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TRE12_DROME
ID   TRE12_DROME             Reviewed;         488 AA.
AC   Q8MKK4; A1Z8N4;
DT   13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 158.
DE   RecName: Full=Facilitated trehalose transporter Tret1-2 homolog {ECO:0000303|PubMed:20035867};
DE            Short=DmTret1-2 {ECO:0000303|PubMed:20035867};
GN   Name=Tret1-2 {ECO:0000312|EMBL:BAF96745.1}; ORFNames=CG8234;
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:BAF96745.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], LACK OF FUNCTION, AND SUBCELLULAR LOCATION.
RC   STRAIN=Canton-S {ECO:0000312|EMBL:BAF96745.1};
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).
RN   [2] {ECO:0000312|EMBL:AAM68715.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley;
RX   PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA   Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA   Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA   George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA   Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA   Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA   Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA   An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA   Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA   Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA   Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA   Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA   Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA   Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA   Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA   Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA   Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA   Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA   Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA   Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA   Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA   Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA   McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA   Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA   Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA   Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA   Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA   Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA   Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA   Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA   Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA   Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA   Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA   Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA   Venter J.C.;
RT   "The genome sequence of Drosophila melanogaster.";
RL   Science 287:2185-2195(2000).
RN   [3] {ECO:0000305, ECO:0000312|EMBL:AAM68715.1}
RP   GENOME REANNOTATION.
RC   STRAIN=Berkeley;
RX   PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA   Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA   Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA   Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA   Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA   Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA   Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT   "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT   review.";
RL   Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN   [4] {ECO:0000312|EMBL:AAM52591.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Berkeley {ECO:0000269|PubMed:12537569};
RC   TISSUE=Testis {ECO:0000269|PubMed:12537569};
RX   PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA   Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA   Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA   Celniker S.E.;
RT   "A Drosophila full-length cDNA resource.";
RL   Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
CC   -!- FUNCTION: Fails to transport 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   -!- 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}.
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DR   EMBL; AB369551; BAF96745.1; -; mRNA.
DR   EMBL; AE013599; AAM68715.1; -; Genomic_DNA.
DR   EMBL; AY122079; AAM52591.1; -; mRNA.
DR   RefSeq; NP_610694.1; NM_136850.4.
DR   AlphaFoldDB; Q8MKK4; -.
DR   SMR; Q8MKK4; -.
DR   STRING; 7227.FBpp0087180; -.
DR   GlyGen; Q8MKK4; 2 sites.
DR   PaxDb; Q8MKK4; -.
DR   PRIDE; Q8MKK4; -.
DR   DNASU; 36249; -.
DR   EnsemblMetazoa; FBtr0088075; FBpp0087180; FBgn0033644.
DR   GeneID; 36249; -.
DR   KEGG; dme:Dmel_CG8234; -.
DR   UCSC; CG8234-RA; d. melanogaster.
DR   UCSC; CG8234-RB; d. melanogaster.
DR   CTD; 36249; -.
DR   FlyBase; FBgn0033644; Tret1-2.
DR   VEuPathDB; VectorBase:FBgn0033644; -.
DR   eggNOG; KOG0254; Eukaryota.
DR   GeneTree; ENSGT00940000173941; -.
DR   HOGENOM; CLU_001265_30_5_1; -.
DR   InParanoid; Q8MKK4; -.
DR   OMA; DIKDMCE; -.
DR   OrthoDB; 430696at2759; -.
DR   PhylomeDB; Q8MKK4; -.
DR   Reactome; R-DME-189200; Cellular hexose transport.
DR   BioGRID-ORCS; 36249; 0 hits in 3 CRISPR screens.
DR   GenomeRNAi; 36249; -.
DR   PRO; PR:Q8MKK4; -.
DR   Proteomes; UP000000803; Chromosome 2R.
DR   Bgee; FBgn0033644; Expressed in brain and 11 other tissues.
DR   Genevisible; Q8MKK4; DM.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016020; C:membrane; IDA:FlyBase.
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:0055085; P:transmembrane transport; IBA:GO_Central.
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; 2.
DR   PROSITE; PS00217; SUGAR_TRANSPORT_2; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Glycoprotein; Membrane; Reference proteome; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..488
FT                   /note="Facilitated trehalose transporter Tret1-2 homolog"
FT                   /id="PRO_0000395534"
FT   TOPO_DOM        1..28
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        29..49
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        50..72
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        73..93
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        94..105
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        106..126
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        127..129
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        130..150
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        151..160
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        161..181
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        182..184
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        185..205
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        206..268
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        269..289
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        290..305
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        306..326
FT                   /note="Helical; Name=8"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        327..332
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        333..353
FT                   /note="Helical; Name=9"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        354..372
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        373..393
FT                   /note="Helical; Name=10"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        394..402
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        403..423
FT                   /note="Helical; Name=11"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        424..433
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        434..454
FT                   /note="Helical; Name=12"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        455..488
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        182
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        305
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   488 AA;  53088 MW;  6554C96EBEA1C08B CRC64;
     MKILMRADTH VSFSVPADGL KANFTFSQVL AALSVSLCSL VVGFVSAYTS PALVSMTDRT
     ITSFEVTKDA GSWVGGIMPL AALAGGITGG PLIEYLGRRS TILATAVPFI VSSLLIACAV
     NVIMILCGRF LTGFCVGIAS LSLPVYLGET LQPEVRGTLG LLPTALGNIG ILVCYVAGSF
     MNWSMLAFLG AALPVPFLIL MIIIPETPRW FVNRGQEERA RKALKWLRGK EADVEPELKE
     LMQSQADADR QATQNTCLEL FKRNNLKPLS ISLGLMFFQQ FSGINAVIFY TVQIFKDAGS
     TIDSNLSTII VGVVNFFATF MGIILIDRLG RKILLYVSDI AMIVTLSILG GFFYCKAHGP
     DVSHLGWLPL TCFVIYILGF SLGFGPIPWL MMGEILPAKI RGPAASVVTA FNWFCTFVVT
     KTFQDLTVAM GAHGAFWLFG AICIVGLFFV IIFVPETRGK SLEEIERKMM GRVPMSSVVN
     IKPFPFNM
 
 
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