TRE11_DROME
ID TRE11_DROME Reviewed; 857 AA.
AC A1Z8N1; A9ZSY5; Q6NQZ8; Q86P59;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Facilitated trehalose transporter Tret1-1 {ECO:0000303|PubMed:20035867};
DE Short=DmTret1-1 {ECO:0000303|PubMed:20035867};
GN Name=Tret1-1 {ECO:0000312|EMBL:BAF96746.1}; ORFNames=CG30035;
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, ECO:0000312|EMBL:BAF96746.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B), NUCLEOTIDE SEQUENCE [MRNA] OF
RP 352-857 (ISOFORM A), FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP SUBCELLULAR LOCATION.
RC STRAIN=Canton-S {ECO:0000312|EMBL:BAF96746.1};
RX PubMed=20035867; DOI=10.1016/j.ibmb.2009.12.006;
RA Kanamori Y., Saito Y., Hagiwara-Komoda Y., Tanaka D., Mitsumasu K.,
RA Kikuta S., Watanabe M., Cornette R., Kikawada T., Okuda T.;
RT "The trehalose transporter 1 gene sequence is conserved in insects and
RT encodes proteins with different kinetic properties involved in trehalose
RT import into peripheral tissues.";
RL Insect Biochem. Mol. Biol. 40:30-37(2010).
RN [2] {ECO:0000312|EMBL:AAF58632.2}
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] {ECO:0000305, ECO:0000312|EMBL:AAF58632.2}
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 [4] {ECO:0000305, ECO:0000312|EMBL:AAQ23604.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS A AND B).
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAQ23604.1};
RC TISSUE=Head, Larva, and Pupae;
RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Champe M.,
RA Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A.,
RA Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., Miranda A.,
RA Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., Patel S.,
RA Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E.;
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000305}
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-248; SER-249; SER-250;
RP SER-320; SER-322; SER-845 AND SER-846 (ISOFORM A), PHOSPHORYLATION [LARGE
RP SCALE ANALYSIS] AT THR-9 AND SER-12 (ISOFORM B), AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Embryo {ECO:0000269|PubMed:18327897};
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
CC -!- FUNCTION: Low-capacity facilitative transporter for trehalose. Does not
CC transport maltose, sucrose or lactose. Mediates the bidirectional
CC transfer of trehalose. Responsible for the transport of trehalose
CC synthesized in the fat body and the incorporation of trehalose into
CC other tissues that require a carbon source, thereby regulating
CC trehalose levels in the hemolymph. {ECO:0000269|PubMed:20035867}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=10.94 mM for trehalose {ECO:0000269|PubMed:20035867};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20035867};
CC Multi-pass membrane protein {ECO:0000255, ECO:0000269|PubMed:20035867}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=A {ECO:0000269|PubMed:10731132};
CC IsoId=A1Z8N1-1; Sequence=Displayed;
CC Name=B {ECO:0000269|PubMed:10731132};
CC IsoId=A1Z8N1-2; Sequence=VSP_039515, VSP_039516;
CC -!- SIMILARITY: Belongs to the major facilitator superfamily. Sugar
CC transporter (TC 2.A.1.1) family. Trehalose transporter subfamily.
CC {ECO:0000255, ECO:0000269|PubMed:20035867}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAO39469.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
CC Sequence=AAO39469.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AB369552; BAF96746.1; -; mRNA.
DR EMBL; AB369553; BAF96747.1; -; mRNA.
DR EMBL; AE013599; AAF58631.1; -; Genomic_DNA.
DR EMBL; AE013599; AAF58632.2; -; Genomic_DNA.
DR EMBL; BT003466; AAO39469.1; ALT_SEQ; mRNA.
DR EMBL; BT010286; AAQ23604.1; -; mRNA.
DR RefSeq; NP_610693.1; NM_136849.2. [A1Z8N1-1]
DR RefSeq; NP_725068.1; NM_165845.2. [A1Z8N1-2]
DR AlphaFoldDB; A1Z8N1; -.
DR SMR; A1Z8N1; -.
DR BioGRID; 62035; 4.
DR IntAct; A1Z8N1; 3.
DR STRING; 7227.FBpp0087178; -.
DR TCDB; 2.A.1.1.99; the major facilitator superfamily (mfs).
DR GlyGen; A1Z8N1; 2 sites.
DR iPTMnet; A1Z8N1; -.
DR PaxDb; A1Z8N1; -.
DR PRIDE; A1Z8N1; -.
DR DNASU; 36248; -.
DR EnsemblMetazoa; FBtr0088073; FBpp0087178; FBgn0050035. [A1Z8N1-1]
DR EnsemblMetazoa; FBtr0088074; FBpp0087179; FBgn0050035. [A1Z8N1-2]
DR GeneID; 36248; -.
DR KEGG; dme:Dmel_CG30035; -.
DR UCSC; CG30035-RA; d. melanogaster. [A1Z8N1-1]
DR UCSC; CG30035-RB; d. melanogaster.
DR CTD; 36248; -.
DR FlyBase; FBgn0050035; Tret1-1.
DR VEuPathDB; VectorBase:FBgn0050035; -.
DR eggNOG; KOG0254; Eukaryota.
DR GeneTree; ENSGT00940000173941; -.
DR HOGENOM; CLU_016710_0_0_1; -.
DR InParanoid; A1Z8N1; -.
DR OMA; WFGRRIT; -.
DR PhylomeDB; A1Z8N1; -.
DR Reactome; R-DME-189200; Cellular hexose transport.
DR Reactome; R-DME-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Reactome; R-DME-8856828; Clathrin-mediated endocytosis.
