TRET1_DROVI
ID TRET1_DROVI Reviewed; 911 AA.
AC B4LPX5;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 13-JUL-2010, sequence version 2.
DT 25-MAY-2022, entry version 57.
DE RecName: Full=Facilitated trehalose transporter Tret1 {ECO:0000250|UniProtKB:A1Z8N1};
GN Name=Tret1 {ECO:0000250|UniProtKB:A1Z8N1}; ORFNames=GJ20366;
OS Drosophila virilis (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila.
OX NCBI_TaxID=7244;
RN [1] {ECO:0000312|EMBL:EDW61315.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 15010-1051.87 {ECO:0000312|EMBL:EDW61315.1};
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EDW61315.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; CH940648; EDW61315.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_002050122.2; XM_002050086.2.
DR AlphaFoldDB; B4LPX5; -.
DR SMR; B4LPX5; -.
DR STRING; 7244.FBpp0234783; -.
DR EnsemblMetazoa; FBtr0435437; FBpp0392404; FBgn0207506.
DR eggNOG; KOG0254; Eukaryota.
DR InParanoid; B4LPX5; -.
DR OrthoDB; 430696at2759; -.
DR Proteomes; UP000008792; 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; 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..911
FT /note="Facilitated trehalose transporter Tret1"
FT /id="PRO_0000395548"
FT TOPO_DOM 1..446
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 447..467
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 468..494
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 495..515
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 516..527
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 528..548
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 549..551
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 552..572
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 573..578
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 579..599
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 600..606
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 607..627
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 628..690
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 691..711
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 712..727
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 728..748
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 749..754
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 755..775
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 776..794
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 795..815
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255"
FT TOPO_DOM 816..821
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 822..842
FT /note="Helical; Name=11"
FT /evidence="ECO:0000255"
FT TOPO_DOM 843..855
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 856..876
FT /note="Helical; Name=12"
FT /evidence="ECO:0000255"
FT TOPO_DOM 877..911
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..256
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 334..355
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 380..402
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 49..64
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 78..129
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 155..172
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 202..216
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 229..248
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 337..355
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 302
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A1Z8N1"
FT MOD_RES 303
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A1Z8N1"
FT MOD_RES 304
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A1Z8N1"
FT MOD_RES 374
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A1Z8N1"
FT MOD_RES 376
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A1Z8N1"
FT MOD_RES 899
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A1Z8N1"
FT MOD_RES 900
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A1Z8N1"
FT CARBOHYD 482
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 911 AA; 101368 MW; 4754A92D2A07905E CRC64;
MSGRDNRGAG GGGGGGGGGG HHHQPLSSAM GKLKEKLTRA GEELGYHRVE SNLSTSNTGT
SLDTILPEDP FPFPQAAPQR HPQQQFPHLQ SPQQQRQQLQ QQQLQQQQLH LQQPQQQLQQ
QQQPQQQLRL LHDVDDEPPL SFRPLLEDVD INEPPQQIHV QQQQQQLPRT ALRASGSLEL
TPLPPPPTSL EPHRDRQQRS IVTGGEELQR SKQSLKGSRV SFEKPRGEQL PAKAAESSDE
DSFEDKRIGF QQQKATSVDH KGILKDLKHI LANDNRRQFQ AKKHVSLDIK GTRFLKDLLK
DSSSEEEFHK TRREFQGRKH QSLDPRVTFK LDKVLQGSST DSDEEGDDAE HKRLIHRPKD
ITKPVIIDLK DLESESDEDF LTSRQNFQQQ RSISTDSRKS RRLYEMDEMG NKRGDNIRHA
VPFVRQITED GKPKLEVYRP TTNPIYIWTQ VLAALSVSLG SLVVGFASAY TSPALVSMTN
TNLTSFVVTP QAASWVGGIM PLAGLAGGIA GGPFIEYLGR RNTILATAVP FIVSWLLIAC
AVNVIMVLCG RFLAGFCVGI ASLSLPVYLG ETVQPEVRGT LGLLPTAFGN IGILLCFVAG
TYMDWSMLAF LGASLPVPFL ILMFLIPETP RWYVSRGREE RARKALVWLR GKEADVEPEL
KGLMRSQADA DRQATQNKML ELLKRSNLKP LSISLGLMFF QQLSGINAVI FYTVQIFQDA
GSTIDGNVCT IIVGVVNFAA TFIATILIDR AGRKVLLYVS NVMMVLTLFV LGGFFYCKSS
GMDTSNVGWL PLSCFVIYIL GFSLGFGPIP WLMMGEILPA KIRGSAASVA TAFNWSCTFV
VTKSFQDMID FMGAHGAFWM FGAICFIGLF FVIFYVPETQ GKTLEDIERK MMGRVRRMSS
VANIKPLSFN M
