADF36357.1; -; Genomic_DNA.
DR EMBL; GU587134; ADF36361.1; -; Genomic_DNA.
DR EMBL; GU587142; ADF36368.1; -; Genomic_DNA.
DR EMBL; GU587146; ADF36372.1; -; Genomic_DNA.
DR EMBL; GU587189; ADF36415.1; -; Genomic_DNA.
DR EMBL; GU587228; ADF36454.1; -; Genomic_DNA.
DR EMBL; GU587235; ADF36461.1; -; Genomic_DNA.
DR EMBL; HM641838; ADR66993.1; -; Genomic_DNA.
DR EMBL; KU531565; ANW61983.1; -; Genomic_DNA.
DR AlphaFoldDB; Q2XND2; -.
DR SMR; Q2XND2; -.
DR PeptideAtlas; Q2XND2; -.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0020037; F:heme binding; IEA:UniProtKB-UniRule.
DR GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule.
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; IEA:InterPro.
DR CDD; cd20663; CYP2D; 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; IPR008069; Cyt_P450_E_grp-I_CYP2D-like.
DR InterPro; IPR036396; Cyt_P450_sf.
DR PANTHER; PTHR24300:SF1; CYTOCHROME P450 2D6-RELATED; 1.
DR PANTHER; PTHR24300; CYTOCHROME P450 508A4-RELATED; 1.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00463; EP450I.
DR PRINTS; PR01686; EP450ICYP2D.
DR PRINTS; PR00385; P450.
DR SUPFAM; SSF48264; Cytochrome P450; 1.
DR PROSITE; PS00086; CYTOCHROME_P450; 1.
PE 3: Inferred from homology;
KW Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|RuleBase:RU000461};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU000461};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU000461};
KW Monooxygenase {ECO:0000256|RuleBase:RU000461};
KW Oxidoreductase {ECO:0000256|RuleBase:RU000461};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..23
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 497 AA; 55762 MW; CF5270FDFF9710F5 CRC64;
MGLEALVPLA MIVAIFLLLV DLMHRRQRWA ARYPPGPLPL PGLGNLLHVD FQNTPYCFDQ
LRRRFGDVFS LQLAWTPVVV LNGLAAVREA LVTHGEDTAD RPPVPITQIL GFGPRSQGVF
LARYGPAWRE QRRFSVSTLR NLGLGKKSLE QWVTEEAACL CAAFANHSGR PFRPNGLLDK
AVSNVIASLT CGRRFEYDDP RFLRLLDLAQ EGLKEESGFL REVLNAVPVL LHIPALAGKV
LRFQKAFLTQ LDELLTEHRM TWDPAQPPRD LTEAFLAEME KAKGNPESSF NDENLCIVVA
DLFSAGMVTT STTLAWGLLL MILHPDVQRR VQQEIDDVIG QVRRPEMGDQ AHMPYTTAVI
HEVQRFGDIV PLGVTHMTSR DIEVQGFRIP KGTTLITNLS SVLKDEAVWE KPFRFHPEHF
LDAQGHFVKP EAFLPFSAGR RACLGEPLAR MELFLFFTSL LQHFSFSVPT GQPRPSHHGV
FAFLVTPSPY ELCAVPR
//
