Reviewed, UniProtKB/Swiss-Prot Q03751 (CSP_DROME)

Names and origin

Protein names

Recommended name:
    Cysteine string protein

Gene names

Name:	Csp
ORF Names:	CG6395

Organism

Drosophila melanogaster (Fruit fly) [Complete proteome]

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora

Protein attributes

Sequence length	249 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	May have an important role in presynaptic function.
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.
Post-translational modification	Fatty acylated. Heavily palmitoylated in the cysteine string motif.
Sequence similarities	Contains 1 J domain.

Ontologies

Keywords
Cellular component	Membrane
Coding sequence diversity	Alternative splicing
Molecular function	Chaperone
PTM	Lipoprotein Palmitate Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	exocytosis Inferred from mutant phenotype. Source: FlyBase neurotransmitter secretion Traceable author statement. Source: FlyBase protein folding Inferred from electronic annotation. Source: InterPro synaptic vesicle uncoating Traceable author statement. Source: FlyBase
Cellular component	membrane Inferred from electronic annotation. Source: UniProtKB-KW membrane fraction Inferred from direct assay. Source: FlyBase synaptic vesicle Traceable author statement. Source: FlyBase
Molecular function	heat shock protein binding Inferred from electronic annotation. Source: InterPro unfolded protein binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 249	249	Cysteine string protein		PRO_0000071075
Regions
	Domain	15 – 84	70	J
	Compositional bias	121 – 131	11	Poly-Cys
Amino acid modifications
	Modified residue	12	1	Phosphoserine
	Modified residue	13	1	Phosphothreonine
	Modified residue	14	1	Phosphoserine
	Modified residue	17	1	Phosphoserine
	Modified residue	19	1	Phosphotyrosine
Natural variations
	Alternative sequence	154 – 174	21	Missing in isoform CSP3 and isoform CSP2.		VSP_001293
	Alternative sequence	243 – 249	7	DMVNQKY → GI in isoform CSP3.		VSP_001294
Experimental info
	Sequence conflict	71	1	N → D in AAA28432. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform CSP1 (CSP32) (B) [UniParc]. Last modified October 1, 1996. Version 1. Checksum: 3EF97C3BF2553EB8	FASTA	249	26,896
	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
	Isoform CSP2 (C) [UniParc]. Checksum: C0F94C47CCA55BE5		228	24,557
	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 HLNEDVDLDD VNLGAGGAPV TSQPREQAGG 190 200 210 220 QPVFAMPPPS GAVGVNPFTG APVAANENTS LNTTEQTTYT PDMVNQKY
	Isoform CSP3 (CSP29) (A) [UniParc]. Checksum: B39935CBBB29D9D1		223	23,848
	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 HLNEDVDLDD VNLGAGGAPV TSQPREQAGG 190 200 210 220 QPVFAMPPPS GAVGVNPFTG APVAANENTS LNTTEQTTYT PGI

References

	« Hide 'large scale' referencesShow '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. , 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. , 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.
[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
EMBLGenBankDDBJ	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.
RefSeq	NP_524213.1. NP_730713.1. NP_730714.2.
UniGene	Dm.5140
3D structure databases
HSSP	HSSP built from PDB template 1HDJ based on UniProtKB P25685.
SMR	Q03751. Positions 8-102.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q03751.
Genome annotation databases
Ensembl	CG6395. Drosophila melanogaster. [Contig view]
GeneID	40459.
KEGG	dme:Dmel_CG6395.
Organism-specific databases
FlyBase	FBgn0004179. Csp.
Phylogenomic databases
HOGENOM	Q03751.
Gene expression databases
ArrayExpress	Q03751.
GermOnline	CG6395. Drosophila melanogaster.
Family and domain databases
InterPro	IPR001623. DnaJ_N. IPR015609. Hsp40/DnaJ_Rel. IPR003095. Hsp_DnaJ. [Graphical view]
Gene3D	G3DSA:1.10.287.110. DnaJ_N. 1 hit.
PANTHER	PTHR11821. Hsp40/DnaJ_Rel. 1 hit.
Pfam	PF00226. DnaJ. 1 hit. [Graphical view]
PRINTS	PR00625. DNAJPROTEIN.
SMART	SM00271. DnaJ. 1 hit. [Graphical view]
PROSITE	PS00636. DNAJ_1. 1 hit. PS50076. DNAJ_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	818882.

Entry information

Entry name

CSP_DROME

Accession

Primary (citable) accession number: Q03751
Secondary accession number(s): O61664 , O61665, Q95TD7, Q9VNV1

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	November 25, 2008
This is version 71 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Drosophila annotation project