ID A0A2Y9LKP4_DELLE Unreviewed; 547 AA.
AC A0A2Y9LKP4;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=DnaJ homolog subfamily C member 2 {ECO:0000256|ARBA:ARBA00014469};
DE AltName: Full=Zuotin-related factor 1 {ECO:0000256|ARBA:ARBA00033310};
GN Name=DNAJC2 {ECO:0000313|RefSeq:XP_022410045.1};
OS Delphinapterus leucas (Beluga whale).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Monodontidae; Delphinapterus.
OX NCBI_TaxID=9749 {ECO:0000313|Proteomes:UP000248483, ECO:0000313|RefSeq:XP_022410045.1};
RN [1] {ECO:0000313|RefSeq:XP_022410045.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_022410045.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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:0000256|ARBA:ARBA00024008}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000256|ARBA:ARBA00004514}.
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DR RefSeq; XP_022410045.1; XM_022554337.2.
DR AlphaFoldDB; A0A2Y9LKP4; -.
DR Proteomes; UP000248483; Unplaced.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0030544; F:Hsp70 protein binding; IEA:InterPro.
DR GO; GO:0043022; F:ribosome binding; IEA:InterPro.
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: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; PS51294; HTH_MYB; 1.
DR PROSITE; PS50090; MYB_LIKE; 1.
DR PROSITE; PS51293; SANT; 1.
PE 4: Predicted;
KW Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW Chromatin regulator {ECO:0000256|ARBA:ARBA00022853};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Reference proteome {ECO:0000313|Proteomes:UP000248483}.
FT DOMAIN 14..87
FT /note="J"
FT /evidence="ECO:0000259|PROSITE:PS50076"
FT DOMAIN 475..530
FT /note="SANT"
FT /evidence="ECO:0000259|PROSITE:PS51293"
FT DOMAIN 479..530
FT /note="HTH myb-type"
FT /evidence="ECO:0000259|PROSITE:PS51294"
FT DOMAIN 479..526
FT /note="Myb-like"
FT /evidence="ECO:0000259|PROSITE:PS50090"
FT REGION 220..241
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 352..379
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 547 AA; 63584 MW; 44CC4F6B931B0396 CRC64;
MLKTLDPKDW KNQDHYAVLG LGHVRYKATQ RQIKAAHKAM VLKHHPDKRK AAGEPIKEGD
NDYFTCITKA YEMLSDPVKR RAFNSVDPTF DNSVPSKSEA KDNFFEVFSP VFERNSRWSN
KKNVPKLGDM NSSFEDVDAF YSFWYNFDSW REFSYLDEEE KEKAECRDER RWIEKQNRAT
RAQRKKEEMN RIRTLVDNAY SCDPRIKKFK EEEKAKKEAE KKAKAEAKRK EQEAKEKQRQ
AELEAARLAK EKEEEEVRQQ ALLAKKEKDI QKKAIKKERQ KLRNSCKTWN HFSDNEAERV
KMMEEVEKLC DRLELASLQC LNETLTSSTK EVGKAALEKQ IEEINEQIRK EKEEAEARMR
QASKNAEKST GGGGNGSKHW SEDDLQLLIK AVNLFPAGTN SRWEVIANYM NIHSSSGVKR
TAKDVIGKAK SLQKLDPHQK DDINRKAFDK FKKEHGVVCQ ADNATPSERF EGPCTDFTPW
TTEEQKLLEQ ALKTYPVNTP ERWEKIAEAV PGRTKKDCMK RYKELVEMVK AKKAAQEQVL
NASRGKK
//
