ID   CP2DH_MACFA             Reviewed;         497 AA.
AC   Q29488;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   24-JAN-2024, entry version 105.
DE   RecName: Full=Cytochrome P450 2D17;
DE            EC=1.14.14.1;
DE   AltName: Full=CYPIID17;
GN   Name=CYP2D17;
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Liver;
RA   Lawton M.P., Laddison K.J., Speirs A.A., Mankowski D.C., Tweedie D.J.;
RL   Submitted (OCT-1995) to the EMBL/GenBank/DDBJ databases.
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   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; U38218; AAA79722.1; -; mRNA.
DR   PIR; G02938; G02938.
DR   AlphaFoldDB; Q29488; -.
DR   SMR; Q29488; -.
DR   STRING; 9541.ENSMFAP00000021296; -.
DR   eggNOG; KOG0156; Eukaryota.
DR   Proteomes; UP000233100; Unplaced.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0070330; F:aromatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; 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   2: Evidence at transcript level;
KW   Endoplasmic reticulum; Heme; Iron; Membrane; Metal-binding; Microsome;
KW   Monooxygenase; Oxidoreductase; Reference proteome.
FT   CHAIN           1..497
FT                   /note="Cytochrome P450 2D17"
FT                   /id="PRO_0000051741"
FT   BINDING         443
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"
SQ   SEQUENCE   497 AA;  56011 MW;  3594AA88F04E58B1 CRC64;
     MELDALVPLA VTVAIFLLLV DLMHRRQRWA ARYPPGPLPL PGLGNLLHVD FKNTPYCFDQ
     LRRRFGNVFS LQLAWTPVVV LNGLAAVREA LVTCGEDTAD RPPVPINQVL GFGPRSQGVF
     LARYGPAWRE QRRFSVSTLR NLGLGKKSLE QWVTEEAACL CAAFTDQAGR PFRPNSLLDK
     AVSNVIASLT YGRRFEYDDP RFLRLFDLTH EALKEESGFL REVLNAIPLL LRIPGLAGKV
     LRSQKAFLTQ LDELLTEHRM TWDPAQPPRD LTEAFLAEME KAKGNPESSF NEENLRMVVA
     DLFSAGMVTT STTLAWGLLL MILHPDVQRR VQQEIDDVIG QVRRPEMGDQ ARMPYTTAVI
     HEVQRFGDIV PLGVTHMTSR DIELQGFLIP KGTTLFTNLS SVLKDEAVWE KPFRFHPEHF
     LDAQGHFVKP EAFLPFSAGR RACLGEPLAR MELFLFFTCL LQRFSFSVPA GQPRPSHHGV
     FAFLVTPSPY ELCAVPR
//