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   16-JUN-2009, entry version 45.
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; Euteleostei; Neoteleostei;
OC   Acanthomorpha; Acanthopterygii; Percomorpha; Atherinomorpha;
OC   Cyprinodontiformes; Fundulidae; Fundulus.
OX   NCBI_TaxID=8078;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX   MEDLINE=22725987; 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
RT   adult killifish (Fundulus heteroclitus).";
RL   Aquat. Toxicol. 64:277-291(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 312-435.
RC   TISSUE=Liver;
RX   MEDLINE=97382427; 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
RT   marine teleost Fundulus heteroclitus and phylogenetic analyses of
RT   CYP3A genes.";
RL   Biochem. Biophys. Res. Commun. 236:306-312(1997).
CC   -!- FUNCTION: Putative steroid 6-beta-hydroxylase.
CC   -!- CATALYTIC ACTIVITY: RH + reduced flavoprotein + O(2) = ROH +
CC       oxidized flavoprotein + H(2)O.
CC   -!- COFACTOR: Heme group (By similarity).
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral
CC       membrane protein (Potential). Microsome membrane; Peripheral
CC       membrane protein (Potential).
CC   -!- TISSUE SPECIFICITY: Highly expressed in liver and intestine.
CC       Moderate expression in gill and spleen. Low expression in kidney,
CC       brain and heart.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family.
CC   -!- CAUTION: Due to a recent gene duplication event, CYP3A30 and
CC       CYP3A56 are very similar. Because of this it was not possible to
CC       distinguish between the two genes when measuring the tissue
CC       expression.
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DR   EMBL; AY143428; AAN38837.1; -; mRNA.
DR   HSSP; P14779; 1JPZ.
DR   HOVERGEN; Q8AXY5; -.
DR   BRENDA; 1.14.14.1; 39477.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005792; C:microsome; IEA:UniProtKB-SubCell.
DR   GO; GO:0070330; F:aromatase activity; IEA:EC.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR001128; Cyt_P450.
DR   InterPro; IPR017973; Cyt_P450_C.
DR   InterPro; IPR017972; Cyt_P450_CS.
DR   InterPro; IPR008072; Cyt_P450_E_CYP3A.
DR   InterPro; IPR002402; Cyt_P450_E_grp-II.
DR   Gene3D; G3DSA:1.10.630.10; Cyt_P450; 1.
DR   PANTHER; PTHR19383; Cyt_P450; 1.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00464; EP450II.
DR   PRINTS; PR01689; EP450IICYP3A.
DR   PRINTS; PR00385; P450.
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       Cytochrome P450 3A56.
FT                                /FTId=PRO_0000051810.
FT   METAL       441    441       Iron (heme axial ligand) (By similarity).
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
//