Q9VGE8 (TACHY_DROME) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Tachykinins

Alternative name(s):
dTk

Cleaved into the following 11 chains:

1. Tachykinin-related peptide 1
   Short name=TK-1
   Short name=dTK-1
   Alternative name(s):
   APTSSFIGMR-amide
2. Tachykinin-associated peptide 1
   Short name=TAP1
   Alternative name(s):
   DEEHDTSEGNWLGSGPDPLDYADEEADSSYAEN-amide
3. Tachykinin-related peptide 2
   Short name=TK-2
   Short name=dTK-2
   Alternative name(s):
   APLAFVGLR-amide
4. Tachykinin-associated peptide 2
   Short name=TAP2
   Alternative name(s):
   FIPINNRLSDVLQSLEEERLRDSLLQDFFDRVAGRDGSAV-amide
5. Tachykinin-related peptide 3
   Short name=TK-3
   Short name=dTK-3
   Alternative name(s):
   APTGFTGMR-amide
6. Tachykinin-associated peptide 3
   Short name=TAP3
   Alternative name(s):
   Brain peptide PALLAGDDDAEADEATELQQ
7. Tachykinin-related peptide 4
   Short name=TK-4
   Short name=dTK-4
   Alternative name(s):
   APVNSFVGMR-amide
8. Tachykinin-associated peptide 4
   Short name=TAP4
   Alternative name(s):
   Brain peptide DVSHQHY
9. Tachykinin-associated peptide 5
   Short name=TAP5
   Alternative name(s):
   AALSDSYDLRGKQQRFADFNSKFVAVR-amide
10. Tachykinin-associated peptide 6
    Short name=TAP6
    Alternative name(s):
    Brain peptide SDLEGNGVGIGDDHEQALVHPWLYLWGE
11. Tachykinin-related peptide 5
    Short name=TK-5
    Short name=dTK-5
    Alternative name(s):
    APNGFLGMR-amide

Gene names

Name:	Tk
ORF Names:	CG14734

Organism

Drosophila melanogaster (Fruit fly)

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora

Protein attributes

Sequence length	289 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Tachykinins are active peptides which excite neurons, evoke behavioral responses, are potent vasodilators and secretagogues, and contract (directly or indirectly) many smooth muscles. Stimulates gut muscle contractions. Ref.1
Subcellular location	Secreted Potential.
Tissue specificity	Strong expression is seen in a group of 14 cells plus one isolated cell in the midgut of stage 17 embryos. Also expressed in a pair of medially located unidentified cells, just posterior to the brain, and in two lateral groups of cells that may be associated with tracheae. Expression in the larval gut is restricted to cells with endocrine cell-like morphology in the posterior midgut, just anterior to the malphigian tubules. In the brain, expression is detected in a restricted number of neuronal cell bodies. Expression in the adult female gut is restricted to the midgut with no expression detected in the hindgut. Ref.1
Sequence similarities	Belongs to the tachykinin family.

Ontologies

Keywords
Cellular component	Secreted
Domain	Signal
Molecular function	Neuropeptide
PTM	Amidation Cleavage on pair of basic residues
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	adult walking behavior Inferred from mutant phenotype. Source: FlyBase neuropeptide signaling pathway Inferred from electronic annotation. Source: UniProtKB-KW sensory perception of smell Inferred from mutant phenotype. Source: FlyBase tachykinin receptor signaling pathway Inferred from mutant phenotype. Source: UniProtKB
Cellular component	extracellular space Inferred from direct assay. Source: UniProtKB
Molecular function	neurotransmitter transporter activity Inferred from mutant phenotype. Source: UniProtKB receptor binding Non-traceable author statement. Source: FlyBase
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CG6904	Q9VFC8	1	EBI-152254,EBI-169205

