ID   CP2G1_RABIT             Reviewed;         494 AA.
AC   P24461;
DT   01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-1992, sequence version 1.
DT   03-AUG-2022, entry version 133.
DE   RecName: Full=Cytochrome P450 2G1;
DE            EC=1.14.14.1;
DE   AltName: Full=CYPIIG1;
DE   AltName: Full=Cytochrome P450 olfactive;
DE   AltName: Full=Cytochrome P450-NMB;
GN   Name=CYP2G1;
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.
RX   PubMed=1703755; DOI=10.1016/0003-9861(91)90337-i;
RA   Ding X., Porter T.D., Peng H.-M., Coon M.J.;
RT   "cDNA and derived amino acid sequence of rabbit nasal cytochrome P450NMb
RT   (P450IIG1), a unique isozyme possibly involved in olfaction.";
RL   Arch. Biochem. Biophys. 285:120-125(1991).
RN   [2]
RP   PROTEIN SEQUENCE OF 1-50.
RX   PubMed=3242590; DOI=10.1021/bi00422a007;
RA   Ding X.X., Coon M.J.;
RT   "Purification and characterization of two unique forms of cytochrome P-450
RT   from rabbit nasal microsomes.";
RL   Biochemistry 27:8330-8337(1988).
CC   -!- FUNCTION: Cytochromes P450 are a group of heme-thiolate monooxygenases.
CC       This isozyme seems to be implicated in olfaction.
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   -!- TISSUE SPECIFICITY: Olfactory epithelium.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   PIR; S13907; B31944.
DR   RefSeq; NP_001182693.1; NM_001195764.1.
DR   AlphaFoldDB; P24461; -.
DR   SMR; P24461; -.
DR   STRING; 9986.ENSOCUP00000004975; -.
DR   Ensembl; ENSOCUT00000005743; ENSOCUP00000004975; ENSOCUG00000005745.
DR   GeneID; 100359338; -.
DR   KEGG; ocu:100359338; -.
DR   CTD; 13108; -.
DR   eggNOG; KOG0156; Eukaryota.
DR   GeneTree; ENSGT00940000161670; -.
DR   HOGENOM; CLU_001570_22_3_1; -.
DR   InParanoid; P24461; -.
DR   OMA; WPVDIFP; -.
DR   OrthoDB; 702827at2759; -.
DR   TreeFam; TF352043; -.
DR   Proteomes; UP000001811; Unplaced.
DR   Bgee; ENSOCUG00000005745; Expressed in upper lobe of left lung and 4 other tissues.
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:0050896; P:response to stimulus; IEA:UniProtKB-KW.
DR   GO; GO:0007608; P:sensory perception of smell; IEA:UniProtKB-KW.
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; IPR008067; Cyt_P450_E_grp-I_CYP2A-like.
DR   InterPro; IPR036396; Cyt_P450_sf.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00463; EP450I.
DR   PRINTS; PR01684; EP450ICYP2A.
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; Olfaction; Oxidoreductase;
KW   Reference proteome; Sensory transduction.
FT   CHAIN           1..494
FT                   /note="Cytochrome P450 2G1"
FT                   /id="PRO_0000051764"
FT   BINDING         439
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"
FT   CONFLICT        46
FT                   /note="L -> E (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   494 AA;  56629 MW;  4DA83F2E1CD230BC CRC64;
     MELGGAFTIF LALCFSCLLI LIAWKRVQKP GRLPPGPTPI PFLGNLLQVR TDATFQSFLK
     LREKYGPVFT VYMGPRPVVI LCGHEAVKEA LVDRADEFSG RGELASVERN FQGHGVALAN
     GERWRILRRF SLTILRDFGM GKRSIEERIQ EEAGYLLEEF RKTKGAPIDP TFFLSRTVSN
     VISSVVFGSR FDYEDKQFLS LLRMINESFI EMSTPWAQLY DMYSGVMQYL PGRHNRIYYL
     IEELKDFIAA RVKVNEASLD PQNPRDFIDC FLIKMHQDKN NPHTEFNLKN LVLTTLNLFF
     AGTETVSSTL RYGFLLIMKH PEVQTKIYEE INQVIGPHRI PSVDDRVKMP FTDAVIHEIQ
     RLTDIVPMGV PHNVIRDTHF RGYLLPKGTD VFPLLGSVLK DPKYFCHPDD FYPQHFLDEQ
     GRFKKNEAFV PFSSGKRICL GEAMARMELF LYFTSILQNF SLHPLVPPVN IDITPKISGF
     GNIPPTYELC LIAR