DNJC5_RAT
ID DNJC5_RAT Reviewed; 198 AA.
AC P60905; P54101;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 13-APR-2004, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=DnaJ homolog subfamily C member 5 {ECO:0000305};
DE AltName: Full=Cysteine string protein {ECO:0000303|PubMed:7535880};
DE Short=CSP {ECO:0000303|PubMed:7535880};
GN Name=Dnajc5 {ECO:0000312|RGD:620516};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RX PubMed=7535880; DOI=10.1016/0169-328x(94)00172-b;
RA Mastrogiacomo A., Gundersen C.B.;
RT "The nucleotide and deduced amino acid sequence of a rat cysteine string
RT protein.";
RL Brain Res. Mol. Brain Res. 28:12-18(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=8606785; DOI=10.1016/0028-3908(95)00114-l;
RA Braun J.E., Scheller R.H.;
RT "Cysteine string protein, a DnaJ family member, is present on diverse
RT secretory vesicles.";
RL Neuropharmacology 34:1361-1369(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Frontal cortex;
RX PubMed=11257428; DOI=10.1016/s0304-3940(01)01638-x;
RA Yamada M., Yamada M., Yamazaki S., Takahashi K., Nara K., Ozawa H.,
RA Yamada S., Kiuchi Y., Oguchi K., Kamijima K., Higuchi T., Momose K.;
RT "Induction of cysteine string protein after chronic antidepressant
RT treatment in rat frontal cortex.";
RL Neurosci. Lett. 301:183-186(2001).
RN [4]
RP PROTEIN SEQUENCE OF 8-24 AND 42-73, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RA Lubec G., Kang S.U., Lubec S.;
RL Submitted (SEP-2007) to UniProtKB.
RN [5]
RP PROTEIN SEQUENCE OF 8-24, AND PHOSPHORYLATION AT SER-10.
RX PubMed=11604405; DOI=10.1074/jbc.m108186200;
RA Evans G.J., Wilkinson M.C., Graham M.E., Turner K.M., Chamberlain L.H.,
RA Burgoyne R.D., Morgan A.;
RT "Phosphorylation of cysteine string protein by protein kinase A.
RT Implications for the modulation of exocytosis.";
RL J. Biol. Chem. 276:47877-47885(2001).
RN [6]
RP PHOSPHORYLATION, AND INTERACTION WITH SYT1.
RX PubMed=11931641; DOI=10.1042/bj20020123;
RA Evans G.J., Morgan A.;
RT "Phosphorylation-dependent interaction of the synaptic vesicle proteins
RT cysteine string protein and synaptotagmin I.";
RL Biochem. J. 364:343-347(2002).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-8; SER-10; SER-12; SER-15 AND
RP SER-151, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [8]
RP INTERACTION WITH ZDHHC17.
RX PubMed=25253725; DOI=10.1091/mbc.e14-06-1169;
RA Lemonidis K., Gorleku O.A., Sanchez-Perez M.C., Grefen C.,
RA Chamberlain L.H.;
RT "The Golgi S-acylation machinery comprises zDHHC enzymes with major
RT differences in substrate affinity and S-acylation activity.";
RL Mol. Biol. Cell 25:3870-3883(2014).
RN [9]
RP REVIEW.
RX PubMed=25800794; DOI=10.1016/j.semcdb.2015.03.008;
RA Burgoyne R.D., Morgan A.;
RT "Cysteine string protein (CSP) and its role in preventing
RT neurodegeneration.";
RL Semin. Cell Dev. Biol. 40:153-159(2015).
CC -!- FUNCTION: Acts as a general chaperone in regulated exocytosis (By
CC similarity). Acts as a co-chaperone for the SNARE protein SNAP-25 (By
CC similarity). Involved in the calcium-mediated control of a late stage
CC of exocytosis (By similarity). May have an important role in
CC presynaptic function. May be involved in calcium-dependent
CC neurotransmitter release at nerve endings (By similarity).
CC {ECO:0000250, ECO:0000250|UniProtKB:P60904,
CC ECO:0000250|UniProtKB:Q29455}.
CC -!- SUBUNIT: Homodimer (By similarity). Interacts with the chaperone
CC complex consisting of HSC70 and SGTA (By similarity). Interacts with
CC ZDHHC13 (via ANK repeats) (By similarity). Interacts with ZDHHC17 (via
CC ANK repeats) (PubMed:25253725). Interacts with SYT1, SYT5 and SYT7, and
CC with SYT9, forming a complex with SNAP25 (By similarity). Interacts
CC with SYT1 in a phosphorylation-dependent manner (PubMed:11931641).
CC {ECO:0000250|UniProtKB:P60904, ECO:0000269|PubMed:11931641,
CC ECO:0000269|PubMed:25253725}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q29455}. Membrane
CC {ECO:0000250|UniProtKB:Q29455}; Lipid-anchor
CC {ECO:0000250|UniProtKB:Q29455}. Cytoplasmic vesicle, secretory vesicle,
CC chromaffin granule membrane {ECO:0000250|UniProtKB:Q29455}. Melanosome
CC {ECO:0000250|UniProtKB:Q9H3Z4}. Cell membrane
CC {ECO:0000250|UniProtKB:Q9H3Z4}. Note=The association with membranes is
CC regulated by palmitoylation. {ECO:0000250|UniProtKB:Q29455}.
