ID   C356_FUNHE              Reviewed;         496 AA.
AC   Q8AXY5;
DT   22-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-MAY-2023, entry version 94.
DE   RecName: Full=Cytochrome P450 3A56;
DE            EC=1.14.14.1;
DE   AltName: Full=CYPIIIA56;
GN   Name=cyp3a56;
OS   Fundulus heteroclitus (Killifish) (Mummichog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Fundulidae; Fundulus.
OX   NCBI_TaxID=8078 {ECO:0000312|EMBL:AAN38837.1};
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX   PubMed=12842592; DOI=10.1016/s0166-445x(03)00057-2;
RA   Hegelund T., Celander M.C.;
RT   "Hepatic versus extrahepatic expression of CYP3A30 and CYP3A56 in adult
RT   killifish (Fundulus heteroclitus).";
RL   Aquat. Toxicol. 64:277-291(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 312-435.
RC   TISSUE=Liver;
RX   PubMed=9240431; DOI=10.1006/bbrc.1997.6956;
RA   Celander M.C., Stegeman J.J.;
RT   "Isolation of a cytochrome P450 3A cDNA sequence (CYP3A30) from the marine
RT   teleost Fundulus heteroclitus and phylogenetic analyses of CYP3A genes.";
RL   Biochem. Biophys. Res. Commun. 236:306-312(1997).
CC   -!- FUNCTION: Putative steroid 6-beta-hydroxylase.
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:0000305};
CC       Peripheral membrane protein {ECO:0000305}. Microsome membrane
CC       {ECO:0000305}; Peripheral membrane protein {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Highly expressed in liver and intestine. Moderate
CC       expression in gill and spleen. Low expression in kidney, brain and
CC       heart. {ECO:0000269|PubMed:12842592}.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
CC   -!- CAUTION: Due to a recent gene duplication event, CYP3A30 and CYP3A56
CC       are very similar. Because of this it was not possible to distinguish
CC       between the two genes when measuring the tissue expression.
CC       {ECO:0000305}.
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DR   EMBL; AY143428; AAN38837.1; -; mRNA.
DR   RefSeq; NP_001296866.1; NM_001309937.1.
DR   AlphaFoldDB; Q8AXY5; -.
DR   SMR; Q8AXY5; -.
DR   STRING; 8078.ENSFHEP00000011598; -.
DR   GeneID; 105940029; -.
DR   OrthoDB; 1611592at2759; -.
DR   Proteomes; UP000265000; Whole Genome Shotgun Assembly.
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; 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; CYTOCHROME P450 FAMILY 3; 1.
DR   PANTHER; PTHR24302:SF32; CYTOCHROME P450, FAMILY 3, SUBFAMILY A, POLYPEPTIDE 65; 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.
FT   CHAIN           1..496
FT                   /note="Cytochrome P450 3A56"
FT                   /id="PRO_0000051810"
FT   BINDING         441
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   496 AA;  57054 MW;  BAF945B260CA0220 CRC64;
     MGYFYLTAET WTLLVAFVTL LLIYAYWPYG TFKRLGISGP KPVPFFGTML HYRRGFFTFD
     EECKKKYGKV WGIYDGRQPV LCVTDPEIIK AVLVKECLSF FTNRRNFHLN GPLYDALSVA
     EDDQWKRIRS VLSPSFTSGR LKEMFEIMKN HSANLIRSMK KKADKDEPLD LKEFFGSYSM
     DVVTSTAFSV DIDSLNNPSD PFVTNIKKML KFDFLNPLFL AVAFFPFLGP ILEKFELSFF
     PKSVTDFFYA SLEKIKSNRE ASQQKSRVDF LQLMIDSQKN SGAQQDKSLT DHEILSQSMI
     FIFAGYETSS SSLTFLAYNL ATNPEVMKKL QEEIDATFPN KAPVHYQPLM EMEYLDCVIN
     ESLRLFPIAA RLERVAKAAV EINGIVIPKD MVVMIPTWPL HRDPEIWPEP EAFKPERFSK
     KNKDNIDPYI YMPFGSGPRN CIGMRFALVL IKLAVVEILQ QYSFSVCKET EVPFEMDIQG
     LLAPKRPIQL KLVPRS
//