DNJC5_BOVIN
ID DNJC5_BOVIN Reviewed; 198 AA.
AC Q29455; Q0VCC7; Q29456;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=DnaJ homolog subfamily C member 5 {ECO:0000250|UniProtKB:Q9H3Z4};
DE AltName: Full=Cysteine string protein {ECO:0000303|PubMed:8631751};
DE Short=CSP {ECO:0000303|PubMed:8631751};
GN Name=DNAJC5 {ECO:0000250|UniProtKB:Q9H3Z4};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS CSP1 AND CSP2).
RC TISSUE=Adrenal medulla;
RX PubMed=8631751; DOI=10.1074/jbc.271.13.7320;
RA Chamberlain L.H., Burgoyne R.D.;
RT "Identification of a novel cysteine string protein variant and expression
RT of cysteine string proteins in non-neuronal cells.";
RL J. Biol. Chem. 271:7320-7323(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM CSP1).
RC STRAIN=Hereford; TISSUE=Fetal cerebellum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP SUBCELLULAR LOCATION.
RX PubMed=8702643; DOI=10.1074/jbc.271.32.19514;
RA Chamberlain L.H., Henry J., Burgoyne R.D.;
RT "Cysteine string proteins are associated with chromaffin granules.";
RL J. Biol. Chem. 271:19514-19517(1996).
RN [4]
RP FUNCTION, INTERACTION WITH HSC70, AND MUTAGENESIS OF HIS-43 AND ASP-45.
RX PubMed=9395474; DOI=10.1074/jbc.272.50.31420;
RA Chamberlain L.H., Burgoyne R.D.;
RT "The molecular chaperone function of the secretory vesicle cysteine string
RT proteins.";
RL J. Biol. Chem. 272:31420-31426(1997).
RN [5]
RP 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 SUBCELLULAR LOCATION, TOPOLOGY, AND PALMITOYLATION.
RX PubMed=18596047; DOI=10.1074/jbc.m802140200;
RA Greaves J., Salaun C., Fukata Y., Fukata M., Chamberlain L.H.;
RT "Palmitoylation and membrane interactions of the neuroprotective chaperone
RT cysteine-string protein.";
RL J. Biol. Chem. 283:25014-25026(2008).
RN [7]
RP INTERACTION WITH ZDHHC17 AND ZDHHC13, AND MUTAGENESIS OF PRO-175.
RX PubMed=26198635; DOI=10.1074/jbc.m115.657668;
RA Lemonidis K., Sanchez-Perez M.C., Chamberlain L.H.;
RT "Identification of a novel sequence motif recognized by the ankyrin repeat
RT domain of zDHHC17/13 S-acyltransferases.";
RL J. Biol. Chem. 290:21939-21950(2015).
RN [8]
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
CC (PubMed:9395474). Acts as a co-chaperone for the SNARE protein SNAP-25
CC (By similarity). Involved in the calcium-mediated control of a late
CC stage 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:0000269|PubMed:9395474}.
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) (PubMed:26198635). Interacts with ZDHHC17
CC (via ANK repeats) (PubMed:26198635). Interacts with HSC70
CC (PubMed:9395474). Interacts with SYT1, SYT5 and SYT7, and with SYT9,
CC forming a complex with SNAP25 (By similarity).
CC {ECO:0000250|UniProtKB:P60904, ECO:0000269|PubMed:26198635,
CC ECO:0000269|PubMed:9395474}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:18596047}.
CC Membrane {ECO:0000269|PubMed:18596047}; Lipid-anchor
CC {ECO:0000269|PubMed:18596047}. Cytoplasmic vesicle, secretory vesicle,
CC chromaffin granule membrane {ECO:0000269|PubMed:8702643}. Melanosome
CC {ECO:0000250|UniProtKB:Q9H3Z4}. Cell membrane
CC {ECO:0000250|UniProtKB:Q9H3Z4}. Note=The association with membranes is
CC regulated by palmitoylation. {ECO:0000269|PubMed:18596047}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=CSP1;
CC IsoId=Q29455-1; Sequence=Displayed;
CC Name=CSP2;
CC IsoId=Q29455-2; Sequence=VSP_001291;
CC -!- PTM: Ser-10 phosphorylation induces an order-to-disorder transition
CC triggering the interaction with Lys-58 (By similarity). This
CC conformational switch modulates DNAJC5's cellular functions by reducing
CC binding to syntaxin and synaptogamin without altering HSC70
CC interactions (By similarity). {ECO:0000250|UniProtKB:Q9H3Z4}.
