L259_DROME
ID L259_DROME Reviewed; 1374 AA.
AC P91660; Q9V571; Q9V572;
DT 19-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 16-MAR-2016, sequence version 4.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Probable multidrug resistance-associated protein lethal(2)03659;
DE AltName: Full=Wunen region A protein;
GN Name=l(2)03659; ORFNames=CG8799;
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] {ECO:0000305}
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.
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] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 891-1004, FUNCTION, AND TISSUE
RP SPECIFICITY.
RX PubMed=8985246; DOI=10.1038/385064a0;
RA Zhang N., Zhang J.P., Purcell K.J., Chen Y., Howard K.;
RT "The Drosophila protein Wunen repels migrating germ cells.";
RL Nature 385:64-67(1997).
CC -!- FUNCTION: Vital for development. {ECO:0000269|PubMed:8985246}.
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: Uniform expression in embryos.
CC {ECO:0000269|PubMed:8985246}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCC family.
CC Conjugate transporter (TC 3.A.1.208) subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC47448.1; Type=Erroneous translation; Note=Wrong choice of frame. Uses complementary DNA strand, thus describing the wrong sequence.; Evidence={ECO:0000305};
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DR EMBL; AE013599; AAF58947.3; -; Genomic_DNA.
DR EMBL; U73821; AAC47448.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; NP_610482.3; NM_136638.4.
DR AlphaFoldDB; P91660; -.
DR SMR; P91660; -.
DR BioGRID; 71049; 1.
DR IntAct; P91660; 3.
DR STRING; 7227.FBpp0291666; -.
DR GlyGen; P91660; 3 sites.
DR PaxDb; P91660; -.
DR PRIDE; P91660; -.
DR EnsemblMetazoa; FBtr0302504; FBpp0291666; FBgn0010549.
DR GeneID; 47905; -.
DR KEGG; dme:Dmel_CG8799; -.
DR FlyBase; FBgn0010549; l(2)03659.
DR VEuPathDB; VectorBase:FBgn0010549; -.
DR eggNOG; KOG0054; Eukaryota.
DR GeneTree; ENSGT00940000165791; -.
DR HOGENOM; CLU_000604_27_1_1; -.
DR InParanoid; P91660; -.
DR OrthoDB; 138195at2759; -.
DR PhylomeDB; P91660; -.
DR Reactome; R-DME-382556; ABC-family proteins mediated transport.
DR Reactome; R-DME-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Reactome; R-DME-8856828; Clathrin-mediated endocytosis.
DR Reactome; R-DME-9646399; Aggrephagy.
DR SignaLink; P91660; -.
DR BioGRID-ORCS; 47905; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 47905; -.
DR PRO; PR:P91660; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0010549; Expressed in adult midgut (Drosophila) and 14 other tissues.
DR ExpressionAtlas; P91660; baseline and differential.
DR Genevisible; P91660; DM.
DR GO; GO:0016021; C:integral component of membrane; IC:FlyBase.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0140359; F:ABC-type transporter activity; IEA:InterPro.
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; IDA:FlyBase.
DR GO; GO:0008514; F:organic anion transmembrane transporter activity; IDA:FlyBase.
DR GO; GO:0015711; P:organic anion transport; IDA:FlyBase.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR CDD; cd18579; ABC_6TM_ABCC_D1; 1.
DR Gene3D; 1.20.1560.10; -; 2.
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; IPR044746; ABCC_6TM_D1.
DR InterPro; IPR027417; P-loop_NTPase.
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; Developmental protein; Glycoprotein; Membrane;
KW Nucleotide-binding; Reference proteome; Repeat; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..1374
FT /note="Probable multidrug resistance-associated protein
FT lethal(2)03659"
FT /id="PRO_0000093433"
FT TRANSMEM 159..179
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 205..225
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 282..302
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 305..325
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 404..424
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 426..446
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 787..807
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 845..865
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 913..933
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 938..958
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 1025..1045
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 168..449
FT /note="ABC transmembrane type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 499..722
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 793..1079
FT /note="ABC transmembrane type-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 1119..1352
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 466..492
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 723..766
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..40
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 733..763
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 534..541
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 1153..1160
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT CARBOHYD 561
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1254
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1353
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1374 AA; 153195 MW; 0E1F4C0FC52CB155 CRC64;
MDKQPVLEPT FDSVSERENT SIEESSLLEN NGFDHRNKDE SLSVNTSPPL VCRKCFELGH
QTENCKQKLT VNSENNSAQN EKEKVLPENP RARSNFISSL CFWYTIPIFR KGYRKTLDST
DLYRPLEEQK SDILGNRLCA SWERELKNDG RSPSLVRALL RVFGWQLGFP GLAIFVVELG
LRTLQPIFLV KLISYFSGEP DAANAGFYYA VAQIVISALT VMILTPTTFG IHHVCFKMRV
AMGSMIFRKA LRLTKGALGD TTSGHVVNLI SNDIPRLDSA PYTVHYLWVG PLQVLVITYL
MYQEIGISAV FGVLFMLLFM PIQMYLGTRT SAIQLKAAER TDNRIRMVNE IISAIQVLKM
YAWEQPFEQM VTHAREKEMN TIRQGQYIRG FDFARRIVLS RVAIFLSLVG YVILGKVFTP
EIAFMITAYY NVLLAAMSIY VPSAIIQTAQ FLTSIRRVEQ FMQSEELGSS DKSEGPSKDT
VPGNPPSNNN EADLLKSAIS IRDLKAKWDP NSPDYTLSGI NLEIKPGSVV AVIGLTGSGK
SSLIQAILGE LKANSGQLQV NGSLSYTSQE SWLFSGTVRQ NILFGQPMDS QRYEEVVKKC
ALERDFDLLP LRDNTIVGER GATLSGGQKA RISLARSVYR KASIYLLDDP LSAVDASVAR
HLFDQCVRGH LRGSTVVLVT HQEQFLPHVD QIVILANGQI KALGDYESLL KTGLITGLGS
LSKTDKAKTE EQEPLNLNSP DNKNEVTPIK ENSEQTVGGS SSGKEHVERQ ESGGISLALY
RKYFQAGGGL VAFLVMLSSS VLAQVAVTGG DYFLTYWVKK ESTAAGHGEM EDMESKSMDV
YKYTLIIILS VIMNLSSSFL LFNIAKKASI RLHNTIFNRV TRADMHFFSI NKHGSILNRF
TKDMSQVDEV LPVVLVDVMQ IALWLAGIII VIANVNPLLL VPTLMLSVIF YHLRNLYLKT
SRDLKRVEAI NRSPVYSHLA ASLNGLTTIR ALDAQRVLEK EFDSYQDAHS SAFFMYISTS
QAFGYCMNCI CVIYISIITL SFFAFPPGNG ADVGLVITQA MGLIDMVQWG VRQTAELENT
MTAVERVVEY ESIEPEGMLE APDDKKPPKT WPEQGEIIFK ELNLRYTPNA KAENVLKSLS
FVIQPREKVG IVGRTGAGKS SLINALFRLS YTDGSVLIDT RDTRQMGLHD LRRQISIIPQ
EPVLFSGTMR YNLDPFDEYS DEKLWGCLEE VKLKEVVSDL PDGLASKISE GGTNFSVGQR
QLVCLARAIL RENRILVMDE ATANVDPQTD GLIQATIRSK FRDCTVLTIA HRLHTIIDSD
KVMVMDAGRV VEFGSPYELM TKSDSKVFHN LVNQSGRASY EGLLKIAQET FESS
