TRET1_DROPE
ID TRET1_DROPE Reviewed; 869 AA.
AC B4GAP7;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 13-JUL-2010, sequence version 2.
DT 25-MAY-2022, entry version 51.
DE RecName: Full=Facilitated trehalose transporter Tret1 {ECO:0000250|UniProtKB:A1Z8N1};
GN Name=Tret1 {ECO:0000250|UniProtKB:A1Z8N1}; ORFNames=GL11419;
OS Drosophila persimilis (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7234;
RN [1] {ECO:0000312|EMBL:EDW31999.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MSH-3 / Tucson 14011-0111.49 {ECO:0000312|EMBL:EDW31999.1};
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=EDW31999.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; CH479181; EDW31999.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_002016109.1; XM_002016073.1.
DR AlphaFoldDB; B4GAP7; -.
DR SMR; B4GAP7; -.
DR STRING; 7234.FBpp0175526; -.
DR eggNOG; KOG0254; Eukaryota.
DR Proteomes; UP000008744; 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..869
FT /note="Facilitated trehalose transporter Tret1"
FT /id="PRO_0000395546"
FT TOPO_DOM 1..404
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 405..425
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 426..452
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 453..473
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 474..485
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 486..506
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 507..509
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 510..530
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 531..536
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 537..557
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 558..564
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 565..585
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 586..654
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 655..675
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 676..685
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 686..706
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 707..712
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 713..733
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 734..752
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 753..773
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255"
FT TOPO_DOM 774..779
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 780..800
FT /note="Helical; Name=11"
FT /evidence="ECO:0000255"
FT TOPO_DOM 801..813
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 814..834
FT /note="Helical; Name=12"
FT /evidence="ECO:0000255"
FT TOPO_DOM 835..869
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..214
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 258..315
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 336..368
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 41..57
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 75..92
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 114..131
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 172..194
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 258..285
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 295..315
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 353..368
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 260
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A1Z8N1"
FT MOD_RES 261
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A1Z8N1"
FT MOD_RES 262
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A1Z8N1"
FT MOD_RES 332
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 857
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A1Z8N1"
FT MOD_RES 858
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A1Z8N1"
FT CARBOHYD 440
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 869 AA; 96826 MW; AEB1C087B5C3435E CRC64;
MSGRDNRGAG GGGGGHQPLS SAMGKLKEKL TRAGDDQGYH RVESNLSTSN TATSLDTILP
EDPFLFPQAA PQRHPLPRPQ QQQQQQQRQQ LRLLEDEPPL SFRPLLEDDD INEPPTQPFQ
QQQQRTPLRA SGSLELTPLP PPPTSQEIRE HRDRQQRSVP VPVEDLQRSK QSLKGSRVSF
EKNNASSKPP AQAESSDEDS FEDKRIGFQQ QKATSVDHKG ILKDLKHILA NDNRRQFQAK
KHVSLDVKGT RFLQDLLKES SSEEEFHKTR REFQGRKHQS LDPRVTFKLD KVLQGSSTDS
DEEGDDPEHK RLIHRPKDIT KPLIIDLKDL ESESDEDFHT SRQHFQQQRS ISTDSRKSRR
PYEMDEMGNK RGENIRHAVP FVRQITEDGK PKLEVYRPTT NPIYIWTQVL AALSVSLGSL
VVGFVSAYTS PALVSMTNRN MTSFEVTPQA ASWVGGIMPL AGLAGGIAGG PFIEYLGRRN
TILATAIPFI VSSLLIACAV NVAMVLAGRF LAGFCVGIAS LSLPVYLGET VQPEVRGTLG
LLPTAFGNIG ILLCFVAGTY MDWSMLAFLG AALPVPFLIL MFLIPETPRW FVSRGREEKA
RKALSWLRGK EADVEPELKG LMRSQADADR QATQNKMMEL LKRNNLKPLS ISLGLMFFQQ
LSGINAVIFY TVSIFKDAGS TIDGNLCTII VGIVNFMATF IATLLIDRAG RKILLYVSNI
AMIITLFVLG GFFYCKSHGQ DVSQLGWLPL SCFVIYILGF SLGFGPIPWL MMGEILPSKI
RGSAASVATA FNWSCTFVVT KTFQDMIDFM GAHGAFWLFG SICFIGLFFV ILYVPETQGK
TLEDIERKMM GRVRRMSSVA NMKPLAFNM