CC -!- PTM: Palmitoylated (PubMed:18596047). Could be palmitoylated by DHHC3,
CC DHHC7, DHHC15 and DHHC17 (PubMed:18596047). Palmitoylation occurs
CC probably in the cysteine-rich domain and regulates DNAJC5 membrane
CC attachment (PubMed:18596047). {ECO:0000269|PubMed:18596047}.
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DR EMBL; X92666; CAA63354.1; -; mRNA.
DR EMBL; X92667; CAA63355.1; -; mRNA.
DR EMBL; BC120234; AAI20235.1; -; mRNA.
DR RefSeq; NP_776958.2; NM_174533.4. [Q29455-1]
DR RefSeq; XP_010809668.1; XM_010811366.2. [Q29455-1]
DR AlphaFoldDB; Q29455; -.
DR SMR; Q29455; -.
DR STRING; 9913.ENSBTAP00000039130; -.
DR iPTMnet; Q29455; -.
DR SwissPalm; Q29455; -.
DR PaxDb; Q29455; -.
DR PRIDE; Q29455; -.
DR Ensembl; ENSBTAT00000035700; ENSBTAP00000035570; ENSBTAG00000015796. [Q29455-2]
DR Ensembl; ENSBTAT00000070817; ENSBTAP00000059567; ENSBTAG00000015796. [Q29455-1]
DR GeneID; 282216; -.
DR KEGG; bta:282216; -.
DR CTD; 80331; -.
DR VEuPathDB; HostDB:ENSBTAG00000015796; -.
DR eggNOG; KOG0716; Eukaryota.
DR GeneTree; ENSGT00940000155597; -.
DR HOGENOM; CLU_017633_14_1_1; -.
DR InParanoid; Q29455; -.
DR OMA; CKPRPRD; -.
DR OrthoDB; 1401920at2759; -.
DR TreeFam; TF105164; -.
DR Reactome; R-BTA-6798695; Neutrophil degranulation.
DR Proteomes; UP000009136; Chromosome 13.
DR Bgee; ENSBTAG00000015796; Expressed in retina and 104 other tissues.
DR GO; GO:0031225; C:anchored component of membrane; IDA:UniProtKB.
DR GO; GO:0042584; C:chromaffin granule membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IDA: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; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0098793; C:presynapse; IBA:GO_Central.
DR GO; GO:0008021; C:synaptic vesicle; IEA:Ensembl.
DR GO; GO:0061077; P:chaperone-mediated protein folding; IBA:GO_Central.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; IEA:Ensembl.
DR GO; GO:0051402; P:neuron apoptotic process; IEA:Ensembl.
DR GO; GO:0098693; P:regulation of synaptic vesicle cycle; IBA:GO_Central.
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; Alternative splicing; Cell membrane; Chaperone; Cytoplasm;
KW Cytoplasmic vesicle; Lipoprotein; Membrane; Palmitate; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..198
FT /note="DnaJ homolog subfamily C member 5"
FT /id="PRO_0000071051"
FT DOMAIN 13..82
FT /note="J"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00286"
FT MOTIF 43..45
FT /note="Required for binding to Hsc70"
FT /evidence="ECO:0000269|PubMed:9395474"
FT MOD_RES 8
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H3Z4"
FT MOD_RES 10
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:11604405"
FT MOD_RES 12
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H3Z4"
FT MOD_RES 15
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H3Z4"
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:0000250|UniProtKB:P60904"
FT VAR_SEQ 165..198
FT /note="EAADTPIVIQPASATETTQLTADSHPSYHTDGFN -> GGH (in
FT isoform CSP2)"
FT /evidence="ECO:0000303|PubMed:8631751"
FT /id="VSP_001291"
FT MUTAGEN 43
FT /note="H->Q: Decreased binding to HSC70. Loss of binding to
FT HSC70; when associated with A-45."
FT /evidence="ECO:0000269|PubMed:9395474"
FT MUTAGEN 45
FT /note="D->A: Decreased binding to HSC70. Loss of binding to
FT HSC70; when associated with Q-43."
FT /evidence="ECO:0000269|PubMed:9395474"
FT MUTAGEN 175
FT /note="P->A: Inhibits interaction with ZDHHC13 and
FT ZDHHC17."
FT /evidence="ECO:0000269|PubMed:26198635"
SQ SEQUENCE 198 AA; 22133 MW; 9A3D139FF5428A27 CRC64;
MADQRQRSLS TSGESLYHVL GLDKNATSDD IKKSYRKLAL KYHPDKNPDN PEAADKFKEI
NNAHAILTDA TKRNIYDKYG SLGLYVAEQF GEENVNTYFV LSSWWAKALF IFCGLLTCCY
CCCCLCCCFN CCCGKCKPKA PEGEETEFYV SPEDLEAQLQ SDEREAADTP IVIQPASATE
TTQLTADSHP SYHTDGFN
