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UniProtKB/Swiss-Prot entry Q03751


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

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Entry information
Entry name CSP_DROME
Primary accession number Q03751
Secondary accession numbers O61664 O61665 Q95TD7 Q9VNV1
Integrated into Swiss-Prot on October 1, 1996
Sequence was last modified on October 1, 1996 (Sequence version 1)
Annotations were last modified on    September 2, 2008 (Entry version 69)
Name and origin of the protein
Protein name Cysteine string protein
Synonyms None
Gene name
Name: Csp
ORFNames: CG6395
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 [MRNA] (ISOFORMS CSP1 AND CSP3), FUNCTION, AND TISSUE SPECIFICITY.
PubMed=2129171 [NCBI, ExPASy, EBI, Israel, Japan]
Zinsmaier K.E., Hofbauer A., Heimbeck G., Pflugfelder G.O., Buchner S., Buchner E.;
"A cysteine-string protein is expressed in retina and brain of Drosophila.";
J. Neurogenet. 7:15-29(1990).
[2]
NUCLEOTIDE SEQUENCE (ISOFORMS CSP1; CSP2 AND CSP3), FUNCTION, AND TISSUE SPECIFICITY.
STRAIN=Berlin;
DOI=10.1007/s004410051170; PubMed=9799436 [NCBI, ExPASy, EBI, Israel, Japan]
Eberle K.K., Zinsmaier K.E., Buchner S., Gruhn M., Jenni M., Arnold C., Leibold C., Reisch D., Walter N., Hafen E., Hofbauer A., Pflugfelder G.O., Buchner E.;
"Wide distribution of the cysteine string proteins in Drosophila tissues revealed by targeted mutagenesis.";
Cell Tissue Res. 294:203-217(1998).
[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, AND ALTERNATIVE SPLICING.
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] OF 154-249 (ISOFORM CSP3).
STRAIN=Berkeley;
TISSUE=Embryo;
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]
FUNCTION, AND TISSUE SPECIFICITY.
STRAIN=Berlin;
PubMed=8310297 [NCBI, ExPASy, EBI, Israel, Japan]
Zinsmaier K.E., Eberle K.K., Buchner E., Walter N., Benzer S.;
"Paralysis and early death in cysteine string protein mutants of Drosophila.";
Science 263:977-980(1994).
[7]
ACYLATION.
DOI=10.1016/0014-5793(96)00026-9; PubMed=8601435 [NCBI, ExPASy, EBI, Israel, Japan]
van de Goor J., Kelly R.B.;
"Association of Drosophila cysteine string proteins with membranes.";
FEBS Lett. 380:251-256(1996).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12; THR-13; SER-14; SER-17 AND TYR-19, AND MASS SPECTROMETRY.
TISSUE=Embryo;
DOI=10.1021/pr700696a; PubMed=18327897 [NCBI, ExPASy, EBI, Israel, Japan]
Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
"Phosphoproteome analysis of Drosophila melanogaster embryos.";
J. Proteome Res. 7:1675-1682(2008).
Comments
  • FUNCTION: May have an important role in presynaptic function.
  • SUBCELLULAR LOCATION: Membrane; Lipid-anchor.
  • ALTERNATIVE PRODUCTS: 3 named isoforms [FASTA] produced by alternative splicing.
    NameCSP1
    SynonymsCSP32, B
    Isoform IDQ03751-1
    This is the isoform sequence displayed in this entry.
    NameCSP2
    SynonymsC
    Isoform IDQ03751-2
    Features which should be applied to build the isoform sequence: VSP_001293.
    NameCSP3
    SynonymsCSP29, A
    Isoform IDQ03751-3
    Features which should be applied to build the isoform sequence: VSP_001293, VSP_001294.
  • TISSUE SPECIFICITY: Expressed in wide range of synaptic terminals: embryonic nervous system, larval neuromuscular junctions, adult visual system (neuropil of optic ganglia and terminal of R1-8 photoreceptors) and thoracic neuromuscular junctions. Also expressed in non-neuronal cells: follicle cells, spermatheca, testis and ejaculatory bulb. Low level of expression is found in many neuronal and non-neuronal tissues.
  • PTM: Fatty acylated. Heavily palmitoylated in the cysteine string motif.
  • SIMILARITY: Contains 1 J domain.
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
