GUTR1_DROME
ID GUTR1_DROME Reviewed; 392 AA.
AC Q9NDM2; Q95NV3; Q95NV9; Q9NKZ6; Q9W498;
DT 02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Protein trapped in endoderm-1;
GN Name=Tre1; ORFNames=CG3171;
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]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Labial palp;
RX PubMed=10884225; DOI=10.1126/science.289.5476.116;
RA Ishimoto H., Matsumoto A., Tanimura T.;
RT "Molecular identification of a taste receptor gene for trehalose in
RT Drosophila.";
RL Science 289:116-119(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND VARIANTS.
RC STRAIN=HG84, Shanghai, Singapore, Tananarive, w cv, and w cx;
RX PubMed=11566105; DOI=10.1016/s0960-9822(01)00450-x;
RA Ueno K., Ohta M., Morita H., Mikuni Y., Nakajima S., Yamamoto K., Isono K.;
RT "Trehalose sensitivity in Drosophila correlates with mutations in and
RT expression of the gustatory receptor gene Gr5a.";
RL Curr. Biol. 11:1451-1455(2001).
RN [3]
RP SEQUENCE REVISION OF 95-100.
RC STRAIN=Shanghai;
RA Ohta M., Isono K.;
RL Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
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 [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
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).
RN [7]
RP FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=14691551; DOI=10.1371/journal.pbio.0000080;
RA Kunwar P.S., Starz-Gaiano M., Bainton R.J., Heberlein U., Lehmann R.;
RT "Tre1, a G protein-coupled receptor, directs transepithelial migration of
RT Drosophila germ cells.";
RL PLoS Biol. 1:E80-E80(2003).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-359; SER-362; SER-366 AND
RP THR-372, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
CC -!- FUNCTION: Essential for the first active step of germ cell migration:
CC transepithelial migration of germ cells through the posterior midgut
CC (PMG) epithelium. {ECO:0000269|PubMed:14691551}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: In embryos, expression is seen at highest levels in
CC the cuprophilic cells and at lower levels in the amnioserosa,
CC developing CNS, cardiac mesoderm primordium and midline glia.
CC {ECO:0000269|PubMed:14691551}.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically
CC throughout embryo to adult stages. {ECO:0000269|PubMed:14691551}.
CC -!- DISRUPTION PHENOTYPE: Most germ cells do not exit the posterior midgut
CC (PMG) and remain clumped together within the midgut pocket. The few
CC germ cells that do leave the midgut early migrate normally to the
CC gonad. {ECO:0000269|PubMed:14691551}.
CC -!- MISCELLANEOUS: Overexpression of the Tre1 gene restores the taste
CC sensitivity to trehalose in a Tre1 mutant (PubMed:10884225). This
CC experiment cannot be explained given that other authors demonstrate
CC that trehalose sensitivity maps to the adjacent gene, Gr5a
CC (PubMed:14691551). {ECO:0000305|PubMed:10884225,
CC ECO:0000305|PubMed:14691551}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; AB034204; BAA95353.1; -; mRNA.
DR EMBL; AB042625; BAA96500.1; -; mRNA.
DR EMBL; AB066613; BAB68237.1; -; Genomic_DNA.
DR EMBL; AB066614; BAB68238.1; -; Genomic_DNA.
DR EMBL; AB066615; BAB68239.1; -; Genomic_DNA.
DR EMBL; AB066616; BAB68240.2; -; Genomic_DNA.
DR EMBL; AB066617; BAB68241.1; -; Genomic_DNA.
DR EMBL; AB066618; BAB68242.1; -; Genomic_DNA.
DR EMBL; AE014298; AAF46059.2; -; Genomic_DNA.
DR EMBL; AY070980; AAL48602.1; -; mRNA.
DR RefSeq; NP_001245534.1; NM_001258605.1.
DR RefSeq; NP_524792.1; NM_080053.4.
DR AlphaFoldDB; Q9NDM2; -.
DR SMR; Q9NDM2; -.
DR BioGRID; 72924; 4.
DR DIP; DIP-23341N; -.
DR IntAct; Q9NDM2; 1.
DR STRING; 7227.FBpp0070813; -.
DR GlyGen; Q9NDM2; 1 site.
DR iPTMnet; Q9NDM2; -.
DR PaxDb; Q9NDM2; -.
DR PRIDE; Q9NDM2; -.
