DJC15_MOUSE
ID DJC15_MOUSE Reviewed; 149 AA.
AC Q78YY6;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=DnaJ homolog subfamily C member 15;
GN Name=Dnajc15; Synonyms=Dnajd1;
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Kidney;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Mammary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, and Testis;
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 [4]
RP FUNCTION, ASSOCIATION WITH MITOCHONDRIAL COMPLEX I, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=23530063; DOI=10.1128/mcb.00189-13;
RA Hatle K.M., Gummadidala P., Navasa N., Bernardo E., Dodge J.,
RA Silverstrim B., Fortner K., Burg E., Suratt B.T., Hammer J.,
RA Radermacher M., Taatjes D.J., Thornton T., Anguita J., Rincon M.;
RT "MCJ/DnaJC15, an endogenous mitochondrial repressor of the respiratory
RT chain that controls metabolic alterations.";
RL Mol. Cell. Biol. 33:2302-2314(2013).
CC -!- FUNCTION: Acts as an import component of the TIM23 translocase complex.
CC Stimulates the ATPase activity of HSPA9 (By similarity). Negative
CC regulator of the mitochondrial respiratory chain. Prevents
CC mitochondrial hyperpolarization state and restricts mitochondrial
CC generation of ATP. {ECO:0000250, ECO:0000269|PubMed:23530063}.
CC -!- SUBUNIT: Interacts with the TIM23 complex. Directly interacts with
CC PAM16/MAGMAS; this interaction counteracts DNAJC15-dependent
CC stimulation of HSPA9 ATPase activity (By similarity). Associates with
CC complex I of the mitochondrial electron transfer chain; this
CC interaction may interfere with the formation of supercomplexes that
CC facilitate the transfer of electrons between complexes. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:23530063}; Single-pass membrane protein
CC {ECO:0000269|PubMed:23530063}.
CC -!- TISSUE SPECIFICITY: Expressed at high levels in liver, heart, at
CC moderate levels in kidney and, at very low levels, in lung (at protein
CC level). High expression levels in testis. Highly expressed in CD8+ T-
CC cells, but barely detectable in CD4+ T-cells (at protein level). Almost
CC undetectable in B-cells. {ECO:0000269|PubMed:23530063}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype. Mutant animals are viable.
CC Both male and female are fertile and do not exhibit any obvious
CC malformations or behavioral abnormalities. CD8+ T-cell mitochondria are
CC hyperpolarized, compared to their wild-type counterparts. In fasted
CC mutant animals, livers do not exhibit any signs of steatosis, but
CC accumulate glycogen, possibly due to a sustained mitochondrial
CC oxidation that leads to rapid metabolism of lipids, hence minimizing
CC their accumulation in the liver and favoring glycogenesis. During
CC fasting, loss of white fat is also more prominent than in wild type
CC animals. {ECO:0000269|PubMed:23530063}.
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DR EMBL; AK002598; BAB22219.1; -; mRNA.
DR EMBL; BC027509; AAH27509.1; -; mRNA.
DR CCDS; CCDS27292.1; -.
DR RefSeq; NP_079660.1; NM_025384.3.
DR AlphaFoldDB; Q78YY6; -.
DR SMR; Q78YY6; -.
DR STRING; 10090.ENSMUSP00000022590; -.
DR iPTMnet; Q78YY6; -.
DR PhosphoSitePlus; Q78YY6; -.
DR EPD; Q78YY6; -.
DR MaxQB; Q78YY6; -.
DR PaxDb; Q78YY6; -.
DR PeptideAtlas; Q78YY6; -.
DR PRIDE; Q78YY6; -.
DR ProteomicsDB; 277459; -.
DR Antibodypedia; 2384; 65 antibodies from 24 providers.
DR DNASU; 66148; -.
DR Ensembl; ENSMUST00000226459; ENSMUSP00000154390; ENSMUSG00000022013.
DR GeneID; 66148; -.
DR KEGG; mmu:66148; -.
DR UCSC; uc007usc.1; mouse.
DR CTD; 29103; -.
DR MGI; MGI:1913398; Dnajc15.
DR VEuPathDB; HostDB:ENSMUSG00000022013; -.
DR eggNOG; KOG0723; Eukaryota.
DR GeneTree; ENSGT00940000159907; -.
DR HOGENOM; CLU_017633_13_3_1; -.
DR InParanoid; Q78YY6; -.
DR OMA; VMILNHP; -.
DR OrthoDB; 1600166at2759; -.
DR PhylomeDB; Q78YY6; -.
DR TreeFam; TF320584; -.
DR BioGRID-ORCS; 66148; 2 hits in 71 CRISPR screens.
DR ChiTaRS; Dnajc15; mouse.
DR PRO; PR:Q78YY6; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q78YY6; protein.
DR Bgee; ENSMUSG00000022013; Expressed in seminiferous tubule of testis and 268 other tissues.
DR ExpressionAtlas; Q78YY6; baseline and differential.
DR Genevisible; Q78YY6; MM.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:MGI.
DR GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR GO; GO:0001405; C:PAM complex, Tim23 associated import motor; IBA:GO_Central.
DR GO; GO:0001671; F:ATPase activator activity; IBA:GO_Central.
DR GO; GO:0009267; P:cellular response to starvation; IMP:MGI.
DR GO; GO:0006120; P:mitochondrial electron transport, NADH to ubiquinone; IMP:MGI.
DR GO; GO:1902957; P:negative regulation of mitochondrial electron transport, NADH to ubiquinone; IMP:MGI.
DR GO; GO:0031333; P:negative regulation of protein-containing complex assembly; IMP:MGI.
DR GO; GO:0030150; P:protein import into mitochondrial matrix; IBA:GO_Central.
DR GO; GO:0065003; P:protein-containing complex assembly; IMP:MGI.
DR GO; GO:0019216; P:regulation of lipid metabolic process; IMP:MGI.
DR CDD; cd06257; DnaJ; 1.
DR Gene3D; 1.10.287.110; -; 1.
DR InterPro; IPR001623; DnaJ_domain.
DR InterPro; IPR036869; J_dom_sf.
DR SMART; SM00271; DnaJ; 1.
DR SUPFAM; SSF46565; SSF46565; 1.
DR PROSITE; PS50076; DNAJ_2; 1.
PE 1: Evidence at protein level;
KW Chaperone; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW Phosphoprotein; Protein transport; Reference proteome; Translocation;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..149
FT /note="DnaJ homolog subfamily C member 15"
FT /id="PRO_0000247140"
FT TOPO_DOM 1..37
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT TRANSMEM 38..54
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 55..149
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000255"
FT DOMAIN 94..149
FT /note="J"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00286"
FT MOD_RES 102
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y5T4"
SQ SEQUENCE 149 AA; 15953 MW; 033EE8F425EC6DF8 CRC64;
MATGGGVTSR EGLRYAEYLP PSAQRSDADI DHTAGRRLLA VGLGVAAVAF AGRYAFQIWK
PLEQVITATA RKISSPSFSS YYKGGFEQKM SKREASLILG VSPSAGKAKI RTAHKRIMIL
NHPDKGGSPY LASKINEAKD LLEASSKAN
