ID   DJC15_HUMAN             Reviewed;         150 AA.
AC   Q9Y5T4; B2R4L0; Q5T219; Q6X963;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   25-JUL-2006, sequence version 2.
DT   28-JAN-2026, entry version 169.
DE   RecName: Full=DnaJ homolog subfamily C member 15;
DE   AltName: Full=Cell growth-inhibiting gene 22 protein;
DE   AltName: Full=Methylation-controlled J protein;
DE            Short=MCJ;
GN   Name=DNAJC15; Synonyms=DNAJD1; ORFNames=GIG22, HSD18;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, INVOLVEMENT IN OVARIAN
RP   ADENOCARCINOMA, AND VARIANT GLY-35.
RX   PubMed=11358853;
RA   Shridhar V., Bible K.C., Staub J., Avula R., Lee Y.K., Kalli K., Huang H.,
RA   Hartmann L.C., Kaufmann S.H., Smith D.I.;
RT   "Loss of expression of a new member of the DNAJ protein family confers
RT   resistance to chemotherapeutic agents used in the treatment of ovarian
RT   cancer.";
RL   Cancer Res. 61:4258-4265(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Testis;
RA   Yang C.B., Miao S.Y., Zhang X.D., Qiao Y., Liang G., Wang L.F.;
RT   "A new spermatogenesis-related gene.";
RL   Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Kim J.W.;
RT   "Identification of a cell growth inhibiting gene.";
RL   Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15057823; DOI=10.1038/nature02379;
RA   Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
RA   Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S.,
RA   Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P.,
RA   Ambrose K.D., Andrews D.T., Ashwell R.I.S., Babbage A.K., Bagguley C.L.,
RA   Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P.,
RA   Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
RA   Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C.,
RA   Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P.,
RA   Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L.,
RA   Frankish A.G., Frankland J., French L., Garner P., Garnett J.,
RA   Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M.,
RA   Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D.,
RA   Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D.,
RA   Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S.,
RA   Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J.,
RA   Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
RA   Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S.,
RA   Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R.,
RA   Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W.,
RA   Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P.,
RA   Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L.,
RA   Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R.,
RA   Rogers J., Ross M.T.;
RT   "The DNA sequence and analysis of human chromosome 13.";
RL   Nature 428:522-528(2004).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT GLY-35.
RC   TISSUE=Skin;
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   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-104, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [9]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [10]
RP   FUNCTION, INTERACTION WITH PAM16, ASSOCIATION WITH THE TIM23 COMPLEX,
RP   SUBCELLULAR LOCATION, AND TOPOLOGY.
RX   PubMed=23263864; DOI=10.1093/hmg/dds541;
RA   Schusdziarra C., Blamowska M., Azem A., Hell K.;
RT   "Methylation-controlled J-protein MCJ acts in the import of proteins into
RT   human mitochondria.";
RL   Hum. Mol. Genet. 22:1348-1357(2013).
RN   [11]
RP   SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
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: Negative regulator of the mitochondrial respiratory chain.
CC       Prevents mitochondrial hyperpolarization state and restricts
CC       mitochondrial generation of ATP (By similarity). Acts as an import
CC       component of the TIM23 translocase complex. Stimulates the ATPase
CC       activity of HSPA9. {ECO:0000250, ECO:0000269|PubMed:23263864}.
CC   -!- SUBUNIT: Interacts with the TIM23 complex. Directly interacts with
CC       PAM16/MAGMAS; this interaction counteracts DNAJC15-dependent
CC       stimulation of HSPA9 ATPase activity. Associates with complex I of the
CC       mitochondrial electron transfer chain; this interaction may interfere
CC       with the formation of supercomplexes that facilitate the transfer of
CC       electrons between complexes (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000269|PubMed:23263864, ECO:0000269|PubMed:23530063}; Single-pass
CC       membrane protein {ECO:0000269|PubMed:23263864,
CC       ECO:0000269|PubMed:23530063}.
