ID   DNJC1_CANLF             Reviewed;          20 AA.
AC   P82539;
DT   10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2004, sequence version 1.
DT   23-FEB-2022, entry version 57.
DE   RecName: Full=DnaJ homolog subfamily C member 1;
DE   AltName: Full=DnaJ protein homolog MTJ1;
DE   Flags: Fragment;
GN   Name=DNAJC1;
OS   Canis lupus familiaris (Dog) (Canis familiaris).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX   NCBI_TaxID=9615;
RN   [1]
RP   PROTEIN SEQUENCE, POSSIBLE FUNCTION, INTERACTION WITH HSPA5, INTERACTION
RP   WITH RIBOSOMES, SUBCELLULAR LOCATION, AND TOPOLOGY.
RC   TISSUE=Pancreas;
RX   PubMed=12065409; DOI=10.1093/emboj/cdf315;
RA   Dudek J., Volkmer J., Bies C., Guth S., Mueller A., Lerner M., Feick P.,
RA   Schaefer K.-H., Morgenstern E., Hennessy F., Blatch G.L., Janoscheck K.,
RA   Heim N., Scholtes P., Frien M., Nastainczyk W., Zimmermann R.;
RT   "A novel type of co-chaperone mediates transmembrane recruitment of DnaK-
RT   like chaperones to ribosomes.";
RL   EMBO J. 21:2958-2967(2002).
CC   -!- SUBUNIT: Interacts (via SANT 2 domain) with SERPINA3; the interaction
CC       delays the formation of the covalent inhibitory complex SERPINA3-
CC       chymotrypsin, but does not alter the catalytic activity of SERPINA3.
CC       Interacts (via SANT 2 domain) with ITIH4 (via C-terminus); the
CC       interaction protects ITIH4 against in vitro cleavage by kallikrein (By
CC       similarity). Interacts (via J domain) with HSPA5. Interacts (via
CC       cytosolic domain) with ribosomes. {ECO:0000250,
CC       ECO:0000269|PubMed:12065409}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000269|PubMed:12065409}; Single-pass type I membrane protein
CC       {ECO:0000269|PubMed:12065409}. Nucleus membrane {ECO:0000250}; Single-
CC       pass type I membrane protein {ECO:0000250}. Microsome membrane
CC       {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
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DR   STRING; 9615.ENSCAFP00000059380; -.
DR   PaxDb; P82539; -.
DR   eggNOG; KOG0724; Eukaryota.
DR   Proteomes; UP000002254; Unplaced.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Chaperone; Direct protein sequencing; DNA-binding; Endoplasmic reticulum;
KW   Membrane; Microsome; Nucleus; Reference proteome; Transmembrane.
FT   CHAIN           1..>20
FT                   /note="DnaJ homolog subfamily C member 1"
FT                   /id="PRO_0000071041"
FT   TOPO_DOM        1..>20
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000269|PubMed:12065409"
FT   DOMAIN          18..>20
FT                   /note="J"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00286"
FT   NON_TER         20
SQ   SEQUENCE   20 AA;  2429 MW;  7AFCCAD1618B8433 CRC64;
     WESGDLELFD LVEEVXLNFY