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UniProtKB/Swiss-Prot entry P09040


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name DSK_DROME
Primary accession number P09040
Secondary accession numbers B2ZB94 Q8MYU9 Q9VMY4
Integrated into Swiss-Prot on November 1, 1988
Sequence was last modified on August 15, 2003 (Sequence version 2)
Annotations were last modified on    September 23, 2008 (Entry version 84)
Name and origin of the protein
Protein name Drosulfakinins [Precursor]
Synonyms None
Contains Drosulfakinin-0
     (DSK-0)
Drosulfakinin-1
     (Drosulfakinin I)
     (DSK-I)
Drosulfakinin-2
     (Drosulfakinin II)
     (DSK-II)
Gene name
Name: Dsk
ORFNames: CG18090
From
Drosophila melanogaster (Fruit fly) [TaxID: 7227] 
Taxonomy Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea; Drosophilidae; Drosophila; Sophophora.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
STRAIN=Canton-S;
PubMed=2842322 [NCBI, ExPASy, EBI, Israel, Japan]
Nichols R., Schneuwly S.A., Dixon J.E.;
"Identification and characterization of a Drosophila homologue to the vertebrate neuropeptide cholecystokinin.";
J. Biol. Chem. 263:12167-12170(1988).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Ke F.;
"A molecular phylogeny for the Drosophila melanogaster subgroup.";
Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley;
DOI=10.1126/science.287.5461.2185; PubMed=10731132 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[4]
GENOME REANNOTATION.
PubMed=12537572 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Berkeley;
TISSUE=Head;
PubMed=12537569 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"A Drosophila full-length cDNA resource.";
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
[6]
PROTEIN SEQUENCE OF 126-139, SULFATION AT TYR-134, AND AMIDATION.
TISSUE=Larva;
DOI=10.1074/jbc.M206257200; PubMed=12171930 [NCBI, ExPASy, EBI, Israel, Japan]
Baggerman G., Cerstiaens A., De Loof A., Schoofs L.;
"Peptidomics of the larval Drosophila melanogaster central nervous system.";
J. Biol. Chem. 277:40368-40374(2002).
[7]
TISSUE SPECIFICITY.
PubMed=8350979 [NCBI, ExPASy, EBI, Israel, Japan]
Tibbetts M.F., Nichols R.;
"Immunocytochemistry of sequence-related neuropeptides in Drosophila.";
Neuropeptides 24:321-325(1993).
[8]
TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
PubMed=8581950 [NCBI, ExPASy, EBI, Israel, Japan]
Nichols R., Lim I.A.;
"Spatial and temporal immunocytochemical analysis of drosulfakinin (Dsk) gene products in the Drosophila melanogaster central nervous system.";
Cell Tissue Res. 283:107-116(1996).
[9]
FUNCTION, AND TISSUE SPECIFICITY.
STRAIN=Oregon-R;
DOI=10.1016/j.jinsphys.2007.06.001; PubMed=17632121 [NCBI, ExPASy, EBI, Israel, Japan]
Palmer G.C., Tran T., Duttlinger A., Nichols R.;
"The drosulfakinin 0 (DSK 0) peptide encoded in the conserved Dsk gene affects adult Drosophila melanogaster crop contractions.";
J. Insect Physiol. 53:1125-1133(2007).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
J03957; AAB03703.1; ALT_FRAME; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
EU635459; ACC99368.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AE014297; AAF52173.2; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY113595; AAM29600.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A31101; A31101.
RefSeq NP_524845.2; -.
UniGene Dm.20555
3D structure databases
ModBase P09040.
Protein-protein interaction databases
DIP DIP:19456N; -.
IntAct P09040; -.
Enzyme and pathway databases
BioCyc DMEL-XXX-02:DMEL-XXX-02-009851-MON; -.
Organism-specific databases
FlyBase FBgn0000500; Dsk.
Gene expression databases
ArrayExpress P09040; -.
GermOnline CG18090; Drosophila melanogaster.
Ontologies
GO
GO:0005184; Molecular function: neuropeptide hormone activity (traceable author statement from FlyBase).
GO:0007218; Biological process: neuropeptide signaling pathway (non-traceable author statement from FlyBase).
QuickGo view.
Family and domain databases
InterPro IPR013152; Gastrin_CCK_CS.
IPR013259; Sulfakinin.
Graphical view of domain structure.
Pfam PF08257; Sulfakinin; 2.
Pfam graphical view of domain structure.
PROSITE PS00259; GASTRIN; 2.
BLOCKS P09040.
Genome annotation databases
Ensembl CG18090; Drosophila melanogaster. [Contig view]
GeneID 45845; -.
KEGG dme:Dmel_CG18090; -.
NMPDR fig|7227.3.peg.5658; -.
Phylogenomic databases
HOGENOM P09040; -.
Other
ProtoNet P09040.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Amidation; Cleavage on pair of basic residues; Complete proteome; Direct protein sequencing; Hormone; Secreted; Signal; Sulfation.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
SIGNAL   1    33  33     Potential. 
PROPEP   34    73  40      PRO_0000010666
PEPTIDE   76    82  7     Drosulfakinin-0 (Potential). PRO_0000010667
PROPEP   86   111  26      PRO_0000010668
PEPTIDE   114   122  9     Drosulfakinin-1 (Potential). PRO_0000010669
PEPTIDE   126   139  14     Drosulfakinin-2. PRO_0000010670
MOD_RES   82    82        Phenylalanine amide (Potential). 
MOD_RES   117   117        Sulfotyrosine (Potential). 
MOD_RES   122   122        Phenylalanine amide (Potential). 
MOD_RES   134   134        Sulfotyrosine. 
MOD_RES   139   139        Phenylalanine amide. 
Sequence information
Length: 141 AA [This is the length of the unprocessed precursor] Molecular weight: 16151 Da [This is the MW of the unprocessed precursor] CRC64: 496AD66494696C88 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MGPRSCTHFA TLFMPLWALA FCFLVVLPIP AQTTSLQNAK DDRRLQELES KIGGEIDQPI 

        70         80         90        100        110        120 
ANLVGPSFSL FGDRRNQKTM SFGRRVPLIS RPIIPIELDL LMDNDDERTK AKRFDDYGHM 

       130        140 
RFGKRGGDDQ FDDYGHMRFG R 

P09040 in FASTA format

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