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DnaJ homolog subfamily C member 24 (CSL-type zinc finger-containing protein 3) (Diphthamide biosynthesis protein 4) (J domain protein DjC7)

 DJC24_MOUSE             Reviewed;         148 AA.
Q91ZF0; Q9D9S7;
24-MAY-2005, integrated into UniProtKB/Swiss-Prot.
12-SEP-2018, sequence version 4.
10-OCT-2018, entry version 126.
RecName: Full=DnaJ homolog subfamily C member 24;
AltName: Full=CSL-type zinc finger-containing protein 3;
AltName: Full=Diphthamide biosynthesis protein 4;
AltName: Full=J domain protein DjC7;
Name=Dnajc24; Synonyms=Dph4, Zcsl3;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
TISSUE=Embryo;
PubMed=11595173; DOI=10.1016/S0378-1119(01)00583-2;
Kroczynska B., Blond S.Y.;
"Cloning and characterization of a new soluble murine J-domain protein
that stimulates BiP, Hsc70 and DnaK ATPase activity with different
efficiencies.";
Gene 273:267-274(2001).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Testis;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J, and FVB/N; TISSUE=Mammary tumor, and Thymus;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
FUNCTION IN DIPHTHAMIDE BIOSYNTHESIS, DISRUPTION PHENOTYPE, AND
SUBCELLULAR LOCATION.
PubMed=18765564; DOI=10.1242/jcs.035550;
Webb T.R., Cross S.H., McKie L., Edgar R., Vizor L., Harrison J.,
Peters J., Jackson I.J.;
"Diphthamide modification of eEF2 requires a J-domain protein and is
essential for normal development.";
J. Cell Sci. 121:3140-3145(2008).
[5]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[6]
STRUCTURE BY NMR OF 1-81.
RIKEN structural genomics initiative (RSGI);
"Solution structure of J-domain of mouse DNAJ-like protein.";
Submitted (NOV-2004) to the PDB data bank.
-!- FUNCTION: The iron-bound form is redox-active and can function as
electron carrier (By similarity). Stimulates the ATPase activity
of several Hsp70-type chaperones. This ability is enhanced by
iron-binding. Plays a role in the diphthamide biosynthesis, a
post-translational modification of histidine which occurs in
translation elongation factor 2 (EEF2). {ECO:0000250,
ECO:0000269|PubMed:11595173, ECO:0000269|PubMed:18765564}.
-!- PATHWAY: Protein modification; peptidyl-diphthamide biosynthesis.
-!- SUBUNIT: Monomer and homooligomer. Iron binding promotes
oligomerization (By similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
{ECO:0000269|PubMed:18765564}.
-!- TISSUE SPECIFICITY: Detected in heart, brain, spleen, lung, liver,
kidney and testis. {ECO:0000269|PubMed:11595173}.
-!- DOMAIN: The DPH-type zinc finger can also bind iron ions instead
of the expected zinc ions. {ECO:0000250}.
-!- DISRUPTION PHENOTYPE: High embryonic lethality at 14.5 dpc. As
early as 10.5 dpc, embryos are smaller than their wild-type
littermates. Embryos that survive long enough to initiate digit
formation show one or more additional preaxial digits.
{ECO:0000269|PubMed:18765564}.
-!- SIMILARITY: Belongs to the DPH4 family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
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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EMBL; AY028460; AAK21968.1; ALT_SEQ; mRNA.
EMBL; AK006521; BAB24631.1; -; mRNA.
EMBL; AL590380; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL928773; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BX649381; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC030072; AAH30072.1; -; mRNA.
EMBL; BC091774; AAH91774.1; -; mRNA.
RefSeq; NP_081268.1; NM_026992.3.
UniGene; Mm.25661; -.
PDB; 1WJZ; NMR; -; A=1-81.
PDBsum; 1WJZ; -.
ProteinModelPortal; Q91ZF0; -.
SMR; Q91ZF0; -.
STRING; 10090.ENSMUSP00000099615; -.
