DNJC2_RAT
ID DNJC2_RAT Reviewed; 621 AA.
AC Q7TQ20; Q5HZY5; Q7TQ18; Q9WVG4;
DT 06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 25-MAY-2022, entry version 132.
DE RecName: Full=DnaJ homolog subfamily C member 2;
DE AltName: Full=Gliosarcoma-related antigen MIDA1;
DE AltName: Full=Zuotin-related factor 1;
GN Name=Dnajc2; Synonyms=Mida1, Zrf1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=Fischer 344; TISSUE=Thymus;
RA Yang T., Figallo L.A., Vujanovic N.L., Jenkins F.J., Okada H.,
RA Pollack I.F., Chambers W.H.;
RT "Characterization of Rat zuotin related factors (ZRFs).";
RL Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Testis;
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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-562.
RC STRAIN=Fischer 344;
RX PubMed=11289140;
RA Okada H., Attanucci J., Giezeman-Smits K.M., Brissette-Storkus C.,
RA Fellows W.K., Gambotto A., Pollack L.F., Pogue-Geile K., Lotze M.T.,
RA Bozik M.E., Chambers W.H.;
RT "Immunization with an antigen identified by cytokine tumor vaccine-assisted
RT SEREX (CAS) suppressed growth of the rat 9L glioma in vivo.";
RL Cancer Res. 61:2625-2631(2001).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-47; SER-60 AND SER-183, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Acts both as a chaperone in the cytosol and as a chromatin
CC regulator in the nucleus. When cytosolic, acts as a molecular
CC chaperone: component of the ribosome-associated complex (RAC), a
CC complex involved in folding or maintaining nascent polypeptides in a
CC folding-competent state. In the RAC complex, stimulates the ATPase
CC activity of the ribosome-associated pool of Hsp70-type chaperones
CC HSPA14 that bind to the nascent polypeptide chain. When nuclear,
CC mediates the switching from polycomb-repressed genes to an active
CC state: specifically recruited at histone H2A ubiquitinated at 'Lys-119'
CC (H2AK119ub), and promotes the displacement of the polycomb PRC1 complex
CC from chromatin, thereby facilitating transcription activation.
CC {ECO:0000250|UniProtKB:Q99543}.
CC -!- SUBUNIT: Component of ribosome-associated complex (RAC), a heterodimer
CC composed of Hsp70/DnaK-type chaperone HSPA14 and Hsp40/DnaJ-type
CC chaperone DNAJC2 (By similarity). Interacts (via ZRF1-UBD region) with
CC ID1 (By similarity). {ECO:0000250|UniProtKB:P54103,
CC ECO:0000250|UniProtKB:Q99543}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q99543}.
CC Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q99543}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q7TQ20-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q7TQ20-2; Sequence=VSP_040720;
CC -!- DOMAIN: The ZRF1-UBD region specifically recognizes and binds
CC H2AK119ub. The ZRF1-UBD region is also involved in protein-protein
CC interactions with other proteins, suggesting that it may be masked by
CC some regulator, thereby preventing its association with H2AK119ub.
CC {ECO:0000250|UniProtKB:Q99543}.
CC -!- PTM: Phosphorylated in M (mitotic) phase.
CC {ECO:0000250|UniProtKB:Q99543}.
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DR EMBL; AY322161; AAP84338.1; -; mRNA.
DR EMBL; AY322163; AAP84340.1; -; mRNA.
DR EMBL; BC088838; AAH88838.1; -; mRNA.
DR EMBL; AF118853; AAD45407.1; -; mRNA.
DR RefSeq; NP_446228.2; NM_053776.2.
DR RefSeq; XP_008760850.1; XM_008762628.2.
DR AlphaFoldDB; Q7TQ20; -.
DR SMR; Q7TQ20; -.
DR CORUM; Q7TQ20; -.
DR STRING; 10116.ENSRNOP00000016909; -.
DR iPTMnet; Q7TQ20; -.
DR PhosphoSitePlus; Q7TQ20; -.
DR jPOST; Q7TQ20; -.
DR PaxDb; Q7TQ20; -.
DR PRIDE; Q7TQ20; -.
DR GeneID; 116456; -.
DR KEGG; rno:116456; -.
DR CTD; 27000; -.
DR RGD; 620524; Dnajc2.
DR eggNOG; KOG0724; Eukaryota.
DR InParanoid; Q7TQ20; -.
DR OrthoDB; 1392575at2759; -.
DR PhylomeDB; Q7TQ20; -.
DR TreeFam; TF105834; -.
DR Reactome; R-RNO-3371453; Regulation of HSF1-mediated heat shock response.
