DNJC2_BOVIN
ID DNJC2_BOVIN Reviewed; 621 AA.
AC Q1RMH9;
DT 06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=DnaJ homolog subfamily C member 2;
DE AltName: Full=Zuotin-related factor 1;
GN Name=DNAJC2; Synonyms=ZRF1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Ascending colon;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (APR-2006) 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; BC114887; AAI14888.1; -; mRNA.
DR RefSeq; NP_001068805.1; NM_001075337.1.
DR RefSeq; XP_005205394.1; XM_005205337.3.
DR AlphaFoldDB; Q1RMH9; -.
DR BMRB; Q1RMH9; -.
DR SMR; Q1RMH9; -.
DR STRING; 9913.ENSBTAP00000004925; -.
DR PaxDb; Q1RMH9; -.
DR PRIDE; Q1RMH9; -.
DR Ensembl; ENSBTAT00000004925; ENSBTAP00000004925; ENSBTAG00000003784.
DR GeneID; 507897; -.
DR KEGG; bta:507897; -.
DR CTD; 27000; -.
DR VEuPathDB; HostDB:ENSBTAG00000003784; -.
DR VGNC; VGNC:53636; DNAJC2.
DR eggNOG; KOG0724; Eukaryota.
DR GeneTree; ENSGT00940000155441; -.
DR HOGENOM; CLU_019916_0_0_1; -.
DR InParanoid; Q1RMH9; -.
DR OMA; QNGVDHK; -.
DR OrthoDB; 1392575at2759; -.
DR TreeFam; TF105834; -.
DR Reactome; R-BTA-3371453; Regulation of HSF1-mediated heat shock response.
DR Proteomes; UP000009136; Chromosome 4.
DR Bgee; ENSBTAG00000003784; Expressed in semen and 108 other tissues.
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; 1.
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_0000280177"
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 426..453
FT /note="Disordered"
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; 71786 MW; D4EDFF715807E687 CRC64;
MLLLPSAADG QGTAITHALT SASTLCQVEP VGRWFEAFVK RRNRNASASF QELEDKKELS
EESEDEELQL EEFPMLKTLD PKDWKNQDHY AVLGLGHVRY KATQRQIKAA HKAMVLKHHP
DKRKAAGEPI KEGDNDYFTC ITKAYEMLSD PVKRRAFNSV DPTFDNSVPS KSEAKDNFFE
VFSPVFERNS RWSNKKNVPK LGDMNSSFED VDAFYSFWYN FDSWREFSYL DEEEKEKAEC
RDERRWIEKQ NRATRAQRKK EEMNRIRTLV DNAYSCDPRI KKFKEEEKAK KEAEKKAKAD
AKRKEQEAKE KQRQAELEAA RLAKEKEEEE VRQQALLAKK EKDIQKKAIK KERQKLRNLC
KTWNHFSDSE AERVKMMEEV EKLCDRLELS SLQCLNETLT SSTKEVGKAA LEKQIEEINE
QIRKEKEEAE ARMRQASKNA EKSAGGGGNG SKHWSEDDLQ LLIKAVNLFP AGTNSRWEVI
ANYMNIHSSS GVKRTAKDVI GKAKSLQKLD PHQKDDINKK AFDKFKKEHG VVPQADNATP
SERFEGPCTD FTPWTTEEQK LLEQALKTYP VNTPERWEKI AEAVPGRTKK DCMKRYKELV
EMVKAKKAAQ EQVLNASRGK K
