TACHY_DROME
ID TACHY_DROME Reviewed; 289 AA.
AC Q9VGE8; B5RJL9; Q8SZ21; Q9NBJ5;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Tachykinins;
DE AltName: Full=dTk;
DE Contains:
DE RecName: Full=Tachykinin-related peptide 1;
DE Short=TK-1;
DE Short=dTK-1;
DE AltName: Full=APTSSFIGMR-amide;
DE Contains:
DE RecName: Full=Tachykinin-associated peptide 1;
DE Short=TAP1;
DE AltName: Full=DEEHDTSEGNWLGSGPDPLDYADEEADSSYAEN-amide;
DE Contains:
DE RecName: Full=Tachykinin-related peptide 2;
DE Short=TK-2;
DE Short=dTK-2;
DE AltName: Full=APLAFVGLR-amide;
DE Contains:
DE RecName: Full=Tachykinin-associated peptide 2;
DE Short=TAP2;
DE AltName: Full=FIPINNRLSDVLQSLEEERLRDSLLQDFFDRVAGRDGSAV-amide;
DE Contains:
DE RecName: Full=Tachykinin-related peptide 3;
DE Short=TK-3;
DE Short=dTK-3;
DE AltName: Full=APTGFTGMR-amide;
DE Contains:
DE RecName: Full=Tachykinin-associated peptide 3;
DE Short=TAP3;
DE AltName: Full=Brain peptide PALLAGDDDAEADEATELQQ;
DE Contains:
DE RecName: Full=Tachykinin-related peptide 4;
DE Short=TK-4;
DE Short=dTK-4;
DE AltName: Full=APVNSFVGMR-amide;
DE Contains:
DE RecName: Full=Tachykinin-associated peptide 4;
DE Short=TAP4;
DE AltName: Full=Brain peptide DVSHQHY;
DE Contains:
DE RecName: Full=Tachykinin-associated peptide 5;
DE Short=TAP5;
DE AltName: Full=AALSDSYDLRGKQQRFADFNSKFVAVR-amide;
DE Contains:
DE RecName: Full=Tachykinin-associated peptide 6;
DE Short=TAP6;
DE AltName: Full=Brain peptide SDLEGNGVGIGDDHEQALVHPWLYLWGE;
DE Contains:
DE RecName: Full=Tachykinin-related peptide 5;
DE Short=TK-5;
DE Short=dTK-5;
DE AltName: Full=APNGFLGMR-amide;
DE Flags: Precursor;
GN Name=Tk {ECO:0000312|EMBL:AAF54735.1}; ORFNames=CG14734;
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:AAF89172.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, SYNTHESIS, AND
RP AMIDATION AT ASN-95; VAL-153 AND ARG-239.
RC TISSUE=Head {ECO:0000312|EMBL:AAF89172.1};
RX PubMed=10801863; DOI=10.1074/jbc.m002875200;
RA Siviter R.J., Coast G.M., Winther A.M.E., Nachman R.J., Taylor C.A.M.,
RA Shirras A.D., Coates D., Isaac R.E., Nassel D.R.;
RT "Expression and functional characterization of a Drosophila neuropeptide
RT precursor with homology to mammalian preprotachykinin A.";
RL J. Biol. Chem. 275:23273-23280(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000269|PubMed:10731132};
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}
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:AAL48801.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAL48801.1};
RC TISSUE=Embryo {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).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley;
RA Carlson J.W., Booth B., Frise E., Park S., Wan K.H., Yu C., Celniker S.E.;
RL Submitted (SEP-2008) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP PROTEIN SEQUENCE OF 50-59; 102-110; 157-165; 191-200 AND 273-281,
RP IDENTIFICATION BY MASS SPECTROMETRY, MASS SPECTROMETRY, AND AMIDATION AT
RP ARG-59; ARG-110; ARG-165; ARG-200 AND ARG-281.
RC TISSUE=Midgut {ECO:0000303|PubMed:21214272};
RX PubMed=21214272; DOI=10.1021/pr101116g;
RA Reiher W., Shirras C., Kahnt J., Baumeister S., Isaac R.E., Wegener C.;
RT "Peptidomics and peptide hormone processing in the Drosophila midgut.";
RL J. Proteome Res. 10:1881-1892(2011).
RN [7]
RP FUNCTION.
RX PubMed=26083710; DOI=10.7554/elife.06914;
RA Shankar S., Chua J.Y., Tan K.J., Calvert M.E., Weng R., Ng W.C., Mori K.,
RA Yew J.Y.;
RT "The neuropeptide tachykinin is essential for pheromone detection in a
RT gustatory neural circuit.";
RL Elife 4:E06914-E06914(2015).
