ID A0A2Y9KSX1_ENHLU Unreviewed; 435 AA.
AC A0A2Y9KSX1;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Sequestosome-1 {ECO:0000313|RefSeq:XP_022376846.1};
GN Name=LOC111158853 {ECO:0000313|RefSeq:XP_022376846.1};
OS Enhydra lutris kenyoni (northern sea otter).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC Lutrinae; Enhydra.
OX NCBI_TaxID=391180 {ECO:0000313|Proteomes:UP000248482, ECO:0000313|RefSeq:XP_022376846.1};
RN [1] {ECO:0000313|RefSeq:XP_022376846.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_022376846.1};
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_022376846.1; XM_022521138.1.
DR AlphaFoldDB; A0A2Y9KSX1; -.
DR STRING; 391180.A0A2Y9KSX1; -.
DR KEGG; elk:111158853; -.
DR OrthoDB; 1329809at2759; -.
DR Proteomes; UP000248482; Unplaced.
DR GO; GO:0005776; C:autophagosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
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 Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000248482};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00228}.
FT DOMAIN 3..100
FT /note="PB1"
FT /evidence="ECO:0000259|PROSITE:PS51745"
FT DOMAIN 121..178
FT /note="ZZ-type"
FT /evidence="ECO:0000259|PROSITE:PS50135"
FT DOMAIN 386..431
FT /note="UBA"
FT /evidence="ECO:0000259|PROSITE:PS50030"
FT REGION 200..232
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 262..379
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 267..292
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 341..370
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 435 AA; 46947 MW; D8A555DD89FBBB8F CRC64;
MASLTVKAYL LGKEEAAREI RRFSFCFSAE AEAEGAAGPG PCERLLSRVA ALFPVLRPGG
FQTHYRDEDG DLVAFSSDEE LTMALSYVKD DIFRIYIKEK KDCRRDHRPP CAQEMPRGLV
HPNVICDGCN GPVVGTRYKC SVCPDYDLCA ACEGKGLHRE HSKLVLPAAF GPFPEGFSHS
RWLRKLKHGH FGWPGWEMGP PGNWSPRPPR AGDARPSSAA EPAAGPAEDP SVNFLKNVGE
SVAAALSPLG IEVDIDVEHG GKRSRLTPVS PGSSSTEEKC SSQPSSCSSD PSKPDGDPEG
VAQSLAEQMD KVALESGPPE EQMESDNCSG GDEDWTHLSS KEVDPSTGEL QSLQMPESEG
PGSLDSSQEG PTGLKEAALY PHLPPEADPR LIESLSQMLS MGFSDEGGWL TRLLQTKNYD
IGAALDTIQY SKHPL
//
