TRET1_AEDAE
ID TRET1_AEDAE Reviewed; 806 AA.
AC Q17NV8;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 1.
DT 25-MAY-2022, entry version 90.
DE RecName: Full=Facilitated trehalose transporter Tret1 {ECO:0000250|UniProtKB:Q7PIR5};
GN Name=Tret1 {ECO:0000250|UniProtKB:Q7PIR5}; ORFNames=AAEL000567;
OS Aedes aegypti (Yellowfever mosquito) (Culex aegypti).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Culicinae; Aedini; Aedes; Stegomyia.
OX NCBI_TaxID=7159;
RN [1] {ECO:0000312|EMBL:EAT48366.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LVPib12;
RX PubMed=17510324; DOI=10.1126/science.1138878;
RA Nene V., Wortman J.R., Lawson D., Haas B.J., Kodira C.D., Tu Z.J.,
RA Loftus B.J., Xi Z., Megy K., Grabherr M., Ren Q., Zdobnov E.M., Lobo N.F.,
RA Campbell K.S., Brown S.E., Bonaldo M.F., Zhu J., Sinkins S.P.,
RA Hogenkamp D.G., Amedeo P., Arensburger P., Atkinson P.W., Bidwell S.L.,
RA Biedler J., Birney E., Bruggner R.V., Costas J., Coy M.R., Crabtree J.,
RA Crawford M., DeBruyn B., DeCaprio D., Eiglmeier K., Eisenstadt E.,
RA El-Dorry H., Gelbart W.M., Gomes S.L., Hammond M., Hannick L.I.,
RA Hogan J.R., Holmes M.H., Jaffe D., Johnston S.J., Kennedy R.C., Koo H.,
RA Kravitz S., Kriventseva E.V., Kulp D., Labutti K., Lee E., Li S.,
RA Lovin D.D., Mao C., Mauceli E., Menck C.F., Miller J.R., Montgomery P.,
RA Mori A., Nascimento A.L., Naveira H.F., Nusbaum C., O'Leary S.B., Orvis J.,
RA Pertea M., Quesneville H., Reidenbach K.R., Rogers Y.-H.C., Roth C.W.,
RA Schneider J.R., Schatz M., Shumway M., Stanke M., Stinson E.O.,
RA Tubio J.M.C., Vanzee J.P., Verjovski-Almeida S., Werner D., White O.R.,
RA Wyder S., Zeng Q., Zhao Q., Zhao Y., Hill C.A., Raikhel A.S., Soares M.B.,
RA Knudson D.L., Lee N.H., Galagan J., Salzberg S.L., Paulsen I.T.,
RA Dimopoulos G., Collins F.H., Bruce B., Fraser-Liggett C.M., Severson D.W.;
RT "Genome sequence of Aedes aegypti, a major arbovirus vector.";
RL Science 316:1718-1723(2007).
CC -!- FUNCTION: High-capacity facilitative transporter for trehalose. Does
CC not 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:Q7PIR5}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q7PIR5,
CC ECO:0000255}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q7PIR5, ECO:0000255}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily. Sugar
CC transporter (TC 2.A.1.1) family. Trehalose transporter subfamily.
CC {ECO:0000250|UniProtKB:Q7PIR5, ECO:0000255}.
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DR EMBL; CH477196; EAT48366.1; -; Genomic_DNA.
DR RefSeq; XP_001648649.1; XM_001648599.1.
DR AlphaFoldDB; Q17NV8; -.
DR SMR; Q17NV8; -.
DR STRING; 7159.AAEL000567-PA; -.
DR VEuPathDB; VectorBase:AAEL014972; -.
DR eggNOG; KOG0254; Eukaryota.
DR HOGENOM; CLU_016710_0_0_1; -.
DR InParanoid; Q17NV8; -.
DR OMA; IFIWTQS; -.
DR PhylomeDB; Q17NV8; -.
DR Proteomes; UP000008820; 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; Reference proteome; Sugar transport;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..806
FT /note="Facilitated trehalose transporter Tret1"
FT /id="PRO_0000395537"
FT TOPO_DOM 1..339
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 340..360
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 361..389
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 390..410
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 411..424
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 425..445
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 446..447
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 448..468
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 469..473
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 474..494
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 495..501
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 502..522
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 523..585
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 586..606
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 607..622
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 623..643
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 644..649
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 650..670
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 671..681
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 682..702
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255"
FT TOPO_DOM 703..723
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 724..744
FT /note="Helical; Name=11"
FT /evidence="ECO:0000255"
FT TOPO_DOM 745..750
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 751..771
FT /note="Helical; Name=12"
FT /evidence="ECO:0000255"
FT TOPO_DOM 772..806
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 48..138
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 15..34
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 48..66
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 101..138
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 377
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 806 AA; 89257 MW; 6E2FAA2A1690AFB3 CRC64;
MFGNEMDDTR DPLQYGYQRV NTGEGSLSTS TTGTSLDTIV LDTNAEDLNS TPRVGAQRTF
SPILETDDTN PFLDPPPPGQ KSPPAVGEAK AKSKSSLKGS RVSFDQEDRF DETDEGFRKQ
REHFQKHKSH STSEHKNQLI KELRHLLAAD NRRQFQGKKH VSLDVQSSKV LEELLKASSS
EDDFEGQRKQ FQERKHKSLD ARHISFKFEK EPTPSSSEED FEPSTSLLKI DADITKPVII
DLKVNRAQSD QALTQFQKNL AHFQDLESSE DEDYISSRKH FQQAKSMSTD SRKSNKSIRF
FEMEMGTKEE NIRTAVPFVR QITEDGKPKL EVYRPTTNPI FIWTQVLAAL SVSLGSMVVG
FSSAYTSPAL VSMKDRNITS FEVTDQSGSW VGGIMPLAGL AGGILGGPLI EYLGRKNTIL
ATATPFIISW LLIACATHVA MVLVGRALSG FSVGVASLSL PVYLGETVQP EVRGTLGLLP
TAFGNIGILL CFVAGKYMDW SGLAFLGAAL PIPFLLLMFL IPETPRWYVS RGRDDRARKA
LQWLRGKKAD VDPELKGIIK SHQDAERHAS QSAMLDLMKK ANLKPLLISL GLMFFQQLSG
INAVIFYTVQ IFQDAGSTID ENLCTIIVGV VNFIATFIAT MLIDRLGRKM LLYISDVAMI
ITLMTLGGFF YVKNSGQDVS QVGWLPLAAF VIYVLGFSLG FGPIPWLMMG EILPGKIRGS
AASVATAFNW SCTFIVTKTF ADIINAIGTH GTFWMFGSIC VIGLAFVIFY VPETQGKSLE
DIERKMMGRV RRMSSVANIK PLSFNM
