ID   CP2AB_RABIT             Reviewed;         494 AA.
AC   Q05556;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   27-MAR-2024, entry version 126.
DE   RecName: Full=Cytochrome P450 2A11;
DE            EC=1.14.14.1;
DE   AltName: Full=CYPIIA11;
DE   AltName: Full=Cytochrome P450-IIA11;
GN   Name=CYP2A11;
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, AND MUTAGENESIS OF 62-ARG-ASP-63; GLN-104; ALA-117;
RP   THR-120 AND ARG-372.
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. Has no or little activity as a coumarin 7-hydroxylase and
CC       in the formation of androstenedione from testosterone.
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; L10237; AAA31372.1; -; mRNA.
DR   PIR; B47494; B47494.
DR   RefSeq; NP_001164519.1; NM_001171048.1.
DR   AlphaFoldDB; Q05556; -.
DR   SMR; Q05556; -.
DR   GeneID; 100328596; -.
DR   KEGG; ocu:100328596; -.
DR   CTD; 100328596; -.
DR   InParanoid; Q05556; -.
DR   OrthoDB; 2900138at2759; -.
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; cd20668; CYP2A; 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; IPR008067; Cyt_P450_E_grp-I_CYP2A-like.
DR   InterPro; IPR036396; Cyt_P450_sf.
DR   PANTHER; PTHR24300:SF180; CYTOCHROME P450 2A13; 1.
DR   PANTHER; PTHR24300; CYTOCHROME P450 508A4-RELATED; 1.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00463; EP450I.
DR   PRINTS; PR01684; EP450ICYP2A.
DR   PRINTS; PR00385; P450.
DR   SUPFAM; SSF48264; Cytochrome P450; 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 2A11"
FT                   /id="PRO_0000051674"
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"
FT   MUTAGEN         62..63
FT                   /note="RD->SE: No effect. Almost as active as CYP2A10 in
FT                   coumarin hydroxylation and approximately half as active as
FT                   CYP2A10 in androstenedione formation; when associated with
FT                   L-104; V-117 and S-120."
FT                   /evidence="ECO:0000269|PubMed:8074681"
FT   MUTAGEN         104
FT                   /note="Q->L: No effect. Almost as active as CYP2A10 in
FT                   coumarin hydroxylation and approximately half as active as
FT                   CYP2A10 in androstenedione formation; when associated with
FT                   62-SE-63; V-117 and S-120."
FT                   /evidence="ECO:0000269|PubMed:8074681"
FT   MUTAGEN         117
FT                   /note="A->V: No effect. Almost as active as CYP2A10 in
FT                   coumarin hydroxylation and approximately half as active as
FT                   CYP2A10 in androstenedione formation; when associated with
FT                   62-SE-63; L-104 and S-120."
FT                   /evidence="ECO:0000269|PubMed:8074681"
FT   MUTAGEN         120
FT                   /note="T->S: No effect. Almost as active as CYP2A10 in
FT                   coumarin hydroxylation and approximately half as active as
FT                   CYP2A10 in androstenedione formation; when associated with
FT                   62-SE-63; L-104 and V-117."
FT                   /evidence="ECO:0000269|PubMed:8074681"
FT   MUTAGEN         372
FT                   /note="R->H: Significant increase in the rate of
FT                   hydroxylation of testosterone, but not of coumarin."
FT                   /evidence="ECO:0000269|PubMed:8074681"
SQ   SEQUENCE   494 AA;  57277 MW;  28D2E5C4E5D0861A CRC64;
     MLASGLLLAA LLACLTVMIL LSVWRQRKLW GKLPPGPTPL PFIGNYLQLN TEQMYDSLMK
     IRDRYGPVFT IHLGPRRIVV LCGQEAVKEA LVDQAEDFSG RGEQATFDWL FKGYGVAFST
     WERARPLRRF AISTLRDFGV GKRGIEERIQ EEAGFLIEAF RDTRGAFIDP TFFLSRTVSN
     VISSIVFGDR FDYEDKEFLS LLRMMLGSFQ FTATPTGQLY EMFYSVMKHL PGPQQQAFKE
     LEGLRDFIAK KVERNQRTLD PNSPRDFIDS FLIRMQEEKK DPKSEFHMKN LVLTTLNLFF
     AGTETVSTTM RYGFLLLMKH PDVEAKVHEE IDRVIGRNRQ PKFEDRAKMP YTEAVIHEIQ
     RFTDMIPMGL ARRVTRDTKF RDFLLPKGTE VFPMLGSVLK DPKFFSKPRE FYPQHFLDEK
     GQFKKSDAFM PFSVGKRYCL GEGLARMELF LFFTTIMQNF RFRSQQAPQD IDVSPKHVGF
     ATIPRTYTMS FVPR
//