CP4B1_RAT
ID CP4B1_RAT Reviewed; 511 AA.
AC P15129;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Cytochrome P450 4B1;
DE EC=1.14.14.1;
DE AltName: Full=CYPIVB1;
DE AltName: Full=Cytochrome P450 L-2;
DE AltName: Full=Cytochrome P450 isozyme 5;
GN Name=Cyp4b1; Synonyms=Cyp4b-1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2725471;
RA Gasser R., Philpot R.M.;
RT "Primary structures of cytochrome P-450 isozyme 5 from rabbit and rat and
RT regulation of species-dependent expression and induction in lung and liver:
RT identification of cytochrome P-450 gene subfamily IVB.";
RL Mol. Pharmacol. 35:617-625(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP PROTEIN SEQUENCE OF 2-11.
RC TISSUE=Lung;
RX PubMed=2229008; DOI=10.1093/oxfordjournals.jbchem.a123157;
RA Imaoka S., Funae Y.;
RT "Purification and characterization of rat pulmonary cytochrome P-450.";
RL J. Biochem. 108:33-36(1990).
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;
CC Evidence={ECO:0000250|UniProtKB:P51869};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral
CC membrane protein. Microsome membrane; Peripheral membrane protein.
CC -!- INDUCTION: P450 can be induced to high levels in liver and other
CC tissues by various foreign compounds, including drugs, pesticides, and
CC carcinogens.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; M29853; AAA41778.1; -; mRNA.
DR EMBL; BC074012; AAH74012.1; -; mRNA.
DR PIR; B40164; B40164.
DR RefSeq; NP_058695.2; NM_016999.2.
DR AlphaFoldDB; P15129; -.
DR SMR; P15129; -.
DR STRING; 10116.ENSRNOP00000013321; -.
DR iPTMnet; P15129; -.
DR PhosphoSitePlus; P15129; -.
DR PaxDb; P15129; -.
DR PRIDE; P15129; -.
DR Ensembl; ENSRNOT00000013321; ENSRNOP00000013321; ENSRNOG00000055078.
DR GeneID; 24307; -.
DR KEGG; rno:24307; -.
DR UCSC; RGD:2480; rat.
DR CTD; 1580; -.
DR RGD; 2480; Cyp4b1.
DR eggNOG; KOG0157; Eukaryota.
DR GeneTree; ENSGT00940000161441; -.
DR HOGENOM; CLU_001570_5_1_1; -.
DR InParanoid; P15129; -.
DR OMA; LFGHAQE; -.
DR OrthoDB; 1247045at2759; -.
DR PhylomeDB; P15129; -.
DR Reactome; R-RNO-211935; Fatty acids.
DR Reactome; R-RNO-211958; Miscellaneous substrates.
DR Reactome; R-RNO-211979; Eicosanoids.
DR Reactome; R-RNO-2142691; Synthesis of Leukotrienes (LT) and Eoxins (EX).
DR PRO; PR:P15129; -.
DR Proteomes; UP000002494; Chromosome 5.
DR Bgee; ENSRNOG00000055078; Expressed in lung and 18 other tissues.
DR Genevisible; P15129; RN.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:RGD.
DR GO; GO:0070330; F:aromatase activity; IEA:UniProtKB-EC.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:1901363; F:heterocyclic compound binding; IPI:RGD.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0004497; F:monooxygenase activity; TAS:RGD.
DR GO; GO:0018879; P:biphenyl metabolic process; IDA:RGD.
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; IPR036396; Cyt_P450_sf.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00463; EP450I.
DR PRINTS; PR00385; P450.
DR SUPFAM; SSF48264; SSF48264; 1.
DR PROSITE; PS00086; CYTOCHROME_P450; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Endoplasmic reticulum; Heme; Iron; Membrane;
KW Metal-binding; Microsome; Monooxygenase; Oxidoreductase;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:2229008"
FT CHAIN 2..511
FT /note="Cytochrome P450 4B1"
FT /id="PRO_0000051822"
FT BINDING 315
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:P51869"
FT BINDING 453
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|UniProtKB:P51869"
SQ SEQUENCE 511 AA; 58936 MW; CEAAFB5BE2ED9944 CRC64;
MVLNFLSPSL SRLGLWASVV ILMVIVLKLF SLLLRRQKLA RAMDSFPGPP THWLFGHALE
IQKLGSLDKV VSWAQQFPHA HPLWFGQFVG FLNIYEPDYA KAVYSRGDPK AADVYDFFLQ
WIGKGLLVLD GPKWFQHRKL LTPGFHYDVL KPYVAIFAES TRMMLDKWEK KASENKSFDI
FCDVGHMALD TLMKCTFGKG DSGLGHRDNS YYLAVSDLTL LMQQRIDSFQ YHNDFIYWLT
PHGRRFLRAC KIAHDHTDEV IRQRKAALQD EKERKKIQQR RHLDFLDILL GVRDESGIKL
SDAELRAEVD TFMFEGHDTT TSGISWFLYC MALYPEHQQL CREEVRGILG DQDSFQWDDL
AKMTYLTMCM KECFRLYPPV PQVYRQLNKP VTFVDGRSLP AGSLISLHIY ALHRNSTVWP
DPEVFDPLRF SPENAAGRHP FAFMPFSAGP RNCIGQQFAM NEMKVVTALC LLRFEFSLDP
SKMPIKVPQL ILRSKNGIHL YLKPLASRSG K
