ID W5N5Z0_LEPOC Unreviewed; 1075 AA.
AC W5N5Z0;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE SubName: Full=Ubiquitin specific peptidase 8 {ECO:0000313|Ensembl:ENSLOCP00000016049.1};
GN Name=USP8 {ECO:0000313|Ensembl:ENSLOCP00000016049.1};
OS Lepisosteus oculatus (Spotted gar).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC Lepisosteus.
OX NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000016049.1, ECO:0000313|Proteomes:UP000018468};
RN [1] {ECO:0000313|Proteomes:UP000018468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT "The Draft Genome of Lepisosteus oculatus.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLOCP00000016049.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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DR EMBL; AHAT01026084; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_015198493.1; XM_015343007.1.
DR RefSeq; XP_015198494.1; XM_015343008.1.
DR AlphaFoldDB; W5N5Z0; -.
DR STRING; 7918.ENSLOCP00000016049; -.
DR Ensembl; ENSLOCT00000016079.1; ENSLOCP00000016049.1; ENSLOCG00000013028.1.
DR GeneID; 102699076; -.
DR KEGG; loc:102699076; -.
DR CTD; 9101; -.
DR eggNOG; KOG1868; Eukaryota.
DR GeneTree; ENSGT00940000157542; -.
DR HOGENOM; CLU_009980_0_0_1; -.
DR InParanoid; W5N5Z0; -.
DR OMA; TCNKESA; -.
DR OrthoDB; 227085at2759; -.
DR Proteomes; UP000018468; Linkage group LG3.
DR Bgee; ENSLOCG00000013028; Expressed in muscle tissue and 13 other cell types or tissues.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0043197; C:dendritic spine; IBA:GO_Central.
DR GO; GO:0019897; C:extrinsic component of plasma membrane; IBA:GO_Central.
DR GO; GO:0030496; C:midbody; IBA:GO_Central.
DR GO; GO:0014069; C:postsynaptic density; IBA:GO_Central.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IBA:GO_Central.
DR GO; GO:0007032; P:endosome organization; IBA:GO_Central.
DR GO; GO:0019538; P:protein metabolic process; IEA:UniProt.
DR GO; GO:0007265; P:Ras protein signal transduction; IBA:GO_Central.
DR CDD; cd02674; Peptidase_C19R; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR Gene3D; 1.20.58.80; Phosphotransferase system, lactose/cellobiose-type IIA subunit; 1.
DR Gene3D; 3.40.250.10; Rhodanese-like domain; 1.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR001763; Rhodanese-like_dom.
DR InterPro; IPR036873; Rhodanese-like_dom_sf.
DR InterPro; IPR015063; USP8_dimer.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR InterPro; IPR048498; WW_USP8.
DR PANTHER; PTHR21646; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR PANTHER; PTHR21646:SF27; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 8; 1.
DR Pfam; PF00443; UCH; 1.
DR Pfam; PF08969; USP8_dimer; 1.
DR Pfam; PF20625; WW_USP8; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF52821; Rhodanese/Cell cycle control phosphatase; 1.
DR SUPFAM; SSF140856; USP8 N-terminal domain-like; 1.
DR PROSITE; PS50206; RHODANESE_3; 1.
DR PROSITE; PS00972; USP_1; 1.
DR PROSITE; PS00973; USP_2; 1.
DR PROSITE; PS50235; USP_3; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000018468}.
FT DOMAIN 193..315
FT /note="Rhodanese"
FT /evidence="ECO:0000259|PROSITE:PS50206"
FT DOMAIN 743..1075
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 121..180
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 335..608
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 647..686
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 121..168
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 342..357
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 458..559
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 581..604
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 664..679
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1075 AA; 123049 MW; AEBE4543D956618C CRC64;
MPTVSAGAKE LYLSTSLGEL NKKAEVKPDK CSTRSYVQSA CKIFKAAEEC RLDRDEERAY
VLYMKYLTVY DLIKKRPDFK QQQEFFLSIL GPSNFKKAIE EAEKLSDSLK LRYEEAEVRK
RLEERERQEE KKRKEEKSEK ESRKSSLKET AESKKEKSKL KGNQKDGRSE TSKAAAPPGG
ITAEKLFQML KDQSMSVIVM DARSLQDYQE SRIQVPEQGC ISVPEEAIKP GITASQIEPK
LPEESKAQWK KRGFVDYIVL LDWFSSVKDL KLGTTLQSLK DALFKWDSTT ILRSEPLVLE
GGYENWLLFY PMYTSNAKVK VPRQERTETL PNLLTFSYPS LEEPKPPAPP EPEPEPPVEV
NGKSSADEEL QKEGAEEQEA PAVQLVPEPA ASPVSAAGLG QVSGSHPAAP AKPIPQFDRT
KKPSAKVLDG AQANNDAPVK DQQPVQNGPF VPDRSIKPTL DLGDKAKREK EQHARERLAE
EEEERLKEEK ERREREERER REKEEKERRL TEELERRRDE AKQEEREKKP KEEREKKSHH
APDAKAKTVS RESSPDHRPV GDTKVPIQPN NPLENGIQKA RIVKDNTEED IEKPKREPLT
RARSEEMGRT VPGLPDGWMK FLDTVTGTYR YYHSPTNRVH LYPPEMSVTQ TPPATPPTLK
QKQVRLPEAD REHSKLKRSY SSPDITQDIQ DEGKKKVTVT PAINRETKPL SLTPYTKAEI
ARPSAAKIRN MNPVFGAPGM CLTGLRNLGN TCYMNSILQC LCNTPGMTDY FNKNYYLEDI
NRSNILGHKG EVAEEFAVIM KALWSGLYKC ISPRDFKITI GKINDRFTSC DHQDSQELLL
FLMDGLHEDL NKADNRKRYK EETNDHLDDF KAAELAWSKH KLLNESIIVA LFQGQFKSTV
QCLTCHKKSR TFETFMYLSL QLTSSNKCTL QDCLKAFSKE EKLTDSNKVE CNNCKTRRDA
TKKLEIWKLP PILLVHLKRF SYEGRWRQKL QTYVDFPLEN LDLSQYVIGP KHNLKRYNLY
GVSNHYGGMD GGHYTAYCKN GLKQRWYKFD DHDISELSAS SVKSSAAYIL FYSSL
//
