ID   Q2UZS7_RAT              Unreviewed;       480 AA.
AC   Q2UZS7;
DT   24-JAN-2006, integrated into UniProtKB/TrEMBL.
DT   24-JAN-2006, sequence version 1.
DT   24-JAN-2024, entry version 123.
DE   SubName: Full=Tid-1 long isoform {ECO:0000313|EMBL:AAQ08229.1};
GN   Name=Dnaja3 {ECO:0000313|RGD:1306527};
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 {ECO:0000313|EMBL:AAQ08229.1};
RN   [1] {ECO:0000313|EMBL:AAQ08229.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Fujita M., Nagai Y., Sawada T., Heese K.;
RT   "Characterizing Tid-1 isoforms in apoptotic processes.";
RL   Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AF516338; AAQ08229.1; -; mRNA.
DR   RefSeq; NP_001033684.1; NM_001038595.1.
DR   AlphaFoldDB; Q2UZS7; -.
DR   GeneID; 360481; -.
DR   KEGG; rno:360481; -.
DR   UCSC; RGD:1306527; rat.
DR   AGR; RGD:1306527; -.
DR   CTD; 9093; -.
DR   RGD; 1306527; Dnaja3.
DR   OrthoDB; 276132at2759; -.
DR   PhylomeDB; Q2UZS7; -.
DR   GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR   GO; GO:0009898; C:cytoplasmic side of plasma membrane; ISO:RGD.
DR   GO; GO:0005829; C:cytosol; ISO:RGD.
DR   GO; GO:0005759; C:mitochondrial matrix; ISO:RGD.
DR   GO; GO:0042645; C:mitochondrial nucleoid; ISO:RGD.
DR   GO; GO:0005739; C:mitochondrion; ISO:RGD.
DR   GO; GO:0031594; C:neuromuscular junction; ISO:RGD.
DR   GO; GO:0005634; C:nucleus; ISO:RGD.
DR   GO; GO:0045211; C:postsynaptic membrane; ISO:RGD.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0030695; F:GTPase regulator activity; ISO:RGD.
DR   GO; GO:0030544; F:Hsp70 protein binding; IPI:RGD.
DR   GO; GO:0106137; F:IkappaB kinase complex binding; ISO:RGD.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0051059; F:NF-kappaB binding; ISO:RGD.
DR   GO; GO:0019901; F:protein kinase binding; ISO:RGD.
DR   GO; GO:0044877; F:protein-containing complex binding; ISO:RGD.
DR   GO; GO:0030971; F:receptor tyrosine kinase binding; ISO:RGD.
DR   GO; GO:0005133; F:type II interferon receptor binding; ISO:RGD.
DR   GO; GO:0051082; F:unfolded protein binding; ISO:RGD.
DR   GO; GO:0006924; P:activation-induced cell death of T cells; ISO:RGD.
DR   GO; GO:0006915; P:apoptotic process; ISO:RGD.
DR   GO; GO:0090398; P:cellular senescence; ISO:RGD.
DR   GO; GO:0006264; P:mitochondrial DNA replication; ISO:RGD.
DR   GO; GO:0007005; P:mitochondrion organization; ISO:RGD.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; IBA:GO_Central.
DR   GO; GO:0008285; P:negative regulation of cell population proliferation; ISO:RGD.
DR   GO; GO:0043069; P:negative regulation of programmed cell death; ISO:RGD.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:RGD.
DR   GO; GO:0060336; P:negative regulation of type II interferon-mediated signaling pathway; ISO:RGD.
DR   GO; GO:0007528; P:neuromuscular junction development; ISO:RGD.
DR   GO; GO:0042102; P:positive regulation of T cell proliferation; ISO:RGD.
DR   GO; GO:0006457; P:protein folding; ISO:RGD.
DR   GO; GO:0009408; P:response to heat; IEA:InterPro.
DR   GO; GO:0034341; P:response to type II interferon; ISO:RGD.
DR   GO; GO:0071340; P:skeletal muscle acetylcholine-gated channel clustering; ISO:RGD.
DR   GO; GO:0007264; P:small GTPase mediated signal transduction; ISO:RGD.
