DNJC5_DROME
ID DNJC5_DROME Reviewed; 249 AA.
AC Q03751; O61664; O61665; Q95TD7; Q9VNV1;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=DnaJ homolog subfamily C member 5 homolog {ECO:0000250|UniProtKB:Q9H3Z4};
DE AltName: Full=Cysteine string protein {ECO:0000303|PubMed:2129171};
GN Name=Csp {ECO:0000312|FlyBase:FBgn0004179}; ORFNames=CG6395;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS CSP1 AND CSP3), FUNCTION, AND TISSUE
RP SPECIFICITY.
RX PubMed=2129171; DOI=10.3109/01677069009084150;
RA Zinsmaier K.E., Hofbauer A., Heimbeck G., Pflugfelder G.O., Buchner S.,
RA Buchner E.;
RT "A cysteine-string protein is expressed in retina and brain of
RT Drosophila.";
RL J. Neurogenet. 7:15-29(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE (ISOFORMS CSP1; CSP2 AND CSP3), FUNCTION, AND TISSUE
RP SPECIFICITY.
RC STRAIN=Berlin;
RX PubMed=9799436; DOI=10.1007/s004410051170;
RA Eberle K.K., Zinsmaier K.E., Buchner S., Gruhn M., Jenni M., Arnold C.,
RA Leibold C., Reisch D., Walter N., Hafen E., Hofbauer A., Pflugfelder G.O.,
RA Buchner E.;
RT "Wide distribution of the cysteine string proteins in Drosophila tissues
RT revealed by targeted mutagenesis.";
RL Cell Tissue Res. 294:203-217(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [4]
RP GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 154-249 (ISOFORM CSP3).
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [6]
RP FUNCTION, AND TISSUE SPECIFICITY.
RC STRAIN=Berlin;
RX PubMed=8310297; DOI=10.1126/science.8310297;
RA Zinsmaier K.E., Eberle K.K., Buchner E., Walter N., Benzer S.;
RT "Paralysis and early death in cysteine string protein mutants of
RT Drosophila.";
RL Science 263:977-980(1994).
RN [7]
RP PALMITOYLATION.
RX PubMed=8601435; DOI=10.1016/0014-5793(96)00026-9;
RA van de Goor J., Kelly R.B.;
RT "Association of Drosophila cysteine string proteins with membranes.";
RL FEBS Lett. 380:251-256(1996).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12; THR-13; SER-14; SER-17
RP AND TYR-19, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
CC -!- FUNCTION: May have an important role in presynaptic function.
CC {ECO:0000269|PubMed:2129171, ECO:0000269|PubMed:8310297,
CC ECO:0000269|PubMed:9799436}.
CC -!- SUBCELLULAR LOCATION: Membrane; Lipid-anchor.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=CSP1; Synonyms=CSP32, B;
CC IsoId=Q03751-1; Sequence=Displayed;
CC Name=CSP2; Synonyms=C;
CC IsoId=Q03751-2; Sequence=VSP_001293;
CC Name=CSP3; Synonyms=CSP29, A;
CC IsoId=Q03751-3; Sequence=VSP_001293, VSP_001294;
CC -!- TISSUE SPECIFICITY: Expressed in wide range of synaptic terminals:
CC embryonic nervous system, larval neuromuscular junctions, adult visual
CC system (neuropil of optic ganglia and terminal of R1-8 photoreceptors)
CC and thoracic neuromuscular junctions. Also expressed in non-neuronal
CC cells: follicle cells, spermatheca, testis and ejaculatory bulb. Low
CC level of expression is found in many neuronal and non-neuronal tissues.
CC {ECO:0000269|PubMed:2129171, ECO:0000269|PubMed:8310297,
CC ECO:0000269|PubMed:9799436}.
CC -!- PTM: Fatty acylated. Heavily palmitoylated in the cysteine string
CC motif. {ECO:0000269|PubMed:8601435}.
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DR EMBL; M63421; AAA28432.1; -; mRNA.
DR EMBL; M63008; AAA28431.1; -; mRNA.
DR EMBL; AF057167; AAD09428.1; -; Genomic_DNA.
DR EMBL; AF057167; AAD09430.1; -; Genomic_DNA.
DR EMBL; AF057167; AAD09431.1; -; Genomic_DNA.
DR EMBL; AE014296; AAF51816.1; -; Genomic_DNA.
DR EMBL; AE014296; AAF51817.1; -; Genomic_DNA.
DR EMBL; AE014296; AAN12195.2; -; Genomic_DNA.
DR EMBL; AY059457; AAL13363.1; ALT_SEQ; mRNA.
DR RefSeq; NP_001287144.1; NM_001300215.1.
DR RefSeq; NP_524213.1; NM_079489.3.
