DNJC2_XENTR
ID DNJC2_XENTR Reviewed; 620 AA.
AC Q6P2Y3;
DT 08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT 08-MAR-2011, sequence version 2.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=DnaJ homolog subfamily C member 2;
GN Name=dnajc2;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (DEC-2003) 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. When nuclear, mediates the switching from
CC polycomb-repressed genes to an active state: specifically recruited at
CC histone H2A ubiquitinated at 'Lys-119' (H2AK119ub), and promotes the
CC displacement of the polycomb PRC1 complex from chromatin, thereby
CC facilitating transcription activation (By similarity).
CC {ECO:0000250|UniProtKB:Q99543}.
CC -!- SUBUNIT: Component of ribosome-associated complex (RAC).
CC {ECO:0000250|UniProtKB:Q99543}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00624}.
CC Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q99543}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH64251.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; BC064251; AAH64251.1; ALT_INIT; mRNA.
DR RefSeq; NP_001186412.1; NM_001199483.1.
DR AlphaFoldDB; Q6P2Y3; -.
DR SMR; Q6P2Y3; -.
DR STRING; 8364.ENSXETP00000049978; -.
DR PaxDb; Q6P2Y3; -.
DR GeneID; 394933; -.
DR KEGG; xtr:394933; -.
DR CTD; 27000; -.
DR Xenbase; XB-GENE-964533; dnajc2.
DR eggNOG; KOG0724; Eukaryota.
DR HOGENOM; CLU_019916_0_0_1; -.
DR InParanoid; Q6P2Y3; -.
DR OrthoDB; 1392575at2759; -.
DR PhylomeDB; Q6P2Y3; -.
DR TreeFam; TF105834; -.
DR Reactome; R-XTR-3371453; Regulation of HSF1-mediated heat shock response.
DR Proteomes; UP000008143; Chromosome 3.
DR Proteomes; UP000790000; Unplaced.
DR Bgee; ENSXETG00000023108; Expressed in heart and 13 other tissues.
DR ExpressionAtlas; Q6P2Y3; differential.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
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; IBA:GO_Central.
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: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; 2.
PE 2: Evidence at transcript level;
KW Activator; Chaperone; Chromatin regulator; Cytoplasm; Nucleus;
KW Reference proteome; Repeat; Transcription; Transcription regulation.
FT CHAIN 1..620
FT /note="DnaJ homolog subfamily C member 2"
FT /id="PRO_0000405823"
FT DOMAIN 86..159
FT /note="J"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00286"
FT DOMAIN 447..509
FT /note="SANT 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00624"
FT DOMAIN 548..603
FT /note="SANT 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00624"
FT REGION 284..309
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 420..450
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 420..434
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 435..450
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 620 AA; 71995 MW; 5DF2494F8428512C CRC64;
MLIEAQAEQC TFVTRGLCAA AVLCQVEPVG RWFEAFIKRR NRNVSASFQE LEDEKESSEE
SEDEEFQLEE FPLLKTLDPK DWKNQDHYAV LGLKNLRYKA TQRQIKAAHK AMVLKHHPDK
RKAAGEQIVE GDNDYFTCIT KAYEILSDPI KRRAFNSIDP TFDNSIPSKS EGKDNFFDAF
SPVFERNSRW SNKKNIPKLG DMNSCIEEVD GFYSFWYNFD SWREFSYLDE EEKEKAECRD
ERRWIEKQNR AARAQRKKEE MIRIRTLVDN AYSSDPRIKK FKEEEKARKE AEKKAKADAR
RKEQEEKERQ KQAELEAVRL AKEKEEEEAR QQALLIKKEK EIQKKAIKKE RQRLRTSCKN
WNYFSDNEAE SVKMMEEIEK LCDRLELASL QSLNESLAVS SKEEGKSAVE KQIAEVNAQL
KREKEQEEAR MKQSTKGAEN SAIGGGSGSK SWSEDDLQLL IKAVNLFPAG TNARWEVIAN
YMNLHSISGI KRTSKDVINK AKSLQKLDPQ QKDDINKKAF DKFKKEHRVV PQSVDNAVPS
ERFEGPAADM SPWTTEEQKL LEQALKTYPV NTPERWEKIA EAVPGRSKKD CMKRYKELVE
MVKAKKAAQE QVLNATKIKK