PhosphoSitePlus; Q91ZF0; -.
EPD; Q91ZF0; -.
MaxQB; Q91ZF0; -.
PaxDb; Q91ZF0; -.
PRIDE; Q91ZF0; -.
Ensembl; ENSMUST00000102555; ENSMUSP00000099615; ENSMUSG00000027166.
GeneID; 99349; -.
KEGG; mmu:99349; -.
UCSC; uc008llf.2; mouse.
CTD; 120526; -.
MGI; MGI:1919522; Dnajc24.
eggNOG; KOG0715; Eukaryota.
eggNOG; COG0484; LUCA.
HOGENOM; HOG000189813; -.
HOVERGEN; HBG066253; -.
InParanoid; Q91ZF0; -.
KO; K17867; -.
UniPathway; UPA00559; -.
EvolutionaryTrace; Q91ZF0; -.
PRO; PR:Q91ZF0; -.
Proteomes; UP000000589; Unplaced.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
GO; GO:0001671; F:ATPase activator activity; ISS:UniProtKB.
GO; GO:0008198; F:ferrous iron binding; ISS:UniProtKB.
GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
GO; GO:0055114; P:oxidation-reduction process; IEA:UniProtKB-KW.
GO; GO:0017183; P:peptidyl-diphthamide biosynthetic process from peptidyl-histidine; IEA:UniProtKB-UniPathway.
GO; GO:0032781; P:positive regulation of ATPase activity; ISS:UniProtKB.
CDD; cd06257; DnaJ; 1.
Gene3D; 1.10.287.110; -; 1.
Gene3D; 3.10.660.10; -; 1.
InterPro; IPR001623; DnaJ_domain.
InterPro; IPR036869; J_dom_sf.
InterPro; IPR007872; Znf_DHP.
InterPro; IPR036671; Znf_DHP_sf.
Pfam; PF00226; DnaJ; 1.
Pfam; PF05207; zf-CSL; 1.
PRINTS; PR00625; JDOMAIN.
SMART; SM00271; DnaJ; 1.
SUPFAM; SSF144217; SSF144217; 1.
SUPFAM; SSF46565; SSF46565; 1.
PROSITE; PS50076; DNAJ_2; 1.
PROSITE; PS51074; ZF_DPH; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Cytoplasm; Cytoskeleton;
Electron transport; Iron; Metal-binding; Reference proteome;
Transport; Zinc; Zinc-finger.
CHAIN 1 148 DnaJ homolog subfamily C member 24.
/FTId=PRO_0000082623.
DOMAIN 10 81 J. {ECO:0000255|PROSITE-
ProRule:PRU00286}.
ZN_FING 92 147 DPH-type. {ECO:0000255|PROSITE-
ProRule:PRU00456}.
CONFLICT 102 102 S -> F (in Ref. 1; AAK21968).
{ECO:0000305}.
CONFLICT 146 146 H -> Q (in Ref. 1; AAK21968).
{ECO:0000305}.
STRAND 4 7 {ECO:0000244|PDB:1WJZ}.
HELIX 11 14 {ECO:0000244|PDB:1WJZ}.
HELIX 23 32 {ECO:0000244|PDB:1WJZ}.
STRAND 35 37 {ECO:0000244|PDB:1WJZ}.
HELIX 48 68 {ECO:0000244|PDB:1WJZ}.
STRAND 69 72 {ECO:0000244|PDB:1WJZ}.
HELIX 73 80 {ECO:0000244|PDB:1WJZ}.
SEQUENCE 148 AA; 16922 MW; D0025C7A02252FC4 CRC64;
MALEQTLKKD WYSILGADPS ANMSDLKQKY QKLILLYHPD KQSADVPAGT MEECMQKFIE
IDQAWKILGN EETKKKYDLQ RHEDELRNVG PVDAQVRLEE MSWNQGDESF FLSCRCGGKY
TVSKDEAQEA TLISCDACSL IVELLHQS


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