ID G5BVW6_HETGA Unreviewed; 680 AA.
AC G5BVW6;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE SubName: Full=BAG family molecular chaperone regulator 3 {ECO:0000313|EMBL:EHB13417.1};
GN ORFNames=GW7_15369 {ECO:0000313|EMBL:EHB13417.1};
OS Heterocephalus glaber (Naked mole rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Bathyergidae;
OC Heterocephalus.
OX NCBI_TaxID=10181 {ECO:0000313|EMBL:EHB13417.1, ECO:0000313|Proteomes:UP000006813};
RN [1] {ECO:0000313|EMBL:EHB13417.1, ECO:0000313|Proteomes:UP000006813}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21993625; DOI=10.1038/nature10533;
RA Kim E.B., Fang X., Fushan A.A., Huang Z., Lobanov A.V., Han L.,
RA Marino S.M., Sun X., Turanov A.A., Yang P., Yim S.H., Zhao X.,
RA Kasaikina M.V., Stoletzki N., Peng C., Polak P., Xiong Z., Kiezun A.,
RA Zhu Y., Chen Y., Kryukov G.V., Zhang Q., Peshkin L., Yang L., Bronson R.T.,
RA Buffenstein R., Wang B., Han C., Li Q., Chen L., Zhao W., Sunyaev S.R.,
RA Park T.J., Zhang G., Wang J., Gladyshev V.N.;
RT "Genome sequencing reveals insights into physiology and longevity of the
RT naked mole rat.";
RL Nature 479:223-227(2011).
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DR EMBL; JH172105; EHB13417.1; -; Genomic_DNA.
DR RefSeq; XP_004838883.1; XM_004838826.2.
DR AlphaFoldDB; G5BVW6; -.
DR STRING; 10181.G5BVW6; -.
DR Ensembl; ENSHGLT00000019036; ENSHGLP00000018847; ENSHGLG00000013505.
DR GeneID; 101716547; -.
DR KEGG; hgl:101716547; -.
DR CTD; 9531; -.
DR eggNOG; KOG0940; Eukaryota.
DR eggNOG; KOG4361; Eukaryota.
DR InParanoid; G5BVW6; -.
DR OMA; QKGEPSM; -.
DR OrthoDB; 5353777at2759; -.
DR Proteomes; UP000006813; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0101031; C:protein folding chaperone complex; IEA:Ensembl.
DR GO; GO:0030018; C:Z disc; IEA:Ensembl.
DR GO; GO:0000774; F:adenyl-nucleotide exchange factor activity; IEA:Ensembl.
DR GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl.
DR GO; GO:0051087; F:protein-folding chaperone binding; IEA:Ensembl.
DR GO; GO:0034605; P:cellular response to heat; IEA:Ensembl.
DR GO; GO:0071260; P:cellular response to mechanical stimulus; IEA:Ensembl.
DR GO; GO:0034620; P:cellular response to unfolded protein; IEA:Ensembl.
DR GO; GO:0097192; P:extrinsic apoptotic signaling pathway in absence of ligand; IEA:Ensembl.
DR GO; GO:0008625; P:extrinsic apoptotic signaling pathway via death domain receptors; IEA:Ensembl.
DR GO; GO:0046716; P:muscle cell cellular homeostasis; IEA:Ensembl.
DR GO; GO:0010664; P:negative regulation of striated muscle cell apoptotic process; IEA:Ensembl.
DR GO; GO:1905337; P:positive regulation of aggrephagy; IEA:Ensembl.
DR GO; GO:0046827; P:positive regulation of protein export from nucleus; IEA:Ensembl.
DR GO; GO:0042307; P:positive regulation of protein import into nucleus; IEA:Ensembl.
DR GO; GO:0050821; P:protein stabilization; IEA:Ensembl.
DR GO; GO:0010658; P:striated muscle cell apoptotic process; IEA:Ensembl.
DR CDD; cd00201; WW; 1.
DR Gene3D; 2.20.70.10; -; 1.
DR Gene3D; 1.20.58.120; BAG domain; 1.
DR InterPro; IPR039773; BAG_chaperone_regulator.
DR InterPro; IPR036533; BAG_dom_sf.
DR InterPro; IPR003103; BAG_domain.
DR InterPro; IPR001202; WW_dom.
DR InterPro; IPR036020; WW_dom_sf.
DR PANTHER; PTHR12329:SF12; BAG FAMILY MOLECULAR CHAPERONE REGULATOR 3; 1.
DR PANTHER; PTHR12329; BCL2-ASSOCIATED ATHANOGENE; 1.
DR Pfam; PF02179; BAG; 1.
DR Pfam; PF00397; WW; 1.
DR SMART; SM00264; BAG; 1.
DR SMART; SM00456; WW; 1.
DR SUPFAM; SSF63491; BAG domain; 1.
DR SUPFAM; SSF51045; WW domain; 1.
DR PROSITE; PS51035; BAG; 1.
DR PROSITE; PS01159; WW_DOMAIN_1; 1.
DR PROSITE; PS50020; WW_DOMAIN_2; 1.
PE 4: Predicted;
KW Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW Reference proteome {ECO:0000313|Proteomes:UP000006813}.
FT DOMAIN 125..159
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 528..605
FT /note="BAG"
FT /evidence="ECO:0000259|PROSITE:PS51035"
FT REGION 39..107
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 152..196
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 211..305
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 358..529
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 634..680
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 243..258
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 275..303
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 380..394
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 418..432
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 458..490
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 643..657
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 680 AA; 72995 MW; 0068B4B438F7BC4B CRC64;
MTQGGAPHPT RAAANFYGWD QKFLAGQLLP PFISSFPVGS GEAISRHFQP SRATSPPPLI
HKGARRRLPG HGGGAQDSRS SRTPRPRTAT PRPGRSGRPR PSMSAATHSP VVQMASGNGA
AGDRDPLPPG WEIKIDPQTG WPFFVDHNSR TTTWNDPRVP PEDLKETASS ANGPSREGSR
LLPTREGHPV YPQLRPGYIP IPVLHEASEN RQPHPFRSYP QPGTQRFRTE AAAAAPQMSQ
SPLRGVPEAT QSDKQCSQVA AAVAAPPPAS HGPERSQSPA ASDCSSSSSS ASLPSSGRSS
LGSHQLPRGY IPIPVIHEQN VIRPAAQPSF HQAQKTHYPA QQGEYQTHQP VYHKIQGEDW
EPRRAASPFR SPVRGASSRE GSPARSSTPV HSPSPIRVHT VVDRPQQPMT HRESPPVTQP
ENKPEDKPES KPGPAGPDLL PGHIPIQVIR KEVDSKPVSQ KPPPPSEKVE VKVPSAPIPC
PSPSPTPSAV PSSPKNVAAE EKATPSPALT EATAPKPEEA EAPPKHPGVL KVEGILEKVQ
GLEQAVDNFE GKKTDKKYLM IEEYLTKELL ALDSVDPEGR ADVRQARRDG VRKVQTILEK
LEQKAIDVPG QVQVYELQPS NLETDQPLQE IIGMNAVAAD KGKKSAGNED PQTETQHPEA
KEAAAANPSS ITDSAGNPAP
//