M63421; AAA28432.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M63008; AAA28431.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF057167; AAD09428.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF057167; AAD09430.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF057167; AAD09431.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AE014296; AAF51816.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AE014296; AAF51817.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AE014296; AAN12195.2; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY059457; AAL13363.1; ALT_SEQ; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_524213.1; -.
NP_730713.1; -.
NP_730714.2; -.
UniGene Dm.5140
3D structure databases
HSSP P25685; 1HDJ. [HSSP ENTRY / PDB]
SMR Q03751; 8-102.
ModBase Q03751.
Protein-protein interaction databases
IntAct Q03751; -.
Organism-specific databases
FlyBase FBgn0004179; Csp.
Gene expression databases
ArrayExpress Q03751; -.
GermOnline CG6395; Drosophila melanogaster.
Ontologies
GO
GO:0005624; Cellular component: membrane fraction (inferred from direct assay from FlyBase).
GO:0008021; Cellular component: synaptic vesicle (traceable author statement from FlyBase).
GO:0006887; Biological process: exocytosis (inferred from mutant phenotype from FlyBase).
GO:0007269; Biological process: neurotransmitter secretion (traceable author statement from FlyBase).
GO:0006457; Biological process: protein folding (non-traceable author statement from FlyBase).
GO:0016191; Biological process: synaptic vesicle uncoating (traceable author statement from FlyBase).
QuickGo view.
Family and domain databases
InterPro IPR001623; DnaJ_N.
IPR015609; Hsp40/DnaJ_Rel.
IPR003095; Hsp_DnaJ.
Graphical view of domain structure.
Gene3D G3DSA:1.10.287.110; DnaJ_N; 1.
PANTHER PTHR11821; Hsp40/DnaJ_Rel; 1.
Pfam PF00226; DnaJ; 1.
Pfam graphical view of domain structure.
PRINTS PR00625; DNAJPROTEIN.
SMART SM00271; DnaJ; 1.
SMART graphical view of domain structure.
PROSITE PS00636; DNAJ_1; 1.
PS50076; DNAJ_2; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS Q03751.
Genome annotation databases
Ensembl CG6395; Drosophila melanogaster. [Contig view]
GeneID 40459; -.
KEGG dme:Dmel_CG6395; -.
Phylogenomic databases
HOGENOM Q03751; -.
Other
ProtoNet Q03751.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Alternative splicing; Chaperone; Complete proteome; Lipoprotein; Membrane; Palmitate; Phosphoprotein.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   249  249     Cysteine string protein. PRO_0000071075
DOMAIN   15    84  70     J. 
COMPBIAS   121   131  11     Poly-Cys. 
MOD_RES   12    12        Phosphoserine. 
MOD_RES   13    13        Phosphothreonine. 
MOD_RES   14    14        Phosphoserine. 
MOD_RES   17    17        Phosphoserine. 
MOD_RES   19    19        Phosphotyrosine. 
VAR_SEQ   154   174        Missing (in isoform CSP3 and isoform CSP2). VSP_001293
VAR_SEQ   243   249        DMVNQKY -> GI (in isoform CSP3). VSP_001294
CONFLICT   71    71        N -> D (in Ref. 1; AAA28432). 
Sequence information
Length: 249 AA [This is the length of the unprocessed precursor] Molecular weight: 26896 Da [This is the MW of the unprocessed precursor] CRC64: 3EF97C3BF2553EB8 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSAPGMDKRK LSTSGDSLYE ILGLPKTATG DDIKKTYRKL ALKYHPDKNP DNVDAADKFK 

        70         80         90        100        110        120 
EVNRAHSILS NQTKRNIYDN YGSLGLYIAE QFGEENVNAY FVVTSPAVKA VVICCAVITG 

       130        140        150        160        170        180 
CCCCCCCCCC CNFCCGKFKP PVNESHDQYS HLNRPDGNRE GNDMPTHLGQ PPRLEDVDLD 

       190        200        210        220        230        240 
DVNLGAGGAP VTSQPREQAG GQPVFAMPPP SGAVGVNPFT GAPVAANENT SLNTTEQTTY 


TPDMVNQKY 

Q03751 in FASTA format

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