TRET1_DROMO
ID TRET1_DROMO Reviewed; 863 AA.
AC B4KR05;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 13-JUL-2010, sequence version 2.
DT 25-MAY-2022, entry version 57.
DE RecName: Full=Facilitated trehalose transporter Tret1 {ECO:0000250|UniProtKB:A1Z8N1};
GN Name=Tret1 {ECO:0000250|UniProtKB:A1Z8N1}; ORFNames=GI18572;
OS Drosophila mojavensis (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila.
OX NCBI_TaxID=7230;
RN [1] {ECO:0000312|EMBL:EDW10361.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 15081-1352.22 {ECO:0000312|EMBL:EDW10361.1};
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=EDW10361.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; CH933808; EDW10361.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_002006426.2; XM_002006390.2.
DR AlphaFoldDB; B4KR05; -.
DR SMR; B4KR05; -.
DR STRING; 7230.FBpp0167789; -.
DR EnsemblMetazoa; FBtr0425257; FBpp0383036; FBgn0141311.
DR GeneID; 6580597; -.
DR KEGG; dmo:Dmoj_GI18572; -.
DR eggNOG; KOG0254; Eukaryota.
DR InParanoid; B4KR05; -.
DR OrthoDB; 430696at2759; -.
DR Proteomes; UP000009192; 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..863
FT /note="Facilitated trehalose transporter Tret1"
FT /id="PRO_0000395545"
FT TOPO_DOM 1..398
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 399..419
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 420..446
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 447..467
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 468..479
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 480..500
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 501..503
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 504..524
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 525..530
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 531..551
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 552..558
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 559..579
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 580..642
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 643..663
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 664..679
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 680..700
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 701..706
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 707..727
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 728..746
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 747..767
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255"
FT TOPO_DOM 768..773
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 774..794
FT /note="Helical; Name=11"
FT /evidence="ECO:0000255"
FT TOPO_DOM 795..807
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 808..828
FT /note="Helical; Name=12"
FT /evidence="ECO:0000255"
FT TOPO_DOM 829..863
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..208
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 286..307
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 332..354
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 46..60
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 88..110
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 113..130
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 155..188
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 289..307
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 254
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A1Z8N1"
FT MOD_RES 255
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A1Z8N1"
FT MOD_RES 256
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A1Z8N1"
FT MOD_RES 326
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A1Z8N1"
FT MOD_RES 328
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A1Z8N1"
FT MOD_RES 851
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A1Z8N1"
FT MOD_RES 852
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A1Z8N1"
FT CARBOHYD 434
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 863 AA; 95705 MW; 9751E08A88802226 CRC64;
MSGRDNRGAG GGGGGGHHHQ PLSSAMGKLK EKLTRAGEEL GYHRVESNLS ASNTGTSLDT
ILPEDPFPFP QAAPQRHPQQ QFPHLHPLRL LHDVDDEPPL SFRPLLEDDD INEPPQQIQQ
QRSALRSSGS LELTPLPPPP TSLEPHRDRQ QRSIVTGGEE LQRSKQSLKG SRVSFEKPQQ
QGNNKAAESS DEDSFEDKRI GFQQQKATSV DHKGILKDLR HILANDNRRQ FQAKKHVSLD
IKGTRFLQDL LKDSSSEEEF HKTRREFQGR KHQSLDPRVT FKLDKVLQGS STDSDEEGDD
AEHKRLIHRP KDITKPVIID LKDLESESDE DFLTSRQNFQ QQRSISTDSR KSRRLYEMDE
MGNKRGDNIR HAVPFVRQIT EDGKPKLEVY RPTTNPIYIW TQVLAALSVS LGSLVVGFAS
AYTSPALVSM TNTNLTSFVV TPQAASWVGG IMPLAGLAGG IAGGPFIEYL GRRNTILATA
VPFIISWLLI ACAVNVVMVL CGRFLAGFCV GIASLSLPVY LGETVQPEVR GTLGLLPTAF
GNIGILLCFV AGTYMDWSML AFLGGTLPVP FLILMFLIPE TPRWYVSRGR EERARKALVW
LRGKEADVEP ELKGLMRSQA DADRQATQNT MLELLKRSNL KPLSISLGLM FFQQLSGINA
VIFYTVQIFQ DAGSTIDGNV CTIIVGVVNF MATFIATVLI DRAGRKILLY VSNVAMILTL
FVLGGFFYCK STGMDTSNVG WLPLSCFVVY ILGFSLGFGP IPWLMMGEIL PAKIRGSAAS
VATAFNWSCT FVVTKSFQDM IDVMGAHGAF WMFGAICFVG LFFVIFYVPE TQGKTLEDIE
RKMMGRVRRM SSVANIKPLS FNM
