TRET1_DROGR
ID TRET1_DROGR Reviewed; 929 AA.
AC B4J913;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 25-MAY-2022, entry version 63.
DE RecName: Full=Facilitated trehalose transporter Tret1 {ECO:0000250|UniProtKB:A1Z8N1};
GN Name=Tret1 {ECO:0000250|UniProtKB:A1Z8N1}; ORFNames=GH21392;
OS Drosophila grimshawi (Hawaiian fruit fly) (Idiomyia grimshawi).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Hawaiian Drosophila.
OX NCBI_TaxID=7222;
RN [1] {ECO:0000312|EMBL:EDW01362.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 15287-2541.00 {ECO:0000312|EMBL:EDW01362.1};
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; CH916367; EDW01362.1; -; Genomic_DNA.
DR RefSeq; XP_001986495.1; XM_001986459.1.
DR AlphaFoldDB; B4J913; -.
DR SMR; B4J913; -.
DR STRING; 7222.FBpp0155298; -.
DR EnsemblMetazoa; FBtr0465561; FBpp0415803; FBgn0128854.
DR GeneID; 6559185; -.
DR KEGG; dgr:6559185; -.
DR eggNOG; KOG0254; Eukaryota.
DR HOGENOM; CLU_016710_0_0_1; -.
DR InParanoid; B4J913; -.
DR OMA; IFIWTQS; -.
DR OrthoDB; 430696at2759; -.
DR PhylomeDB; B4J913; -.
DR Proteomes; UP000001070; 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; Reference proteome;
KW Sugar transport; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..929
FT /note="Facilitated trehalose transporter Tret1"
FT /id="PRO_0000395544"
FT TOPO_DOM 1..462
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 463..483
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 484..512
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 513..533
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 534..541
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 542..562
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 563..569
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 570..590
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 591..596
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 597..617
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 618..624
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 625..645
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 646..708
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 709..729
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 730..745
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 746..766
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 767..772
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 773..793
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 794..804
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 805..825
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255"
FT TOPO_DOM 826..839
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 840..860
FT /note="Helical; Name=11"
FT /evidence="ECO:0000255"
FT TOPO_DOM 861..873
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 874..894
FT /note="Helical; Name=12"
FT /evidence="ECO:0000255"
FT TOPO_DOM 895..929
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..275
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 352..371
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 398..420
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 59..73
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 87..141
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 142..167
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 168..185
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 214..254
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 320
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 322
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A1Z8N1"
FT MOD_RES 392
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A1Z8N1"
FT MOD_RES 394
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A1Z8N1"
FT MOD_RES 917
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A1Z8N1"
FT MOD_RES 918
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A1Z8N1"
FT CARBOHYD 500
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 929 AA; 103238 MW; EB493B09443624DB CRC64;
MSGRDNRAAG AGGGSGGGGG GGGGGGNHHH HHQPLSNAMG KLKEKLTRAG EELGYHRVES
NLSASNTATS LDTILPEDPF PFPQAAPQRH PQQQFPFLQQ QPQQQQQPQQ QQQPQQQQQL
QQHHTQHTQY QQQQQQQQPL RLLHDIDDEQ PLSFRPLLED DDIHEPPQEI QQQQLQQQRG
NLRASGSLEL TPLPPPPTSL EPHRDRQQRS VVNEELQRSK QSLKGSRVSF ERAPQQSNSN
NNSKNNSKTT VAADASDDDS FEDRRVGYQQ QKATSVDHKG ILKDLRHILA SDNRRQFQAK
KHVSLDIKGT PFLQDLLKDS SSEEEFHKTR REFQGRKHQS LDPRVTFKLD KVLHGSSTDS
DEEGEDAEHK RLIHRPKDIT KPVIIDLKDL ESESDEDFLS SRQNFQQQRS ISTDSRKSRR
LYEMDEMGNK RGENIRHAVP FVRQITEDGK PKLEVYRPTT NPIYIWTQVL AALSVSLGSL
VVGFSSAYTS PALVSMTDRN LTSFDVSTED ASWVGGIMPL AGLAGGIAGG PLIEYLGRRN
TILATAVPFI ISWLLIACAV NVPMVLSGRF LAGFCVGIAS LSLPVYLGET VQPEVRGTLG
LLPTAFGNIG ILLCFIAGTY MDWSMLAFLG GALPVPFLIL MFLIPETPRW YVSRGREERA
RKALVWLRGV EADVEPELKG LMRSQADADR QATHNTMLEL LKRSNLKPLS ISLGLMFFQQ
LSGINAVIFY TVQIFKDAGS TLDGNVCTII VGTVNFIATF IGILLIDRAG RKILLYVSNI
AMILTLFVLG GFFYCKANGM DVSNVGLLPL CCFVVYILGF SLGFGPIPWL MMGEILPAKI
RGSAASVATA FNWTCTFVVT KSFLDMIKLI GAHGAFWLFG VICCIGMFFV IFCVPETQGK
TLEDIERKMM GRVRRMSSVA NIKPLSFNM
