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CP4B1_MOUSE
ID   CP4B1_MOUSE             Reviewed;         511 AA.
AC   Q64462;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 170.
DE   RecName: Full=Cytochrome P450 4B1;
DE            EC=1.14.14.1;
DE   AltName: Full=CYPIVB1;
GN   Name=Cyp4b1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC   STRAIN=BALB/cJ; TISSUE=Kidney;
RX   PubMed=7639529; DOI=10.1006/abbi.1995.1393;
RA   Imaoka S., Hiroi T., Tamura Y., Yamazaki H., Shimada T., Komori M.,
RA   Degawa M., Funae Y.;
RT   "Mutagenic activation of 3-methoxy-4-aminoazobenzene by mouse renal
RT   cytochrome P450 CYP4B1: cloning and characterization of mouse CYP4B1.";
RL   Arch. Biochem. Biophys. 321:255-262(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brown adipose tissue, Heart, Kidney, and Lung;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: Responsible for mutagenic activation of 3-methoxy-4-
CC       aminoazobenzene (3-MeO-AAB); a potent procarcinogen. Also active on 2-
CC       aminofluorene and 2-aminoanthracene.
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   -!- TISSUE SPECIFICITY: Present abundantly in renal microsomes of male mice
CC       but not in those of female mice. Also present in pulmonary microsomes
CC       of male and female mice. Not found in liver.
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; D50834; BAA09446.1; -; mRNA.
DR   EMBL; BC008996; AAH08996.1; -; mRNA.
DR   CCDS; CCDS18493.1; -.
DR   PIR; S66472; S66472.
DR   RefSeq; NP_031849.1; NM_007823.2.
DR   AlphaFoldDB; Q64462; -.
DR   SMR; Q64462; -.
DR   BioGRID; 199036; 24.
DR   STRING; 10090.ENSMUSP00000099768; -.
DR   iPTMnet; Q64462; -.
DR   PhosphoSitePlus; Q64462; -.
DR   jPOST; Q64462; -.
DR   MaxQB; Q64462; -.
DR   PaxDb; Q64462; -.
DR   PRIDE; Q64462; -.
DR   ProteomicsDB; 284153; -.
DR   Antibodypedia; 981; 166 antibodies from 29 providers.
DR   DNASU; 13120; -.
DR   Ensembl; ENSMUST00000102707; ENSMUSP00000099768; ENSMUSG00000028713.
DR   GeneID; 13120; -.
DR   KEGG; mmu:13120; -.
DR   UCSC; uc008ufc.1; mouse.
DR   CTD; 1580; -.
DR   MGI; MGI:103225; Cyp4b1.
DR   VEuPathDB; HostDB:ENSMUSG00000028713; -.
DR   eggNOG; KOG0157; Eukaryota.
DR   GeneTree; ENSGT00940000161441; -.
DR   InParanoid; Q64462; -.
DR   OMA; LFGHAQE; -.
DR   OrthoDB; 1247045at2759; -.
DR   PhylomeDB; Q64462; -.
DR   TreeFam; TF105088; -.
DR   Reactome; R-MMU-211935; Fatty acids.
DR   Reactome; R-MMU-211958; Miscellaneous substrates.
DR   Reactome; R-MMU-211979; Eicosanoids.
DR   Reactome; R-MMU-2142691; Synthesis of Leukotrienes (LT) and Eoxins (EX).
DR   BioGRID-ORCS; 13120; 2 hits in 73 CRISPR screens.
DR   ChiTaRS; Cyp4b1; mouse.
DR   PRO; PR:Q64462; -.
DR   Proteomes; UP000000589; Chromosome 4.
DR   RNAct; Q64462; protein.
DR   Bgee; ENSMUSG00000028713; Expressed in right kidney and 125 other tissues.
DR   ExpressionAtlas; Q64462; baseline and differential.
DR   Genevisible; Q64462; MM.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
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; ISO:MGI.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0018879; P:biphenyl metabolic process; ISO:MGI.
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   CHAIN           1..511
FT                   /note="Cytochrome P450 4B1"
FT                   /id="PRO_0000051820"
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;  58900 MW;  35463ACDFFE6328B CRC64;
     MALSFLSPSL SRLGLWASVV ILMVTVLKLL SLLFRRQKLA RALDSFPGPP KHWLFGHALE
     IQKTGGLDKV VTWTEQFPYA HPLWLGQFIV FLNIYEPDYA KAVYSRGDPK AAYVYDFFLQ
     WIGKGLLVLE GPKWFQHRKL LTPGFHYDVL KPYVAIFAES TRVMLDKWEK KASENKSFDI
     FCDVGHMALD TLMKCTFGKG DSGLSHSDNS YYLAVSDLTL LMQQRIDSFQ YHNDFIYWLT
     PHGRRFLRAC QIAHDHTDHV IRQRKAALQD EKEQKKLQER RHLDFLDILL GARDESGIKL
     SDADLRAEVD TFMFEGHDTT TSGISWFLYC MALYPMHQQR CREEVREILG DRDSFQWDDL
     AQMTYLTMCM KECFRLYPPV PQVYRQLSKP VTFVDGRSLP AGSLISLHIY ALHRNSAVWP
     DPEVFDPLRF SPENMTGRHP FAFMPFSAGP RNCIGQQFAM NEMKVVTALC LLRFEFSPDP
     SKIPIKVPQL ILRSKNGIHL YLKPLGPGSG K
 
 
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