CP2AB_RABIT
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 03-AUG-2022, entry version 121.
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}.
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; 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; 702827at2759; -.
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 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
