ID   DNJC5_XENLA             Reviewed;         197 AA.
AC   O42196;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=DnaJ homolog subfamily C member 5 {ECO:0000250|UniProtKB:Q9H3Z4};
DE   AltName: Full=Cysteine string protein {ECO:0000250|UniProtKB:Q9H3Z4};
DE            Short=CSP {ECO:0000250|UniProtKB:Q9H3Z4};
DE   AltName: Full=Xcsp {ECO:0000303|PubMed:9540815};
GN   Name=dnajc5 {ECO:0000250|UniProtKB:Q9H3Z4};
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Dorsal lip;
RX   PubMed=9540815; DOI=10.1016/s0167-4889(97)00160-2;
RA   Mastrogiacomo A., Kornblum H.I., Umbach J.A., Gundersen C.B.;
RT   "A Xenopus cysteine string protein with a cysteine residue in the J
RT   domain.";
RL   Biochim. Biophys. Acta 1401:239-241(1998).
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. Palmitoylation occurs probably in the cysteine-rich
CC       domain and regulates DNAJC5 stable membrane attachment.
CC       {ECO:0000250|UniProtKB:Q29455}.
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DR   EMBL; AF015662; AAB69692.1; -; mRNA.
DR   RefSeq; NP_001083797.1; NM_001090328.1.
DR   RefSeq; XP_018092872.1; XM_018237383.1.
DR   RefSeq; XP_018092873.1; XM_018237384.1.
DR   RefSeq; XP_018092874.1; XM_018237385.1.
DR   AlphaFoldDB; O42196; -.
DR   SMR; O42196; -.
DR   GeneID; 399123; -.
DR   KEGG; xla:399123; -.
DR   CTD; 399123; -.
DR   Xenbase; XB-GENE-6254416; dnajc5.S.
DR   OMA; CKPRPRD; -.
DR   OrthoDB; 1401920at2759; -.
DR   Proteomes; UP000186698; Chromosome 9_10S.
DR   Bgee; 399123; Expressed in brain and 19 other tissues.
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; 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; PS50076; DNAJ_2; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Chaperone; Cytoplasm; Cytoplasmic vesicle; Lipoprotein;
KW   Membrane; Palmitate; Reference proteome.
FT   CHAIN           1..197
FT                   /note="DnaJ homolog subfamily C member 5"
FT                   /id="PRO_0000071074"
FT   DOMAIN          13..82
FT                   /note="J"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00286"
FT   REGION          153..197
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        173..197
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   197 AA;  22021 MW;  83CEC38B2DD4F75B CRC64;
     MADQRQRSLS TSGESLYHVL GLDKNATTDD IKKCYRKLAL KYHPDKNPDN PEASEKFKEI
     NNAHGILADS TKRNIYDKYG SLGLYVAEQF GEENVNTYFV LSSWWAKALF MFCGLITGCY
     CCCCLCCCCN CCCGKCKPRP PEGEDQDIYV SPEDLEAQMQ SDERDTEGPV LVQPASATET
     TQLTSDSHAS YHTDGFN