TRET1_DROWI
ID TRET1_DROWI Reviewed; 872 AA.
AC B4MYA4;
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=GK22112;
OS Drosophila willistoni (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7260;
RN [1] {ECO:0000312|EMBL:EDW77093.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 14030-0811.24 {ECO:0000312|EMBL:EDW77093.1};
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; CH963894; EDW77093.1; -; Genomic_DNA.
DR RefSeq; XP_002066107.1; XM_002066071.2.
DR AlphaFoldDB; B4MYA4; -.
DR SMR; B4MYA4; -.
DR STRING; 7260.FBpp0251255; -.
DR EnsemblMetazoa; FBtr0252763; FBpp0251255; FBgn0224097.
DR GeneID; 6643376; -.
DR KEGG; dwi:6643376; -.
DR eggNOG; KOG0254; Eukaryota.
DR HOGENOM; CLU_016710_0_0_1; -.
DR InParanoid; B4MYA4; -.
DR OMA; IFIWTQS; -.
DR OrthoDB; 430696at2759; -.
DR PhylomeDB; B4MYA4; -.
DR Proteomes; UP000007798; 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..872
FT /note="Facilitated trehalose transporter Tret1"
FT /id="PRO_0000395549"
FT TOPO_DOM 1..406
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 407..427
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 428..454
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 455..475
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 476..488
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 489..509
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 510..511
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 512..532
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 533..538
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 539..559
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 560..566
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 567..587
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 588..650
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 651..671
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 672..687
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 688..708
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 709..714
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 715..735
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 736..755
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 756..776
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255"
FT TOPO_DOM 777..784
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 785..803
FT /note="Helical; Name=11"
FT /evidence="ECO:0000255"
FT TOPO_DOM 804..816
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 817..837
FT /note="Helical; Name=12"
FT /evidence="ECO:0000255"
FT TOPO_DOM 838..872
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 53..217
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 262..281
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 293..315
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 340..361
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 53..68
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 82..101
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 103..117
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 119..144
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 170..192
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 193..208
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 297..315
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 262
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A1Z8N1"
FT MOD_RES 263
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A1Z8N1"
FT MOD_RES 264
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A1Z8N1"
FT MOD_RES 334
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A1Z8N1"
FT MOD_RES 336
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A1Z8N1"
FT MOD_RES 860
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A1Z8N1"
FT MOD_RES 861
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A1Z8N1"
FT CARBOHYD 442
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 872 AA; 96531 MW; 5AA1ABE731333DA9 CRC64;
MSGRDNRGAG GGGGGGGGGS GGGHHHHQPL SSAMGKLKEK LTRVGDDLGY HRVESNLSTS
NTATSLDTIL PEDPFLFPQE APQRHPQQSP SQSQQQQRRF LDDEPPLSFR PLLEDDDINE
PPTQQQPQQQ HQQQHRSPLS ASGSLELTPL PPPPTTLEPR DRQQRSIPGE DLQRSKQSLK
GSRVSFEKTN SKQAAESSDE DSFEDKRIGF QQQKATSVDH KGILKDLKHI LANDNRRQFQ
AKKHVSLDVK GTRFLQDLLK ESSSEEEFHK TRREFQGRKH QSLDPRVTFK LDKVLQGSST
DSDEEGDDAE HKRLIHRPKD ITKPVIIDLK DLESESDEDF LTSRQHFQQQ RSISTDSRKS
RRLYEMDDMG NKRGDNIRHA VPFVRQITED GKPKLEVYRP TTNPIYIWTQ VLAALSVSLG
SLVVGFVSAY TSPALITMTN GNITSFEVTP QAASWVGGIM PLAGLLGGIA GGPFIEYLGR
RNTILTTAVP FIVSSLLIAC AVNITMVLLG RFLAGFCVGI ASLSLPVYLG ETVQPEVRGT
LGLLPTAFGN IGILLCFVAG TYMDWSMLAF LGAALPVPFL ILMFLIPETP RWYVSRGREE
RARKALSWLR GKEADVEPEL KGLLRSQADA DRSATQNTML ELLKRNNLKP LSISLGLMFF
QQLSGINAVI FYTVQIFKDA GSTIDGNVCT IIVGIVNFMA TFIGIILIDR AGRKILLYVS
NVAMIITLFV LGGFFYCKDK AGIDVSNVGW LPLSCFVVYI LGFSLGFGPI PWLMMGEILP
AKIRGSAASV ATAFNWTCTF VVTKTFQDML DVIGSYGAFW LFGAICFIGL FFVIIYVPET
QGKTLEDIER KMMGRVRRMS SVANIKPLSF NM
