TRET1_CULQU
ID TRET1_CULQU Reviewed; 517 AA.
AC B0WC46;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=Facilitated trehalose transporter Tret1 {ECO:0000250|UniProtKB:Q7PIR5};
GN Name=Tret1 {ECO:0000250|UniProtKB:Q7PIR5}; ORFNames=CPIJ004516;
OS Culex quinquefasciatus (Southern house mosquito) (Culex pungens).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Culicinae; Culicini; Culex; Culex.
OX NCBI_TaxID=7176;
RN [1] {ECO:0000312|EMBL:EDS43198.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JHB {ECO:0000312|EMBL:EDS43198.1};
RG The Broad Institute Genome Sequencing Platform;
RA Atkinson P.W., Hemingway J., Christensen B.M., Higgs S., Kodira C.D.,
RA Hannick L.I., Megy K., O'Leary S.B., Pearson M., Haas B.J., Mauceli E.,
RA Wortman J.R., Lee N.H., Guigo R., Stanke M., Alvarado L., Amedeo P.,
RA Antoine C.H., Arensburger P., Bidwell S.L., Crawford M., Camaro F.,
RA Devon K., Engels R., Hammond M., Howarth C., Koehrsen M., Lawson D.,
RA Montgomery P., Nene V., Nusbaum C., Puiu D., Romero-Severson J.,
RA Severson D.W., Shumway M., Sisk P., Stolte C., Zeng Q., Eisenstadt E.,
RA Fraser-Liggett C.M., Strausberg R., Galagan J., Birren B., Collins F.H.;
RT "Annotation of Culex pipiens quinquefasciatus.";
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
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; DS231885; EDS43198.1; -; Genomic_DNA.
DR RefSeq; XP_001846280.1; XM_001846228.1.
DR AlphaFoldDB; B0WC46; -.
DR SMR; B0WC46; -.
DR STRING; 7176.CPIJ004516-PA; -.
DR GeneID; 6036204; -.
DR KEGG; cqu:CpipJ_CPIJ004516; -.
DR VEuPathDB; VectorBase:CPIJ004516; -.
DR VEuPathDB; VectorBase:CQUJHB011511; -.
DR eggNOG; KOG0254; Eukaryota.
DR HOGENOM; CLU_001265_30_5_1; -.
DR InParanoid; B0WC46; -.
DR OMA; WFGRRIT; -.
DR OrthoDB; 430696at2759; -.
DR PhylomeDB; B0WC46; -.
DR Proteomes; UP000002320; Partially assembled 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..517
FT /note="Facilitated trehalose transporter Tret1"
FT /id="PRO_0000395541"
FT TOPO_DOM 1..56
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 57..77
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 78..100
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 101..121
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 122..135
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 136..156
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 157..158
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 159..179
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 180..184
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 185..205
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 206..212
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 213..233
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 234..296
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 297..317
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 318..333
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 334..354
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 355..360
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 361..381
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 382..392
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 393..413
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255"
FT TOPO_DOM 414..437
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 438..458
FT /note="Helical; Name=11"
FT /evidence="ECO:0000255"
FT TOPO_DOM 459..461
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 462..482
FT /note="Helical; Name=12"
FT /evidence="ECO:0000255"
FT TOPO_DOM 483..517
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 88
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 517 AA; 56343 MW; 86E821D670377311 CRC64;
MWIEIPECYE VLRNVFSKFR RHSLTAAMVK LLMRADTHVS FTVPAEEPVA KCTFSQVLAA
LSVSLGSMVV GFSSAYTSPA LVSMKDRNIT SFEVTDQSGS WVGGIMPLAG LVGGILGGPL
IEYLGRKNTI LATATPFIIS WLLIACATHV AMVLVGRALS GFSVGVASLS LPVYLGETVQ
PEVRGTLGLL PTAFGNIGIL LCFVAGNYMD WSELAFLGAT LPVPFLILMF LIPETPRWYV
SRGRDDRARK ALQWLRGKKA DVDPELKGII KSHQDAERHA SQSAMLDLLK KTNLKPLLIS
LGLMFFQQLS GINAVIFYTV QIFQDAGSTI DENLCTIIVG VVNFIATFIA TLLIDRLGRK
MLLYISDIAM IITLMTLGGF FYVKNNGGDV SHIGWLPLAS FVIFVLGFSL GFGPIPWLMM
GEILPGKIRG SAASVATAFN WSCTFVVTKT FADIIASIGT HGAFWMFGSV CVVGLVFVIM
YVPETQGKSL EDIERKMCGR VRRMSSVANI KPLSFNM
