DJC24_MOUSE
ID DJC24_MOUSE Reviewed; 148 AA.
AC Q91ZF0; Q9D9S7;
DT 24-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 12-SEP-2018, sequence version 4.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=DnaJ homolog subfamily C member 24;
DE AltName: Full=CSL-type zinc finger-containing protein 3;
DE AltName: Full=Diphthamide biosynthesis protein 4;
DE AltName: Full=J domain protein DjC7;
GN Name=Dnajc24; Synonyms=Dph4, Zcsl3;
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], FUNCTION, AND TISSUE SPECIFICITY.
RC TISSUE=Embryo;
RX PubMed=11595173; DOI=10.1016/s0378-1119(01)00583-2;
RA Kroczynska B., Blond S.Y.;
RT "Cloning and characterization of a new soluble murine J-domain protein that
RT stimulates BiP, Hsc70 and DnaK ATPase activity with different
RT efficiencies.";
RL Gene 273:267-274(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Testis;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Mammary tumor, and Thymus;
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 [4]
RP FUNCTION IN DIPHTHAMIDE BIOSYNTHESIS, DISRUPTION PHENOTYPE, AND SUBCELLULAR
RP LOCATION.
RX PubMed=18765564; DOI=10.1242/jcs.035550;
RA Webb T.R., Cross S.H., McKie L., Edgar R., Vizor L., Harrison J.,
RA Peters J., Jackson I.J.;
RT "Diphthamide modification of eEF2 requires a J-domain protein and is
RT essential for normal development.";
RL J. Cell Sci. 121:3140-3145(2008).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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 [6]
RP STRUCTURE BY NMR OF 1-81.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of J-domain of mouse DNAJ-like protein.";
RL Submitted (NOV-2004) to the PDB data bank.
CC -!- FUNCTION: The iron-bound form is redox-active and can function as
CC electron carrier (By similarity). Stimulates the ATPase activity of
CC several Hsp70-type chaperones. This ability is enhanced by iron-
CC binding. Plays a role in the diphthamide biosynthesis, a post-
CC translational modification of histidine which occurs in translation
CC elongation factor 2 (EEF2). {ECO:0000250, ECO:0000269|PubMed:11595173,
CC ECO:0000269|PubMed:18765564}.
CC -!- PATHWAY: Protein modification; peptidyl-diphthamide biosynthesis.
CC -!- SUBUNIT: Monomer and homooligomer. Iron binding promotes
CC oligomerization (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:18765564}.
CC -!- TISSUE SPECIFICITY: Detected in heart, brain, spleen, lung, liver,
CC kidney and testis. {ECO:0000269|PubMed:11595173}.
CC -!- DOMAIN: The DPH-type metal-binding (MB) domain can bind either zinc or
CC iron ions. {ECO:0000255|PROSITE-ProRule:PRU00456}.
CC -!- DISRUPTION PHENOTYPE: High embryonic lethality at 14.5 dpc. As early as
CC 10.5 dpc, embryos are smaller than their wild-type littermates. Embryos
CC that survive long enough to initiate digit formation show one or more
CC additional preaxial digits. {ECO:0000269|PubMed:18765564}.
CC -!- SIMILARITY: Belongs to the DPH4 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK21968.1; Type=Miscellaneous discrepancy; Note=A nucleotide mismatch versus the mouse genome results in the formation of an upstream ATG start codon.; Evidence={ECO:0000305};
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DR EMBL; AY028460; AAK21968.1; ALT_SEQ; mRNA.
DR EMBL; AK006521; BAB24631.1; -; mRNA.
DR EMBL; AL590380; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL928773; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BX649381; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC030072; AAH30072.1; -; mRNA.
DR EMBL; BC091774; AAH91774.1; -; mRNA.
DR CCDS; CCDS16501.1; -.
DR RefSeq; NP_081268.1; NM_026992.3.
DR PDB; 1WJZ; NMR; -; A=1-81.
DR PDBsum; 1WJZ; -.
DR AlphaFoldDB; Q91ZF0; -.
DR BMRB; Q91ZF0; -.
DR SMR; Q91ZF0; -.
DR STRING; 10090.ENSMUSP00000099615; -.
DR PhosphoSitePlus; Q91ZF0; -.
DR EPD; Q91ZF0; -.
DR MaxQB; Q91ZF0; -.
DR PaxDb; Q91ZF0; -.
DR PRIDE; Q91ZF0; -.
DR ProteomicsDB; 279714; -.
DR Antibodypedia; 12795; 112 antibodies from 23 providers.
