CP4F5_RAT
ID CP4F5_RAT Reviewed; 526 AA.
AC P51870;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Cytochrome P450 4F5;
DE EC=1.14.14.1;
DE AltName: Full=CYPIVF5;
GN Name=Cyp4f5;
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].
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RX PubMed=8554568; DOI=10.1006/bbrc.1995.2887;
RA Kawashima H., Strobel H.W.;
RT "cDNA cloning of three new forms of rat brain cytochrome P450 belonging to
RT the CYP4F subfamily.";
RL Biochem. Biophys. Res. Commun. 217:1137-1144(1995).
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: High expression in liver and kidney. Lower
CC expression in brain.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; U39207; AAC52359.1; -; mRNA.
DR PIR; JC4533; JC4533.
DR RefSeq; NP_775147.1; NM_173124.1.
DR AlphaFoldDB; P51870; -.
DR SMR; P51870; -.
DR IntAct; P51870; 1.
DR STRING; 10116.ENSRNOP00000007428; -.
DR ChEMBL; CHEMBL3509598; -.
DR PhosphoSitePlus; P51870; -.
DR PaxDb; P51870; -.
DR GeneID; 286905; -.
DR KEGG; rno:286905; -.
DR UCSC; RGD:708364; rat.
DR CTD; 286905; -.
DR RGD; 708364; Cyp4f5.
DR eggNOG; KOG0157; Eukaryota.
DR InParanoid; P51870; -.
DR OrthoDB; 825914at2759; -.
DR PhylomeDB; P51870; -.
DR PRO; PR:P51870; -.
DR Proteomes; UP000002494; 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 GO; GO:0006954; P:inflammatory response; TAS:RGD.
DR GO; GO:0006691; P:leukotriene metabolic process; IMP:RGD.
DR Gene3D; 1.10.630.10; -; 1.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR017972; Cyt_P450_CS.
DR InterPro; IPR002403; Cyt_P450_E_grp-IV.
DR InterPro; IPR036396; Cyt_P450_sf.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00465; EP450IV.
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; Reference proteome.
FT CHAIN 1..526
FT /note="Cytochrome P450 4F5"
FT /id="PRO_0000051853"
FT BINDING 470
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 526 AA; 60681 MW; 7F0F1DED4B07EEEC CRC64;
MPWLTVSGLD LGSVVTSTWH LLLLGAASWI LARILAWTYS FCENCSRLRC FPQSPKRNWF
LGHLGTIQSN EEGMRLVTEM GQTFRDIHLC WLGPVIPVLR LVDPAFVAPL LQAPALVAPK
DTTFLRFLKP WLGDGLFLSS GDKWSRHRRL LTPAFHFDIL KPYVKIFNQS VNIMHAKWKH
LCLEGSARLE MFENISLMTL DSLQKCLFGF DSNCQESPSE YISAILELSS LIIKRSQQLF
LYLDFLYYRT ADGRRFRKAC DLVHNFTDAV IRERRRLLSS QGTDEFLESK TKSKSKTLDF
IDVLLLAKDE HGKELSDEDI RAEADTFMFG GHDTTASALS WILYNLARHP EYQERCRQEV
WELLRDREPE EIEWDDLAQL PFLTMCIKES LRLHPPAIDL LRRCTQDIVL PDGRVIPKGN
ICVISIFGIH HNPSVWPDPE VFDPFRFDSE NRQKRSPLSF IPFSAGPRNC IGQTFAMNEM
KVVVALTLLR FRVLPDDKEP RRKPEIILRA EGGLWLRMEP LSTDTQ