CP4B1_RABIT
ID CP4B1_RABIT Reviewed; 506 AA.
AC P15128; Q9TU22;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Cytochrome P450 4B1;
DE EC=1.14.14.1;
DE AltName: Full=CYPIVB1;
DE AltName: Full=Cytochrome P450 isozyme 5;
GN Name=CYP4B1;
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=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 [MRNA].
RC TISSUE=Corneal epithelium;
RA Mastyugin V., Schwartzman M.L.;
RT "Rabbit corneal hypoxia-inducible CYP4B1-like isoform, 3'-coding and
RT noncoding regions.";
RL Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEIN SEQUENCE OF 1-21.
RX PubMed=2881760;
RA Parandoosh Z., Fujita V.S., Coon M.J., Philpot R.M.;
RT "Cytochrome P-450 isozymes 2 and 5 in rabbit lung and liver. Comparisons of
RT structure and inducibility.";
RL Drug Metab. Dispos. 15:59-67(1987).
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; M29852; AAA31214.1; -; mRNA.
DR EMBL; AF176914; AAD52658.4; -; mRNA.
DR EMBL; AF332576; AAG52885.1; -; mRNA.
DR PIR; A40164; A40164.
DR RefSeq; NP_001075572.1; NM_001082103.1.
DR PDB; 5T6Q; X-ray; 2.70 A; A=20-506.
DR PDBsum; 5T6Q; -.
DR AlphaFoldDB; P15128; -.
DR SMR; P15128; -.
DR STRING; 9986.ENSOCUP00000009637; -.
DR GeneID; 100008805; -.
DR KEGG; ocu:100008805; -.
DR CTD; 1580; -.
DR eggNOG; KOG0157; Eukaryota.
DR InParanoid; P15128; -.
DR OrthoDB; 1247045at2759; -.
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; 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 3D-structure; Direct protein sequencing; Endoplasmic reticulum; Heme; Iron;
KW Membrane; Metal-binding; Microsome; Monooxygenase; Oxidoreductase;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..506
FT /note="Cytochrome P450 4B1"
FT /id="PRO_0000051821"
FT BINDING 310
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:P51869"
FT BINDING 448
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"
FT MOD_RES 431
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P20816"
FT HELIX 21..38
FT /evidence="ECO:0007829|PDB:5T6Q"
FT TURN 48..50
FT /evidence="ECO:0007829|PDB:5T6Q"
FT HELIX 53..56
FT /evidence="ECO:0007829|PDB:5T6Q"
FT HELIX 61..71
FT /evidence="ECO:0007829|PDB:5T6Q"
FT STRAND 72..83
FT /evidence="ECO:0007829|PDB:5T6Q"
FT STRAND 85..89
FT /evidence="ECO:0007829|PDB:5T6Q"
FT HELIX 92..99
FT /evidence="ECO:0007829|PDB:5T6Q"
FT HELIX 107..110
FT /evidence="ECO:0007829|PDB:5T6Q"
FT HELIX 111..113
FT /evidence="ECO:0007829|PDB:5T6Q"
FT TURN 114..116
FT /evidence="ECO:0007829|PDB:5T6Q"
FT TURN 121..123
FT /evidence="ECO:0007829|PDB:5T6Q"
FT HELIX 127..136
FT /evidence="ECO:0007829|PDB:5T6Q"
FT HELIX 142..145
FT /evidence="ECO:0007829|PDB:5T6Q"
FT HELIX 148..167
FT /evidence="ECO:0007829|PDB:5T6Q"
FT TURN 168..170
FT /evidence="ECO:0007829|PDB:5T6Q"
FT HELIX 176..191
FT /evidence="ECO:0007829|PDB:5T6Q"
FT HELIX 202..222
FT /evidence="ECO:0007829|PDB:5T6Q"
FT HELIX 224..226
FT /evidence="ECO:0007829|PDB:5T6Q"
FT HELIX 229..232
FT /evidence="ECO:0007829|PDB:5T6Q"
FT HELIX 236..262
FT /evidence="ECO:0007829|PDB:5T6Q"
FT TURN 263..265
FT /evidence="ECO:0007829|PDB:5T6Q"
FT HELIX 267..270
FT /evidence="ECO:0007829|PDB:5T6Q"
FT HELIX 280..285
FT /evidence="ECO:0007829|PDB:5T6Q"
FT HELIX 287..289
FT /evidence="ECO:0007829|PDB:5T6Q"
FT HELIX 297..328
FT /evidence="ECO:0007829|PDB:5T6Q"
FT HELIX 330..344
FT /evidence="ECO:0007829|PDB:5T6Q"
FT HELIX 352..355
FT /evidence="ECO:0007829|PDB:5T6Q"
FT HELIX 359..371
FT /evidence="ECO:0007829|PDB:5T6Q"
FT STRAND 377..381
FT /evidence="ECO:0007829|PDB:5T6Q"
FT STRAND 399..403
FT /evidence="ECO:0007829|PDB:5T6Q"
FT HELIX 404..407
FT /evidence="ECO:0007829|PDB:5T6Q"
FT TURN 411..413
FT /evidence="ECO:0007829|PDB:5T6Q"
FT STRAND 414..416
FT /evidence="ECO:0007829|PDB:5T6Q"
FT HELIX 422..425
FT /evidence="ECO:0007829|PDB:5T6Q"
FT TURN 427..432
FT /evidence="ECO:0007829|PDB:5T6Q"
FT HELIX 444..446
FT /evidence="ECO:0007829|PDB:5T6Q"
FT HELIX 451..468
FT /evidence="ECO:0007829|PDB:5T6Q"
FT STRAND 469..472
FT /evidence="ECO:0007829|PDB:5T6Q"
FT STRAND 481..489
FT /evidence="ECO:0007829|PDB:5T6Q"
FT STRAND 494..499
FT /evidence="ECO:0007829|PDB:5T6Q"
SQ SEQUENCE 506 AA; 58604 MW; EB406EB7453A53CB CRC64;
MLGFLSRLGL WASGLILILG FLKLLRLLLR RQRLARAMDS FPGPPTHWLF GHALEIQKTG
SLDKVVTWTQ QFPYAHPLWV GQFIGFLNIY EPDYAKAVYS RGDPKAPDVY DFFLQWIGKG
LLVLDGPKWF QHRKLLTPGF HYDVLKPYVA IFADSTRIML EKWEKKACEG KSFDIFSDVG
HMALDTLMKC TFGKGDSGLN HRDSSYYVAV SELTLLMQQR IDSFQYHNDF IYWLTPHGRR
FLRACRAAHD HTDRVIRQRK AALQDEKERE KIQNRRHLDF LDILLDVRGE SGVQLSDTDL
RAEVDTFMFE GHDTTTSGIS WFLYCMALYP EHQQRCREEV REILGDQDSF QWEDLAKMTY
LTMCMKECFR LYPPVPQVYR QLSKPVSFVD GRSLPAGSLI SLHIYALHRN SDVWPDPEVF
DPLRFSPENS SGRHPYAFIP FSAGPRNCIG QQFAMNEMKV VTALCLLRFE FSVDPLRLPI
KLPQLVLRSK NGIHLYLKPL GPKAEK
