ID   CP3A6_RABIT             Reviewed;         501 AA.
AC   P11707; Q29506;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1999, sequence version 2.
DT   27-MAR-2024, entry version 138.
DE   RecName: Full=Cytochrome P450 3A6;
DE            EC=1.14.14.1;
DE   AltName: Full=CYPIIIA6;
DE   AltName: Full=Cytochrome P450-3C;
GN   Name=CYP3A6;
OS   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX   NCBI_TaxID=9986;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=3349903; DOI=10.1089/dna.1988.7.39;
RA   Dalet C., Clair P., Daujat M., Fort P., Blanchard J.-M., Maurel P.;
RT   "Complete sequence of cytochrome P450 3c cDNA and presence of two mRNA
RT   species with 3' untranslated regions of different lengths.";
RL   DNA 7:39-46(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=2777787; DOI=10.1016/s0021-9258(18)71610-4;
RA   Potenza C.L., Pendurthi U.R., Strom D.K., Tukey R.H., Griffin K.J.,
RA   Schwab G.E., Johnson E.F.;
RT   "Regulation of the rabbit cytochrome P-450 3c gene. Age-dependent
RT   expression and transcriptional activation by rifampicin.";
RL   J. Biol. Chem. 264:16222-16228(1989).
CC   -!- FUNCTION: Exhibits progesterone 6 beta-hydroxylase activity.
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: By rifampicin.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; M19139; AAA31430.1; -; mRNA.
DR   EMBL; J05034; AAA31178.1; -; mRNA.
DR   PIR; A29487; A29487.
DR   PIR; A34236; A34236.
DR   RefSeq; NP_001164739.1; NM_001171268.2.
DR   AlphaFoldDB; P11707; -.
DR   SMR; P11707; -.
DR   STRING; 9986.ENSOCUP00000034396; -.
DR   BindingDB; P11707; -.
DR   ChEMBL; CHEMBL1743541; -.
DR   PaxDb; 9986-ENSOCUP00000016348; -.
DR   GeneID; 100328954; -.
DR   KEGG; ocu:100328954; -.
DR   CTD; 100328954; -.
DR   eggNOG; KOG0158; Eukaryota.
DR   InParanoid; P11707; -.
DR   OrthoDB; 1611592at2759; -.
DR   PRO; PR:P11707; -.
DR   Proteomes; UP000001811; 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   GO; GO:0004497; F:monooxygenase activity; ISS:UniProtKB.
DR   CDD; cd20650; CYP3A; 1.
DR   Gene3D; 1.10.630.10; Cytochrome P450; 1.
DR   InterPro; IPR001128; Cyt_P450.
DR   InterPro; IPR017972; Cyt_P450_CS.
DR   InterPro; IPR008072; Cyt_P450_E_CYP3A.
DR   InterPro; IPR002402; Cyt_P450_E_grp-II.
DR   InterPro; IPR036396; Cyt_P450_sf.
DR   PANTHER; PTHR24302:SF38; CYTOCHROME P450 3A7; 1.
DR   PANTHER; PTHR24302; CYTOCHROME P450 FAMILY 3; 1.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00464; EP450II.
DR   PRINTS; PR01689; EP450IICYP3A.
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..501
FT                   /note="Cytochrome P450 3A6"
FT                   /id="PRO_0000051789"
FT   BINDING         440
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        54..55
FT                   /note="GI -> VIN (in Ref. 1; AAA31430)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        165..169
FT                   /note="GKPVD -> ASPST (in Ref. 1; AAA31430)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        393
FT                   /note="Missing (in Ref. 1; AAA31430)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        494..495
FT                   /note="RD -> ES (in Ref. 1; AAA31430)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   501 AA;  57450 MW;  251D21061863ACFB CRC64;
     MDLIFSLETW VLLAASLVLL YLYGTSTHGL FKKMGIPGPT PLPFIGTILE YRKGIWDFDI
     ECRKKYGKMW GLFDGRQPLM VITDPDMIKT VLVKECYSVF TNRRSFGPVG FMKKAVSISE
     DEDWKRVRTL LSPTFTSGKL KEMLPIIAQY GDVLVKNLRQ EAEKGKPVDL KEIFGAYSMD
     VITGTSFGVN IDSLRNPQDP FVKNVRRLLK FSFFDPLLLS ITLFPFLTPI FEALHISMFP
     KDVMDFLKTS VEKIKDDRLK DKQKRRVDFL QLMINSQNSK EIDSHKALDD IEVVAQSIII
     LFAGYETTSS TLSFIMHLLA THPDVQQKLQ EEIDTLLPNK ELATYDTLVK MEYLDMVVNE
     TLRLYPIAGR LERVCKKDVD INGTFIPKGT IVMMPTYALH RDPQHWTEPD EFRPERFSKK
     NKDNINPYIY HPFGAGPRNC LGMRFALMNI KLALVRLMQN FSFKLCKETQ VPLKLGKQGL
     LQPEKPIVLK VVSRDGIIRG A
//