CC -!- TISSUE SPECIFICITY: Brain. Predominantly associated with nerve endings
CC and synaptic vesicles.
CC -!- PTM: Phosphorylated (PubMed:11931641). Phosphorylation results in a
CC profound decrease in the affinity for syntaxin but has no effect on the
CC affinity for HSC70 (PubMed:11604405, PubMed:11931641). Ser-10
CC phosphorylation induces an order-to-disorder transition triggering the
CC interaction with Lys-58 (By similarity). This conformational switch
CC modulates DNAJC5's cellular functions by reducing binding to syntaxin
CC and synaptogamin without altering HSC70 interactions (By similarity).
CC {ECO:0000250|UniProtKB:Q9H3Z4, ECO:0000269|PubMed:11604405,
CC ECO:0000269|PubMed:11931641}.
CC -!- PTM: Palmitoylated. Could be palmitoylated by DHHC3, DHHC7, DHHC15 and
CC DHHC17. Palmitoylation occurs probably in the cysteine-rich domain and
CC regulates DNAJC5 membrane attachment. {ECO:0000250|UniProtKB:Q29455}.
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DR EMBL; U39320; AAA81372.1; -; mRNA.
DR EMBL; S81917; AAB36303.1; -; mRNA.
DR EMBL; AF323955; AAL04453.1; -; mRNA.
DR PIR; I52655; I52655.
DR RefSeq; NP_077075.1; NM_024161.2.
DR RefSeq; XP_008760766.1; XM_008762544.2.
DR RefSeq; XP_008760767.1; XM_008762545.2.
DR AlphaFoldDB; P60905; -.
DR SMR; P60905; -.
DR BioGRID; 249414; 2.
DR CORUM; P60905; -.
DR STRING; 10116.ENSRNOP00000020581; -.
DR iPTMnet; P60905; -.
DR PhosphoSitePlus; P60905; -.
DR SwissPalm; P60905; -.
DR jPOST; P60905; -.
DR PaxDb; P60905; -.
DR PRIDE; P60905; -.
DR Ensembl; ENSRNOT00000020581; ENSRNOP00000020581; ENSRNOG00000015202.
DR GeneID; 79130; -.
DR KEGG; rno:79130; -.
DR UCSC; RGD:620516; rat.
DR CTD; 80331; -.
DR RGD; 620516; Dnajc5.
DR eggNOG; KOG0716; Eukaryota.
DR GeneTree; ENSGT00940000155597; -.
DR InParanoid; P60905; -.
DR OMA; CKPRPRD; -.
DR OrthoDB; 1401920at2759; -.
DR PhylomeDB; P60905; -.
DR TreeFam; TF105164; -.
DR Reactome; R-RNO-6798695; Neutrophil degranulation.
DR Reactome; R-RNO-888590; GABA synthesis, release, reuptake and degradation.
DR PRO; PR:P60905; -.
DR Proteomes; UP000002494; Chromosome 3.
DR Bgee; ENSRNOG00000015202; Expressed in frontal cortex and 19 other tissues.
DR ExpressionAtlas; P60905; baseline and differential.
DR Genevisible; P60905; RN.
DR GO; GO:0031225; C:anchored component of membrane; ISS:UniProtKB.
DR GO; GO:0098993; C:anchored component of synaptic vesicle membrane; IDA:SynGO.
DR GO; GO:0042584; C:chromaffin granule membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0031594; C:neuromuscular junction; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0098793; C:presynapse; ISO:RGD.
DR GO; GO:0008021; C:synaptic vesicle; ISO:RGD.
DR GO; GO:0043195; C:terminal bouton; HDA:ParkinsonsUK-UCL.
DR GO; GO:0043008; F:ATP-dependent protein binding; IPI:RGD.
DR GO; GO:0061077; P:chaperone-mediated protein folding; ISO:RGD.
DR GO; GO:0007268; P:chemical synaptic transmission; TAS:RGD.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; ISO:RGD.
DR GO; GO:0051402; P:neuron apoptotic process; IEA:Ensembl.
DR GO; GO:0098693; P:regulation of synaptic vesicle cycle; ISO:RGD.
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 Acetylation; Cell membrane; Chaperone; Cytoplasm; Cytoplasmic vesicle;
KW Direct protein sequencing; Lipoprotein; Membrane; Palmitate;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..198
FT /note="DnaJ homolog subfamily C member 5"
FT /id="PRO_0000071054"
FT DOMAIN 13..82
FT /note="J"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00286"
FT MOD_RES 8
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 10
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:11604405,
FT ECO:0007744|PubMed:22673903"
FT MOD_RES 12
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 15
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 17
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9H3Z4"
FT MOD_RES 56
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9H3Z4"
FT MOD_RES 151
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 198 AA; 22101 MW; 52F98261FBAD978F CRC64;
MADQRQRSLS TSGESLYHVL GLDKNATSDD IKKSYRKLAL KYHPDKNPDN PEAADKFKEI
NNAHAILTDA TKRNIYDKYG SLGLYVAEQF GEENVNTYFV LSSWWAKALF VVCGLLTCCY
CCCCLCCCFN CCCGKCKPKA PEGEETEFYV SPEDLEAQLQ SDEREATDTP IVIQPASATE
TTQLTADSHP SYHTDGFN
