C330_FUNHE
ID C330_FUNHE Reviewed; 496 AA.
AC Q9PVE8;
DT 27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2003, sequence version 2.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Cytochrome P450 3A30;
DE EC=1.14.14.1;
DE AltName: Full=CYPIIIA30;
GN Name=cyp3a30;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Intestine, and Liver;
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; AF105068; AAF14117.2; -; mRNA.
DR PIR; A58612; A58612.
DR AlphaFoldDB; Q9PVE8; -.
DR SMR; Q9PVE8; -.
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 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..496
FT /note="Cytochrome P450 3A30"
FT /id="PRO_0000051809"
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; 57045 MW; C19FF4CE75AB37D4 CRC64;
MGYFYLTAET WTLLVAFVTL LLVYAYWPYG TFKRLGISGP KPVPFFGTML HYRRGFFTFD
EECKKKYGKV WGIYDGRQPV LCVTDPEIIK AVLVKECLSF FTNRRNFRLN GPLYDAVSIA
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 EINGVVIPKD MVVMIPTWPL HRDPEIWPEP EAFKPERFSK
KNKDNIDPYI YMPFGSGPRN CIGMRFALVL IKLAVVEILQ QYSFSVCKET EVPFEMDIQG
LLAPKRPIQL KLVPRS