DR DNASU; 140439; -.
DR EnsemblMetazoa; FBtr0070848; FBpp0070813; FBgn0046687.
DR EnsemblMetazoa; FBtr0308339; FBpp0300658; FBgn0046687.
DR GeneID; 140439; -.
DR KEGG; dme:Dmel_CG3171; -.
DR CTD; 140439; -.
DR FlyBase; FBgn0046687; Tre1.
DR VEuPathDB; VectorBase:FBgn0046687; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT00940000170714; -.
DR HOGENOM; CLU_009579_3_10_1; -.
DR InParanoid; Q9NDM2; -.
DR OMA; QVLHMFC; -.
DR PhylomeDB; Q9NDM2; -.
DR Reactome; R-DME-373076; Class A/1 (Rhodopsin-like receptors).
DR Reactome; R-DME-375276; Peptide ligand-binding receptors.
DR Reactome; R-DME-416476; G alpha (q) signalling events.
DR Reactome; R-DME-418555; G alpha (s) signalling events.
DR Reactome; R-DME-418594; G alpha (i) signalling events.
DR Reactome; R-DME-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Reactome; R-DME-8856828; Clathrin-mediated endocytosis.
DR BioGRID-ORCS; 140439; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 140439; -.
DR PRO; PR:Q9NDM2; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0046687; Expressed in embryonic/larval hemocyte (Drosophila) and 89 other tissues.
DR ExpressionAtlas; Q9NDM2; baseline and differential.
DR Genevisible; Q9NDM2; DM.
DR GO; GO:0005938; C:cell cortex; IDA:FlyBase.
DR GO; GO:0016021; C:integral component of membrane; ISS:FlyBase.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004930; F:G protein-coupled receptor activity; ISS:FlyBase.
DR GO; GO:0035234; P:ectopic germ cell programmed cell death; TAS:FlyBase.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISS:FlyBase.
DR GO; GO:0007281; P:germ cell development; IMP:FlyBase.
DR GO; GO:0008354; P:germ cell migration; IMP:FlyBase.
DR GO; GO:0007280; P:pole cell migration; TAS:FlyBase.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR SMART; SM01381; 7TM_GPCR_Srsx; 1.
DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE 1: Evidence at protein level;
KW Cell membrane; G-protein coupled receptor; Glycoprotein; Membrane;
KW Phosphoprotein; Receptor; Reference proteome; Transducer; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..392
FT /note="Protein trapped in endoderm-1"
FT /id="PRO_0000069672"
FT TOPO_DOM 1..39
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 40..60
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 61..73
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 74..94
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 95..110
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 111..131
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 132..156
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 157..177
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 178..202
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 203..223
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 224..268
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 269..289
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 290..302
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 303..323
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 324..392
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MOD_RES 359
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 362
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 366
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 372
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT CARBOHYD 298
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VARIANT 7
FT /note="M -> MDMGMGM (in strain: HG84, Singapore and w cv)"
FT VARIANT 12
FT /note="F -> I (in strain: HG84, Singapore and w cv)"
FT VARIANT 95..100
FT /note="Missing (in strain: Shanghai)"
FT VARIANT 348
FT /note="L -> M (in strain: Shanghai and Tananarive)"
FT CONFLICT 226
FT /note="L -> P (in Ref. 1; BAA95353)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 392 AA; 43844 MW; 41A58C69479BBFDA CRC64;
MDQDMGMATG YFQDADMQMD EPAAATQSIY PHSATLFAAI SACVFVTIGV LGNLITLLAL
LKSPTIREHA TTAFVISLSI SDLLFCSFSL PLTAVRFFQE SWTFGTTLCK IFPVIFYGNV
AVSLLSMVGI TLNRYILIAC HSRYSQIYKP KFITLQLLFV WAVSFLLLLP PILGIWGEMG
LDEATFSCTI LKKEGRSIKK TLFVIGFLLP CLVIIVSYSC IYITVLHQKK KIRNHDNFQI
AAAKGSSSSG GGSYMTTTCT RKAREDNRLT VMMVTIFLCF LVCFLPLMLA NVVDDERNTS
YPWLHIIASV MAWASSVINP IIYAASNRNY RVAYYKIFAL LKFWGEPLSP MPSRNYHQSK
NSKELSGVIR STPLFHAVQK NSINQMCQTY SV
