TRET1_POLVA
ID TRET1_POLVA Reviewed; 504 AA.
AC A5LGM7;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 1.
DT 25-MAY-2022, entry version 51.
DE RecName: Full=Facilitated trehalose transporter Tret1 {ECO:0000303|PubMed:17606922, ECO:0000312|EMBL:BAF63703.1};
DE Short=PvTret1 {ECO:0000303|PubMed:20035867};
GN Name=Tret1 {ECO:0000312|EMBL:BAF63703.1};
OS Polypedilum vanderplanki (Sleeping chironomid midge).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Chironomoidea; Chironomidae;
OC Chironominae; Polypedilum; Polypedilum.
OX NCBI_TaxID=319348;
RN [1] {ECO:0000305, ECO:0000312|EMBL:BAF63703.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES,
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=17606922; DOI=10.1073/pnas.0702538104;
RA Kikawada T., Saito A., Kanamori Y., Nakahara Y., Iwata K., Tanaka D.,
RA Watanabe M., Okuda T.;
RT "Trehalose transporter 1, a facilitated and high-capacity trehalose
RT transporter, allows exogenous trehalose uptake into cells.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:11585-11590(2007).
RN [2] {ECO:0000305}
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=20035867; DOI=10.1016/j.ibmb.2009.12.006;
RA Kanamori Y., Saito Y., Hagiwara-Komoda Y., Tanaka D., Mitsumasu K.,
RA Kikuta S., Watanabe M., Cornette R., Kikawada T., Okuda T.;
RT "The trehalose transporter 1 gene sequence is conserved in insects and
RT encodes proteins with different kinetic properties involved in trehalose
RT import into peripheral tissues.";
RL Insect Biochem. Mol. Biol. 40:30-37(2010).
CC -!- FUNCTION: High-capacity facilitative transporter for trehalose,
CC required to induce anhydrobiosis. Anhydrobiotic larvae can survive
CC almost complete dehydration. Does not transport maltose, sucrose or
CC lactose. Mediates the bidirectional transfer of trehalose. Responsible
CC for the transport of trehalose synthesized in the fat body and the
CC incorporation of trehalose into other tissues that require a carbon
CC source, thereby regulating trehalose levels in the hemolymph.
CC {ECO:0000269|PubMed:17606922, ECO:0000269|PubMed:20035867}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=114.5 mM for trehalose {ECO:0000269|PubMed:17606922,
CC ECO:0000269|PubMed:20035867};
CC pH dependence:
CC Wide extracellular pH range, between 4.0 and 9.0.
CC {ECO:0000269|PubMed:17606922, ECO:0000269|PubMed:20035867};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17606922,
CC ECO:0000269|PubMed:20035867}; Multi-pass membrane protein {ECO:0000255,
CC ECO:0000269|PubMed:17606922, ECO:0000269|PubMed:20035867}.
CC -!- TISSUE SPECIFICITY: Highest expression in the fat body. Not expressed
CC in other tissues including the midgut, muscle, and integuments after 24
CC h of dehydration. {ECO:0000269|PubMed:17606922,
CC ECO:0000269|PubMed:20035867}.
CC -!- INDUCTION: By hypersalinity. {ECO:0000269|PubMed:17606922}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily. Sugar
CC transporter (TC 2.A.1.1) family. Trehalose transporter subfamily.
CC {ECO:0000255, ECO:0000269|PubMed:17606922}.
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DR EMBL; AB272983; BAF63703.1; -; mRNA.
DR AlphaFoldDB; A5LGM7; -.
DR SMR; A5LGM7; -.
DR TCDB; 2.A.1.1.129; the major facilitator superfamily (mfs).
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0051119; F:sugar transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0015574; F:trehalose transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0015771; P:trehalose transport; IDA: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 1: Evidence at protein level;
KW Cell membrane; Glycoprotein; Membrane; Stress response; Sugar transport;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..504
FT /note="Facilitated trehalose transporter Tret1"
FT /id="PRO_0000395551"
FT TOPO_DOM 1..39
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 40..60
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 61..87
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 88..108
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 109..120
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 121..141
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 142..145
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 146..166
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 167..171
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 172..192
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 193..199
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 200..220
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 221..283
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 284..304
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 305..320
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 321..341
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 342..347
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 348..368
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 369..387
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 388..408
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255"
FT TOPO_DOM 409..424
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 425..445
FT /note="Helical; Name=11"
FT /evidence="ECO:0000255"
FT TOPO_DOM 446..448
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 449..469
FT /note="Helical; Name=12"
FT /evidence="ECO:0000255"
FT TOPO_DOM 470..504
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 73
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 197
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 504 AA; 55057 MW; F317E6BA365ED7C8 CRC64;
MELNNKEDSP RHTVPFVRQI TEDGKAKLEI YRPTTNPIYI YTQILAAIAV SMGSMVVGFA
SAYTSPALVS MQNTTITSFK VTEQEASWVG GIMPLAGLAG GIAGGPFIEY LGRKNTILAT
AVPFIVAWLL IAFANSIWMV LAGRALSGFC VGIASLSLPV YLGETVQPEV RGTLGLLPTA
FGNIGILICF VAGKYVNWSG LAFIGSILPI PFMVLTLLIP ETPRWFVTRG REERARKALQ
WLRGKKADVE PELKGIVKSH CEAERHASQN AIFDLMKRSN LKPLLIALGL MFFQQLSGIN
AVIFYTVSIF KDAGSTIDEN LCTIIVGVVN FGATFFATVL IDRLGRKILL YISEVAMVIT
LLTLGTFFYY KNSGNDVSNI GWLPLASFVI YVIGFSSGVG PIPWLMLGEI LPGKIRGSAA
SVATGFNWTC TFIVTKTFAD IVAAIGNHGA FWFFGVICLI GLFFVIFFVP ETQGKSLEEI
ERKMMGRVRR MSSVANMKPL SFNM
