ID   CP2F5_GORGO             Reviewed;         491 AA.
AC   Q8WNE1;
DT   29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 2.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=Cytochrome P450 2F5;
DE            Short=CYP4502F5;
DE            EC=1.14.14.1;
DE   AltName: Full=CYPIIF5;
GN   Name=CYP2F5;
OS   Gorilla gorilla gorilla (Western lowland gorilla).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Gorilla.
OX   NCBI_TaxID=9595;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=11827709; DOI=10.1016/s0027-5107(01)00274-3;
RA   Chen N., Whitehead S.E., Caillat A.W., Gavit K., Isphording D.R.,
RA   Kovacevic D., McCreary M.B., Hoffman S.M.G.;
RT   "Identification and cross-species comparisons of CYP2F subfamily genes in
RT   mammals.";
RL   Mutat. Res. 499:155-161(2002).
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; Evidence={ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral
CC       membrane protein. Microsome membrane; Peripheral membrane protein.
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; AF372494; AAL72278.2; -; Genomic_DNA.
DR   EMBL; AF372488; AAL72278.2; JOINED; Genomic_DNA.
DR   EMBL; AF372489; AAL72278.2; JOINED; Genomic_DNA.
DR   EMBL; AF372490; AAL72278.2; JOINED; Genomic_DNA.
DR   EMBL; AF372492; AAL72278.2; JOINED; Genomic_DNA.
DR   AlphaFoldDB; Q8WNE1; -.
DR   SMR; Q8WNE1; -.
DR   InParanoid; Q8WNE1; -.
DR   Proteomes; UP000001519; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR   GO; GO:0008392; F:arachidonic acid epoxygenase activity; IBA:GO_Central.
DR   GO; GO:0070330; F:aromatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0020037; F:heme binding; IBA:GO_Central.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0016712; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen; IBA:GO_Central.
DR   GO; GO:0019825; F:oxygen binding; IEA:InterPro.
DR   GO; GO:0008395; F:steroid hydroxylase activity; IBA:GO_Central.
DR   GO; GO:0019373; P:epoxygenase P450 pathway; IBA:GO_Central.
DR   GO; GO:0006082; P:organic acid metabolic process; IBA:GO_Central.
DR   GO; GO:0006805; P:xenobiotic metabolic process; IBA:GO_Central.
DR   Gene3D; 1.10.630.10; -; 1.
DR   InterPro; IPR001128; Cyt_P450.
DR   InterPro; IPR017972; Cyt_P450_CS.
DR   InterPro; IPR020469; Cyt_P450_CYP2_fam.
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; PR01957; EP450ICYP2F.
DR   PRINTS; PR00385; P450.
DR   SUPFAM; SSF48264; SSF48264; 1.
DR   PROSITE; PS00086; CYTOCHROME_P450; 1.
PE   3: Inferred from homology;
KW   Endoplasmic reticulum; Heme; Iron; Membrane; Metal-binding; Microsome;
KW   Monooxygenase; Oxidoreductase; Reference proteome.
FT   CHAIN           1..491
FT                   /note="Cytochrome P450 2F5"
FT                   /id="PRO_0000051763"
FT   BINDING         436
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"
SQ   SEQUENCE   491 AA;  55702 MW;  60B220260A9FEF07 CRC64;
     MDSVSTAILL LLLALICLLL TLSSRDKGKL PPGPRPLPLL GNLLLLRSQD MLTSLTKLSK
     EYGSMYTVHL GPRRVVVLSG YQAVKEALVD QGEEFSGRRD FPAFFNFTKG NGIAFSNGDR
     WKVLRRFSIQ ILRNFGMGKR SIEERILEEG SFLLAELRKT EGEPFDPTFV LSRSVSNIIC
     SVLFGSRFDY DDERLLTIIR HINDNFQIMS SPWGELYDIF PSLLDWVPGP HQRIFQNFKC
     LRDLIAHSVH DHQASLDPRS PRDFIDCFLT KMAEENEDPL SHFHMDTLLM TTHNLLFGGT
     ETVGTTLRYA FLALMKYPKV QARVQEEIDL VVGRARLPAL KDRAAMPYTD AVIHEVQRFA
     DIIPMSLPHR VTRDTAFRGF LIPKGTDIIT LLNTVHYDPS QFLTPQEFNP EHFLDANQSF
     KKSPAFMPFS AGRRLCLGES LARMELFLYL TAILQSFSLQ PLGAPKDIDL TPLSSGLGNL
     PRPFQLCLRP R