ID DJC30_HUMAN Reviewed; 226 AA. AC Q96LL9; Q9BSG8; DT 10-OCT-2002, integrated into UniProtKB/Swiss-Prot. DT 19-OCT-2002, sequence version 3. DT 28-JAN-2026, entry version 171. DE RecName: Full=DnaJ homolog subfamily C member 30, mitochondrial {ECO:0000303|PubMed:30318146}; DE AltName: Full=Williams-Beuren syndrome chromosomal region 18 protein {ECO:0000303|PubMed:12073013}; DE Flags: Precursor; GN Name=DNAJC30 {ECO:0000303|PubMed:30318146, GN ECO:0000312|HGNC:HGNC:16410}; GN Synonyms=WBSCR18 {ECO:0000303|PubMed:12073013}; 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, AND ROLE IN WILLIAMS-BEUREN RP SYNDROME. 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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Testis; 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 [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=12853948; DOI=10.1038/nature01782; RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H., RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., RA Wilson R.K.; RT "The DNA sequence of human chromosome 7."; RL Nature 424:157-164(2003). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ARG-34. RC TISSUE=Lung; 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 [5] RP INTERACTION WITH MT-ATP6 AND ATP5MC2, ASSOCIATION WITH THE ATP SYNTHASE RP COMPLEX, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INVOLVEMENT IN WBS. 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). RN [6] RP STRUCTURE BY NMR OF 32-128. RG RIKEN structural genomics initiative (RSGI); RT "Solution structure of the DNAJ domain from human Williams-Beuren syndrome RT chromosome region 18 protein."; RL Submitted (OCT-2007) to the PDB data bank. RN [7] RP VARIANTS LHONAR1 CYS-51; SER-78 AND GLN-101, INVOLVEMENT IN LHONAR1, RP CHARACTERIZATION OF VARIANTS LHONAR1 CYS-51; SER-78 AND GLN-101, AND RP FUNCTION. RX PubMed=33465056; DOI=10.1172/jci138267; RA Stenton S.L., Sheremet N.L., Catarino C.B., Andreeva N.A., Assouline Z., RA Barboni P., Barel O., Berutti R., Bychkov I., Caporali L., Capristo M., RA Carbonelli M., Cascavilla M.L., Charbel Issa P., Freisinger P., Gerber S., RA Ghezzi D., Graf E., Heidler J., Hempel M., Heon E., Itkis Y.S., Javasky E., RA Kaplan J., Kopajtich R., Kornblum C., Kovacs-Nagy R., Krylova T.D., RA Kunz W.S., La Morgia C., Lamperti C., Ludwig C., Malacarne P.F., RA Maresca A., Mayr J.A., Meisterknecht J., Nevinitsyna T.A., Palombo F., RA Pode-Shakked B., Shmelkova M.S., Strom T.M., Tagliavini F., Tzadok M., RA van der Ven A.T., Vignal-Clermont C., Wagner M., Zakharova E.Y., RA Zhorzholadze N.V., Rozet J.M., Carelli V., Tsygankova P.G., Klopstock T., RA Wittig I., Prokisch H.; RT "Impaired complex I repair causes recessive Leber's hereditary optic RT neuropathy."; RL J. Clin. Invest. 131:0-0(2021). CC -!- FUNCTION: Mitochondrial protein enriched in neurons that acts as a CC regulator of mitochondrial respiration (By similarity). Associates with CC the ATP synthase complex and facilitates ATP synthesis (By similarity). CC May be a chaperone protein involved in the turnover of the subunits of CC mitochondrial complex I N-module. It facilitates the degradation of N- CC module subunits damaged by oxidative stress, and contributes to complex CC I functional efficiency (PubMed:33465056). CC {ECO:0000250|UniProtKB:P59041, ECO:0000269|PubMed:33465056}. CC -!