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 24-JAN-2024, entry version 127. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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.ENSOCUP00000036428; -. DR PaxDb; 9986-ENSOCUP00000009637; -. DR GeneID; 100008805; -. DR KEGG; ocu:100008805; -. DR CTD; 1580; -. DR eggNOG; KOG0157; Eukaryota. DR InParanoid; P15128; -. DR OrthoDB; 1611592at2759; -. 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 CDD; cd20678; CYP4B-like; 1. DR Gene3D; 1.10.630.10; Cytochrome P450; 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 PANTHER; PTHR24291:SF149; CYTOCHROME P450 4B1; 1. DR PANTHER; PTHR24291; CYTOCHROME P450 FAMILY 4; 1. DR Pfam; PF00067; p450; 1. DR PRINTS; PR00463; EP450I. DR PRINTS; PR00385; P450. DR SUPFAM; SSF48264; Cytochrome P450; 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 //