DNJC5_TETCF
ID DNJC5_TETCF Reviewed; 195 AA.
AC P56101;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 25-MAY-2022, entry version 84.
DE RecName: Full=DnaJ homolog subfamily C member 5 {ECO:0000250|UniProtKB:Q9H3Z4};
DE AltName: Full=CCCS1 {ECO:0000312|EMBL:M99327};
DE AltName: Full=Cysteine string protein {ECO:0000250|UniProtKB:Q9H3Z4};
DE Short=CSP {ECO:0000250|UniProtKB:Q9H3Z4};
GN Name=dnajc5 {ECO:0000250|UniProtKB:Q9H3Z4};
OS Tetronarce californica (Pacific electric ray) (Torpedo californica).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC Elasmobranchii; Batoidea; Torpediniformes; Torpedinidae; Tetronarce.
OX NCBI_TaxID=7787;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1326297; DOI=10.1016/0896-6273(92)90190-o;
RA Gundersen C.B., Umbach J.A.;
RT "Suppression cloning of the cDNA for a candidate subunit of a presynaptic
RT calcium channel.";
RL Neuron 9:527-537(1992).
RN [2]
RP PALMITOYLATION.
RX PubMed=8034679; DOI=10.1016/s0021-9258(17)32151-8;
RA Gundersen C.B., Mastrogiacomo A., Faull K., Umbach J.A.;
RT "Extensive lipidation of a Torpedo cysteine string protein.";
RL J. Biol. Chem. 269:19197-19199(1994).
CC -!- FUNCTION: May have an important role in presynaptic function. May be
CC involved in calcium-dependent neurotransmitter release at nerve
CC endings.
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 -!- PTM: Palmitoylated (By similarity) (PubMed:8034679). Palmitoylation
CC occurs probably in the cysteine-rich domain and regulates DNAJC5 stable
CC membrane attachment (PubMed:8034679). {ECO:0000250|UniProtKB:Q29455,
CC ECO:0000269|PubMed:8034679}.
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DR EMBL; M99327; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; JH0719; JH0719.
DR AlphaFoldDB; P56101; -.
DR SMR; P56101; -.
DR SwissPalm; P56101; -.
DR GO; GO:0031225; C:anchored component of membrane; ISS:UniProtKB.
DR GO; GO:0042584; C:chromaffin granule membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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 Cell membrane; Chaperone; Cytoplasm; Cytoplasmic vesicle; Lipoprotein;
KW Membrane; Palmitate.
FT CHAIN 1..195
FT /note="DnaJ homolog subfamily C member 5"
FT /id="PRO_0000071073"
FT DOMAIN 13..82
FT /note="J"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00286"
FT REGION 162..195
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 174..195
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 195 AA; 21791 MW; 5230F35A72D7790F CRC64;
MGDQRQRSLS TSGDSLYIVL GLDKNASPED IKKSYRKLAL KYHPDKNPDN PEASEKFKEI
NNAHAILTDA TKRNIYDKYG SLGLYVAEQF GEENVNTYFV LSSWWAKALF VFCGVITGCY
FCCCLCCCCN CCCGKCKPKP PEGEEQEYYV SPEDLEAQLQ SDMEKEGDGA IVVQPTSATE
TTQLTSDSHP SYHTE
