ID A0A2K6QYN6_RHIRO Unreviewed; 565 AA.
AC A0A2K6QYN6;
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=USP21 {ECO:0000313|Ensembl:ENSRROP00000033874.1};
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:ENSRROP00000033874.1, ECO:0000313|Proteomes:UP000233200};
RN [1] {ECO:0000313|Ensembl:ENSRROP00000033874.1}
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; A0A2K6QYN6; -.
DR STRING; 61622.ENSRROP00000033874; -.
DR Ensembl; ENSRROT00000058316.1; ENSRROP00000033874.1; ENSRROG00000040489.1.
DR GeneTree; ENSGT00940000155545; -.
DR OMA; RYWAQYY; -.
DR Proteomes; UP000233200; Unplaced.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0019784; F:deNEDDylase activity; IEA:Ensembl.
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 InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR PANTHER; PTHR21646; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR PANTHER; PTHR21646:SF6; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 21; 1.
DR Pfam; PF00443; UCH; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 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 212..558
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 1..103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 57..72
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 565 AA; 62654 MW; 565F89F700252B10 CRC64;
MPQASEHRLG RTREPPVNIQ PRVGSKLPFA PRARSKERRN PASGPNPMLR PLPPRPGPPD
ERLKKLELGR GRTSGPRPRG PLRADHGVPL PGSPPPTVAL PLPSRTNLAR SKSVSSGDLR
PMGIALGGHR GTGELGAALS RLALRPEPPT LRRSTSLRRL GGFPGPPTLF SIRTEPPASH
GSFHMISARS SEPFYSDDKM AHHTLLLGSG HVGLRNLGNT CFLNAVLQCL SSTRPLRDFC
LRRDFRQEVP GGGRAQELTE AFADVIGALW HPDSCEAVNP TRFRAVFQKY VPSFSGYSQQ
DAQEFLKLLM ERLHLEINRR GRRAPPILAN GPLPSPPRRG GALLEEPELS DDDRANLMWK
RYLEREDSKI VDLFVGQLKS CLKCQACGYR STTFEVFCDL SLPIPKKGFA GGKVSLRDCF
NLFTKEEELE SENAPVCDRC RQKTRSTKKL TVQRFPRILV LHLNRFSASR GSIKKSSVGV
DFPLQRLSLG DFASDKAGSP VYQLYALCNH SGSVHYGHYT ALCRCQTGWH VYNDSRVSPV
SENQVASSEG YVLFYQLMQE PPRCL
//
