MDR49_DROME
ID MDR49_DROME Reviewed; 1302 AA.
AC Q00449; B5RIT2; C1C3C4; Q9V6I6;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 2.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=Multidrug resistance protein homolog 49;
DE EC=7.6.2.2;
DE AltName: Full=P-glycoprotein 49;
GN Name=Mdr49; ORFNames=CG3879;
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 [MRNA], AND VARIANTS ASN-697 AND ASN-712.
RC STRAIN=Canton-S; TISSUE=Head;
RX PubMed=2072901; DOI=10.1128/mcb.11.8.3940-3948.1991;
RA Wu C.-T., Budding M., Griffin M.S., Croop J.M.;
RT "Isolation and characterization of Drosophila multidrug resistance gene
RT homologs.";
RL Mol. Cell. Biol. 11:3940-3948(1991).
RN [2]
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 [3]
RP GENOME REANNOTATION.
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley;
RA Carlson J.W., Booth B., Frise E., Park S., Sandler J., Wan K.H., Yu C.,
RA Celniker S.E.;
RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + xenobioticSide 1 = ADP + phosphate +
CC xenobioticSide 2.; EC=7.6.2.2;
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCB family.
CC Multidrug resistance exporter (TC 3.A.1.201) subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ACO25636.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
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DR EMBL; M59076; AAA28679.1; -; mRNA.
DR EMBL; AE013599; AAF58437.2; -; Genomic_DNA.
DR EMBL; AY058791; AAL14020.1; -; mRNA.
DR EMBL; BT044206; ACH92271.1; -; mRNA.
DR EMBL; BT081353; ACO25636.1; ALT_SEQ; mRNA.
DR PIR; A41249; A41249.
DR RefSeq; NP_001163132.1; NM_001169661.1.
DR RefSeq; NP_523724.2; NM_079000.4.
DR AlphaFoldDB; Q00449; -.
DR SMR; Q00449; -.
DR BioGRID; 62198; 6.
DR IntAct; Q00449; 9.
DR STRING; 7227.FBpp0086914; -.
DR TCDB; 3.A.1.201.24; the atp-binding cassette (abc) superfamily.
DR GlyGen; Q00449; 1 site.
DR PaxDb; Q00449; -.
DR PRIDE; Q00449; -.
DR DNASU; 36428; -.
DR EnsemblMetazoa; FBtr0087801; FBpp0086914; FBgn0004512.
DR GeneID; 36428; -.
DR KEGG; dme:Dmel_CG3879; -.
DR CTD; 36428; -.
DR FlyBase; FBgn0004512; Mdr49.
DR VEuPathDB; VectorBase:FBgn0004512; -.
DR eggNOG; KOG0055; Eukaryota.
DR InParanoid; Q00449; -.
DR OMA; YIYLNYG; -.
DR OrthoDB; 186078at2759; -.
DR PhylomeDB; Q00449; -.
DR SignaLink; Q00449; -.
DR BioGRID-ORCS; 36428; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 36428; -.
DR PRO; PR:Q00449; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0004512; Expressed in adult midgut (Drosophila) and 29 other tissues.
DR ExpressionAtlas; Q00449; baseline and differential.
DR Genevisible; Q00449; DM.
DR GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; ISS:FlyBase.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; NAS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:FlyBase.
DR GO; GO:0008559; F:ABC-type xenobiotic transporter activity; ISS:FlyBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042626; F:ATPase-coupled transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015562; F:efflux transmembrane transporter activity; ISS:FlyBase.
DR GO; GO:0042910; F:xenobiotic transmembrane transporter activity; NAS:UniProtKB.
DR GO; GO:0008354; P:germ cell migration; IMP:FlyBase.
DR GO; GO:0097254; P:renal tubular secretion; IEP:FlyBase.
DR GO; GO:0001666; P:response to hypoxia; IMP:FlyBase.
DR GO; GO:0017085; P:response to insecticide; IMP:FlyBase.
DR GO; GO:0009636; P:response to toxic substance; IEP:FlyBase.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR GO; GO:0006855; P:xenobiotic transmembrane transport; NAS:UniProtKB.
DR GO; GO:0042908; P:xenobiotic transport; ISS:FlyBase.
DR Gene3D; 1.20.1560.10; -; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR011527; ABC1_TM_dom.
DR InterPro; IPR036640; ABC1_TM_sf.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR039421; Type_1_exporter.
DR PANTHER; PTHR24221; PTHR24221; 1.
DR Pfam; PF00664; ABC_membrane; 2.
DR Pfam; PF00005; ABC_tran; 2.