CC -!- FUNCTION: Tachykinins are active peptides which excite neurons, evoke
CC behavioral responses, are potent vasodilators and secretagogues, and
CC contract (directly or indirectly) many smooth muscles. Stimulates gut
CC muscle contractions (PubMed:10801863). Required for the response to the
CC male sex pheromone CH503 which is transferred from males to females
CC during mating and inhibits courtship behavior by other males
CC (PubMed:26083710). The Gr68a gustatory receptor is required for
CC detection of the pheromone and Gr68a-expressing neurons in the male
CC foreleg relay signals to the suboesophageal zone (SEZ) which leads to
CC courtship suppression through release of tachykinin from a cluster of
CC 8-10 neurons in the SEZ (PubMed:26083710).
CC {ECO:0000269|PubMed:10801863, ECO:0000269|PubMed:26083710,
CC ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Strong expression is seen in a group of 14 cells
CC plus one isolated cell in the midgut of stage 17 embryos. Also
CC expressed in a pair of medially located unidentified cells, just
CC posterior to the brain, and in two lateral groups of cells that may be
CC associated with tracheae. Expression in the larval gut is restricted to
CC cells with endocrine cell-like morphology in the posterior midgut, just
CC anterior to the malphigian tubules. In the brain, expression is
CC detected in a restricted number of neuronal cell bodies. Expression in
CC the adult female gut is restricted to the midgut with no expression
CC detected in the hindgut. {ECO:0000269|PubMed:10801863}.
CC -!- MASS SPECTROMETRY: [Tachykinin-related peptide 1]: Mass=1065.55;
CC Method=MALDI; Evidence={ECO:0000269|PubMed:21214272};
CC -!- MASS SPECTROMETRY: [Tachykinin-related peptide 2]: Mass=942.59;
CC Method=MALDI; Evidence={ECO:0000269|PubMed:21214272};
CC -!- MASS SPECTROMETRY: [Tachykinin-related peptide 3]: Mass=936.47;
CC Method=MALDI; Evidence={ECO:0000269|PubMed:21214272};
CC -!- MASS SPECTROMETRY: [Tachykinin-related peptide 4]: Mass=1076.57;
CC Method=MALDI; Evidence={ECO:0000269|PubMed:21214272};
CC -!- MASS SPECTROMETRY: [Tachykinin-related peptide 5]: Mass=961.50;
CC Method=MALDI; Evidence={ECO:0000269|PubMed:21214272};
CC -!- SIMILARITY: Belongs to the tachykinin family. {ECO:0000255}.
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; AF248040; AAF89172.1; -; mRNA.
DR EMBL; AE014297; AAF54735.1; -; Genomic_DNA.
DR EMBL; AY071179; AAL48801.1; -; mRNA.
DR EMBL; BT044493; ACH95267.1; -; mRNA.
DR RefSeq; NP_650141.2; NM_141884.4.
DR AlphaFoldDB; Q9VGE8; -.
DR BioGRID; 66573; 4.
DR IntAct; Q9VGE8; 1.
DR STRING; 7227.FBpp0081962; -.
DR PaxDb; Q9VGE8; -.
DR PRIDE; Q9VGE8; -.
DR DNASU; 41456; -.
DR EnsemblMetazoa; FBtr0082488; FBpp0081962; FBgn0037976.
DR GeneID; 41456; -.
DR KEGG; dme:Dmel_CG14734; -.
DR UCSC; CG14734-RA; d. melanogaster.
DR CTD; 21874; -.
DR FlyBase; FBgn0037976; Tk.
DR VEuPathDB; VectorBase:FBgn0037976; -.
DR eggNOG; ENOG502S9VB; Eukaryota.
DR InParanoid; Q9VGE8; -.
DR OMA; QYLVHPW; -.
DR PhylomeDB; Q9VGE8; -.
DR BioGRID-ORCS; 41456; 0 hits in 1 CRISPR screen.
DR ChiTaRS; Tk; fly.
DR GenomeRNAi; 41456; -.
DR PRO; PR:Q9VGE8; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0037976; Expressed in brain and 13 other tissues.
DR ExpressionAtlas; Q9VGE8; baseline and differential.
DR Genevisible; Q9VGE8; DM.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0005184; F:neuropeptide hormone activity; ISS:FlyBase.
DR GO; GO:0005326; F:neurotransmitter transmembrane transporter activity; IMP:UniProtKB.
DR GO; GO:0005102; F:signaling receptor binding; NAS:FlyBase.
DR GO; GO:0071861; F:tachykinin receptor binding; IPI:FlyBase.
DR GO; GO:0007628; P:adult walking behavior; IMP:FlyBase.
DR GO; GO:0002121; P:inter-male aggressive behavior; IMP:FlyBase.
DR GO; GO:0006629; P:lipid metabolic process; IMP:FlyBase.
DR GO; GO:0007218; P:neuropeptide signaling pathway; ISS:FlyBase.
DR GO; GO:0060450; P:positive regulation of hindgut contraction; IMP:UniProtKB.
DR GO; GO:1904058; P:positive regulation of sensory perception of pain; IMP:FlyBase.
DR GO; GO:0019236; P:response to pheromone; IMP:FlyBase.