CC   -!- TISSUE SPECIFICITY: Expressed at highest levels in heart, followed by
CC       liver and kidney. {ECO:0000269|PubMed:11358853,
CC       ECO:0000269|PubMed:23530063}.
CC   -!- DISEASE: Note=Absent or down-regulated in many advanced cases of
CC       ovarian adenocarcinoma, due to hypermethylation and allelic loss. Loss
CC       of expression correlates with increased resistance to antineoplastic
CC       drugs, such as cisplatin. {ECO:0000269|PubMed:11358853}.
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DR   EMBL; AF126743; AAD38506.1; -; mRNA.
DR   EMBL; AY248898; AAP20049.1; -; mRNA.
DR   EMBL; AY512565; AAS80157.1; -; mRNA.
DR   EMBL; AK311866; BAG34807.1; -; mRNA.
DR   EMBL; AL445217; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471075; EAX08688.1; -; Genomic_DNA.
DR   EMBL; BC010910; AAH10910.1; -; mRNA.
DR   EMBL; BC095400; AAH95400.1; -; mRNA.
DR   CCDS; CCDS9388.1; -.
DR   RefSeq; NP_037370.2; NM_013238.3.
DR   AlphaFoldDB; Q9Y5T4; -.
DR   SMR; Q9Y5T4; -.
DR   BioGRID; 118871; 166.
DR   ComplexPortal; CPX-6129; TIM23 mitochondrial inner membrane pre-sequence translocase complex, TIM17A variant.
DR   ComplexPortal; CPX-6130; TIM23 mitochondrial inner membrane pre-sequence translocase complex, TIM17B variant.
DR   FunCoup; Q9Y5T4; 105.
DR   STRING; 9606.ENSP00000368523; -.
DR   GlyGen; Q9Y5T4; 3 sites, 1 O-linked glycan (3 sites).
DR   iPTMnet; Q9Y5T4; -.
DR   PhosphoSitePlus; Q9Y5T4; -.
DR   BioMuta; DNAJC15; -.
DR   DMDM; 110808202; -.
DR   jPOST; Q9Y5T4; -.
DR   MassIVE; Q9Y5T4; -.
DR   PaxDb; 9606-ENSP00000368523; -.
DR   PeptideAtlas; Q9Y5T4; -.
DR   ProteomicsDB; 86496; -.
DR   Pumba; Q9Y5T4; -.
DR   Antibodypedia; 2384; 60 antibodies from 25 providers.
DR   DNASU; 29103; -.
DR   Ensembl; ENST00000379221.4; ENSP00000368523.2; ENSG00000120675.7.
DR   GeneID; 29103; -.
DR   KEGG; hsa:29103; -.
DR   MANE-Select; ENST00000379221.4; ENSP00000368523.2; NM_013238.3; NP_037370.2.
DR   UCSC; uc001uyy.4; human.
DR   AGR; HGNC:20325; -.
DR   ClinPGx; PA134932264; -.
DR   CTD; 29103; -.
DR   DisGeNET; 29103; -.
DR   GeneCards; DNAJC15; -.
DR   HGNC; HGNC:20325; DNAJC15.
DR   HPA; ENSG00000120675; Low tissue specificity.
DR   MIM; 615339; gene.
DR   OpenTargets; ENSG00000120675; -.
DR   VEuPathDB; HostDB:ENSG00000120675; -.
DR   eggNOG; KOG0723; Eukaryota.
DR   GeneTree; ENSGT00940000159907; -.
DR   HOGENOM; CLU_017633_13_3_1; -.
DR   InParanoid; Q9Y5T4; -.
DR   OMA; MRYAEYT; -.
DR   OrthoDB; 240298at2759; -.
DR   PAN-GO; Q9Y5T4; 3 GO annotations based on evolutionary models.
DR   PhylomeDB; Q9Y5T4; -.
DR   PathwayCommons; Q9Y5T4; -.
DR   SignaLink; Q9Y5T4; -.
DR   SIGNOR; Q9Y5T4; -.
DR   Agora; ENSG00000120675; -.
