GenomeNet

Database: UniProt
Entry: G3UH43_LOXAF
LinkDB: G3UH43_LOXAF
Original site: G3UH43_LOXAF 
ID   G3UH43_LOXAF            Unreviewed;       445 AA.
AC   G3UH43;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   24-JAN-2024, entry version 70.
DE   SubName: Full=Sequestosome 1 {ECO:0000313|Ensembl:ENSLAFP00000027151.1};
GN   Name=SQSTM1 {ECO:0000313|Ensembl:ENSLAFP00000027151.1};
OS   Loxodonta africana (African elephant).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Afrotheria; Proboscidea; Elephantidae; Loxodonta.
OX   NCBI_TaxID=9785 {ECO:0000313|Ensembl:ENSLAFP00000027151.1, ECO:0000313|Proteomes:UP000007646};
RN   [1] {ECO:0000313|Ensembl:ENSLAFP00000027151.1, ECO:0000313|Proteomes:UP000007646}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000027151.1,
RC   ECO:0000313|Proteomes:UP000007646};
RA   Di Palma F., Heiman D., Young S., Johnson J., Lander E.S., Lindblad-Toh K.;
RT   "The Genome Sequence of Loxodonta africana (African elephant).";
RL   Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSLAFP00000027151.1}
RP   IDENTIFICATION.
RC   STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000027151.1};
RG   Ensembl;
RL   Submitted (JUL-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   STRING; 9785.ENSLAFP00000027151; -.
DR   Ensembl; ENSLAFT00000033113.1; ENSLAFP00000027151.1; ENSLAFG00000028515.1.
DR   eggNOG; KOG4582; Eukaryota.
DR   GeneTree; ENSGT00390000002781; -.
DR   InParanoid; G3UH43; -.
DR   OMA; NCNGWLT; -.
DR   TreeFam; TF328470; -.
DR   Proteomes; UP000007646; Unassembled WGS sequence.
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:0005080; F:protein kinase C binding; 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:0034614; P:cellular response to reactive oxygen species; 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:0000122; P:negative regulation of transcription by RNA polymerase II; 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   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007646};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00228}.
FT   DOMAIN          3..105
FT                   /note="PB1"
FT                   /evidence="ECO:0000259|PROSITE:PS51745"
FT   DOMAIN          126..176
FT                   /note="ZZ-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50135"
FT   DOMAIN          394..439
FT                   /note="UBA"
FT                   /evidence="ECO:0000259|PROSITE:PS50030"
FT   REGION          202..239
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          333..395
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        349..377
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   445 AA;  48399 MW;  CD08077C2A69A506 CRC64;
     MASLTVKAYL LGKEDAAREI RRFSFCFSPE AEAEAEAATG PGPCERLLSR VAALFPALRP
     GGFQAHYRDH LDEDGDLVAF SSDEELTMAM SYVKDDIFRI YIKEKKECRR DHRPPCAQEV
     PRSMVHPNVI CDGCNGPVVG TRYKCSVCPD YDLCAACEGK GLHGEHSKLA FPTPFGHLSE
     GFSHSRWLRK LKHGHFGWPG WEMGPPGNWS PRPPRAGDAR PGPTAGSEIK ASGPSEDPSV
     NFLKNVGESV AAALSPLGPC QVLKNEGMAE KGCLVSLLSR ASHFRAGRSV ECVTCCSCPF
     SGVINFRSAQ RSCGVRXHVL MCSHEFIPGQ MESDNCSGGD DDWTHLSSKE VDPSTGELQS
     LQMPESEGPS SLDPSQEGPT GLKEAALYPH LPPEADPRLI ESLSQMLSMG FSDEGGWLTR
     LLQTKNYDIG AALDTIQYSK HPPPL
//
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