ID   DJC24_HUMAN             Reviewed;         149 AA.
AC   Q6P3W2; A8K0V0; B1ALC1; I6L9B4;
DT   24-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT   12-SEP-2018, sequence version 2.
DT   25-MAY-2022, entry version 145.
DE   RecName: Full=DnaJ homolog subfamily C member 24 {ECO:0000305};
DE   AltName: Full=CSL-type zinc finger-containing protein 3;
DE   AltName: Full=Diphthamide biosynthesis protein 4;
GN   Name=DNAJC24 {ECO:0000312|HGNC:HGNC:26979}; Synonyms=DPH4, ZCSL3;
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 [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Amygdala;
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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16554811; DOI=10.1038/nature04632;
RA   Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA   Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA   Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA   Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA   Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA   Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT   "Human chromosome 11 DNA sequence and analysis including novel gene
RT   identification.";
RL   Nature 440:497-500(2006).
RN   [3]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Brain, and Uterus;
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   FUNCTION IN DIPHTHAMIDE BIOSYNTHESIS.
RX   PubMed=22509046; DOI=10.1073/pnas.1204523109;
RA   Wei H., Xiang L., Wayne A.S., Chertov O., FitzGerald D.J., Bera T.K.,
RA   Pastan I.;
RT   "Immunotoxin resistance via reversible methylation of the DPH4 promoter is
RT   a unique survival strategy.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:6898-6903(2012).
RN   [6]
RP   STRUCTURE BY NMR IN COMPLEX WITH ZINC ION, PARTIAL PROTEIN SEQUENCE,
RP   FUNCTION AS HSP70-TYPE CO-CHAPERONE, SUBUNIT, IRON-BINDING, AND MUTAGENESIS
RP   OF CYS-139.
RX   PubMed=22367199; DOI=10.1074/jbc.m112.339655;
RA   Thakur A., Chitoor B., Goswami A.V., Pareek G., Atreya H.S., D'Silva P.;
RT   "Structure and mechanistic insights into novel iron-mediated moonlighting
RT   functions of human J-protein cochaperone, Dph4.";
RL   J. Biol. Chem. 287:13194-13205(2012).
RN   [7]
RP   VARIANT [LARGE SCALE ANALYSIS] ASP-23.
RX   PubMed=16959974; DOI=10.1126/science.1133427;
RA   Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA   Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA   Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA   Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA   Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA   Velculescu V.E.;
RT   "The consensus coding sequences of human breast and colorectal cancers.";
RL   Science 314:268-274(2006).
CC   -!- FUNCTION: Stimulates the ATPase activity of several Hsp70-type
CC       chaperones. This ability is enhanced by iron-binding. The iron-bound
CC       form is redox-active and can function as electron carrier. Plays a role
CC       in the diphthamide biosynthesis, a post-translational modification of
CC       histidine which occurs in translation elongation factor 2 (EEF2) which
CC       can be ADP-ribosylated by diphtheria toxin and by Pseudomonas exotoxin
CC       A (Eta). {ECO:0000269|PubMed:22367199, ECO:0000269|PubMed:22509046}.
CC   -!- PATHWAY: Protein modification; peptidyl-diphthamide biosynthesis.
CC   -!- SUBUNIT: Monomer and homooligomer. Iron binding promotes
CC       oligomerization. {ECO:0000269|PubMed:22367199}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q6P3W2-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q6P3W2-2; Sequence=VSP_056274;
CC   -!- DOMAIN: The DPH-type metal-binding (MB) domain can bind either zinc or
CC       iron ions. {ECO:0000255|PROSITE-ProRule:PRU00456,
CC       ECO:0000269|PubMed:22367199}.
CC   -!- SIMILARITY: Belongs to the DPH4 family. {ECO:0000305}.
CC   -!- CAUTION: It is uncertain whether Met-1 or Met-2 is the initiator.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH36571.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=AAH63804.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=BAF82354.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AK289665; BAF82354.1; ALT_INIT; mRNA.
DR   EMBL; AC108456; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL137804; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471064; EAW68245.1; -; Genomic_DNA.
DR   EMBL; BC036571; AAH36571.1; ALT_INIT; mRNA.
DR   EMBL; BC063804; AAH63804.1; ALT_INIT; mRNA.
DR   CCDS; CCDS7873.2; -. [Q6P3W2-1]
DR   RefSeq; NP_859057.4; NM_181706.4. [Q6P3W2-1]
DR   PDB; 2L6L; NMR; -; A=2-149.
DR   PDBsum; 2L6L; -.
DR   AlphaFoldDB; Q6P3W2; -.
DR   BMRB; Q6P3W2; -.
DR   SMR; Q6P3W2; -.
DR   BioGRID; 125688; 6.
DR   STRING; 9606.ENSP00000417548; -.
DR   iPTMnet; Q6P3W2; -.
DR   PhosphoSitePlus; Q6P3W2; -.
DR   BioMuta; DNAJC24; -.
DR   DMDM; 66773991; -.
DR   EPD; Q6P3W2; -.
DR   MassIVE; Q6P3W2; -.
DR   MaxQB; Q6P3W2; -.
DR   PaxDb; Q6P3W2; -.
DR   PeptideAtlas; Q6P3W2; -.
DR   PRIDE; Q6P3W2; -.
DR   ProteomicsDB; 66934; -. [Q6P3W2-1]
DR   Antibodypedia; 12795; 110 antibodies from 22 providers.
DR   DNASU; 120526; -.
DR   Ensembl; ENST00000465995.6; ENSP00000417548.1; ENSG00000170946.15.
DR   Ensembl; ENST00000526042.5; ENSP00000435771.1; ENSG00000170946.15. [Q6P3W2-2]
DR   GeneID; 120526; -.
DR   KEGG; hsa:120526; -.
DR   MANE-Select; ENST00000465995.6; ENSP00000417548.1; NM_181706.5; NP_859057.4.
DR   CTD; 120526; -.
DR   DisGeNET; 120526; -.
DR   GeneCards; DNAJC24; -.
DR   HGNC; HGNC:26979; DNAJC24.
DR   HPA; ENSG00000170946; Low tissue specificity.
DR   MIM; 611072; gene.
DR   neXtProt; NX_Q6P3W2; -.
DR   OpenTargets; ENSG00000170946; -.
DR   PharmGKB; PA162383906; -.
DR   VEuPathDB; HostDB:ENSG00000170946; -.
DR   eggNOG; KOG0715; Eukaryota.
DR   GeneTree; ENSGT00390000005430; -.
DR   InParanoid; Q6P3W2; -.
DR   OMA; SWPVDAC; -.
DR   OrthoDB; 1580122at2759; -.
DR   PhylomeDB; Q6P3W2; -.
DR   TreeFam; TF326955; -.
DR   PathwayCommons; Q6P3W2; -.
DR   Reactome; R-HSA-5358493; Synthesis of diphthamide-EEF2.
DR   UniPathway; UPA00559; -.
DR   BioGRID-ORCS; 120526; 36 hits in 1052 CRISPR screens.
DR   ChiTaRS; DNAJC24; human.
DR   GenomeRNAi; 120526; -.
DR   Pharos; Q6P3W2; Tbio.
DR   PRO; PR:Q6P3W2; -.
DR   Proteomes; UP000005640; Chromosome 11.
DR   RNAct; Q6P3W2; protein.
DR   ExpressionAtlas; Q6P3W2; 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; IDA:UniProtKB.
DR   GO; GO:0008198; F:ferrous iron binding; IDA:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
DR   GO; GO:0061077; P:chaperone-mediated protein folding; TAS: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; IDA:UniProtKB.
DR   CDD; cd06257; DnaJ; 1.
DR   DisProt; DP00865; -.
DR   Gene3D; 1.10.287.110; -; 1.
DR   Gene3D; 3.10.660.10; -; 1.
DR   InterPro; IPR007872; DHP_MB_dom.
DR   InterPro; IPR036671; DHP_MB_sf.
DR   InterPro; IPR001623; DnaJ_domain.
DR   InterPro; IPR042978; DNAJC24.
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; Alternative splicing; Cytoplasm; Cytoskeleton;
KW   Direct protein sequencing; Electron transport; Iron; Metal-binding;
KW   Reference proteome; Transport; Zinc.
FT   CHAIN           1..149
FT                   /note="DnaJ homolog subfamily C member 24"
FT                   /id="PRO_0000082622"
FT   DOMAIN          11..82
FT                   /note="J"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00286"
FT   DOMAIN          93..148
FT                   /note="DPH-type MB"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00456"
FT   METAL           115
FT                   /note="Zinc"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00456,
FT                   ECO:0000269|PubMed:22367199"
FT   METAL           117
FT                   /note="Zinc"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00456,
FT                   ECO:0000269|PubMed:22367199, ECO:0007744|PDB:2L6L"
FT   METAL           136
FT                   /note="Zinc"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00456,
FT                   ECO:0000269|PubMed:22367199"
FT   METAL           139
FT                   /note="Zinc"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00456,
FT                   ECO:0000269|PubMed:22367199, ECO:0007744|PDB:2L6L"
FT   VAR_SEQ         84..149
FT                   /note="EDDLRNVGPVDAQVYLEEMSWNEGDHSFYLSCRCGGKYSVSKDEAEEVSLIS
FT                   CDTCSLIIELLHYN -> GS (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_056274"
FT   VARIANT         23
FT                   /note="N -> D (in a breast cancer sample; somatic mutation;
FT                   dbSNP:rs111299050)"
FT                   /evidence="ECO:0000269|PubMed:16959974"
FT                   /id="VAR_036397"
FT   MUTAGEN         139
FT                   /note="C->S: Loss of iron-binding."
FT                   /evidence="ECO:0000269|PubMed:22367199"
FT   HELIX           11..16
FT                   /evidence="ECO:0007829|PDB:2L6L"
FT   HELIX           24..38
FT                   /evidence="ECO:0007829|PDB:2L6L"
FT   HELIX           50..68
FT                   /evidence="ECO:0007829|PDB:2L6L"
FT   STRAND          69..71
FT                   /evidence="ECO:0007829|PDB:2L6L"
FT   TURN            72..75
FT                   /evidence="ECO:0007829|PDB:2L6L"
FT   HELIX           77..88
FT                   /evidence="ECO:0007829|PDB:2L6L"
FT   STRAND          92..98
FT                   /evidence="ECO:0007829|PDB:2L6L"
FT   TURN            99..101
FT                   /evidence="ECO:0007829|PDB:2L6L"
FT   STRAND          102..105
FT                   /evidence="ECO:0007829|PDB:2L6L"
FT   TURN            106..109
FT                   /evidence="ECO:0007829|PDB:2L6L"
FT   STRAND          110..114
FT                   /evidence="ECO:0007829|PDB:2L6L"
FT   STRAND          116..118
FT                   /evidence="ECO:0007829|PDB:2L6L"
FT   STRAND          120..124
FT                   /evidence="ECO:0007829|PDB:2L6L"
FT   HELIX           127..130
FT                   /evidence="ECO:0007829|PDB:2L6L"
FT   STRAND          133..135
FT                   /evidence="ECO:0007829|PDB:2L6L"
FT   STRAND          137..140
FT                   /evidence="ECO:0007829|PDB:2L6L"
FT   STRAND          142..146
FT                   /evidence="ECO:0007829|PDB:2L6L"
SQ   SEQUENCE   149 AA;  17139 MW;  84A4BC5F6D2A3F4C CRC64;
     MMAVEQMPKK DWYSILGADP SANISDLKQK YQKLILMYHP DKQSTDVPAG TVEECVQKFI
     EIDQAWKILG NEETKREYDL QRCEDDLRNV GPVDAQVYLE EMSWNEGDHS FYLSCRCGGK
     YSVSKDEAEE VSLISCDTCS LIIELLHYN
//