- SUBUNIT: Associates with the ATP synthase complex (PubMed:30318146). CC Interacts with MT-ATP6; interaction is direct (PubMed:30318146). CC Interacts with ATP5MC2; interaction is direct (PubMed:30318146). CC {ECO:0000269|PubMed:30318146}. CC -!- INTERACTION: CC Q96LL9; Q13520: AQP6; NbExp=3; IntAct=EBI-8639143, EBI-13059134; CC Q96LL9; Q8NFU1: BEST2; NbExp=3; IntAct=EBI-8639143, EBI-19947314; CC Q96LL9; Q9BXU9: CALN1; NbExp=3; IntAct=EBI-8639143, EBI-12187137; CC Q96LL9; Q15125: EBP; NbExp=3; IntAct=EBI-8639143, EBI-3915253; CC Q96LL9; Q5JX71: FAM209A; NbExp=3; IntAct=EBI-8639143, EBI-18304435; CC Q96LL9; Q969F0: FATE1; NbExp=3; IntAct=EBI-8639143, EBI-743099; CC Q96LL9; Q8TED1: GPX8; NbExp=3; IntAct=EBI-8639143, EBI-11721746; CC Q96LL9; Q8N5M9: JAGN1; NbExp=3; IntAct=EBI-8639143, EBI-10266796; CC Q96LL9; Q8N6L0: KASH5; NbExp=3; IntAct=EBI-8639143, EBI-749265; CC Q96LL9; Q8N386: LRRC25; NbExp=3; IntAct=EBI-8639143, EBI-11304917; CC Q96LL9; Q5SR56: MFSD14B; NbExp=3; IntAct=EBI-8639143, EBI-373355; CC Q96LL9; Q99735: MGST2; NbExp=3; IntAct=EBI-8639143, EBI-11324706; CC Q96LL9; Q6IN84: MRM1; NbExp=3; IntAct=EBI-8639143, EBI-5454865; CC Q96LL9; Q15800: MSMO1; NbExp=3; IntAct=EBI-8639143, EBI-949102; CC Q96LL9; O00623: PEX12; NbExp=3; IntAct=EBI-8639143, EBI-594836; CC Q96LL9; Q9H6H4: REEP4; NbExp=3; IntAct=EBI-8639143, EBI-7545592; CC Q96LL9; Q96K19-5: RNF170; NbExp=3; IntAct=EBI-8639143, EBI-12055631; CC Q96LL9; Q96PQ1: SIGLEC12; NbExp=3; IntAct=EBI-8639143, EBI-17640454; CC Q96LL9; Q96EP9: SLC10A4; NbExp=3; IntAct=EBI-8639143, EBI-17456472; CC Q96LL9; Q9NQQ7-3: SLC35C2; NbExp=3; IntAct=EBI-8639143, EBI-17295964; CC Q96LL9; Q86UW1: SLC51A; NbExp=3; IntAct=EBI-8639143, EBI-945738; CC Q96LL9; Q4KMG9: TMEM52B; NbExp=3; IntAct=EBI-8639143, EBI-18178701; CC Q96LL9; Q8N661: TMEM86B; NbExp=3; IntAct=EBI-8639143, EBI-2548832; CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane CC {ECO:0000269|PubMed:30318146}; Single-pass membrane protein CC {ECO:0000255}. CC -!- TISSUE SPECIFICITY: Expressed in brain, heart, kidney, liver, lung, CC spleen, stomach and testis (PubMed:12073013). Highly expressed in the CC brain (PubMed:30318146). In the neocortex, expressed in most, if not CC all, glutamatergic excitatory projection neurons (pyramidal) and many CC interneurons, with the strongest signal noticeably in large pyramidal CC neurons of layer 3C. Also present in pyramidal neurons of layer 3C PNs CC of the superior temporal cortex, as well as in pyramidal neurons (Betz CC cells) of the layer 5B primary motor cortex (at protein level) CC (PubMed:30318146). {ECO:0000269|PubMed:12073013, CC ECO:0000269|PubMed:30318146}. CC -!- DISEASE: Note=DNAJC30 is located in the Williams-Beuren syndrome (WBS) CC critical region (PubMed:12073013, PubMed:30318146). WBS results from a CC hemizygous deletion of several genes on chromosome 7q11.23 thought to CC arise as a consequence of unequal crossing over between highly CC homologous low-copy repeat sequences flanking the deleted region CC (PubMed:30318146). WBS is an autosomal dominant disorder characterized CC by multiple clinical manifestations including neurologic features such CC as intellectual disability, cardiovascular, urogenital and skeletal CC features, and distinctive facies (PubMed:30318146). Deletion of DNAJC30 CC is responsible for mitochondrial dysfunction underlyining certain CC neurodevelopmental abnormalities observed in WBS (PubMed:30318146). CC {ECO:0000269|PubMed:12073013, ECO:0000269|PubMed:30318146}. CC -!