TRET1_DROPS
ID TRET1_DROPS Reviewed; 868 AA.
AC Q291H8;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 13-JUL-2010, sequence version 3.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Facilitated trehalose transporter Tret1 {ECO:0000250|UniProtKB:A1Z8N1};
GN Name=Tret1 {ECO:0000250|UniProtKB:A1Z8N1}; ORFNames=GA15593;
OS Drosophila pseudoobscura pseudoobscura (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=46245;
RN [1] {ECO:0000312|EMBL:EAL25134.2}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MV2-25 / Tucson 14011-0121.94;
RX PubMed=15632085; DOI=10.1101/gr.3059305;
RA Richards S., Liu Y., Bettencourt B.R., Hradecky P., Letovsky S.,
RA Nielsen R., Thornton K., Hubisz M.J., Chen R., Meisel R.P., Couronne O.,
RA Hua S., Smith M.A., Zhang P., Liu J., Bussemaker H.J., van Batenburg M.F.,
RA Howells S.L., Scherer S.E., Sodergren E., Matthews B.B., Crosby M.A.,
RA Schroeder A.J., Ortiz-Barrientos D., Rives C.M., Metzker M.L., Muzny D.M.,
RA Scott G., Steffen D., Wheeler D.A., Worley K.C., Havlak P., Durbin K.J.,
RA Egan A., Gill R., Hume J., Morgan M.B., Miner G., Hamilton C., Huang Y.,
RA Waldron L., Verduzco D., Clerc-Blankenburg K.P., Dubchak I., Noor M.A.F.,
RA Anderson W., White K.P., Clark A.G., Schaeffer S.W., Gelbart W.M.,
RA Weinstock G.M., Gibbs R.A.;
RT "Comparative genome sequencing of Drosophila pseudoobscura: chromosomal,
RT gene, and cis-element evolution.";
RL Genome Res. 15:1-18(2005).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EAL25134.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; CM000071; EAL25134.2; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_001360559.3; XM_001360522.3.
DR AlphaFoldDB; Q291H8; -.
DR SMR; Q291H8; -.
DR STRING; 7237.FBpp0277612; -.
DR EnsemblMetazoa; FBtr0370198; FBpp0332626; FBgn0075610.
DR GeneID; 4803914; -.
DR KEGG; dpo:Dpse_GA15593; -.
DR eggNOG; KOG0254; Eukaryota.
DR InParanoid; Q291H8; -.
DR Proteomes; UP000001819; Chromosome 3.
DR Bgee; FBgn0075610; Expressed in insect adult head and 2 other tissues.
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; 1.
DR PROSITE; PS00217; SUGAR_TRANSPORT_2; 1.
PE 3: Inferred from homology;
KW Cell membrane; Glycoprotein; Membrane; Phosphoprotein; Reference proteome;
KW Sugar transport; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..868
FT /note="Facilitated trehalose transporter Tret1"
FT /id="PRO_0000395547"
FT TOPO_DOM 1..403
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 404..424
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 425..451
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 452..472
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 473..484
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 485..505
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 506..508
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 509..529
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 530..535
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 536..556
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 557..563
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 564..584
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 585..653
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 654..674
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 675..684
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 685..705
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 706..711
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 712..732
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 733..751
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 752..772
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255"
FT TOPO_DOM 773..778
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 779..799
FT /note="Helical; Name=11"
FT /evidence="ECO:0000255"
FT TOPO_DOM 800..812
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 813..833
FT /note="Helical; Name=12"
FT /evidence="ECO:0000255"
FT TOPO_DOM 834..868
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..213
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 257..314
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 335..367
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 41..57
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 75..91
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 113..130
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 171..193
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 257..284
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 294..314
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 352..367
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 259
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A1Z8N1"
FT MOD_RES 260
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A1Z8N1"
FT MOD_RES 261
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A1Z8N1"
FT MOD_RES 331
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A1Z8N1"
FT MOD_RES 333
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A1Z8N1"
FT MOD_RES 856
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A1Z8N1"
FT MOD_RES 857
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A1Z8N1"
FT CARBOHYD 439
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 868 AA; 96698 MW; BFD8BAE1CDB5AE10 CRC64;
MSGRDNRGAG GGGGGHQPLS SAMGKLKEKL TRAGDDQGYH RVESNLSTSN TATSLDTILP
EDPFLFPQAA PQRHPLPRPQ QQQQQQRQQL RLLEDEPPLS FRPLLEDDDI NEPPTQPFQQ
QQQRTPLRAS GSLELTPLPP PPTSQEIREH RDRQQRSVPV PVEDLQRSKQ SLKGSRVSFE
KNNASSKPPA QAESSDEDSF EDKRIGFQQQ KATSVDHKGI LKDLKHILAN DNRRQFQAKK
HVSLDVKGTR FLQDLLKESS SEEEFHKTRR EFQGRKHQSL DPRVTFKLDK VLQGSSTDSD
EEGDDPEHKR LIHRPKDITK PLIIDLKDLE SESDEDFHTS RQHFQQQRSI STDSRKSRRP
YEMDEMGNKR GENIRHAVPF VRQITEDGKP KLEVYRPTTN PIYIWTQVLA ALSVSLGSLV
VGFVSAYTSP ALVSMTNRNM TSFEVTPQAA SWVGGIMPLA GLAGGIAGGP FIEYLGRRNT
ILATAIPFIV SSLLIACAVN VAMVLAGRFL AGFCVGIASL SLPVYLGETV QPEVRGTLGL
LPTAFGNIGI LLCFVAGTYM DWSMLAFLGA ALPVPFLILM FLIPETPRWF VSRGREEKAR
KALSWLRGKE ADVEPELKGL MRSQADADRQ ATQNKMMELL KRNNLKPLSI SLGLMFFQQL
SGINAVIFYT VSIFKDAGST IDGNLCTIIV GIVNFMATFI ATLLIDRAGR KILLYVSNIA
MIITLFVLGG FFYCKSHGQD VSQLGWLPLS CFVIYILGFS LGFGPIPWLM MGEILPSKIR
GSAASVATAF NWSCTFVVTK TFQDMIDFMG AHGAFWLFGS ICFIGLFFVI LYVPETQGKT
LEDIERKMMG RVRRMSSVAN MKPLAFNM