DR GO; GO:0007608; P:sensory perception of smell; IMP:FlyBase.
DR GO; GO:0007217; P:tachykinin receptor signaling pathway; IDA:FlyBase.
PE 1: Evidence at protein level;
KW Amidation; Behavior; Cleavage on pair of basic residues;
KW Direct protein sequencing; Neuropeptide; Reference proteome; Secreted;
KW Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT PROPEP 25..47
FT /evidence="ECO:0000255, ECO:0000303|PubMed:10801863"
FT /id="PRO_0000343488"
FT PEPTIDE 50..59
FT /note="Tachykinin-related peptide 1"
FT /evidence="ECO:0000269|PubMed:21214272"
FT /id="PRO_0000343489"
FT PEPTIDE 63..95
FT /note="Tachykinin-associated peptide 1"
FT /evidence="ECO:0000255"
FT /id="PRO_0000343490"
FT PEPTIDE 102..110
FT /note="Tachykinin-related peptide 2"
FT /evidence="ECO:0000269|PubMed:21214272"
FT /id="PRO_0000343491"
FT PEPTIDE 114..153
FT /note="Tachykinin-associated peptide 2"
FT /evidence="ECO:0000255"
FT /id="PRO_0000343492"
FT PEPTIDE 157..165
FT /note="Tachykinin-related peptide 3"
FT /evidence="ECO:0000269|PubMed:21214272"
FT /id="PRO_0000343493"
FT PEPTIDE 169..188
FT /note="Tachykinin-associated peptide 3"
FT /evidence="ECO:0000255"
FT /id="PRO_0000343494"
FT PEPTIDE 191..200
FT /note="Tachykinin-related peptide 4"
FT /evidence="ECO:0000269|PubMed:21214272"
FT /id="PRO_0000343495"
FT PEPTIDE 204..210
FT /note="Tachykinin-associated peptide 4"
FT /evidence="ECO:0000255"
FT /id="PRO_0000343496"
FT PEPTIDE 213..239
FT /note="Tachykinin-associated peptide 5"
FT /evidence="ECO:0000255"
FT /id="PRO_0000343497"
FT PEPTIDE 243..270
FT /note="Tachykinin-associated peptide 6"
FT /evidence="ECO:0000255"
FT /id="PRO_0000343498"
FT PEPTIDE 273..281
FT /note="Tachykinin-related peptide 5"
FT /evidence="ECO:0000269|PubMed:21214272"
FT /id="PRO_0000343499"
FT PROPEP 285..289
FT /evidence="ECO:0000255, ECO:0000303|PubMed:10801863"
FT /id="PRO_0000343500"
FT REGION 24..94
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 59
FT /note="Arginine amide"
FT /evidence="ECO:0000269|PubMed:21214272"
FT MOD_RES 95
FT /note="Asparagine amide"
FT /evidence="ECO:0000255, ECO:0000303|PubMed:10801863"
FT MOD_RES 110
FT /note="Arginine amide"
FT /evidence="ECO:0000269|PubMed:21214272"
FT MOD_RES 153
FT /note="Valine amide"
FT /evidence="ECO:0000255, ECO:0000303|PubMed:10801863"
FT MOD_RES 165
FT /note="Arginine amide"
FT /evidence="ECO:0000269|PubMed:21214272"
FT MOD_RES 200
FT /note="Arginine amide"
FT /evidence="ECO:0000269|PubMed:21214272"
FT MOD_RES 239
FT /note="Arginine amide"
FT /evidence="ECO:0000255, ECO:0000303|PubMed:10801863"
FT MOD_RES 281
FT /note="Arginine amide"
FT /evidence="ECO:0000269|PubMed:21214272"
FT CONFLICT 175
FT /note="D -> G (in Ref. 1; AAF89172)"
FT /evidence="ECO:0000305"
FT CONFLICT 254
FT /note="D -> E (in Ref. 4; AAL48801)"
FT /evidence="ECO:0000305"
FT CONFLICT 255
FT /note="D -> N (in Ref. 1; AAF89172)"
FT /evidence="ECO:0000305"
FT CONFLICT 288
FT /note="F -> S (in Ref. 1; AAF89172)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 289 AA; 31678 MW; 52CAA79825D0725E CRC64;
MRPLSGLIAL ALLLLLLLTA PSSAADTETE SSGSPLTPGA EEPRRVVKRA PTSSFIGMRG
KKDEEHDTSE GNWLGSGPDP LDYADEEADS SYAENGRRLK KAPLAFVGLR GKKFIPINNR
LSDVLQSLEE ERLRDSLLQD FFDRVAGRDG SAVGKRAPTG FTGMRGKRPA LLAGDDDAEA
DEATELQQKR APVNSFVGMR GKKDVSHQHY KRAALSDSYD LRGKQQRFAD FNSKFVAVRG
KKSDLEGNGV GIGDDHEQAL VHPWLYLWGE KRAPNGFLGM RGKRPALFE