DR DNASU; 99349; -.
DR Ensembl; ENSMUST00000102555; ENSMUSP00000099615; ENSMUSG00000027166.
DR GeneID; 99349; -.
DR KEGG; mmu:99349; -.
DR UCSC; uc008llf.2; mouse.
DR CTD; 120526; -.
DR MGI; MGI:1919522; Dnajc24.
DR VEuPathDB; HostDB:ENSMUSG00000027166; -.
DR eggNOG; KOG0715; Eukaryota.
DR GeneTree; ENSGT00390000005430; -.
DR InParanoid; Q91ZF0; -.
DR OMA; SWPVDAC; -.
DR OrthoDB; 1580122at2759; -.
DR Reactome; R-MMU-5358493; Synthesis of diphthamide-EEF2.
DR UniPathway; UPA00559; -.
DR BioGRID-ORCS; 99349; 7 hits in 73 CRISPR screens.
DR ChiTaRS; Dnajc24; mouse.
DR EvolutionaryTrace; Q91ZF0; -.
DR PRO; PR:Q91ZF0; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q91ZF0; protein.
DR Bgee; ENSMUSG00000027166; Expressed in seminal vesicle and 232 other tissues.
DR ExpressionAtlas; Q91ZF0; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0001671; F:ATPase activator activity; ISS:UniProtKB.
DR GO; GO:0008198; F:ferrous iron binding; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR GO; GO:0017183; P:peptidyl-diphthamide biosynthetic process from peptidyl-histidine; IEA:UniProtKB-UniPathway.
DR GO; GO:0032781; P:positive regulation of ATP-dependent activity; ISS:UniProtKB.
DR CDD; cd06257; DnaJ; 1.
DR Gene3D; 1.10.287.110; -; 1.
DR Gene3D; 3.10.660.10; -; 1.
DR InterPro; IPR001623; DnaJ_domain.
DR InterPro; IPR042978; DNAJC24.
DR InterPro; IPR007872; DPH_MB_dom.
DR InterPro; IPR036671; DPH_MB_sf.
DR InterPro; IPR036869; J_dom_sf.
DR PANTHER; PTHR45255; PTHR45255; 1.
DR Pfam; PF00226; DnaJ; 1.
DR Pfam; PF05207; zf-CSL; 1.
DR PRINTS; PR00625; JDOMAIN.
DR SMART; SM00271; DnaJ; 1.
DR SUPFAM; SSF144217; SSF144217; 1.
DR SUPFAM; SSF46565; SSF46565; 1.
DR PROSITE; PS50076; DNAJ_2; 1.
DR PROSITE; PS51074; DPH_MB; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Cytoskeleton; Electron transport; Iron;
KW Metal-binding; Reference proteome; Transport; Zinc.
FT CHAIN 1..148
FT /note="DnaJ homolog subfamily C member 24"
FT /id="PRO_0000082623"
FT DOMAIN 10..81
FT /note="J"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00286"
FT DOMAIN 92..147
FT /note="DPH-type MB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00456"
FT BINDING 114
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00456"
FT BINDING 116
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00456"
FT BINDING 135
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00456"
FT BINDING 138
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00456"
FT CONFLICT 102
FT /note="S -> F (in Ref. 1; AAK21968)"
FT /evidence="ECO:0000305"
FT CONFLICT 146
FT /note="H -> Q (in Ref. 1; AAK21968)"
FT /evidence="ECO:0000305"
FT STRAND 4..7
FT /evidence="ECO:0007829|PDB:1WJZ"
FT HELIX 11..14
FT /evidence="ECO:0007829|PDB:1WJZ"
FT HELIX 23..32
FT /evidence="ECO:0007829|PDB:1WJZ"
FT STRAND 35..37
FT /evidence="ECO:0007829|PDB:1WJZ"
FT HELIX 48..68
FT /evidence="ECO:0007829|PDB:1WJZ"
FT STRAND 69..72
FT /evidence="ECO:0007829|PDB:1WJZ"
FT HELIX 73..80
FT /evidence="ECO:0007829|PDB:1WJZ"
SQ SEQUENCE 148 AA; 16922 MW; D0025C7A02252FC4 CRC64;
MALEQTLKKD WYSILGADPS ANMSDLKQKY QKLILLYHPD KQSADVPAGT MEECMQKFIE
IDQAWKILGN EETKKKYDLQ RHEDELRNVG PVDAQVRLEE MSWNQGDESF FLSCRCGGKY
TVSKDEAQEA TLISCDACSL IVELLHQS
