TRET1_DROER
ID TRET1_DROER Reviewed; 856 AA.
AC B3NSE1;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 1.
DT 25-MAY-2022, entry version 61.
DE RecName: Full=Facilitated trehalose transporter Tret1 {ECO:0000250|UniProtKB:A1Z8N1};
GN Name=Tret1 {ECO:0000250|UniProtKB:A1Z8N1}; ORFNames=GG20213;
OS Drosophila erecta (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7220;
RN [1] {ECO:0000312|EMBL:EDV56443.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 14021-0224.01 {ECO:0000312|EMBL:EDV56443.1};
RX PubMed=17994087; DOI=10.1038/nature06341;
RG Drosophila 12 genomes consortium;
RT "Evolution of genes and genomes on the Drosophila phylogeny.";
RL Nature 450:203-218(2007).
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 (By similarity).
CC {ECO:0000250|UniProtKB:A1Z8N1}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:A1Z8N1};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:A1Z8N1}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily. Sugar
CC transporter (TC 2.A.1.1) family. Trehalose transporter subfamily.
CC {ECO:0000250|UniProtKB:A1Z8N1, ECO:0000255}.
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DR EMBL; CH954179; EDV56443.1; -; Genomic_DNA.
DR RefSeq; XP_001976043.2; XM_001976007.2.
DR AlphaFoldDB; B3NSE1; -.
DR SMR; B3NSE1; -.
DR STRING; 7220.FBpp0138759; -.
DR eggNOG; KOG0254; Eukaryota.
DR HOGENOM; CLU_016710_0_0_1; -.
DR OMA; IFIWTQS; -.
DR PhylomeDB; B3NSE1; -.
DR Proteomes; UP000008711; Unassembled WGS sequence.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0051119; F:sugar transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0015574; F:trehalose transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:0015771; P:trehalose transport; ISS: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 3: Inferred from homology;
KW Cell membrane; Glycoprotein; Membrane; Phosphoprotein; Sugar transport;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..856
FT /note="Facilitated trehalose transporter Tret1"
FT /id="PRO_0000395543"
FT TOPO_DOM 1..389
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 390..410
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 411..439
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 440..460
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 461..472
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 473..493
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 494..496
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 497..517
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 518..527
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 528..548
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 549..551
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 552..572
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 573..635
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 636..656
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 657..672
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 673..693
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 694..699
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 700..720
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 721..739
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 740..760
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255"
FT TOPO_DOM 761..766
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 767..787
FT /note="Helical; Name=11"
FT /evidence="ECO:0000255"
FT TOPO_DOM 788..800
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 801..821
FT /note="Helical; Name=12"
FT /evidence="ECO:0000255"
FT TOPO_DOM 822..856
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..27
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 326..345
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 91..105
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 132..147
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 166..181
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 247
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A1Z8N1"
FT MOD_RES 248
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A1Z8N1"
FT MOD_RES 249
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A1Z8N1"
FT MOD_RES 319
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A1Z8N1"
FT MOD_RES 321
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A1Z8N1"
FT MOD_RES 844
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A1Z8N1"
FT MOD_RES 845
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A1Z8N1"
FT CARBOHYD 427
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 549
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 856 AA; 94878 MW; EB32EE926BB46951 CRC64;
MSGRDNRGAG GGGGGHQPLS NAMGKLKEKL TRVGDELGYH RVESNLSTSN TATSLDTILP
EDPFLFPQVS PQRHPQTVRT QRLLEDEPPL SFRPLLEDDD INEPPTQQPH RSPLRASGSL
ELTPLPPPPT SLEIREHRDR QQRGAQGDEL QRSKQSLKGS RVSFERRDTG NSNTNNNKAA
ESSDEDSFEE KRTGFQQQKA TSVDHKGILK DLKHILANDN RRQFQAKKHV SLDVKGTRFL
QDLLKESSSE EEFHKTRREF QGRKHQSLDP RVTFKLDKVL QGSSTDSDEE GEDAEHKRLI
HRPKDITKPV IIDLKDLESE SDEDFLTSRQ HFQQQRSIST DSRKSRRLYE MDEMGNKRGE
NIRHAVPFVR QITEDGKPKL EVYRPTTNPI FIWTQVLAAL SVSLGSLVVG FVSAYTSPAL
VSMTDRNITS FEVTQDAGSW VGGIMPLAGL AGGIAGGPLI EYLGRRNTIL ATAVPFIVSS
LLIACAVNVA MVLCGRFLAG FCVGIASLSL PVYLGETVQP EVRGTLGLLP TAFGNIGILL
CFVAGSFMNW SMLAFLGAAL PVPFLILMFL IPETPRWFVS RGREERARKA LSWLRGKEAD
VEPELKGLMR SQADADRQAT QNTMLELLKR NNLKPLSISL GLMFFQQLSG INAVIFYTVQ
IFKDAGSTID GNICTIIVGV VNFLATFIGI VLIDRAGRKI LLYVSNIAMI LTLFVLGGFF
YCKAHGPDVS NLGWLPLTCF VIYILGFSLG FGPIPWLMMG EILPAKIRGS AASVATAFNW
SCTFVVTKTF QDLTVAMGAH GAFWLFGAIC FVGLFFVIIY VPETQGKTLE DIERKMMGRV
RRMSSVANIK PLSFNM
