TRET1_ANOGA
ID TRET1_ANOGA Reviewed; 793 AA.
AC Q7PIR5; A7UTR3; A9ZSY1;
DT 13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 3.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Facilitated trehalose transporter Tret1 {ECO:0000303|PubMed:20035867};
DE Short=AgTRET1 {ECO:0000303|PubMed:20035867};
GN Name=Tret1 {ECO:0000312|EMBL:BAF96742.1}; ORFNames=AGAP005563;
OS Anopheles gambiae (African malaria mosquito).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=7165;
RN [1] {ECO:0000305, ECO:0000312|EMBL:EAA44045.3}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING.
RC STRAIN=PEST {ECO:0000312|EMBL:EAA44045.3};
RX PubMed=12364791; DOI=10.1126/science.1076181;
RA Holt R.A., Subramanian G.M., Halpern A., Sutton G.G., Charlab R.,
RA Nusskern D.R., Wincker P., Clark A.G., Ribeiro J.M.C., Wides R.,
RA Salzberg S.L., Loftus B.J., Yandell M.D., Majoros W.H., Rusch D.B., Lai Z.,
RA Kraft C.L., Abril J.F., Anthouard V., Arensburger P., Atkinson P.W.,
RA Baden H., de Berardinis V., Baldwin D., Benes V., Biedler J., Blass C.,
RA Bolanos R., Boscus D., Barnstead M., Cai S., Center A., Chaturverdi K.,
RA Christophides G.K., Chrystal M.A.M., Clamp M., Cravchik A., Curwen V.,
RA Dana A., Delcher A., Dew I., Evans C.A., Flanigan M.,
RA Grundschober-Freimoser A., Friedli L., Gu Z., Guan P., Guigo R.,
RA Hillenmeyer M.E., Hladun S.L., Hogan J.R., Hong Y.S., Hoover J.,
RA Jaillon O., Ke Z., Kodira C.D., Kokoza E., Koutsos A., Letunic I.,
RA Levitsky A.A., Liang Y., Lin J.-J., Lobo N.F., Lopez J.R., Malek J.A.,
RA McIntosh T.C., Meister S., Miller J.R., Mobarry C., Mongin E., Murphy S.D.,
RA O'Brochta D.A., Pfannkoch C., Qi R., Regier M.A., Remington K., Shao H.,
RA Sharakhova M.V., Sitter C.D., Shetty J., Smith T.J., Strong R., Sun J.,
RA Thomasova D., Ton L.Q., Topalis P., Tu Z.J., Unger M.F., Walenz B.,
RA Wang A.H., Wang J., Wang M., Wang X., Woodford K.J., Wortman J.R., Wu M.,
RA Yao A., Zdobnov E.M., Zhang H., Zhao Q., Zhao S., Zhu S.C., Zhimulev I.,
RA Coluzzi M., della Torre A., Roth C.W., Louis C., Kalush F., Mural R.J.,
RA Myers E.W., Adams M.D., Smith H.O., Broder S., Gardner M.J., Fraser C.M.,
RA Birney E., Bork P., Brey P.T., Venter J.C., Weissenbach J., Kafatos F.C.,
RA Collins F.H., Hoffman S.L.;
RT "The genome sequence of the malaria mosquito Anopheles gambiae.";
RL Science 298:129-149(2002).
RN [2] {ECO:0000305, ECO:0000312|EMBL:BAF96742.1}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 290-793 (ISOFORM A), FUNCTION,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND SUBCELLULAR LOCATION.
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. 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. {ECO:0000269|PubMed:20035867}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=45.74 mM for trehalose {ECO:0000269|PubMed:20035867};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20035867};
CC Multi-pass membrane protein {ECO:0000255, ECO:0000269|PubMed:20035867}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=A {ECO:0000269|PubMed:12364791};
CC IsoId=Q7PIR5-1; Sequence=Displayed;
CC Name=B {ECO:0000269|PubMed:12364791}; Synonyms=C
CC {ECO:0000269|PubMed:12364791};
CC IsoId=Q7PIR5-2; Sequence=VSP_039518, VSP_039519;
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:20035867}.
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DR EMBL; AAAB01008960; EAA44045.3; -; Genomic_DNA.
DR EMBL; AAAB01008960; EDO63685.1; -; Genomic_DNA.
DR EMBL; AAAB01008960; EDO63686.1; -; Genomic_DNA.
DR EMBL; AB369548; BAF96742.1; -; mRNA.
