CP3AV_MESAU
ID CP3AV_MESAU Reviewed; 501 AA.
AC O70537;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Cytochrome P450 3A31;
DE EC=1.14.14.1;
DE AltName: Full=CYPIIIA31;
DE AltName: Full=Cytochrome P450 SH3A-1;
GN Name=CYP3A31;
OS Mesocricetus auratus (Golden hamster).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Mesocricetus.
OX NCBI_TaxID=10036;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=9545515; DOI=10.1016/s0167-4781(97)00220-0;
RA Alabouch S., Kurose K., Tohkin M., Bani M.-H., Fukuhara M., Nagata K.,
RA Yamazoe Y.;
RT "cDNA cloning and expression of a novel CYP3A from the Syrian hamster,
RT CYP3A31.";
RL Biochim. Biophys. Acta 1397:9-13(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 -!- TISSUE SPECIFICITY: Expressed constitutively in liver.
CC -!- INDUCTION: Induced by phenobarbital and repressed by 3-
CC methylcholanthrene or dexamethasone.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; D86951; BAA25811.1; -; mRNA.
DR RefSeq; NP_001268529.1; NM_001281600.1.
DR AlphaFoldDB; O70537; -.
DR SMR; O70537; -.
DR STRING; 10036.XP_005080074.1; -.
DR GeneID; 101836914; -.
DR eggNOG; KOG0158; Eukaryota.
DR OrthoDB; 467733at2759; -.
DR Proteomes; UP000189706; 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 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; Reference proteome.
FT CHAIN 1..501
FT /note="Cytochrome P450 3A31"
FT /id="PRO_0000051811"
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"
SQ SEQUENCE 501 AA; 57772 MW; D6C32CEEAB056589 CRC64;
MDLTSVLSLE TWVLLAISLV LLYRLGTHKY DIFKKQGIPG PKPLPFLGNV LNYYKGIWTF
DIECHKKYGK IWGLFEGQRP LFTVTDTEMI KNVLVKECYS IFTNRRDFGP VGIMSKAVSI
SKDEEWKRIR ALLSPTFTSG KLKEMFPIIE QYGDILVKFL RREAEKGNPV TTKEVFGAYS
MDVITSTAFG VSVDSLNNPK DLLWKGRKLL RFDFFDPLFL SVVLFPFLIP IYEKLNVSMF
PKDSISFFRK FVDKTKENRL DYNQKHRVDF LQLMMNSHDN SKDSHKALSD MEIIAQSIIF
IFAGYDTTSS TLSFALYLLA THPDVQKKLQ EEIDIALPNK ARPSYDKVME MEYLDMVLNE
TLRLYPIGSR LERVCKQDVE MDGVFVPKGS IVMVPVFALH YDPQYWPEPE KFRPERFSKE
NKGSIDPYIF LPFGNGPRNC IGMRFALMNM KLALTKVLQN FSLQPCKETQ IPMKLSRKAM
LQPEKPIILK VVPRDAIITG A