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Database: UniProt
Entry: A0A1U7QS70_MESAU
LinkDB: A0A1U7QS70_MESAU
Original site: A0A1U7QS70_MESAU 
ID   A0A1U7QS70_MESAU        Unreviewed;       442 AA.
AC   A0A1U7QS70;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   SubName: Full=Sequestosome-1 isoform X1 {ECO:0000313|RefSeq:XP_005071915.1};
GN   Name=Sqstm1 {ECO:0000313|RefSeq:XP_005071915.1};
OS   Mesocricetus auratus (Golden hamster).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC   Cricetidae; Cricetinae; Mesocricetus.
OX   NCBI_TaxID=10036 {ECO:0000313|Proteomes:UP000189706, ECO:0000313|RefSeq:XP_005071915.1};
RN   [1] {ECO:0000313|RefSeq:XP_005071915.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, autophagosome
CC       {ECO:0000256|ARBA:ARBA00004419}. Lysosome
CC       {ECO:0000256|ARBA:ARBA00004371}. Nucleus
CC       {ECO:0000256|ARBA:ARBA00004123}.
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DR   RefSeq; XP_005071915.1; XM_005071858.3.
DR   AlphaFoldDB; A0A1U7QS70; -.
DR   STRING; 10036.ENSMAUP00000014683; -.
DR   GeneID; 101829794; -.
DR   KEGG; maua:101829794; -.
DR   CTD; 8878; -.
DR   eggNOG; KOG4582; Eukaryota.
DR   OrthoDB; 1329809at2759; -.
DR   Proteomes; UP000189706; Unplaced.
DR   GO; GO:0016235; C:aggresome; IEA:Ensembl.
DR   GO; GO:0044753; C:amphisome; IEA:Ensembl.
DR   GO; GO:0044754; C:autolysosome; IEA:Ensembl.
DR   GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
DR   GO; GO:0000932; C:P-body; IEA:Ensembl.
DR   GO; GO:0000407; C:phagophore assembly site; IEA:Ensembl.
DR   GO; GO:0016605; C:PML body; IEA:Ensembl.
DR   GO; GO:0097225; C:sperm midpiece; IEA:Ensembl.
DR   GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR   GO; GO:0035255; F:ionotropic glutamate receptor binding; IEA:Ensembl.
DR   GO; GO:0070530; F:K63-linked polyubiquitin modification-dependent protein binding; IEA:Ensembl.
DR   GO; GO:0140693; F:molecular condensate scaffold activity; IEA:Ensembl.
DR   GO; GO:0005080; F:protein kinase C binding; IEA:Ensembl.
DR   GO; GO:0140311; F:protein sequestering activity; IEA:Ensembl.
DR   GO; GO:0042169; F:SH2 domain binding; IEA:Ensembl.
DR   GO; GO:0035591; F:signaling adaptor activity; IEA:Ensembl.
DR   GO; GO:0038023; F:signaling receptor activity; IEA:Ensembl.
DR   GO; GO:0043130; F:ubiquitin binding; IEA:Ensembl.
DR   GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:Ensembl.
DR   GO; GO:0140036; F:ubiquitin-dependent protein binding; IEA:Ensembl.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0035973; P:aggrephagy; IEA:Ensembl.
DR   GO; GO:0070342; P:brown fat cell proliferation; IEA:Ensembl.
DR   GO; GO:0007032; P:endosome organization; IEA:Ensembl.
DR   GO; GO:0097009; P:energy homeostasis; IEA:Ensembl.
DR   GO; GO:0000423; P:mitophagy; IEA:Ensembl.
DR   GO; GO:0031397; P:negative regulation of protein ubiquitination; IEA:Ensembl.
DR   GO; GO:0034144; P:negative regulation of toll-like receptor 4 signaling pathway; IEA:Ensembl.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR   GO; GO:0140694; P:non-membrane-bounded organelle assembly; IEA:Ensembl.
DR   GO; GO:0000425; P:pexophagy; IEA:Ensembl.
DR   GO; GO:0010508; P:positive regulation of autophagy; IEA:Ensembl.
DR   GO; GO:1900273; P:positive regulation of long-term synaptic potentiation; IEA:Ensembl.
DR   GO; GO:1903078; P:positive regulation of protein localization to plasma membrane; IEA:Ensembl.