- DISEASE: Leber-like hereditary optic neuropathy, autosomal recessive 1 CC (LHONAR1) [MIM:619382]: An autosomal recessive form of Leber hereditary CC optic neuropathy, a mitochondrial disease resulting in bilateral CC painless loss of central vision due to selective degeneration of the CC retinal ganglion cells and their axons. The disorder shows incomplete CC penetrance and male predominance. {ECO:0000269|PubMed:33465056}. CC Note=The disease is caused by variants affecting the gene represented CC in this entry. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF412025; AAM62307.1; -; mRNA. DR EMBL; AK058113; BAB71671.1; -; mRNA. DR EMBL; AC073846; AAS07471.1; -; Genomic_DNA. DR EMBL; BC005056; AAH05056.1; -; mRNA. DR CCDS; CCDS5556.1; -. DR RefSeq; NP_115693.2; NM_032317.2. DR PDB; 2YUA; NMR; -; A=39-124. DR PDBsum; 2YUA; -. DR AlphaFoldDB; Q96LL9; -. DR BMRB; Q96LL9; -. DR SMR; Q96LL9; -. DR BioGRID; 124004; 221. DR FunCoup; Q96LL9; 573. DR IntAct; Q96LL9; 140. DR MINT; Q96LL9; -. DR STRING; 9606.ENSP00000378605; -. DR iPTMnet; Q96LL9; -. DR PhosphoSitePlus; Q96LL9; -. DR SwissPalm; Q96LL9; -. DR BioMuta; DNAJC30; -. DR DMDM; 24212614; -. DR jPOST; Q96LL9; -. DR MassIVE; Q96LL9; -. DR PaxDb; 9606-ENSP00000378605; -. DR PeptideAtlas; Q96LL9; -. DR ProteomicsDB; 77223; -. DR Pumba; Q96LL9; -. DR Antibodypedia; 2642; 86 antibodies from 13 providers. DR DNASU; 84277; -. DR Ensembl; ENST00000395176.3; ENSP00000378605.1; ENSG00000176410.8. DR GeneID; 84277; -. DR KEGG; hsa:84277; -. DR MANE-Select; ENST00000395176.3; ENSP00000378605.1; NM_032317.3; NP_115693.2. DR UCSC; uc003tys.2; human. DR AGR; HGNC:16410; -. DR ClinPGx; PA162383931; -. DR CTD; 84277; -. DR DisGeNET; 84277; -. DR GeneCards; DNAJC30; -. DR HGNC; HGNC:16410; DNAJC30. DR HPA; ENSG00000176410; Low tissue specificity. DR MalaCards; DNAJC30; -. DR MIM; 618202; gene. DR MIM; 619382; phenotype. DR OpenTargets; ENSG00000176410; -. DR Orphanet; 104; Leber hereditary optic neuropathy. DR Orphanet; 904; Williams syndrome. DR VEuPathDB; HostDB:ENSG00000176410; -. DR eggNOG; KOG0691; Eukaryota. DR GeneTree; ENSGT00510000048685; -. DR HOGENOM; CLU_104327_2_0_1; -. DR InParanoid; Q96LL9; -. DR OMA; ANRTMFD; -. DR OrthoDB; 376357at2759; -. DR PAN-GO; Q96LL9; 0 GO annotations based on evolutionary models. DR PhylomeDB; Q96LL9; -. DR PathwayCommons; Q96LL9; -. DR SignaLink; Q96LL9; -. DR Agora; ENSG00000176410; -. DR BioGRID-ORCS; 84277; 14 hits in 1155 CRISPR screens. DR ChiTaRS; DNAJC30; human. DR EvolutionaryTrace; Q96LL9; -. DR GenomeRNAi; 84277; -. DR Pharos; Q96LL9; Tbio. DR PRO; PR:Q96LL9; -. DR Proteomes; UP000005640; Chromosome 7. DR RNAct; Q96LL9; protein. DR Bgee; ENSG00000176410; Expressed in tibialis anterior and 192 other cell types or tissues. DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:UniProtKB. DR GO; GO:0005739; C:mitochondrion; HTP:FlyBase. DR GO; GO:0006754; P:ATP biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0007420; P:brain development; ISS:UniProtKB. DR GO; GO:1905706; P:regulation of mitochondrial ATP synthesis coupled proton transport; ISS:UniProtKB. DR CDD; cd06257; DnaJ; 1. DR FunFam; 1.10.287.110:FF:000060; DnaJ (Hsp40) homolog, subfamily C, member 30; 1. DR Gene3D; 1.10.287.110; DnaJ domain; 1. DR InterPro; IPR001623; DnaJ_domain. DR InterPro; IPR036869; J_dom_sf. DR InterPro; IPR053025; Mito_ATP_Synthase-Asso. DR PANTHER; PTHR44873; DNAJ HOMOLOG SUBFAMILY C MEMBER 30, MITOCHONDRIAL; 1. DR PANTHER; PTHR44873:SF1; DNAJ HOMOLOG SUBFAMILY C MEMBER 30, MITOCHONDRIAL; 1. DR Pfam; PF00226; DnaJ; 1. DR PRINTS; PR00625; JDOMAIN. 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 3D-structure; ATP synthesis; Chaperone; Disease variant; KW Leber hereditary optic neuropathy; Membrane; Mitochondrion; KW Mitochondrion inner membrane; Primary mitochondrial disease; KW Proteomics identification; Reference proteome; Transit peptide; KW Transmembrane; Transmembrane helix; Williams-Beuren syndrome. FT TRANSIT 1..38 FT /note="Mitochondrion" FT /evidence="ECO:0000255" FT CHAIN 39..226 FT /note="DnaJ homolog subfamily C member 30, mitochondrial" FT /evidence="ECO:0000255" FT /id="PRO_0000071137" FT TRANSMEM 208..225 FT /note="Helical" FT /evidence="ECO:0000255" FT DOMAIN 49..114 FT /note="J" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00286" FT REGION 116..157 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 130..144 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT VARIANT 34 FT /note="G -> R (in dbSNP:rs1128349)" FT /evidence="ECO:0000269|PubMed:15489334" FT /id="VAR_024433" FT VARIANT 51 FT /note="Y -> C (in LHONAR1; results in reduced turnover of FT N-module subunits of the respiratory chain complex I and FT reduced complex I activity in homozygous patient-derived FT cells; dbSNP:rs61732167)" FT /evidence="ECO:0000269|PubMed:33465056" FT /id="VAR_085951" FT VARIANT 78 FT /note="P -> S (in LHONAR1; results in reduced turnover of FT N-module subunits of the respiratory chain complex I and FT reduced complex I activity in homozygous patient-derived FT cells; dbSNP:rs2116654445)" FT /evidence="ECO:0000269|PubMed:33465056" FT /id="VAR_085952" FT VARIANT 101 FT /note="L -> Q (in LHONAR1; results in reduced turnover of FT N-module subunits of the respiratory chain complex I and FT reduced complex I activity in homozygous patient-derived FT cells; dbSNP:rs2116654140)" FT /evidence="ECO:0000269|PubMed:33465056" FT /id="VAR_085953" FT VARIANT 167 FT /note="F -> L (in dbSNP:rs13244259)" FT /id="VAR_048915" FT HELIX 49..54 FT /evidence="ECO:0007829|PDB:2YUA" FT HELIX 62..75 FT /evidence="ECO:0007829|PDB:2YUA" FT TURN 78..80 FT /evidence="ECO:0007829|PDB:2YUA" FT HELIX 86..100 FT /evidence="ECO:0007829|PDB:2YUA" FT HELIX 104..111 FT /evidence="ECO:0007829|PDB:2YUA" FT HELIX 117..121 FT /evidence="ECO:0007829|PDB:2YUA" SQ SEQUENCE 226 AA; 25961 MW; 8687C2A45790381D CRC64; MAAMRWRWWQ RLLPWRLLQA RGFPQNSAPS LGLGARTYSQ GDCSYSRTAL YDLLGVPSTA TQAQIKAAYY RQCFLYHPDR NSGSAEAAER FTRISQAYVV LGSATLRRKY DRGLLSDEDL RGPGVRPSRT PAPDPGSPRT PPPTSRTHDG SRASPGANRT MFNFDAFYQA HYGEQLERER RLRARREALR KRQEYRSMKG LRWEDTRDTA AIFLIFSIFI IIGFYI //