DR PRO; PR:Q7TQ20; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005730; C:nucleolus; ISO:RGD.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
DR GO; GO:0042393; F:histone binding; ISS:UniProtKB.
DR GO; GO:0030544; F:Hsp70 protein binding; ISO:RGD.
DR GO; GO:0043022; F:ribosome binding; IBA:GO_Central.
DR GO; GO:0061649; F:ubiquitin modification-dependent histone binding; ISS:UniProtKB.
DR GO; GO:0051083; P:'de novo' cotranslational protein folding; IBA:GO_Central.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0006260; P:DNA replication; ISO:RGD.
DR GO; GO:0030308; P:negative regulation of cell growth; IDA:RGD.
DR GO; GO:2000279; P:negative regulation of DNA biosynthetic process; ISO:RGD.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0006450; P:regulation of translational fidelity; IEA:InterPro.
DR CDD; cd06257; DnaJ; 1.
DR CDD; cd00167; SANT; 2.
DR Gene3D; 1.10.287.110; -; 1.
DR Gene3D; 1.10.8.840; -; 1.
DR InterPro; IPR001623; DnaJ_domain.
DR InterPro; IPR018253; DnaJ_domain_CS.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR036869; J_dom_sf.
DR InterPro; IPR017930; Myb_dom.
DR InterPro; IPR032003; RAC_head.
DR InterPro; IPR042569; RAC_head_sf.
DR InterPro; IPR001005; SANT/Myb.
DR InterPro; IPR017884; SANT_dom.
DR InterPro; IPR044634; Zuotin/DnaJC2.
DR PANTHER; PTHR43999; PTHR43999; 1.
DR Pfam; PF00226; DnaJ; 1.
DR Pfam; PF00249; Myb_DNA-binding; 2.
DR Pfam; PF16717; RAC_head; 1.
DR SMART; SM00271; DnaJ; 1.
DR SMART; SM00717; SANT; 2.
DR SUPFAM; SSF46565; SSF46565; 1.
DR SUPFAM; SSF46689; SSF46689; 2.
DR PROSITE; PS00636; DNAJ_1; 1.
DR PROSITE; PS50076; DNAJ_2; 1.
DR PROSITE; PS51293; SANT; 1.
PE 1: Evidence at protein level;
KW Acetylation; Activator; Alternative splicing; Chaperone;
KW Chromatin regulator; Cytoplasm; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Transcription; Transcription regulation.
FT CHAIN 1..621
FT /note="DnaJ homolog subfamily C member 2"
FT /id="PRO_0000280179"
FT DOMAIN 88..161
FT /note="J"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00286"
FT DOMAIN 449..511
FT /note="SANT 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00624"
FT DOMAIN 549..604
FT /note="SANT 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00624"
FT REGION 160..250
FT /note="ZRF1-UBD"
FT REGION 287..312
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 426..453
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 438..453
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q99543"
FT MOD_RES 47
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 49
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99543"
FT MOD_RES 60
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 63
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99543"
FT MOD_RES 183
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT VAR_SEQ 1..74
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_040720"
FT CONFLICT 446
FT /note="G -> R (in Ref. 2; AAH88838)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 621 AA; 71769 MW; 06ED1C7AA56267A6 CRC64;
MLLLPSAAEG QGTAITHALT SASAVCQVEP VGRWFEAFVK RRNRNASTSF QELEDKKELS
EESEDEELQL EEFPMLKTLD PKDWKNQDHY AVLGLGHVRY KATQRQIKAA HKTMVLKHHP
DKRKAAGEPI KEGDNDYFTC ITKAYEMLSD PVKRRAFNSV DPTFDNSVPS KSEAKENFFQ
VFSPVFERNS RWSNKKNVPK LGDMNSSFED VDAFYSFWYN FDSWREFSYL DEEEKEKAEC
RDERKWIEKQ NRATRAQRKK EEMNRIRTLV DNAYSCDPRI KKFKEEGKAK KEAEKRAKAE
ARRKEQEAKE KQRQAELEAV RLAKEKEEEE VRQQALLAKK EKEIQKKAIK KERQKLRNSC
KNWNHFSDNE ADRVKMMEEV EKLCDRLELA SLQCLNEILA SSTREVGKAA LEKQIEEVNE
LMRKEKEEAD ARMRQASKNA EKSTGGSGSG SKNWSEDDLQ LLIKAVNLFP AGTNSRWEVI
ANYMNIHSSS GVKRTAKDVI GKAKSLQKLD PHQKDDINKK AFDKFKKEHG VAPQADSAAP
SERFEGPCID SIPWTTEEQK LLEQALKTYP VNTPERWEKI AEAVPGRTKK DCMRRYKELV
EMVKAKKAAQ EQVLNASRAR K
