ID   CP2AA_RABIT             Reviewed;         494 AA.
AC   Q05555;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   03-AUG-2022, entry version 120.
DE   RecName: Full=Cytochrome P450 2A10;
DE            EC=1.14.14.1;
DE   AltName: Full=CYPIIA10;
DE   AltName: Full=Cytochrome P450-IIA10;
GN   Name=CYP2A10;
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].
RC   STRAIN=New Zealand white; TISSUE=Nasal mucosa;
RX   PubMed=8349611; DOI=10.1016/s0021-9258(19)85330-9;
RA   Peng H.-M., Ding X., Coon M.J.;
RT   "Isolation and heterologous expression of cloned cDNAs for two rabbit nasal
RT   microsomal proteins, CYP2A10 and CYP2A11, that are related to nasal
RT   microsomal cytochrome P450 form a.";
RL   J. Biol. Chem. 268:17253-17260(1993).
RN   [2]
RP   CHARACTERIZATION.
RX   PubMed=8074681; DOI=10.1006/bbrc.1994.2192;
RA   Ding X., Peng H.-M., Coon M.J.;
RT   "Structure-function analysis of CYP2A10 and CYP2A11, P450 cytochromes that
RT   differ in only eight amino acids but have strikingly different activities
RT   toward testosterone and coumarin.";
RL   Biochem. Biophys. Res. Commun. 203:373-378(1994).
CC   -!- FUNCTION: Catalyzes the oxygenation of a variety of substrates,
CC       including ethanol and procarcinogens such as N-nitrosodiethylamine and
CC       phenacetin. Exhibits a high coumarin 7-hydroxylase activity. Converts
CC       also testosterone to androstenedione.
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: Expressed in liver and lung as well as in nasal
CC       tissues.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; L10236; AAA31371.1; -; mRNA.
DR   PIR; A47494; A47494.
DR   RefSeq; NP_001164520.1; NM_001171049.1.
DR   AlphaFoldDB; Q05555; -.
DR   SMR; Q05555; -.
DR   STRING; 9986.ENSOCUP00000005874; -.
DR   GeneID; 100328598; -.
DR   KEGG; ocu:100328598; -.
DR   CTD; 100328598; -.
DR   eggNOG; KOG0156; Eukaryota.
DR   InParanoid; Q05555; -.
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; 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   Acetylation; Endoplasmic reticulum; Heme; Iron; Membrane; Metal-binding;
KW   Microsome; Monooxygenase; Oxidoreductase; Reference proteome.
FT   CHAIN           1..494
FT                   /note="Cytochrome P450 2A10"
FT                   /id="PRO_0000051673"
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   MOD_RES         379
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q64458"
SQ   SEQUENCE   494 AA;  57190 MW;  82A58B6A064BDAD3 CRC64;
     MLASGLLLAA LLACLTVMIL LSVWRQRKLW GKLPPGPTPL PFIGNYLQLN TEQMYDSLMK
     ISERYGPVFT IHLGPRRIVV LCGQEAVKEA LVDQAEDFSG RGELATFDWL FKGYGVVFSS
     WERARPLRRF AISTLRDFGV GKRGIEERIQ EEAGFLIEAF RDTRGAFIDP TFFLSRTVSN
     VISSIVFGDR FDYEDKEFLS LLRMMLGSFQ FTATPTGQLY EMFYSVMKHL PGPQQQAFKE
     LEGLRDFIAK KVERNQRTLD PNSPRDFIDS FLIRMQEEKK DPKSEFHMKN LVMTTLNLFF
     AGTETVSTTM RYGFLLLMKH PDVEAKVHEE IDRVIGRNRQ PKFEDRAKMP YTEAVIHEIQ
     RFTDMIPMGL AHRVTRDTKF RDFLLPKGAE VFPMLGSVLK DPKFFSKPRE FYPQHFLDEK
     GQFKKSDAFM PFSVGKRYCL GEGLARMELF LFFTTIMQNF RFRSQQAPQD IDVSPKHVGF
     ATIPRTYTMS FVPR