TLR2_DROME
ID TLR2_DROME Reviewed; 519 AA.
AC P30975; Q8T0S8; Q9VAD2;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 21-JUN-2005, sequence version 2.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Tachykinin-like peptides receptor 99D;
DE AltName: Full=Tachykinin-like receptor at 99D;
DE AltName: Full=dTKR;
GN Name=TkR99D; Synonyms=Takr99D; ORFNames=CG7887;
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], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=Canton-S;
RX PubMed=1717263; DOI=10.1002/j.1460-2075.1991.tb04885.x;
RA Li X.-J., Wolfgang W., Wu Y.-N., North R.A., Forte M.A.;
RT "Cloning, heterologous expression and developmental regulation of a
RT Drosophila receptor for tachykinin-like peptides.";
RL EMBO J. 10:3221-3229(1991).
RN [2]
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]
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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Head;
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: Receptor for tachykinin-like peptides.
CC {ECO:0000269|PubMed:1717263}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:1717263};
CC Multi-pass membrane protein {ECO:0000269|PubMed:1717263}.
CC -!- TISSUE SPECIFICITY: During late embryogenesis (stages 11-15), expressed
CC in the brain and in a specific subset of neurons in each neuromere of
CC the developing ventral ganglion. Expressed in the cortex of the adult
CC brain, which contains the neuronal cell bodies.
CC {ECO:0000269|PubMed:1717263}.
CC -!- DEVELOPMENTAL STAGE: Expressed throughout development and in the adult.
CC Highest level of expression observed during late embryogenesis.
CC {ECO:0000269|PubMed:1717263}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X62711; CAA44595.1; -; mRNA.
DR EMBL; AE014297; AAF56979.2; -; Genomic_DNA.
DR EMBL; AY069085; AAL39230.1; -; mRNA.
DR PIR; S17783; S17783.
DR RefSeq; NP_524556.2; NM_079832.3.
DR AlphaFoldDB; P30975; -.
DR SMR; P30975; -.
DR BioGRID; 68408; 9.
DR STRING; 7227.FBpp0084873; -.
DR GlyGen; P30975; 4 sites.
DR PaxDb; P30975; -.
DR PRIDE; P30975; -.
DR EnsemblMetazoa; FBtr0085507; FBpp0084873; FBgn0004622.
DR GeneID; 43551; -.
DR KEGG; dme:Dmel_CG7887; -.
DR CTD; 43551; -.
DR FlyBase; FBgn0004622; TkR99D.
DR VEuPathDB; VectorBase:FBgn0004622; -.
DR eggNOG; KOG4219; Eukaryota.
DR GeneTree; ENSGT00940000155512; -.
DR InParanoid; P30975; -.
DR OrthoDB; 715197at2759; -.
DR PhylomeDB; P30975; -.
DR BioGRID-ORCS; 43551; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 43551; -.
DR PRO; PR:P30975; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0004622; Expressed in adult central nervous system and 13 other tissues.
DR ExpressionAtlas; P30975; baseline and differential.
DR Genevisible; P30975; DM.
DR GO; GO:0016021; C:integral component of membrane; ISM:FlyBase.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:FlyBase.
DR GO; GO:0008188; F:neuropeptide receptor activity; ISM:FlyBase.
DR GO; GO:0004995; F:tachykinin receptor activity; IDA:FlyBase.
DR GO; GO:0050911; P:detection of chemical stimulus involved in sensory perception of smell; IMP:FlyBase.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISM:FlyBase.
DR GO; GO:0050805; P:negative regulation of synaptic transmission; IMP:FlyBase.
DR GO; GO:0007218; P:neuropeptide signaling pathway; IDA:FlyBase.
DR GO; GO:0042048; P:olfactory behavior; IMP:FlyBase.
DR GO; GO:1904058; P:positive regulation of sensory perception of pain; IMP:FlyBase.
DR GO; GO:0007217; P:tachykinin receptor signaling pathway; IDA:FlyBase.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR InterPro; IPR001681; Neurokn_rcpt.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PRINTS; PR00244; NEUROKININR.
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 2: Evidence at transcript level;
KW Cell membrane; Disulfide bond; G-protein coupled receptor; Glycoprotein;
KW Lipoprotein; Membrane; Palmitate; Receptor; Reference proteome; Transducer;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..519
FT /note="Tachykinin-like peptides receptor 99D"
FT /id="PRO_0000070185"
FT TOPO_DOM 1..100
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 101..123
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 124..134
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 135..155
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 156..175
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 176..197
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 198..217
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 218..238
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 239..270
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 271..292
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 293..324
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 325..346
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 347..361
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 362..384
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 385..519
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 444..519
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 444..473
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 490..519
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT LIPID 399
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000255"
FT CARBOHYD 3
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 19
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 22
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 61
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 174..254
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT CONFLICT 46..58
FT /note="LPDFGQELALSTS -> CRTLARSSPYPPV (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 345
FT /note="I -> T (in Ref. 4; AAL39230)"
FT /evidence="ECO:0000305"
FT CONFLICT 456..457
FT /note="Missing (in Ref. 4; AAL39230)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 519 AA; 58396 MW; 57105170D4CA5AA5 CRC64;
MENRSDFEAD DYGDISWSNW SNWSTPAGVL FSAMSSVLSA SNHTPLPDFG QELALSTSSF
NHSQTLSTDL PAVGDVEDAA EDAAASMETG SFAFVVPWWR QVLWSILFGG MVIVATGGNL
IVVWIVMTTK RMRTVTNYFI VNLSIADAMV SSLNVTFNYY YMLDSDWPFG EFYCKLSQFI
AMLSICASVF TLMAISIDRY VAIIRPLQPR MSKRCNLAIA AVIWLASTLI SCPMMIIYRT
EEVPVRGLSN RTVCYPEWPD GPTNHSTMES LYNILIIILT YFLPIVSMTV TYSRVGIELW
GSKTIGECTP RQVENVRSKR RVVKMMIVVV LIFAICWLPF HSYFIITSCY PAITEAPFIQ
ELYLAIYWLA MSNSMYNPII YCWMNSRFRY GFKMVFRWCL FVRVGTEPFS RRENLTSRYS
CSGSPDHNRI KRNDTQKSIL YTCPSSPKSH RISHSGTGRS ATLRNSLPAE SLSSGGSGGG
GHRKRLSYQQ EMQQRWSGPN SATAVTNSSS TANTTQLLS