DR RefSeq; NP_730713.1; NM_168949.2.
DR RefSeq; NP_730714.2; NM_168950.4.
DR AlphaFoldDB; Q03751; -.
DR SMR; Q03751; -.
DR BioGRID; 65696; 9.
DR IntAct; Q03751; 2.
DR STRING; 7227.FBpp0078146; -.
DR iPTMnet; Q03751; -.
DR SwissPalm; Q03751; -.
DR PaxDb; Q03751; -.
DR DNASU; 40459; -.
DR GeneID; 40459; -.
DR KEGG; dme:Dmel_CG6395; -.
DR CTD; 40459; -.
DR FlyBase; FBgn0004179; Csp.
DR VEuPathDB; VectorBase:FBgn0004179; -.
DR eggNOG; KOG0716; Eukaryota.
DR InParanoid; Q03751; -.
DR Reactome; R-DME-6798695; Neutrophil degranulation.
DR Reactome; R-DME-888590; GABA synthesis, release, reuptake and degradation.
DR BioGRID-ORCS; 40459; 0 hits in 3 CRISPR screens.
DR ChiTaRS; Csp; fly.
DR GenomeRNAi; 40459; -.
DR PRO; PR:Q03751; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR ExpressionAtlas; Q03751; baseline and differential.
DR Genevisible; Q03751; DM.
DR GO; GO:0005886; C:plasma membrane; ISS:FlyBase.
DR GO; GO:0008021; C:synaptic vesicle; IDA:FlyBase.
DR GO; GO:0043195; C:terminal bouton; IDA:FlyBase.
DR GO; GO:0061176; C:type Ib terminal bouton; IDA:FlyBase.
DR GO; GO:0061177; C:type Is terminal bouton; IDA:FlyBase.
DR GO; GO:0006887; P:exocytosis; IMP:FlyBase.
DR GO; GO:1903035; P:negative regulation of response to wounding; IMP:FlyBase.
DR GO; GO:0070050; P:neuron cellular homeostasis; IGI:FlyBase.
DR GO; GO:0006457; P:protein folding; NAS:FlyBase.
DR GO; GO:1900073; P:regulation of neuromuscular synaptic transmission; IGI:FlyBase.
DR GO; GO:0098693; P:regulation of synaptic vesicle cycle; IDA:SynGO.
DR GO; GO:0016079; P:synaptic vesicle exocytosis; ISS:FlyBase.
DR CDD; cd06257; DnaJ; 1.
DR Gene3D; 1.10.287.110; -; 1.
DR InterPro; IPR001623; DnaJ_domain.
DR InterPro; IPR018253; DnaJ_domain_CS.
DR InterPro; IPR036869; J_dom_sf.
DR Pfam; PF00226; DnaJ; 1.
DR PRINTS; PR00625; JDOMAIN.
DR SMART; SM00271; DnaJ; 1.
DR SUPFAM; SSF46565; SSF46565; 1.
DR PROSITE; PS00636; DNAJ_1; 1.
DR PROSITE; PS50076; DNAJ_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Chaperone; Lipoprotein; Membrane; Palmitate;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..249
FT /note="DnaJ homolog subfamily C member 5 homolog"
FT /id="PRO_0000071075"
FT DOMAIN 15..84
FT /note="J"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00286"
FT REGION 146..177
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 218..249
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 223..249
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 12
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 13
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 14
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 17
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 19
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT VAR_SEQ 154..174
FT /note="Missing (in isoform CSP3 and isoform CSP2)"
FT /evidence="ECO:0000303|PubMed:12537569,
FT ECO:0000303|PubMed:2129171"
FT /id="VSP_001293"
FT VAR_SEQ 243..249
FT /note="DMVNQKY -> GI (in isoform CSP3)"
FT /evidence="ECO:0000303|PubMed:12537569,
FT ECO:0000303|PubMed:2129171"
FT /id="VSP_001294"
FT CONFLICT 71
FT /note="N -> D (in Ref. 1; AAA28432)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 249 AA; 26896 MW; 3EF97C3BF2553EB8 CRC64;
MSAPGMDKRK LSTSGDSLYE ILGLPKTATG DDIKKTYRKL ALKYHPDKNP DNVDAADKFK
EVNRAHSILS NQTKRNIYDN YGSLGLYIAE QFGEENVNAY FVVTSPAVKA VVICCAVITG
CCCCCCCCCC CNFCCGKFKP PVNESHDQYS HLNRPDGNRE GNDMPTHLGQ PPRLEDVDLD
DVNLGAGGAP VTSQPREQAG GQPVFAMPPP SGAVGVNPFT GAPVAANENT SLNTTEQTTY
TPDMVNQKY
