DJC30_MOUSE
ID DJC30_MOUSE Reviewed; 219 AA.
AC P59041;
DT 19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 19-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=DnaJ homolog subfamily C member 30, mitochondrial {ECO:0000303|PubMed:30318146};
DE AltName: Full=Williams-Beuren syndrome chromosomal region 18 protein homolog {ECO:0000303|PubMed:12073013};
DE Flags: Precursor;
GN Name=Dnajc30 {ECO:0000303|PubMed:30318146, ECO:0000312|MGI:MGI:1913364};
GN Synonyms=Wbscr18 {ECO:0000303|PubMed:12073013};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=12073013; DOI=10.1007/s00439-002-0710-x;
RA Merla G., Ucla C., Guipponi M., Reymond A.;
RT "Identification of additional transcripts in the Williams-Beuren syndrome
RT critical region.";
RL Hum. Genet. 110:429-438(2002).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, and Kidney;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [3]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=30318146; DOI=10.1016/j.cell.2018.09.014;
RA Tebbenkamp A.T.N., Varela L., Choi J., Paredes M.I., Giani A.M., Song J.E.,
RA Sestan-Pesa M., Franjic D., Sousa A.M.M., Liu Z.W., Li M., Bichsel C.,
RA Koch M., Szigeti-Buck K., Liu F., Li Z., Kawasawa Y.I., Paspalas C.D.,
RA Mineur Y.S., Prontera P., Merla G., Picciotto M.R., Arnsten A.F.T.,
RA Horvath T.L., Sestan N.;
RT "The 7q11.23 protein DNAJC30 interacts with ATP synthase and links
RT mitochondria to brain development.";
RL Cell 0:0-0(2018).
CC -!- FUNCTION: Mitochondrial protein enriched in neurons that acts as a
CC regulator of mitochondrial respiration (PubMed:30318146). Associates
CC with the ATP synthase complex and facilitates ATP synthesis
CC (PubMed:30318146). May be a chaperone protein involved in the turnover
CC of the subunits of mitochondrial complex I N-module. It facilitates the
CC degradation of N-module subunits damaged by oxidative stress, and
CC contributes to complex I functional efficiency (By similarity).
CC {ECO:0000250|UniProtKB:Q96LL9, ECO:0000269|PubMed:30318146}.
CC -!- SUBUNIT: Associates with the ATP synthase complex. Interacts with MT-
CC ATP6; interaction is direct. Interacts with ATP5MC2; interaction is
CC direct. {ECO:0000250|UniProtKB:Q96LL9}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:Q96LL9}; Single-pass membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: In brain, expressed in gray matter structures.
CC {ECO:0000269|PubMed:30318146}.
CC -!- DISRUPTION PHENOTYPE: Mice are smaller and have a decreased weight
CC (PubMed:30318146). Neocortical projection neurons display morphological
CC defects reminiscent of Williams-Beuren syndrome (WBS) in human,
CC characterized by less complex dendritic architecture and a smaller
CC corpus callosum (PubMed:30318146). Mitochondria show decreased ATP
CC production (PubMed:30318146). Mice do not show significant systemic
CC metabolic defects (PubMed:30318146). {ECO:0000269|PubMed:30318146}.
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DR EMBL; AF412026; AAM62308.1; -; mRNA.
DR CCDS; CCDS39315.1; -.
DR RefSeq; NP_079638.2; NM_025362.3.
DR AlphaFoldDB; P59041; -.
DR SMR; P59041; -.
DR STRING; 10090.ENSMUSP00000094318; -.
DR iPTMnet; P59041; -.
DR PhosphoSitePlus; P59041; -.
DR SwissPalm; P59041; -.
DR MaxQB; P59041; -.
DR PaxDb; P59041; -.
DR PeptideAtlas; P59041; -.
DR PRIDE; P59041; -.
DR ProteomicsDB; 279716; -.
DR Antibodypedia; 2642; 98 antibodies from 15 providers.
DR DNASU; 66114; -.
DR Ensembl; ENSMUST00000071263; ENSMUSP00000094318; ENSMUSG00000061118.
DR GeneID; 66114; -.
DR KEGG; mmu:66114; -.
DR UCSC; uc008zxp.1; mouse.
DR CTD; 84277; -.
DR MGI; MGI:1913364; Dnajc30.
DR VEuPathDB; HostDB:ENSMUSG00000061118; -.
DR eggNOG; KOG0691; Eukaryota.
DR GeneTree; ENSGT00510000048685; -.
DR HOGENOM; CLU_104327_2_0_1; -.
DR InParanoid; P59041; -.
DR OMA; HYGKSFD; -.
DR OrthoDB; 1404041at2759; -.
DR PhylomeDB; P59041; -.
DR TreeFam; TF332749; -.
DR BioGRID-ORCS; 66114; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Dnajc30; mouse.
DR PRO; PR:P59041; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; P59041; protein.
DR Bgee; ENSMUSG00000061118; Expressed in proximal tubule and 62 other tissues.
DR Genevisible; P59041; MM.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005743; C:mitochondrial inner membrane; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0006754; P:ATP biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0007420; P:brain development; IMP:UniProtKB.
DR GO; GO:1905706; P:regulation of mitochondrial ATP synthesis coupled proton transport; IMP:UniProtKB.
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 1: Evidence at protein level;
KW ATP synthesis; Chaperone; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Reference proteome; Transit peptide;
KW Transmembrane; Transmembrane helix.
FT TRANSIT 1..38
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 39..219
FT /note="DnaJ homolog subfamily C member 30, mitochondrial"
FT /evidence="ECO:0000255"
FT /id="PRO_0000071138"
FT TRANSMEM 202..218
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 42..107
FT /note="J"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00286"
FT REGION 109..148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 123..141
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 219 AA; 24762 MW; E7490F472D38456D CRC64;
MAAARCLGWT LSPLWRWWQV RGLPPSSATG LCSRGRTYSR TALYELLGVP STATQAQIKA
AYYRQSFLYH PDRNPGSAEA AERFTRVSEA YLVLGSTILR RKYDRGLLSD QDLRGPGVKP
SKTPVADPAP PRPPPYTPRA PGGSRASPGD GRTMFDFDAF YQAHYGEQLE RERRLRARRE
ALRKKQENQA NKGTSWDDTR DATFFVVLFL IFVFVGFRI
