ID DNJC2_MACFA Reviewed; 621 AA.
AC Q4R8H2;
DT 06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 24-JAN-2024, entry version 96.
DE RecName: Full=DnaJ homolog subfamily C member 2;
DE AltName: Full=Zuotin-related factor 1;
GN Name=DNAJC2; Synonyms=ZRF1; ORFNames=QtsA-12474;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RG International consortium for macaque cDNA sequencing and analysis;
RT "DNA sequences of macaque genes expressed in brain or testis and its
RT evolutionary implications.";
RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
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 -!- 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; AB168480; BAE00600.1; -; mRNA.
DR RefSeq; NP_001270315.1; NM_001283386.1.
DR AlphaFoldDB; Q4R8H2; -.
DR BMRB; Q4R8H2; -.
DR SMR; Q4R8H2; -.
DR STRING; 9541.ENSMFAP00000026650; -.
DR Ensembl; ENSMFAT00000000832.2; ENSMFAP00000026650.2; ENSMFAG00000044726.2.
DR eggNOG; KOG0724; Eukaryota.
DR GeneTree; ENSGT00940000155441; -.
DR OrthoDB; 168809at2759; -.
DR Proteomes; UP000233100; Chromosome 3.
DR Bgee; ENSMFAG00000044726; Expressed in lymph node and 13 other cell types or tissues.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0031965; C:nuclear membrane; IEA:Ensembl.
DR GO; GO:0005730; C:nucleolus; IEA:Ensembl.
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; IEA:Ensembl.
DR GO; GO:0043022; F:ribosome binding; IEA:InterPro.
DR GO; GO:0061649; F:ubiquitin modification-dependent histone binding; ISS:UniProtKB.
DR GO; GO:0051083; P:'de novo' cotranslational protein folding; IEA:InterPro.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0006260; P:DNA replication; IEA:Ensembl.
DR GO; GO:2000279; P:negative regulation of DNA biosynthetic process; IEA:Ensembl.
DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; 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; DnaJ domain; 1.
DR Gene3D; 1.10.10.60; Homeodomain-like; 2.
DR Gene3D; 1.10.8.840; Ribosome-associated complex head domain; 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; DNAJ HOMOLOG SUBFAMILY C MEMBER 2; 1.
DR PANTHER; PTHR43999:SF1; DNAJ HOMOLOG SUBFAMILY C MEMBER 2; 1.
DR Pfam; PF00226; DnaJ; 1.
DR Pfam; PF00249; Myb_DNA-binding; 1.
DR Pfam; PF16717; RAC_head; 1.
DR SMART; SM00271; DnaJ; 1.
DR SMART; SM00717; SANT; 2.
DR SUPFAM; SSF46565; Chaperone J-domain; 1.
DR SUPFAM; SSF46689; Homeodomain-like; 2.
DR PROSITE; PS00636; DNAJ_1; 1.
DR PROSITE; PS50076; DNAJ_2; 1.
DR PROSITE; PS51293; SANT; 2.
PE 2: Evidence at transcript level;
KW Acetylation; Activator; Chaperone; Chromatin regulator; Cytoplasm; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Transcription;
KW Transcription regulation.
FT CHAIN 1..621
FT /note="DnaJ homolog subfamily C member 2"
FT /id="PRO_0000280178"
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 294..315
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 427..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:0000250|UniProtKB:Q99543"
FT MOD_RES 49
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99543"
FT MOD_RES 60
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99543"
FT MOD_RES 63
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99543"
FT MOD_RES 183
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P54103"
SQ SEQUENCE 621 AA; 71931 MW; 802B75EE1A4CD755 CRC64;
MLLLPSPADG RGTAITHALT SASTLCRVEP VGRWFEAFVK RRNRNASASF QELEDKKELS
EESEDEELQL EEFAMLKTLD PKDWKNQDHY AVLGLGHVRY KATQRQIKAA HKAMVLKHHP
DKRKAAGEPI KEGDNDYFTC ITKAYEMLSD PVKRRAFNSV DPTFDNSVPS KSEAKDNFFE
VFSPVFERNS RWSNKKNVPK LGDMNSSFED VDIFYSFWYN FDSWREFSYL DEEEKEKAEC
RDERRWIEKQ NRATRAQRKK EEMNRIRTLV DNAYSCDPRI KKFKEEEKAK KEAEKKAKAE
AKRKEQEAKE KQRQAELEAA RLAKEKEEEE VRQQALLAKK EKDLQKKAIK KERQKLRNSC
KTWNHFSDNE AERVKMMEEV EKLCDRLELA SLQCLNETLT SCTKEVGKAA LEKQIEEINE
QIRKEKEEAE AHMRQASKNT EKSAGGGGNG SKNWSEDDLQ LLIKAVNLFP AGTNSRWEVI
ANYMNIHSSS GVKRTAKDVI GKAKSLQKLD PHQKDDINKK AFDKFKKEHG VVPQADNAAP
SERFEGPYTD FTPWTTEEQK LLEQALKTYP VNTPERWEKI AEAVPGRTKK DCMKRYKELV
EMVKAKKAAQ EQVLNASRAK K
//
