ID A0A2K6PGS7_RHIRO Unreviewed; 931 AA.
AC A0A2K6PGS7;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000256|RuleBase:RU366025};
DE EC=3.4.19.12 {ECO:0000256|RuleBase:RU366025};
GN Name=USP8 {ECO:0000313|Ensembl:ENSRROP00000015733.1};
OS Rhinopithecus roxellana (Golden snub-nosed monkey) (Pygathrix roxellana).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Colobinae; Rhinopithecus.
OX NCBI_TaxID=61622 {ECO:0000313|Ensembl:ENSRROP00000015733.1, ECO:0000313|Proteomes:UP000233200};
RN [1] {ECO:0000313|Ensembl:ENSRROP00000015733.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- FUNCTION: Deubiquitinating enzyme that removes conjugated ubiquitin
CC from specific proteins to regulate different cellular processes.
CC {ECO:0000256|RuleBase:RU366025}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide
CC and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-
CC residue protein attached to proteins as an intracellular targeting
CC signal).; EC=3.4.19.12; Evidence={ECO:0000256|RuleBase:RU366025};
CC -!- SIMILARITY: Belongs to the peptidase C19 family.
CC {ECO:0000256|RuleBase:RU366025}.
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DR AlphaFoldDB; A0A2K6PGS7; -.
DR Ensembl; ENSRROT00000039875.1; ENSRROP00000015733.1; ENSRROG00000032034.1.
DR GeneTree; ENSGT00940000157542; -.
DR Proteomes; UP000233200; Unplaced.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd02674; Peptidase_C19R; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 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; 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; PF00581; Rhodanese; 1.
DR Pfam; PF00443; UCH; 1.
DR Pfam; PF20625; WW_USP8; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF52821; Rhodanese/Cell cycle control phosphatase; 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 3: Inferred from homology;
KW Hydrolase {ECO:0000256|RuleBase:RU366025};
KW Protease {ECO:0000256|RuleBase:RU366025};
KW Reference proteome {ECO:0000313|Proteomes:UP000233200};
KW Thiol protease {ECO:0000256|RuleBase:RU366025};
KW Ubl conjugation pathway {ECO:0000256|RuleBase:RU366025}.
FT DOMAIN 37..155
FT /note="Rhodanese"
FT /evidence="ECO:0000259|PROSITE:PS50206"
FT DOMAIN 590..922
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 241..288
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 316..468
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 492..559
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 254..270
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 316..422
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 426..443
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 496..510
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 513..528
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 931 AA; 105913 MW; 154BEE902A2FB5C0 CRC64;
MFCDVSTSYA VSCHLYCLSQ FQGAITAKEL YTMMTDKNIS LIIMDARRMQ DYQDSCILHS
LSVPEEAISP GVTASWIEAH LPDDSKDTWK KRGNVEYVVL LDWFSSAKDL QIGTILRSLK
DALFKWESKT ILRNEPLVLE GGYENWLLCY PQYTTNAKVT PPPRRQNEEV SISLDFTYPS
LEESVPSKPA AQIPPPSIEV DENIELISDQ NERMGPLNIS TPAEPVAASK SDVSPIIQPV
PSIKNIPQID RTKKPAVKLP EEHRTKSEST NHEQQSPQNG KVIPDRSTKP VVFSPTLMLT
DEEKARIHAE TALLMEKNKQ EKELRERQQE EQKEKLRREE QEQKAKKKQE AEENEITEKQ
QKAKEEMEKK ESEQAKKEDK ETSAKRGKEI TGVKRQSKSE HETSDAKKSV EDRGKRCPTP
EVQKKSTGDV PHTSATGDSG SGKAQREPLT RARSEEMGRI VPGLPSGWAK FLDPITGTFR
YYHSPTNTVH MYPPEMAPSS APPSTPPTHK AKPQIPAERD REPSKLKRSY SSPDITQAIQ
EEEKRKPTVT PTVNRENKPT CYPKAEISRL SASQIRNLNP VFGGSGPALT GLRNLGNTCY
MNSILQCLCN APHLADYFNR NCYQDDINRS NLLGHKGEVA EEFGIIMKAL WTGQYRYISP
KDFKITIGKI NDQFAGYSQQ DSQELLLFLM DGLHEDLNKA DNRKRYKEEN NEHLDDFKAA
EHAWQKHKQL NESIIVALFQ GQFKSTVQCL TCHKKSRTFE AFMYLSLPLA STSKCTLQDC
LRLFSKEEKL TDNNRFYCSH CRARRDSLKK IEIWKLPPVL LVHLKRFSYD GRWKQKLQTS
VDFPLENLDL SQYVIGPKNN LKKYNLFSVS NHYGGLDGGH YTAYCKNAAR QRWFKFDDHE
VSDISVSSVK SSAAYILFYT SLGPRVTDVA T
//
