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Reviewed, UniProtKB/Swiss-Prot Q9VGE8 (TACHY_DROME)

Last modified June 16, 2009. Version 46. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Tachykinins
Alternative name(s):
    dTk
Cleaved into the following 11 chains:
    1- Recommended name:
            Tachykinin-related peptide 1
                Short name=TK-1
                Short name=dTK-1
        Alternative name(s):
            APTSSFIGMR-amide
    2- Recommended name:
            Tachykinin-associated peptide 1
                Short name=TAP1
        Alternative name(s):
            DEEHDTSEGNWLGSGPDPLDYADEEADSSYAEN-amide
    3- Recommended name:
            Tachykinin-related peptide 2
                Short name=TK-2
                Short name=dTK-2
        Alternative name(s):
            APLAFVGLR-amide
    4- Recommended name:
            Tachykinin-associated peptide 2
                Short name=TAP2
        Alternative name(s):
            FIPINNRLSDVLQSLEEERLRDSLLQDFFDRVAGRDGSAV-amide
    5- Recommended name:
            Tachykinin-related peptide 3
                Short name=TK-3
                Short name=dTK-3
        Alternative name(s):
            APTGFTGMR-amide
    6- Recommended name:
            Tachykinin-associated peptide 3
                Short name=TAP3
        Alternative name(s):
            Brain peptide PALLAGDDDAEADEATELQQ
    7- Recommended name:
            Tachykinin-related peptide 4
                Short name=TK-4
                Short name=dTK-4
        Alternative name(s):
            APVNSFVGMR-amide
    8- Recommended name:
            Tachykinin-associated peptide 4
                Short name=TAP4
        Alternative name(s):
            Brain peptide DVSHQHY
    9- Recommended name:
            Tachykinin-associated peptide 5
                Short name=TAP5
        Alternative name(s):
            AALSDSYDLRGKQQRFADFNSKFVAVR-amide
    10- Recommended name:
            Tachykinin-associated peptide 6
                Short name=TAP6
        Alternative name(s):
            Brain peptide SDLEGNGVGIGDDHEQALVHPWLYLWGE
    11- Recommended name:
            Tachykinin-related peptide 5
                Short name=TK-5
                Short name=dTK-5
        Alternative name(s):
            APNGFLGMR-amide
Gene names
Name: Tk
ORF Names: CG14734
OrganismDrosophila melanogaster (Fruit fly) [Complete proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length289 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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 componentSecreted
   DomainSignal
   Molecular functionNeuropeptide
   PTMAmidation
Cleavage on pair of basic residues
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processbehavior

Inferred from mutant phenotype. Source: UniProtKB

neuropeptide signaling pathway

Inferred from electronic annotation. Source: UniProtKB-KW

tachykinin receptor signaling pathway

Inferred from mutant phenotype. Source: UniProtKB

   Cellular componentextracellular space

Inferred from direct assay. Source: UniProtKB

   Molecular functionneurotransmitter 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

Q9VFC81EBI-152254,EBI-169205

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2424 Potential
Propeptide25 – 4723 Potential
PRO_0000343488
Peptide50 – 5910Tachykinin-related peptide 1 Potential Ref.1
PRO_0000343489
Peptide63 – 9533Tachykinin-associated peptide 1 Potential Ref.1
PRO_0000343490
Peptide102 – 1109Tachykinin-related peptide 2 Potential Ref.1
PRO_0000343491
Peptide114 – 15340Tachykinin-associated peptide 2 Potential Ref.1
PRO_0000343492
Peptide157 – 1659Tachykinin-related peptide 3 Potential Ref.1
PRO_0000343493
Peptide169 – 18820Tachykinin-associated peptide 3 Potential Ref.1
PRO_0000343494
Peptide191 – 20010Tachykinin-related peptide 4 Potential Ref.1
PRO_0000343495
Peptide204 – 2107Tachykinin-associated peptide 4 Potential Ref.1
PRO_0000343496
Peptide213 – 23927Tachykinin-associated peptide 5 Potential Ref.1
PRO_0000343497
Peptide243 – 27028Tachykinin-associated peptide 6 Potential Ref.1
PRO_0000343498
Peptide273 – 2819Tachykinin-related peptide 5 Potential Ref.1
PRO_0000343499
Propeptide285 – 2895 Potential Ref.1
PRO_0000343500

Amino acid modifications

Modified residue591Arginine amide Potential Ref.1
Modified residue951Asparagine amide Potential Ref.1
Modified residue1101Arginine amide Potential Ref.1
Modified residue1531Valine amide Potential Ref.1
Modified residue1651Arginine amide Potential Ref.1
Modified residue2001Arginine amide Potential Ref.1
Modified residue2391Arginine amide Potential Ref.1
Modified residue2811Arginine amide Potential Ref.1

Experimental info

Sequence conflict1751D → G in AAF89172. Ref.1
Sequence conflict2541D → E in AAL48801. Ref.4
Sequence conflict2551D → N in AAF89172. Ref.1
Sequence conflict2881F → S in AAF89172. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9VGE8-1 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 52CAA79825D0725E

FASTA28931,678
        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 

« Hide

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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.
[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

AF248040 mRNA. Translation: AAF89172.1.
AE014297 Genomic DNA. Translation: AAF54735.1.
AY071179 mRNA. Translation: AAL48801.1.
BT044493 mRNA. Translation: ACH95267.1.
RefSeqNP_650141.2.
UniGeneDm.3420

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

IntActQ9VGE8. 3 interactions.

Proteomic databases

PRIDEQ9VGE8.

Genome annotation databases

EnsemblFBgn0037976. Drosophila melanogaster. [Contig view]
GeneID41456.
KEGGdme:Dmel_CG14734.
NMPDRfig|7227.3.peg.12357.

Organism-specific databases

FlyBaseFBgn0037976. Tk.

Phylogenomic databases

OMAQ9VGE8. GMRGKRP.

Gene expression databases

ArrayExpressQ9VGE8.

Family and domain databases

ProtoNetSearch...

Other Resources

NextBio823978.

Entry information

Entry nameTACHY_DROME
AccessionPrimary (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: June 16, 2009
This is version 46 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectDrosophila annotation project

Relevant documents

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents