DJC30_HUMAN
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 03-AUG-2022, entry version 155.
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, 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 LHONAR CYS-51; SER-78 AND GLN-101, INVOLVEMENT IN LHONAR,
RP CHARACTERIZATION OF VARIANTS LHONAR 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 hereditary optic neuropathy, autosomal recessive
CC (LHONAR) [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.
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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; 218.
DR IntAct; Q96LL9; 41.
DR MINT; Q96LL9; -.
DR STRING; 9606.ENSP00000378605; -.
DR iPTMnet; Q96LL9; -.
DR PhosphoSitePlus; Q96LL9; -.
DR BioMuta; DNAJC30; -.
DR DMDM; 24212614; -.
DR EPD; Q96LL9; -.
DR jPOST; Q96LL9; -.
DR MassIVE; Q96LL9; -.
DR MaxQB; Q96LL9; -.
DR PaxDb; Q96LL9; -.
DR PeptideAtlas; Q96LL9; -.
DR PRIDE; Q96LL9; -.
DR ProteomicsDB; 77223; -.
DR Antibodypedia; 2642; 98 antibodies from 15 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 CTD; 84277; -.
DR DisGeNET; 84277; -.
DR GeneCards; DNAJC30; -.
DR HGNC; HGNC:16410; DNAJC30.
DR HPA; ENSG00000176410; Low tissue specificity.
DR MIM; 618202; gene.
DR MIM; 619382; phenotype.
DR neXtProt; NX_Q96LL9; -.
DR OpenTargets; ENSG00000176410; -.
DR Orphanet; 104; Leber hereditary optic neuropathy.
DR Orphanet; 904; Williams syndrome.
DR PharmGKB; PA162383931; -.
DR VEuPathDB; HostDB:ENSG00000176410; -.
DR eggNOG; KOG0691; Eukaryota.
DR GeneTree; ENSGT00510000048685; -.
DR HOGENOM; CLU_104327_2_0_1; -.
DR InParanoid; Q96LL9; -.
DR OMA; HYGKSFD; -.
DR OrthoDB; 1404041at2759; -.
DR PhylomeDB; Q96LL9; -.
DR TreeFam; TF332749; -.
DR PathwayCommons; Q96LL9; -.
DR SignaLink; Q96LL9; -.
DR BioGRID-ORCS; 84277; 14 hits in 1077 CRISPR screens.
DR ChiTaRS; DNAJC30; human.
DR EvolutionaryTrace; Q96LL9; -.
DR GenomeRNAi; 84277; -.
DR Pharos; Q96LL9; Tdark.
DR PRO; PR:Q96LL9; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q96LL9; protein.
DR Bgee; ENSG00000176410; Expressed in tibialis anterior and 191 other tissues.
DR Genevisible; Q96LL9; HS.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:UniProtKB.
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 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 3D-structure; ATP synthesis; Chaperone; Disease variant;
KW Leber hereditary optic neuropathy; Membrane; Mitochondrion;
KW Mitochondrion inner membrane; Primary mitochondrial disease;
KW Reference proteome; Transit peptide; Transmembrane; Transmembrane helix;
KW 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 128..142
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 143..157
FT /note="Polar 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 LHONAR; results in reduced turnover of N-
FT module subunits of the respiratory chain complex I and
FT reduced complex I activity in homozygous patient-derived
FT cells)"
FT /evidence="ECO:0000269|PubMed:33465056"
FT /id="VAR_085951"
FT VARIANT 78
FT /note="P -> S (in LHONAR; results in reduced turnover of N-
FT module subunits of the respiratory chain complex I and
FT reduced complex I activity in homozygous patient-derived
FT cells)"
FT /evidence="ECO:0000269|PubMed:33465056"
FT /id="VAR_085952"
FT VARIANT 101
FT /note="L -> Q (in LHONAR; results in reduced turnover of N-
FT module subunits of the respiratory chain complex I and
FT reduced complex I activity in homozygous patient-derived
FT cells)"
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