DR   GO; GO:0033077; P:T cell differentiation in thymus; ISO:RGD.
DR   CDD; cd06257; DnaJ; 1.
DR   CDD; cd10747; DnaJ_C; 1.
DR   CDD; cd10719; DnaJ_zf; 1.
DR   Gene3D; 1.10.287.110; DnaJ domain; 1.
DR   Gene3D; 2.10.230.10; Heat shock protein DnaJ, cysteine-rich domain; 1.
DR   Gene3D; 2.60.260.20; Urease metallochaperone UreE, N-terminal domain; 2.
DR   HAMAP; MF_01152; DnaJ; 1.
DR   InterPro; IPR012724; DnaJ.
DR   InterPro; IPR002939; DnaJ_C.
DR   InterPro; IPR001623; DnaJ_domain.
DR   InterPro; IPR018253; DnaJ_domain_CS.
DR   InterPro; IPR008971; HSP40/DnaJ_pept-bd.
DR   InterPro; IPR001305; HSP_DnaJ_Cys-rich_dom.
DR   InterPro; IPR036410; HSP_DnaJ_Cys-rich_dom_sf.
DR   InterPro; IPR036869; J_dom_sf.
DR   PANTHER; PTHR44145; DNAJ HOMOLOG SUBFAMILY A MEMBER 3, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR44145:SF3; DNAJ HOMOLOG SUBFAMILY A MEMBER 3, MITOCHONDRIAL; 1.
DR   Pfam; PF00226; DnaJ; 1.
DR   Pfam; PF01556; DnaJ_C; 1.
DR   Pfam; PF00684; DnaJ_CXXCXGXG; 1.
DR   PRINTS; PR00625; JDOMAIN.
DR   SMART; SM00271; DnaJ; 1.
DR   SUPFAM; SSF46565; Chaperone J-domain; 1.
DR   SUPFAM; SSF57938; DnaJ/Hsp40 cysteine-rich domain; 1.
DR   SUPFAM; SSF49493; HSP40/DnaJ peptide-binding domain; 2.
DR   PROSITE; PS00636; DNAJ_1; 1.
DR   PROSITE; PS50076; DNAJ_2; 1.
DR   PROSITE; PS51188; ZF_CR; 1.
DR   Genevisible; Q2UZS7; RN.
PE   2: Evidence at transcript level;
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW   ProRule:PRU00546}; Methylation {ECO:0000256|ARBA:ARBA00022481};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU00546};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00546}.
FT   DOMAIN          93..158
FT                   /note="J"
FT                   /evidence="ECO:0000259|PROSITE:PS50076"
FT   DOMAIN          223..301
FT                   /note="CR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51188"
FT   ZN_FING         223..301
FT                   /note="CR-type"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00546"
FT   REGION          437..468
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        437..453
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        454..468
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   480 AA;  52399 MW;  D8F57BE86905FEAD CRC64;
     MAAWCSPRWL RVAVGTPRLP AAAGRGVQQP QGGVVAASLC RKLCVSAFGL SMGAHGPRAL
     LTLRPGVRLT GTKSFPFVCT ASFHTSASLA KDDYYQILGV PRNASQKDIK KAYYQLAKKY
     HPDTNKDDPK AKEKFSQLAE AYEVLSDEVK RKQYDAYGSA GFDPGASSSG QGYWRGGPSV
     DPEELFRKIF GEFSSSPFGD FQNVFDQPQE YIMELTFNQA AKGVNKEFTV NIMDTCERCD
     GKGNEPGTKV QHCHYCSGSG METINTGPFV MRSTCRRCGG RGSIITNPCV VCRGAGQAKQ
     KKRVTVPVPA GVEDGQTVRM PVGKREIFVT FRVQKSPVFR RDGADIHSDL FISIAQAILG
     GTAKAQGLYE TINVTIPAGI QTDQKIRLTG KGIPRINSYG YGDHYIHIKI RVPKRLSSRQ
     QNLILSYAED ETDVEGTVNG VTHTSTGGRT MDSSTGSKDR REAGEDNEGF LSKLKKIFTS
//