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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}.
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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
 
 
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