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Protein

Cysteine string protein

Gene

Csp

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

May have an important role in presynaptic function.3 Publications

GO - Biological processi

  • brain morphogenesis Source: FlyBase
  • exocytosis Source: FlyBase
  • locomotion involved in locomotory behavior Source: FlyBase
  • neurotransmitter secretion Source: FlyBase
  • protein folding Source: FlyBase
  • startle response Source: FlyBase
  • synaptic vesicle exocytosis Source: FlyBase
  • synaptic vesicle uncoating Source: FlyBase
  • vesicle-mediated transport Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Names & Taxonomyi

Protein namesi
Recommended name:
Cysteine string protein
Gene namesi
Name:Csp
ORF Names:CG6395
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803 Componenti: Chromosome 3L

Organism-specific databases

FlyBaseiFBgn0004179. Csp.

Subcellular locationi

GO - Cellular componenti

  • plasma membrane Source: FlyBase
  • synaptic vesicle Source: FlyBase
  • terminal bouton Source: FlyBase
  • type Ib terminal bouton Source: FlyBase
  • type Is terminal bouton Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 249249Cysteine string proteinPRO_0000071075Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei12 – 121Phosphoserine1 Publication
Modified residuei13 – 131Phosphothreonine1 Publication
Modified residuei14 – 141Phosphoserine1 Publication
Modified residuei17 – 171Phosphoserine1 Publication
Modified residuei19 – 191Phosphotyrosine1 Publication

Post-translational modificationi

Fatty acylated. Heavily palmitoylated in the cysteine string motif.1 Publication

Keywords - PTMi

Lipoprotein, Palmitate, Phosphoprotein

Proteomic databases

PaxDbiQ03751.
PRIDEiQ03751.

Expressioni

Tissue specificityi

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.3 Publications

Gene expression databases

BgeeiQ03751.
GenevisibleiQ03751. DM.

Interactioni

Protein-protein interaction databases

BioGridi65696. 3 interactions.
IntActiQ03751. 2 interactions.
STRINGi7227.FBpp0078146.

Structurei

3D structure databases

ProteinModelPortaliQ03751.
SMRiQ03751. Positions 8-102.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini15 – 8470JPROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi121 – 13111Poly-CysAdd
BLAST

Sequence similaritiesi

Contains 1 J domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0484.
InParanoidiQ03751.
KOiK09525.
OrthoDBiEOG7WHHBD.

Family and domain databases

Gene3Di1.10.287.110. 1 hit.
InterProiIPR001623. DnaJ_domain.
IPR018253. DnaJ_domain_CS.
[Graphical view]
PfamiPF00226. DnaJ. 1 hit.
[Graphical view]
PRINTSiPR00625. JDOMAIN.
SMARTiSM00271. DnaJ. 1 hit.
[Graphical view]
SUPFAMiSSF46565. SSF46565. 1 hit.
PROSITEiPS00636. DNAJ_1. 1 hit.
PS50076. DNAJ_2. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform CSP1 (identifier: Q03751-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MSAPGMDKRK LSTSGDSLYE ILGLPKTATG DDIKKTYRKL ALKYHPDKNP
60 70 80 90 100
DNVDAADKFK EVNRAHSILS NQTKRNIYDN YGSLGLYIAE QFGEENVNAY
110 120 130 140 150
FVVTSPAVKA VVICCAVITG CCCCCCCCCC CNFCCGKFKP PVNESHDQYS
160 170 180 190 200
HLNRPDGNRE GNDMPTHLGQ PPRLEDVDLD DVNLGAGGAP VTSQPREQAG
210 220 230 240
GQPVFAMPPP SGAVGVNPFT GAPVAANENT SLNTTEQTTY TPDMVNQKY
Length:249
Mass (Da):26,896
Last modified:October 1, 1996 - v1
Checksum:i3EF97C3BF2553EB8
GO
Isoform CSP2 (identifier: Q03751-2) [UniParc]FASTAAdd to basket

Also known as: C

The sequence of this isoform differs from the canonical sequence as follows:
     154-174: Missing.

Show »
Length:228
Mass (Da):24,557
Checksum:iC0F94C47CCA55BE5
GO
Isoform CSP3 (identifier: Q03751-3) [UniParc]FASTAAdd to basket

Also known as: CSP29, A

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

Show »
Length:223
Mass (Da):23,848
Checksum:iB39935CBBB29D9D1
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti71 – 711N → D in AAA28432 (PubMed:2129171).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei154 – 17421Missing in isoform CSP3 and isoform CSP2. 2 PublicationsVSP_001293Add
BLAST
Alternative sequencei243 – 2497DMVNQKY → GI in isoform CSP3. 2 PublicationsVSP_001294

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
RefSeqiNP_001287144.1. NM_001300215.1.
NP_524213.1. NM_079489.3.
NP_730713.1. NM_168949.2.
NP_730714.2. NM_168950.4.
UniGeneiDm.5140.

Genome annotation databases

GeneIDi40459.
KEGGidme:Dmel_CG6395.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
RefSeqiNP_001287144.1. NM_001300215.1.
NP_524213.1. NM_079489.3.
NP_730713.1. NM_168949.2.
NP_730714.2. NM_168950.4.
UniGeneiDm.5140.

3D structure databases

ProteinModelPortaliQ03751.
SMRiQ03751. Positions 8-102.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi65696. 3 interactions.
IntActiQ03751. 2 interactions.
STRINGi7227.FBpp0078146.

Proteomic databases

PaxDbiQ03751.
PRIDEiQ03751.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi40459.
KEGGidme:Dmel_CG6395.

Organism-specific databases

CTDi40459.
FlyBaseiFBgn0004179. Csp.

Phylogenomic databases

eggNOGiCOG0484.
InParanoidiQ03751.
KOiK09525.
OrthoDBiEOG7WHHBD.

Miscellaneous databases

ChiTaRSiCsp. fly.
GenomeRNAii40459.
NextBioi818882.
PROiQ03751.

Gene expression databases

BgeeiQ03751.
GenevisibleiQ03751. DM.

Family and domain databases

Gene3Di1.10.287.110. 1 hit.
InterProiIPR001623. DnaJ_domain.
IPR018253. DnaJ_domain_CS.
[Graphical view]
PfamiPF00226. DnaJ. 1 hit.
[Graphical view]
PRINTSiPR00625. JDOMAIN.
SMARTiSM00271. DnaJ. 1 hit.
[Graphical view]
SUPFAMiSSF46565. SSF46565. 1 hit.
PROSITEiPS00636. DNAJ_1. 1 hit.
PS50076. DNAJ_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [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] [Europe PMC] [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.
    , 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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  4. Cited for: GENOME REANNOTATION, ALTERNATIVE SPLICING.
    Strain: Berkeley.
  5. 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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: PALMITOYLATION.
  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] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12; THR-13; SER-14; SER-17 AND TYR-19, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Embryo.

Entry informationi

Entry nameiCSP_DROME
AccessioniPrimary (citable) accession number: Q03751
Secondary accession number(s): O61664
, O61665, Q95TD7, Q9VNV1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: June 24, 2015
This is version 115 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.