DR BioGRID-ORCS; 36248; 0 hits in 3 CRISPR screens.
DR ChiTaRS; Tret1-1; fly.
DR GenomeRNAi; 36248; -.
DR PRO; PR:A1Z8N1; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0050035; Expressed in capitellum (Drosophila) and 27 other tissues.
DR Genevisible; A1Z8N1; DM.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IDA:FlyBase.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0005355; F:glucose transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015574; F:trehalose transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:1904659; P:glucose transmembrane transport; IDA:UniProtKB.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR GO; GO:0015771; P:trehalose transport; IDA:UniProtKB.
DR CDD; cd17358; MFS_GLUT6_8_Class3_like; 1.
DR Gene3D; 1.20.1250.20; -; 1.
DR InterPro; IPR020846; MFS_dom.
DR InterPro; IPR044775; MFS_ERD6/Tret1-like.
DR InterPro; IPR005828; MFS_sugar_transport-like.
DR InterPro; IPR036259; MFS_trans_sf.
DR InterPro; IPR003663; Sugar/inositol_transpt.
DR InterPro; IPR005829; Sugar_transporter_CS.
DR Pfam; PF00083; Sugar_tr; 1.
DR PRINTS; PR00171; SUGRTRNSPORT.
DR SUPFAM; SSF103473; SSF103473; 1.
DR TIGRFAMs; TIGR00879; SP; 1.
DR PROSITE; PS50850; MFS; 1.
DR PROSITE; PS00216; SUGAR_TRANSPORT_1; 2.
DR PROSITE; PS00217; SUGAR_TRANSPORT_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Glycoprotein; Membrane;
KW Phosphoprotein; Reference proteome; Sugar transport; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..857
FT /note="Facilitated trehalose transporter Tret1-1"
FT /id="PRO_0000395531"
FT TOPO_DOM 1..392
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 393..413
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 414..440
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 441..461
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 462..473
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 474..494
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 495..497
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 498..518
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 519..528
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 529..549
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 550..552
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 553..573
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 574..636
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 637..657
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 658..673
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 674..694
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 695..700
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 701..721
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 722..740
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 741..761
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255"
FT TOPO_DOM 762..767
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 768..788
FT /note="Helical; Name=11"
FT /evidence="ECO:0000255"
FT TOPO_DOM 789..801
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 802..822
FT /note="Helical; Name=12"
FT /evidence="ECO:0000255"
FT TOPO_DOM 823..857
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 62..202
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 249..269
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 280..299
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 327..346
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 103..118
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 133..148
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 167..182
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 283..299
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 248
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 249
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 250
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 320
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 322
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 845
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 846
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT CARBOHYD 428
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 550
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..27
FT /note="MSGRDNRGAGGGGGGHQPLSNAMGKLK -> MKILMRADTHVSFSVPVEEPK
FT AICTFS (in isoform B)"
FT /evidence="ECO:0000303|PubMed:10731132,
FT ECO:0000303|PubMed:20035867, ECO:0000303|Ref.4"
FT /id="VSP_039515"
FT VAR_SEQ 28..395
FT /note="Missing (in isoform B)"
FT /evidence="ECO:0000303|PubMed:10731132,
FT ECO:0000303|PubMed:20035867, ECO:0000303|Ref.4"
FT /id="VSP_039516"
FT MOD_RES A1Z8N1-2:9
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18327897"
FT MOD_RES A1Z8N1-2:12
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18327897"
SQ SEQUENCE 857 AA; 95188 MW; 8408E1191B8B7A5F CRC64;
MSGRDNRGAG GGGGGHQPLS NAMGKLKEKL TRVGDELGYH RVESNLSTSN TATSLDTILP
EDPFLFPQVS PQRHPQNTVR TQRLLEDEPP LSFRPLLEDD DINEPPTQQQ QRTPLRASGS
LELTPLPPPP TSLEIREHRD RQQRGAQGDE LQRSKQSLKG SRVSFERRDT GNSNTNSNKA
AESSDEDSFE EKRTGFQQQK ATSVDHKGIL KDLKHILAND NRRQFQAKKH VSLDVKGTRF
LQDLLKESSS EEEFHKTRRE FQGRKHQSLD PRVTFKLDKV LQGSSTDSDE EGEDAEHKRL
IHRPKDITKP VIIDLKDLES ESDEDFLTSR QHFQQQRSIS TDSRKSRRLY EMDEMDNKRG
ENIRHAVPFV RQITEDGKPK LEVYRPTTNP IYIWTQVLAA LSVSLGSLVV GFVSAYTSPA
LVSMTDRNIT SFEVTQDAGS WVGGIMPLAG LAGGIAGGPL IEYLGRRNTI LATAVPFIVS
SLLIACAVNV AMVLCGRFLA GFCVGIASLS LPVYLGETVQ PEVRGTLGLL PTAFGNIGIL
LCFVAGSFMN WSMLAFLGAA LPVPFLILMF LIPETPRWFV GRGLEERARK ALKWLRGKEA
DVEPELKGLM RSQADADRQA SRNTMLELLK LNNLKPLSIS LGLMFFQQFS GINAVIFYTV
QIFKDAGSTI DGNLCTIIVG IVNFLATFIG IVLIDRAGRK ILLYVSDIAM VLTLFVLGGF
FYCKTYGPDV SHLGWLPLTC FVIYILGFSL GFGPIPWLMM GEILPAKIRG SAASVATAFN
WFCTFVVTKT FQDLTVAMGA HGAFWLFGAI CFVGLFFVII YVPETQGKTL EDIERKMMGR
VRRMSSVANI KPLSFNM