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 24	24	Potential
	Propeptide	25 – 47	23	Potential		PRO_0000343488
	Peptide	50 – 59	10	Tachykinin-related peptide 1 Potential Ref.1		PRO_0000343489
	Peptide	63 – 95	33	Tachykinin-associated peptide 1 Potential Ref.1		PRO_0000343490
	Peptide	102 – 110	9	Tachykinin-related peptide 2 Potential Ref.1		PRO_0000343491
	Peptide	114 – 153	40	Tachykinin-associated peptide 2 Potential Ref.1		PRO_0000343492
	Peptide	157 – 165	9	Tachykinin-related peptide 3 Potential Ref.1		PRO_0000343493
	Peptide	169 – 188	20	Tachykinin-associated peptide 3 Potential Ref.1		PRO_0000343494
	Peptide	191 – 200	10	Tachykinin-related peptide 4 Potential Ref.1		PRO_0000343495
	Peptide	204 – 210	7	Tachykinin-associated peptide 4 Potential Ref.1		PRO_0000343496
	Peptide	213 – 239	27	Tachykinin-associated peptide 5 Potential Ref.1		PRO_0000343497
	Peptide	243 – 270	28	Tachykinin-associated peptide 6 Potential Ref.1		PRO_0000343498
	Peptide	273 – 281	9	Tachykinin-related peptide 5 Potential Ref.1		PRO_0000343499
	Propeptide	285 – 289	5	Potential Ref.1		PRO_0000343500
Amino acid modifications
	Modified residue	59	1	Arginine amide Potential Ref.1
	Modified residue	95	1	Asparagine amide Potential Ref.1
	Modified residue	110	1	Arginine amide Potential Ref.1
	Modified residue	153	1	Valine amide Potential Ref.1
	Modified residue	165	1	Arginine amide Potential Ref.1
	Modified residue	200	1	Arginine amide Potential Ref.1
	Modified residue	239	1	Arginine amide Potential Ref.1
	Modified residue	281	1	Arginine amide Potential Ref.1
Experimental info
	Sequence conflict	175	1	D → G in AAF89172. Ref.1
	Sequence conflict	254	1	D → E in AAL48801. Ref.4
	Sequence conflict	255	1	D → N in AAF89172. Ref.1
	Sequence conflict	288	1	F → S in AAF89172. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q9VGE8 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: 52CAA79825D0725E	FASTA	289	31,678
	10 20 30 40 50 60 MRPLSGLIAL ALLLLLLLTA PSSAADTETE SSGSPLTPGA EEPRRVVKRA PTSSFIGMRG 70 80 90 100 110 120 KKDEEHDTSE GNWLGSGPDP LDYADEEADS SYAENGRRLK KAPLAFVGLR GKKFIPINNR 130 140 150 160 170 180 LSDVLQSLEE ERLRDSLLQD FFDRVAGRDG SAVGKRAPTG FTGMRGKRPA LLAGDDDAEA 190 200 210 220 230 240 DEATELQQKR APVNSFVGMR GKKDVSHQHY KRAALSDSYD LRGKQQRFAD FNSKFVAVRG 250 260 270 280 KKSDLEGNGV GIGDDHEQAL VHPWLYLWGE KRAPNGFLGM RGKRPALFE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Expression and functional characterization of a Drosophila neuropeptide precursor with homology to mammalian preprotachykinin A." Siviter R.J., Coast G.M., Winther A.M.E., Nachman R.J., Taylor C.A.M., Shirras A.D., Coates D., Isaac R.E., Nassel D.R. J. Biol. Chem. 275:23273-23280(2000) [PubMed: 10801863] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, SYNTHESIS. Tissue: Head.
[2]	"The genome sequence of Drosophila melanogaster." Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D. , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C. Science 287:2185-2195(2000) [PubMed: 10731132] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Berkeley.
[3]	"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review." Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E. Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed: 12537572] [Abstract] Cited for: GENOME REANNOTATION. Strain: Berkeley.
[4]	"A Drosophila full-length cDNA resource." Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E. Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed: 12537569] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Berkeley. Tissue: Embryo.
[5]	Carlson J.W., Booth B., Frise E., Park S., Wan K.H., Yu C., Celniker S.E. Submitted (SEP-2008) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Berkeley.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF248040 mRNA. Translation: AAF89172.1. AE014297 Genomic DNA. Translation: AAF54735.1. AY071179 mRNA. Translation: AAL48801.1. BT044493 mRNA. Translation: ACH95267.1.
RefSeq	NP_650141.2. NM_141884.3.
UniGene	Dm.3420.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9VGE8. 1 interaction.
MINT	MINT-1025106.
STRING	Q9VGE8.
Proteomic databases
PRIDE	Q9VGE8.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblMetazoa	FBtr0082488; FBpp0081962; FBgn0037976.
GeneID	41456.
KEGG	dme:Dmel_CG14734.
NMPDR	fig|7227.3.peg.12357.
UCSC	CG14734-RA. d. melanogaster.
Organism-specific databases
CTD	21874.
FlyBase	FBgn0037976. Tk.
Phylogenomic databases
GeneTree	EMGT00050000017792.
InParanoid	Q9VGE8.
OMA	FIGMRGK.
OrthoDB	EOG43FFD7.
PhylomeDB	Q9VGE8.
Gene expression databases
Bgee	Q9VGE8.
Family and domain databases
ProtoNet	Search...
Other
NextBio	823978.

Entry information

Entry name

TACHY_DROME

Accession

Primary (citable) accession number: Q9VGE8
Secondary accession number(s): B5RJL9, Q8SZ21, Q9NBJ5

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 2008
Last sequence update:	May 1, 2000
Last modified:	January 25, 2012
This is version 63 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Drosophila annotation project