DR   BioGRID-ORCS; 29103; 14 hits in 1146 CRISPR screens.
DR   ChiTaRS; DNAJC15; human.
DR   GenomeRNAi; 29103; -.
DR   Pharos; Q9Y5T4; Tbio.
DR   PRO; PR:Q9Y5T4; -.
DR   Proteomes; UP000005640; Chromosome 13.
DR   RNAct; Q9Y5T4; protein.
DR   Bgee; ENSG00000120675; Expressed in jejunal mucosa and 208 other cell types or tissues.
DR   GO; GO:0005743; C:mitochondrial inner membrane; NAS:ComplexPortal.
DR   GO; GO:0005739; C:mitochondrion; HTP:FlyBase.
DR   GO; GO:0001405; C:PAM complex, Tim23 associated import motor; IBA:GO_Central.
DR   GO; GO:0005744; C:TIM23 mitochondrial import inner membrane translocase complex; NAS:ComplexPortal.
DR   GO; GO:0001671; F:ATPase activator activity; IBA:GO_Central.
DR   GO; GO:0009267; P:cellular response to starvation; IEA:Ensembl.
DR   GO; GO:0006886; P:intracellular protein transport; NAS:ComplexPortal.
DR   GO; GO:0006120; P:mitochondrial electron transport, NADH to ubiquinone; IEA:Ensembl.
DR   GO; GO:1902957; P:negative regulation of mitochondrial electron transport, NADH to ubiquinone; IEA:Ensembl.
DR   GO; GO:0031333; P:negative regulation of protein-containing complex assembly; IEA:Ensembl.
DR   GO; GO:0030150; P:protein import into mitochondrial matrix; IBA:GO_Central.
DR   GO; GO:0065003; P:protein-containing complex assembly; IEA:Ensembl.
DR   GO; GO:0019216; P:regulation of lipid metabolic process; IEA:Ensembl.
DR   CDD; cd06257; DnaJ; 1.
DR   FunFam; 1.10.287.110:FF:000001; Import inner membrane translocase subunit tim14; 1.
DR   Gene3D; 1.10.287.110; DnaJ domain; 1.
DR   InterPro; IPR001623; DnaJ_domain.
DR   InterPro; IPR036869; J_dom_sf.
DR   PANTHER; PTHR12763; -; 1.
DR   PANTHER; PTHR12763:SF7; DNAJ HOMOLOG SUBFAMILY C MEMBER 15; 1.
DR   SMART; SM00271; DnaJ; 1.
DR   SUPFAM; SSF46565; Chaperone J-domain; 1.
DR   PROSITE; PS50076; DNAJ_2; 1.
PE   1: Evidence at protein level;
KW   Chaperone; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW   Phosphoprotein; Protein transport; Proteomics identification;
KW   Reference proteome; Translocation; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN           1..150
FT                   /note="DnaJ homolog subfamily C member 15"
FT                   /id="PRO_0000247139"
FT   TOPO_DOM        1..35
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        36..58
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        59..150
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          96..150
FT                   /note="J"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00286"
FT   MOD_RES         104
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   VARIANT         35
FT                   /note="R -> G (in dbSNP:rs12015)"
FT                   /evidence="ECO:0000269|PubMed:11358853,
FT                   ECO:0000269|PubMed:15489334"
FT                   /id="VAR_027077"
FT   CONFLICT        34
FT                   /note="Q -> R (in Ref. 2; AAP20049)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        131
FT                   /note="P -> S (in Ref. 2; AAP20049)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   150 AA;  16383 MW;  988059B686D39967 CRC64;
     MAARGVIAPV GESLRYAEYL QPSAKRPDAD VDQQRLVRSL IAVGLGVAAL AFAGRYAFRI
     WKPLEQVITE TAKKISTPSF SSYYKGGFEQ KMSRREAGLI LGVSPSAGKA KIRTAHRRVM
     ILNHPDKGGS PYVAAKINEA KDLLETTTKH
//