DR SMART; SM00382; AAA; 2.
DR SUPFAM; SSF52540; SSF52540; 2.
DR SUPFAM; SSF90123; SSF90123; 2.
DR PROSITE; PS50929; ABC_TM1F; 2.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 2.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE 2: Evidence at transcript level;
KW ATP-binding; Glycoprotein; Membrane; Nucleotide-binding;
KW Reference proteome; Repeat; Translocase; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..1302
FT /note="Multidrug resistance protein homolog 49"
FT /id="PRO_0000093347"
FT TOPO_DOM 1..46
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 47..67
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 117..145
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 193..213
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 221..240
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 301..322
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 340..360
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 361..734
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 735..756
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 780..801
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 856..876
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 878..897
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 960..980
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 997..1017
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 1018..1302
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 46..367
FT /note="ABC transmembrane type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 402..638
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 735..1023
FT /note="ABC transmembrane type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 1059..1297
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT REGION 644..714
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 665..682
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 696..713
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 437..444
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 1094..1101
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT CARBOHYD 101
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VARIANT 697
FT /note="S -> N"
FT /evidence="ECO:0000269|PubMed:2072901"
FT VARIANT 712
FT /note="D -> N"
FT /evidence="ECO:0000269|PubMed:2072901"
FT CONFLICT 952
FT /note="I -> V (in Ref. 1; AAA28679 and 4; AAL14020)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1302 AA; 142739 MW; 4FA14DC62B2D661A CRC64;
MVKKEESRLP QAGDFQLKEG SVVDATRKYS YFDLFRYSTR CERFLLVVSL LVATAASAFI
PYFMIIYGEF TSLLVDRTVG VGTSSPAFAL PMFGGGQQLT NASKEENNQA IIDDATAFGI
GSLVGSVAMF LLITLAIDLA NRIALNQIDR IRKLFLEAML RQDIAWYDTS SGSNFASKMT
EDLDKLKEGI GEKIVIVVFL IMTFVIGIVS AFVYGWKLTL VVLSCVPFII AATSVVARLQ
GSLAEKELKS YSDAANVVEE VFSGIRTVFA FSGQEKEKER FGKLLIPAEN TGRKKGLYSG
MGNALSWLII YLCMALAIWY GVTLILDERD LPDRVYTPAV LVIVLFAVIM GAQNLGFASP
HVEAIAVATA AGQTLFNIID RPSQVDPMDE KGNRPENTAG HIRFEGIRFR YPARPDVEIL
KGLTVDVLPG QTVAFVGASG CGKSTLIQLM QRFYDPEAGS VKLDGRDLRT LNVGWLRSQI
GVVGQEPVLF ATTIGENIRY GRPSATQADI EKAARAANCH DFITRLPKGY DTQVGEKGAQ
ISGGQKQRIA IARALVRQPQ VLLLDEATSA LDPTSEKRVQ SALELASQGP TTLVVAHRLS
TITNADKIVF LKDGVVAEQG THEELMERRG LYCELVSITQ RKEATEADEG AVAGRPLQKS
QNLSDEETDD DEEDEEEDEE PELQTSGSSR DSGFRASTRR KRRSQRRKKK KDKEVVSKVS
FTQLMKLNSP EWRFIVVGGI ASVMHGATFP LWGLFFGDFF GILSDGDDDV VRAEVLKISM
IFVGIGLMAG LGNMLQTYMF TTAGVKMTTR LRKRAFGTII GQDIAYFDDE RNSVGALCSR
LASDCSNVQG ATGARVGTML QAVATLVVGM VVGFVFSWQQ TLLTLVTLPL VCLSVYLEGR
FIMKSAQKAK ASIEEASQVA VEAITNIRTV NGLCLERQVL DQYVQQIDRV DIACRRKVRF
RGLVFALGQA APFLAYGISM YYGGILVAEE RMNYEDIIKV AEALIFGSWM LGQALAYAPN
VNDAILSAGR LMDLFKRTST QPNPPQSPYN TVEKSEGDIV YENVGFEYPT RKGTPILQGL
NLTIKKSTTV ALVGPSGSGK STCVQLLLRY YDPVSGSVNL SGVPSTEFPL DTLRSKLGLV
SQEPVLFDRT IAENIAYGNN FRDDVSMQEI IEAAKKSNIH NFISALPQGY DTRLGKTSQL
SGGQKQRIAI ARALVRNPKI LILDEATSAL DLESEKVVQQ ALDEARSGRT CLTIAHRLTT
VRNADLICVL KRGVVVEHGT HDELMALNKI YANLYLMQQV SG
