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Q03751 (CSP_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified April 18, 2012. Version 95. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cysteine string protein
Gene names
Name:Csp
ORF Names:CG6395
OrganismDrosophila melanogaster (Fruit fly)
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora

Protein attributes

Sequence length249 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May have an important role in presynaptic function. Ref.1 Ref.2 Ref.6

Subcellular location

Membrane; Lipid-anchor.

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. Ref.1 Ref.2 Ref.6

Post-translational modification

Fatty acylated. Heavily palmitoylated in the cysteine string motif.

Sequence similarities

Contains 1 J domain.

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform CSP1 (identifier: Q03751-1)

Also known as: CSP32; B;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform CSP2 (identifier: Q03751-2)

Also known as: C;

The sequence of this isoform differs from the canonical sequence as follows:
     154-174: Missing.
Isoform CSP3 (identifier: Q03751-3)

Also known as: CSP29; A;

The sequence of this isoform differs from the canonical sequence as follows:
     154-174: Missing.
     243-249: DMVNQKY → GI

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 249249Cysteine string protein
PRO_0000071075

Regions

Domain15 – 8470J
Compositional bias121 – 13111Poly-Cys

Amino acid modifications

Modified residue121Phosphoserine Ref.8
Modified residue131Phosphothreonine Ref.8
Modified residue141Phosphoserine Ref.8
Modified residue171Phosphoserine Ref.8
Modified residue191Phosphotyrosine Ref.8

Natural variations

Alternative sequence154 – 17421Missing in isoform CSP3 and isoform CSP2.
VSP_001293
Alternative sequence243 – 2497DMVNQKY → GI in isoform CSP3.
VSP_001294

Experimental info

Sequence conflict711N → D in AAA28432. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform CSP1 (CSP32) (B) [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 3EF97C3BF2553EB8

FASTA24926,896
        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

« Hide

Isoform CSP2 (C) [UniParc].

Checksum: C0F94C47CCA55BE5
Show »

FASTA22824,557
Isoform CSP3 (CSP29) (A) [UniParc].

Checksum: B39935CBBB29D9D1
Show »

FASTA22323,848

References

« Hide 'large scale' references
[1]"A cysteine-string protein is expressed in retina and brain of Drosophila."
Zinsmaier K.E., Hofbauer A., Heimbeck G., Pflugfelder G.O., Buchner S., Buchner E.
J. Neurogenet. 7:15-29(1990) [PubMed: 2129171] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS CSP1 AND CSP3), FUNCTION, TISSUE SPECIFICITY.
[2]"Wide distribution of the cysteine string proteins in Drosophila tissues revealed by targeted mutagenesis."
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.
Cell Tissue Res. 294:203-217(1998) [PubMed: 9799436] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE (ISOFORMS CSP1; CSP2 AND CSP3), FUNCTION, TISSUE SPECIFICITY.
Strain: Berlin.
[3]"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.
[4]"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, ALTERNATIVE SPLICING.
Strain: Berkeley.
[5]"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] OF 154-249 (ISOFORM CSP3).
Strain: Berkeley.
Tissue: Embryo.
[6]"Paralysis and early death in cysteine string protein mutants of Drosophila."
Zinsmaier K.E., Eberle K.K., Buchner E., Walter N., Benzer S.
Science 263:977-980(1994) [PubMed: 8310297] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY.
Strain: Berlin.
[7]"Association of Drosophila cysteine string proteins with membranes."
van de Goor J., Kelly R.B.
FEBS Lett. 380:251-256(1996) [PubMed: 8601435] [Abstract]
Cited for: ACYLATION.
[8]"Phosphoproteome analysis of Drosophila melanogaster embryos."
Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.
J. Proteome Res. 7:1675-1682(2008) [PubMed: 18327897] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12; THR-13; SER-14; SER-17 AND TYR-19, MASS SPECTROMETRY.
Tissue: Embryo.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		M63421 mRNA. Translation: AAA28432.1.
M63008 mRNA. Translation: AAA28431.1.
AF057167 Genomic DNA. Translation: AAD09428.1.
AF057167 Genomic DNA. Translation: AAD09430.1.
AF057167 Genomic DNA. Translation: AAD09431.1.
AE014296 Genomic DNA. Translation: AAF51816.1.
AE014296 Genomic DNA. Translation: AAF51817.1.
AE014296 Genomic DNA. Translation: AAN12195.2.
AY059457 mRNA. Translation: AAL13363.1. Sequence problems.
RefSeqNP_524213.1. NM_079489.2.
NP_730713.1. NM_168949.1.
NP_730714.2. NM_168950.2.
UniGeneDm.5140.

3D structure databases

ProteinModelPortalQ03751.
SMRQ03751. Positions 8-102.
ModBaseSearch...

Protein-protein interaction databases

IntActQ03751. 2 interactions.
STRINGQ03751.

Proteomic databases

PRIDEQ03751.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID40459.
KEGGdme:Dmel_CG6395.

Organism-specific databases

CTD40459.
FlyBaseFBgn0004179. Csp.

Phylogenomic databases

eggNOGCOG0484.
InParanoidQ03751.
KOK09525.
OrthoDBEOG4C5B1S.

Gene expression databases

BgeeQ03751.
GermOnlineCG6395. Drosophila melanogaster.

Family and domain databases

Gene3DG3DSA:1.10.287.110. DnaJ_N. 1 hit.
InterProIPR001623. DnaJ_N.
IPR018253. Heat_shock_DnaJ_CS.
IPR003095. Hsp_DnaJ.
[Graphical view]
PfamPF00226. DnaJ. 1 hit.
[Graphical view]
PRINTSPR00625. JDOMAIN.
SMARTSM00271. DnaJ. 1 hit.
[Graphical view]
SUPFAMSSF46565. DnaJ_N. 1 hit.
PROSITEPS00636. DNAJ_1. 1 hit.
PS50076. DNAJ_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio818882.

Entry information

Entry nameCSP_DROME
AccessionPrimary (citable) accession number: Q03751
Secondary accession number(s): O61664 expand/collapse secondary AC list , O61665, Q95TD7, Q9VNV1
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: April 18, 2012
This is version 95 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

Drosophila

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

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents