TRE11_DROSE
ID TRE11_DROSE Reviewed; 857 AA.
AC B4HNS0;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 25-MAY-2022, entry version 58.
DE RecName: Full=Facilitated trehalose transporter Tret1-1 {ECO:0000250|UniProtKB:A1Z8N1};
GN Name=Tret1-1 {ECO:0000250|UniProtKB:A1Z8N1}; ORFNames=GM21298;
OS Drosophila sechellia (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7238;
RN [1] {ECO:0000312|EMBL:EDW47435.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Rob3c / Tucson 14021-0248.25 {ECO:0000312|EMBL:EDW47435.1};
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; CH480816; EDW47435.1; -; Genomic_DNA.
DR RefSeq; XP_002033422.1; XM_002033386.1.
DR AlphaFoldDB; B4HNS0; -.
DR SMR; B4HNS0; -.
DR STRING; 7238.B4HNS0; -.
DR EnsemblMetazoa; FBtr0204283; FBpp0202775; FBgn0176179.
DR GeneID; 6608698; -.
DR KEGG; dse:6608698; -.
DR HOGENOM; CLU_016710_0_0_1; -.
DR OMA; IFIWTQS; -.
DR PhylomeDB; B4HNS0; -.
DR ChiTaRS; Tret1-1; fly.
DR Proteomes; UP000001292; 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..857
FT /note="Facilitated trehalose transporter Tret1-1"
FT /id="PRO_0000395532"
FT TOPO_DOM 1..392
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 393..413
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 414..440
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 441..461
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 462..473
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 474..494
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 495..497
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 498..518
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 519..528
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 529..549
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 550..552
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 553..573
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 574..636
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 637..657
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 658..673
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 674..694
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 695..700
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 701..721
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 722..740
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 741..761
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255"
FT TOPO_DOM 762..767
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 768..788
FT /note="Helical; Name=11"
FT /evidence="ECO:0000255"
FT TOPO_DOM 789..801
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 802..822
FT /note="Helical; Name=12"
FT /evidence="ECO:0000255"
FT TOPO_DOM 823..857
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 92..203
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 327..346
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 103..118
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 133..148
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 167..182
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 248
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A1Z8N1"
FT MOD_RES 249
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A1Z8N1"
FT MOD_RES 250
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A1Z8N1"
FT MOD_RES 320
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 845
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A1Z8N1"
FT MOD_RES 846
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A1Z8N1"
FT CARBOHYD 428
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 550
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 857 AA; 95050 MW; B863BB58C5C00131 CRC64;
MSGRDNRGAG GGGGGHQPLS NAMGKLKEKL TRVGDELGYH RVESNLSTSN TATSLDTILP
EDPFLFPQVS PQRHPQNIVR TQLLLEDEPP LSFRPLLEDD DINEPPTQQQ QRTPLRASGS
LELTPLPPPP TSLEIREHRD RQQRGAQGDD LQRSKQSLKG SRVSFERRDT GNSNTNSNKA
AESSDEDSFE EKRTGFQQQK ATSVDHKGIL KDLKHILAND NRRQFQAKKH VSLDVKGTRF
LQDLLKESSS EEEFHKTRRE FQGRKHQSLD PRVTFKLDKV LQGSSTDSDE EGEDAEHKRL
IHRPKDITKP VIIDLKDLES ESDEDFLTSR QHFQQQRSIS TDSRKSRRLY EMDEMGNKRG
ENIRHAVPFV RQITEDGKPK LEVYRPTTNP IYIWTQVLAA LSVSLGSLVV GFVSAYTSPA
LVSMTDRNIT SFEVTQDAGS WVGGIMPLAA LAGGITGGPL IEYLGRRNTI LATAVPFIVS
SLLIACAVNV AMVLCGRFLA GFCVGIASLS LPVYLGETVQ PEVRGTLGLL PTAFGNIGIL
LCFVAGSFMN WSMLAFLGAA LPVPFLILMF LIPETPRWFV GRGLEERARK ALKWLRGKEA
DVEPELKGLM RSQADADRQA SRNTMLELLK LNNLKPLSIS LGLMFFQQFS GINAVIFYTV
QIFKDAGSTI DGNLCTIIVG IVNFLATFIG IVLIDRAGRK ILLYVSDIAM VLTLFVLGGF
FYCKANGPDV SHLGWLPLTC FVIYILGFSL GFGPIPWLMM GEILPAKIRG SAASVATAFN
WFCTFVVTKT FQDLTVAMGA HGAFWLFGAI CFVGLFFVII YVPETQGKTL EDIERKMMGR
VRRMSSVANI KPLSFNM
