CP2B5_RABIT
ID CP2B5_RABIT Reviewed; 491 AA.
AC P12789;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Cytochrome P450 2B5;
DE EC=1.14.14.1;
DE AltName: Full=CYPIIB5;
DE AltName: Full=Cytochrome P450 form HP1;
DE AltName: Full=Cytochrome P450 type B2;
GN Name=CYP2B5;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2826996;
RA Gasser R., Negishi M., Philpot R.M.;
RT "Primary structures of multiple forms of cytochrome P-450 isozyme 2 derived
RT from rabbit pulmonary and hepatic cDNAs.";
RL Mol. Pharmacol. 33:22-30(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-56.
RX PubMed=7654758; DOI=10.1016/0304-4165(95)00075-m;
RA Lehnerer M., Schulze J., Petzold A., Bernhardt R., Hlavica P.;
RT "Rabbit liver cytochrome P-450 2B5: high-level expression of the full-
RT length protein in Escherichia coli, purification, and catalytic activity.";
RL Biochim. Biophys. Acta 1245:107-115(1995).
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: By phenobarbital.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; M20855; AAA31223.1; -; mRNA.
DR EMBL; S78830; AAB35177.1; -; mRNA.
DR PIR; D27717; D27717.
DR PIR; S31278; S31278.
DR RefSeq; NP_001164601.1; NM_001171130.1.
DR AlphaFoldDB; P12789; -.
DR SMR; P12789; -.
DR PRIDE; P12789; -.
DR KEGG; ocu:100328947; -.
DR InParanoid; P12789; -.
DR Proteomes; UP000001811; 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; IPR002401; Cyt_P450_E_grp-I.
DR InterPro; IPR008068; Cyt_P450_E_grp-I_CYP2B-like.
DR InterPro; IPR036396; Cyt_P450_sf.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00463; EP450I.
DR PRINTS; PR01685; EP450ICYP2B.
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; Phosphoprotein; Reference proteome.
FT CHAIN 1..491
FT /note="Cytochrome P450 2B5"
FT /id="PRO_0000051682"
FT BINDING 436
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 MOD_RES 128
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000250|UniProtKB:P00176"
SQ SEQUENCE 491 AA; 55770 MW; ABE2B978B8408DCF CRC64;
MEFSLLLLLA FLAGLLLLLF RGHPKAHGRL PPGPPPLPVL GNLLQMDRKG LLRSFLRLRE
KYGDVFTVYL GSRPVVVLCG TDAIREALVD QAEAFSGRGK IAVVDPIFQG YGVFFANGEH
WRALRRFSLA TMRDFGMGKR SVEERIQEEA RCLVEELRKS KGALLDNTLL FHSVTSNIIC
SIVFGKRFDY KDPVFLRLLD LFFQSFSLIS SFSSQVFELF PGFLKHFPGT HRQIYRNLQE
INTFIGQTVE KHRATLDPSN PRDFIDVYLL RMEKDKSDPS SEFHHRNLIL TVLTLFFAGT
ETTSTTLRYG FLLMLKYPHV TERVQKEIEQ VIGSHRPPAL DDRAKMPYTD AVIHEIQRLG
DLVPFGAPHM VTKDTQFRGY VIPKNTEVFP VLSSALHDPR YFETPNTFNP GHFLDADGAL
KRNEGFMPFS LGKRICLGEG IARTELFLFF TTILQNFSIA SPVPPEDIDL TPRESGVGNV
PPSYQIRFLA R