C49A1_DROME
ID C49A1_DROME Reviewed; 589 AA.
AC Q9V5L3; A4UZC2; B8A3V2; Q8MZH1; Q8SY18;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 02-AUG-2002, sequence version 3.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Probable cytochrome P450 49a1;
DE EC=1.14.-.-;
DE AltName: Full=CYPXLIXA1;
GN Name=Cyp49a1; ORFNames=CG18377;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2]
RP GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS A AND C).
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM C).
RC STRAIN=Berkeley;
RA Carlson J.W., Booth B., Frise E., Park S., Wan K.H., Yu C., Celniker S.E.;
RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: May be involved in the metabolism of insect hormones and in
CC the breakdown of synthetic insecticides. {ECO:0000250}.
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305};
CC Peripheral membrane protein {ECO:0000305}. Microsome membrane
CC {ECO:0000305}; Peripheral membrane protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=A; Synonyms=D;
CC IsoId=Q9V5L3-1; Sequence=Displayed;
CC Name=C;
CC IsoId=Q9V5L3-3; Sequence=VSP_000616, VSP_000617;
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM27517.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
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DR EMBL; AE013599; AAF58791.3; -; Genomic_DNA.
DR EMBL; AE013599; AAF58793.2; -; Genomic_DNA.
DR EMBL; AE013599; AAM68760.2; -; Genomic_DNA.
DR EMBL; AY075453; AAL68266.1; -; mRNA.
DR EMBL; AY102688; AAM27517.1; ALT_SEQ; mRNA.
DR EMBL; BT056244; ACL68691.1; -; mRNA.
DR RefSeq; NP_001246256.1; NM_001259327.2. [Q9V5L3-1]
DR RefSeq; NP_610588.2; NM_136744.4. [Q9V5L3-1]
DR RefSeq; NP_724937.1; NM_165774.3. [Q9V5L3-3]
DR RefSeq; NP_995803.1; NM_206081.2. [Q9V5L3-1]
DR AlphaFoldDB; Q9V5L3; -.
DR SMR; Q9V5L3; -.
DR BioGRID; 61923; 1.
DR DIP; DIP-22876N; -.
DR IntAct; Q9V5L3; 2.
DR STRING; 7227.FBpp0087403; -.
DR PaxDb; Q9V5L3; -.
DR DNASU; 36105; -.
DR EnsemblMetazoa; FBtr0088311; FBpp0087403; FBgn0033524. [Q9V5L3-1]
DR EnsemblMetazoa; FBtr0088312; FBpp0087404; FBgn0033524. [Q9V5L3-3]
DR EnsemblMetazoa; FBtr0088313; FBpp0089308; FBgn0033524. [Q9V5L3-1]
DR EnsemblMetazoa; FBtr0304592; FBpp0293134; FBgn0033524. [Q9V5L3-1]
DR GeneID; 36105; -.
DR KEGG; dme:Dmel_CG18377; -.
DR UCSC; CG18377-RA; d. melanogaster. [Q9V5L3-1]
DR CTD; 36105; -.
DR FlyBase; FBgn0033524; Cyp49a1.
DR VEuPathDB; VectorBase:FBgn0033524; -.
DR eggNOG; KOG0159; Eukaryota.
DR InParanoid; Q9V5L3; -.
DR OMA; CPHAGQK; -.
DR PhylomeDB; Q9V5L3; -.
DR SignaLink; Q9V5L3; -.
DR BioGRID-ORCS; 36105; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 36105; -.
DR PRO; PR:Q9V5L3; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0033524; Expressed in adult hindgut (Drosophila) and 28 other tissues.
DR ExpressionAtlas; Q9V5L3; baseline and differential.
DR Genevisible; Q9V5L3; DM.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; 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; IPR036396; Cyt_P450_sf.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00463; EP450I.
DR PRINTS; PR00385; P450.
DR SUPFAM; SSF48264; SSF48264; 1.
DR PROSITE; PS00086; CYTOCHROME_P450; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Endoplasmic reticulum; Heme; Iron; Membrane;
KW Metal-binding; Microsome; Monooxygenase; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..589
FT /note="Probable cytochrome P450 49a1"
FT /id="PRO_0000051996"
FT REGION 56..90
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 536
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 VAR_SEQ 1..174
FT /note="Missing (in isoform C)"
FT /evidence="ECO:0000303|PubMed:12537569, ECO:0000303|Ref.4"
FT /id="VSP_000616"
FT VAR_SEQ 175..177
FT /note="MPH -> MEL (in isoform C)"
FT /evidence="ECO:0000303|PubMed:12537569, ECO:0000303|Ref.4"
FT /id="VSP_000617"
FT CONFLICT 461
FT /note="S -> N (in Ref. 3; AAL68266)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 589 AA; 65902 MW; A0DE2D1118807817 CRC64;
MSGLRKTSIA LMRRSTSSTT ILPHSGGVGG AVSPPSSGVG VATEIEKSIA MQRLRTGESS
NPKKLNVSQQ PVTSVATTRT TASSLPAETT SSPAAAVRPY SEVPGPYPLP LIGNSWRFAP
LIGTYKISDL DKVMNELHVN YGKMAKVGGL IGHPDLLFVF DGDEIRNIFK KEEAMPHRPS
MPSLRHYKGD LRRDFFGDVA GLIGVHGPKW EAFRQEVQHI LLQPQTAKKY IPPLNDIASE
FMGRIELMRD EKDELPANFL HELYKWALES VGRVSLDTRL GCLSPEGSEE AQQIIEAINT
FFWAVPELEL RMPLWRIYPT KAYRSFVKAL DQFTAICMKN IGKTMDKADA DEARGLSKSE
ADISIVERIV RKTGNRKLAA ILALDLFLVG VDTTSVAASS TIYQLAKNPD KQKKLFDELQ
KVFPHREADI NQNVLEQMPY LRACVKETLR MRPVVIANGR SLQSDAVING YHVPKGTHVI
FPHLVVSNDP AYFPEPKRFL PERWLKQSTD AAGCPHANQK IHPFVSLPFG FGRRMCVGRR
FAEIELHTLL AKIFRKYKVS YNSGEFVYRV NSTYIPQSPL NFKLTLRDE
