ID   CP3AR_ONCMY             Reviewed;         518 AA.
AC   O42563;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=Cytochrome P450 3A27;
DE            EC=1.14.14.1;
DE   AltName: Full=CYPIIIA27;
GN   Name=cyp3a27;
OS   Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC   Salmonidae; Salmoninae; Oncorhynchus.
OX   NCBI_TaxID=8022;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Shasta; TISSUE=Liver;
RX   PubMed=9826429; DOI=10.1006/abbi.1998.0943;
RA   Lee S.-J., Wang-Buhler J.-L., Cok I., Yu T.S., Yang Y.H., Miranda C.L.,
RA   Lech J., Buhler D.R.;
RT   "Cloning, sequencing, and tissue expression of CYP3A27, a new member of the
RT   CYP3A subfamily from embryonic and adult rainbow trout livers.";
RL   Arch. Biochem. Biophys. 360:53-61(1998).
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; U96077; AAB82422.1; -; mRNA.
DR   AlphaFoldDB; O42563; -.
DR   SMR; O42563; -.
DR   Ensembl; ENSOMYT00000138544; ENSOMYP00000129915; ENSOMYG00000061833.
DR   GO; GO:0005737; C:cytoplasm; IDA:AgBase.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IDA:AgBase.
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:0050649; F:testosterone 6-beta-hydroxylase activity; IDA:AgBase.
DR   GO; GO:0042448; P:progesterone metabolic process; IDA:AgBase.
DR   Gene3D; 1.10.630.10; -; 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   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00464; EP450II.
DR   PRINTS; PR01689; EP450IICYP3A.
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.
FT   CHAIN           1..518
FT                   /note="Cytochrome P450 3A27"
FT                   /id="PRO_0000051806"
FT   BINDING         447
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   518 AA;  59211 MW;  9B93AA12E617D0DF CRC64;
     MMSFLPYFSA ETWTLLALLI TLIVVYGYWP YGVFTKMGIP GPKPLPYFGT MLEYKKGFTN
     FDTECFQKYG RIWGIYDGRQ PVLCIMDKSM IKTVLIKECY NIFTNRRNFH LNGELFDALS
     VAEDDTWRRI RSVLSPSFTS GRLKEMFGIM KQHSSTLLSG MKKQADKDQT IEVKEFFGPY
     SMDVVTSTAF SVDIDSLNNP SDPFVSNVKK MLKFDLFNPL FLLVALFPFT GPILEKMKFS
     FFPTAVTDFF YASLAKIKSG RDTGNSTNRV DFLQLMIDSQ KGSDTKTGEE QTKGLTDHEI
     LSQAMIFIFA GYETSSSTMS FLAYNLATNH HVMTKLQEEI DTVFPNKAPI QYEALMQMDY
     LDCVLNESLR LYPIAPRLER VAKKTVEING IVIPKDCIVL VPTWTLHRDP EIWSDPEEFK
     PERFSKENKE SIDPYTYMPF GAGPRNCIGM RFALIMIKLA MVEILQSFTF SVCDETEIPL
     EMDNQGLLMP KRPIKLRLEA RRNTPSNTTA TTLKSPTT