DR RefSeq; XP_001688679.1; XM_001688627.1.
DR RefSeq; XP_001688680.1; XM_001688628.1.
DR RefSeq; XP_315568.3; XM_315568.4.
DR AlphaFoldDB; Q7PIR5; -.
DR SMR; Q7PIR5; -.
DR STRING; 7165.AGAP005563-PA; -.
DR PaxDb; Q7PIR5; -.
DR GeneID; 1276247; -.
DR KEGG; aga:AgaP_AGAP005563; -.
DR CTD; 1276247; -.
DR VEuPathDB; VectorBase:AGAP005563; -.
DR eggNOG; KOG0254; Eukaryota.
DR HOGENOM; CLU_016710_0_0_1; -.
DR InParanoid; Q7PIR5; -.
DR OMA; WFGRRIT; -.
DR OrthoDB; 430696at2759; -.
DR PhylomeDB; Q7PIR5; -.
DR Proteomes; UP000007062; Chromosome 2L.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0051119; F:sugar transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015574; F:trehalose transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
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 Alternative splicing; Cell membrane; Glycoprotein; Membrane;
KW Reference proteome; Sugar transport; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..793
FT /note="Facilitated trehalose transporter Tret1"
FT /id="PRO_0000395538"
FT TOPO_DOM 1..326
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 327..347
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 348..376
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 377..397
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 398..411
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 412..432
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 433..434
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 435..455
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 456..460
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 461..481
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 482..488
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 489..509
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 510..572
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 573..593
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 594..609
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 610..630
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 631..636
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 637..657
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 658..668
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 669..689
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255"
FT TOPO_DOM 690..703
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 704..724
FT /note="Helical; Name=11"
FT /evidence="ECO:0000255"
FT TOPO_DOM 725..737
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 738..758
FT /note="Helical; Name=12"
FT /evidence="ECO:0000255"
FT TOPO_DOM 759..793
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 99..148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 213..235
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 213..228
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 364
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..28
FT /note="MNRKVGPVLEYSRRFSRVLCALRDEIRD -> MVKILMRADTHVSFSVPIEE
FT PVAKCTFS (in isoform B)"
FT /evidence="ECO:0000303|PubMed:12364791"
FT /id="VSP_039518"
FT VAR_SEQ 29..331
FT /note="Missing (in isoform B)"
FT /evidence="ECO:0000303|PubMed:12364791"
FT /id="VSP_039519"
SQ SEQUENCE 793 AA; 88226 MW; 9A6B582919FDCAD7 CRC64;
MNRKVGPVLE YSRRFSRVLC ALRDEIRDPL QYGYQRVNTA EGSLSTSTTA TSLDTIVLDT
NAEDLASVPP RTLQHHQPQR TFSPILETDD TNPFLEPVEK AKSKSSLKSS RVSFDQEDDR
FDEDENSFRK QREHFQKHKS HSTSEHKSQL IKELRHLLAT DNRRQFQGKK HVSLDVKSAK
VLEQLLKASS SSDDFEGQRK EFQERKHKSL DARHISFKFD KEPSPSSSDE DFEPSTSLLR
IDADITKPVI IDLKDLDSSD EEDYISSRKH FQQSKSMSTD SRKSIRFLEM EMGTKEENMR
TAVPFVRQIT EEGKPKLEVY RPTTNPIYIW TQVLAALSVS LGSMVVGFSS AYTSPALVSM
KDRNITSFEV TDQSGSWVGG IMPLAGLAGG ILGGPMIEYL GRKNTILATA TPFIISWLLI
GCATHVAMVL VGRALSGLCV GIASLSLPVY LGETVQPEVR GTLGLLPTAF GNIGILLCFV
AGKYLDWSGL AFLGAALPIP FLLLMFLIPE TPRWYVSRNR EDRARKALQW LRGRKADVEP
ELKGISKSHQ DAERHASSSA MLDLLNKANL KPLLISLGLM FFQQLSGINA VIFYTVQIFQ
SAGSTIDEKL CTIIVGVVNF IATFIATVLI DRLGRKILLY ISDVAMIITL MTLGTFFYMK
NNGDDVSEIG WLPLAAFVVF VVGFSLGFGP IPWLMMGEIL PGKIRGSAAS VATAFNWSCT
FVVTKTFADI TASIGNHGAF WMFGSICIVG LLFVIVYVPE TQGKSLEDIE RKMMGRVRRM
SSVANIKPLS FNM
