TRET1_DROAN
ID TRET1_DROAN Reviewed; 866 AA.
AC B3MG58;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 13-JUL-2010, sequence version 2.
DT 25-MAY-2022, entry version 55.
DE RecName: Full=Facilitated trehalose transporter Tret1 {ECO:0000250|UniProtKB:A1Z8N1};
GN Name=Tret1 {ECO:0000250|UniProtKB:A1Z8N1}; ORFNames=GF13114;
OS Drosophila ananassae (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7217;
RN [1] {ECO:0000312|EMBL:EDV36753.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 14024-0371.13 {ECO:0000312|EMBL:EDV36753.1};
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=EDV36753.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; CH902619; EDV36753.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_001959931.2; XM_001959895.2.
DR AlphaFoldDB; B3MG58; -.
DR SMR; B3MG58; -.
DR STRING; 7217.FBpp0116306; -.
DR EnsemblMetazoa; FBtr0391456; FBpp0350904; FBgn0090147.
DR GeneID; 6495957; -.
DR KEGG; dan:6495957; -.
DR eggNOG; KOG0254; Eukaryota.
DR InParanoid; B3MG58; -.
DR OrthoDB; 430696at2759; -.
DR Proteomes; UP000007801; 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..866
FT /note="Facilitated trehalose transporter Tret1"
FT /id="PRO_0000395542"
FT TOPO_DOM 1..399
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 400..420
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 421..449
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 450..470
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 471..482
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 483..503
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 504..506
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 507..527
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 528..533
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 534..554
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 555..561
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 562..582
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 583..651
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 652..672
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 673..682
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 683..703
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 704..709
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 710..730
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 731..749
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 750..770
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255"
FT TOPO_DOM 771..776
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 777..797
FT /note="Helical; Name=11"
FT /evidence="ECO:0000255"
FT TOPO_DOM 798..810
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 811..831
FT /note="Helical; Name=12"
FT /evidence="ECO:0000255"
FT TOPO_DOM 832..866
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 67..212
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 282..311
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 335..357
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 109..127
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 156..170
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 292..311
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 257
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A1Z8N1"
FT MOD_RES 258
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A1Z8N1"
FT MOD_RES 259
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A1Z8N1"
FT MOD_RES 329
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 854
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A1Z8N1"
FT MOD_RES 855
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A1Z8N1"
FT CARBOHYD 437
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 866 AA; 95862 MW; FAE9B03B4D4B0451 CRC64;
MSGRDNRGAG GGGGGGGGGG HQPLSSAMGK LKEKLTRVGD ELGYHRVESN LSTSNTATSL
DTILPEDPFL FPQVSPQRHP QSTVRTQRLL EDEPPLSFRP LLEDDDINEP PTQQLTTQQQ
RTPLRASGSL ELTPLPPPPT SLEIREHRDR QQRSAQVAAE ELQRSKQSLK GSRVSFERRD
TGNSNSNKQA ESSDEDSFEE RRTGFQQQKA TSVDHKGILK DLKHILANDN RRQFQAKKHV
SLDVKGTRFL QDLLKESSSE EEFHKTRREF QGRKHQSLDP RVTFKLDKVL QGSSTDSDEE
GDDAEHKRLI HRPKDITKPV IIDLKDLESE SDEDFHTSRQ HFQQQRSIST DSRKSRRLYE
MDEMGNKRGE NIRHAVPFVR QITEDGKPKL EVYRPTTNPI FIWTQVLAAL SVSLGSLVVG
FVSAYTSPAL VSMVDRNITS FEVTPQAASW VGGIMPLAGL AGGIAGGPFI EYLGRRNTIL
ATAVPFIVSS LLIACAVNVA MVLAGRFLAG FCVGIASLSL PVYLGETVQP EVRGTLGLLP
TAFGNIGILL CFVAGTYMDW SMLAFLGAAL PVPFLVLMFL IPETPRWFVS RGREERARKA
LSWLRGKEAD VEPELKGLMR SQADADRQGT QNTMLELLKR SNFKPLSISL GLMFFQQLSG
INAVIFYTVS IFKDAGSTID GNVCTIIVGV VNFLATFIAT LLIDRAGRKI LLYVSNIAMI
ITLFVLGGFF YCKAHGPDVS HLGWLPLSCF VIYILGFSLG FGPIPWLMMG EILPAKIRGS
AASVATAFNW TCTFVVTKTF QDMIDVMGAH GAFWLFGAIC FIGLFFVILY VPETQGKTLE
DIERKMMGRV RRMSSVANIK PLSFNM