DR   GO; GO:0030163; P:protein catabolic process; IEA:Ensembl.
DR   GO; GO:0006606; P:protein import into nucleus; IEA:Ensembl.
DR   GO; GO:1905719; P:protein localization to perinuclear region of cytoplasm; IEA:Ensembl.
DR   GO; GO:0071211; P:protein targeting to vacuole involved in autophagy; IEA:Ensembl.
DR   GO; GO:0043122; P:regulation of canonical NF-kappaB signal transduction; IEA:Ensembl.
DR   GO; GO:0061635; P:regulation of protein complex stability; IEA:Ensembl.
DR   GO; GO:0098780; P:response to mitochondrial depolarisation; IEA:Ensembl.
DR   GO; GO:0001659; P:temperature homeostasis; IEA:Ensembl.
DR   GO; GO:0006366; P:transcription by RNA polymerase II; IEA:Ensembl.
DR   CDD; cd06402; PB1_p62; 1.
DR   CDD; cd14320; UBA_SQSTM; 1.
DR   CDD; cd02340; ZZ_NBR1_like; 1.
DR   Gene3D; 3.30.60.90; -; 1.
DR   Gene3D; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 1.
DR   InterPro; IPR000270; PB1_dom.
DR   InterPro; IPR034866; PB1_p62.
DR   InterPro; IPR033741; SQSTM_UBA.
DR   InterPro; IPR015940; UBA.
DR   InterPro; IPR009060; UBA-like_sf.
DR   InterPro; IPR000433; Znf_ZZ.
DR   InterPro; IPR043145; Znf_ZZ_sf.
DR   PANTHER; PTHR15090; SEQUESTOSOME 1-RELATED; 1.
DR   PANTHER; PTHR15090:SF0; SEQUESTOSOME-1; 1.
DR   Pfam; PF00564; PB1; 1.
DR   Pfam; PF16577; UBA_5; 1.
DR   Pfam; PF00569; ZZ; 1.
DR   SMART; SM00666; PB1; 1.
DR   SMART; SM00165; UBA; 1.
DR   SMART; SM00291; ZnF_ZZ; 1.
DR   SUPFAM; SSF54277; CAD & PB1 domains; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   SUPFAM; SSF46934; UBA-like; 1.
DR   PROSITE; PS51745; PB1; 1.
DR   PROSITE; PS50030; UBA; 1.
DR   PROSITE; PS01357; ZF_ZZ_1; 1.
DR   PROSITE; PS50135; ZF_ZZ_2; 1.
PE   4: Predicted;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00023329};
KW   Lysosome {ECO:0000256|ARBA:ARBA00023228};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000189706};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00228}.
FT   DOMAIN          3..102
FT                   /note="PB1"
FT                   /evidence="ECO:0000259|PROSITE:PS51745"
FT   DOMAIN          123..173
FT                   /note="ZZ-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50135"
FT   DOMAIN          391..436
FT                   /note="UBA"
FT                   /evidence="ECO:0000259|PROSITE:PS50030"
FT   REGION          204..234
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          262..308
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          321..392
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        268..308
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        346..374
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   442 AA;  48097 MW;  A3FF803A960E8052 CRC64;
     MASLTVKAYL LGKEEAAREI RRFSFCFSPE PEAEAEAAAG PGPCERLLSR VASLFPALRP
     GGFQAHYRDE DGDLVAFSSD EELTMAMSYV KDDIFRIYIK EKKECRRDHR PPCAQEASRS
     MVHPNVICDG CNGPVVGTRY KCSVCPDYDL CSVCEGKGLH REHSKLIFPN PFGHLSDGFS
     HGRWLRKLKH GHFGWPGWEM GPPGNWSPRP PRAGDARPCP TAESASGPSE DPSVNFLKSV
     GESVAAALSP LGIEVDIDVE HGGKRSRLTP TSPESSSMDT EDKCSTQPSS CSSEVNKADE
     AGEGTSQSLT EQMKKIALES VGQPEEQMES DNCSGGDDDW THLSSKEVDP STGELQSLQM
     PESEGPSSLD PSQEGPTGLK EAALYPHLPP EADPRLIESL SQMLSMGFSD EGGWLTRLLQ
     TKNYDIGAAL DTIQYSKHPP PL
//
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