ID UBP20_XENTR Reviewed; 884 AA. AC A0JM59; DT 15-DEC-2009, integrated into UniProtKB/Swiss-Prot. DT 12-DEC-2006, sequence version 1. DT 27-MAR-2024, entry version 82. DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase 20; DE EC=3.4.19.12; DE AltName: Full=Deubiquitinating enzyme 20; DE AltName: Full=Ubiquitin thioesterase 20; DE AltName: Full=Ubiquitin-specific-processing protease 20; GN Name=usp20; OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia; OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana. OX NCBI_TaxID=8364; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Testis; RG NIH - Xenopus Gene Collection (XGC) project; RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Deubiquitinating enzyme involved in beta-2 adrenergic CC receptor (adrb2) recycling. Acts as a regulator of G-protein coupled CC receptor (GPCR) signaling by mediating the deubiquitination beta-2 CC adrenergic receptor (adrb2). Plays a central role in adrb2 recycling CC and resensitization after prolonged agonist stimulation by CC constitutively binding adrb2, mediating deubiquitination of adrb2 and CC inhibiting lysosomal trafficking of adrb2. Mediates deubiquitination of CC both 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains (By CC similarity). {ECO:0000250}. 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; CC -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000250}. CC Cytoplasm, cytoskeleton, microtubule organizing center, centrosome CC {ECO:0000250}. CC -!- DOMAIN: The UBP-type zinc finger binds 3 zinc ions. However, it does CC not bind ubiquitin, probably because the conserved Arg in position 55 CC is replaced by a Glu residue (By similarity). {ECO:0000250}. CC -!- SIMILARITY: Belongs to the peptidase C19 family. USP20/USP33 subfamily. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; BC125749; AAI25750.1; -; mRNA. DR RefSeq; NP_001090641.1; NM_001097172.1. DR AlphaFoldDB; A0JM59; -. DR STRING; 8364.ENSXETP00000049622; -. DR MEROPS; C19.025; -. DR PaxDb; 8364-ENSXETP00000028068; -. DR DNASU; 100036606; -. DR GeneID; 100036606; -. DR KEGG; xtr:100036606; -. DR AGR; Xenbase:XB-GENE-966528; -. DR CTD; 10868; -. DR Xenbase; XB-GENE-966528; usp20. DR eggNOG; KOG1870; Eukaryota. DR InParanoid; A0JM59; -. DR OrthoDB; 227085at2759; -. DR Proteomes; UP000008143; Chromosome 8. DR GO; GO:0005813; C:centrosome; ISS:UniProtKB. DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; ISS:UniProtKB. DR GO; GO:0004197; F:cysteine-type endopeptidase activity; ISS:UniProtKB. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW. DR GO; GO:0016579; P:protein deubiquitination; ISS:UniProtKB. DR GO; GO:0071108; P:protein K48-linked deubiquitination; ISS:UniProtKB. DR GO; GO:0070536; P:protein K63-linked deubiquitination; ISS:UniProtKB. DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW. DR GO; GO:0008277; P:regulation of G protein-coupled receptor signaling pathway; ISS:UniProtKB. DR CDD; cd02674; Peptidase_C19R; 1. DR Gene3D; 3.90.70.10; Cysteine proteinases; 2. DR Gene3D; 3.30.2230.10; DUSP-like; 2. DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1. DR InterPro; IPR035927; DUSP-like_sf. DR InterPro; IPR038765; Papain-like_cys_pep_sf. DR InterPro; IPR006615; Pept_C19_DUSP. DR InterPro; IPR001394; Peptidase_C19_UCH. DR InterPro; IPR018200; USP_CS. DR InterPro; IPR028889; USP_dom. DR InterPro; IPR013083; Znf_RING/FYVE/PHD. DR InterPro; IPR001607; Znf_UBP. DR PANTHER; PTHR21646; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1. DR PANTHER; PTHR21646:SF13; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 20; 1. DR Pfam; PF06337; DUSP; 2. DR Pfam; PF00443; UCH; 1. DR Pfam; PF02148; zf-UBP; 1. DR SMART; SM00695; DUSP; 2. DR SMART; SM00290; ZnF_UBP; 1. DR SUPFAM; SSF54001; Cysteine proteinases; 1. DR SUPFAM; SSF143791; DUSP-like; 2. DR SUPFAM; SSF57850; RING/U-box; 1. DR PROSITE; PS51283; DUSP; 2. DR PROSITE; PS00972; USP_1; 1. DR PROSITE; PS00973; USP_2; 1. DR PROSITE; PS50235; USP_3; 1. DR PROSITE; PS50271; ZF_UBP; 1. PE 2: Evidence at transcript level; KW Cytoplasm; Cytoskeleton; Endocytosis; Hydrolase; Metal-binding; Protease; KW Reference proteome; Repeat; Thiol protease; Ubl conjugation pathway; Zinc; KW Zinc-finger. FT CHAIN 1..884 FT /note="Ubiquitin carboxyl-terminal hydrolase 20" FT /id="PRO_0000390422" FT DOMAIN 145..655 FT /note="USP" FT DOMAIN 657..750 FT /note="DUSP 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00613" FT DOMAIN 759..862 FT /note="DUSP 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00613" FT ZN_FING 6..109 FT /note="UBP-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502" FT REGION 95..142 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 247..296 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 368..388 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 247..277 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 154 FT /note="Nucleophile" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092, FT ECO:0000255|PROSITE-ProRule:PRU10093" FT ACT_SITE 613 FT /note="Proton acceptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092, FT ECO:0000255|PROSITE-ProRule:PRU10093" FT BINDING 8 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502" FT BINDING 10 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502" FT BINDING 30 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502" FT BINDING 33 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502" FT BINDING 43 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502" FT BINDING 48 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502" FT BINDING 53 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502" FT BINDING 60 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502" FT BINDING 64 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502" FT BINDING 70 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502" FT BINDING 83 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502" FT BINDING 86 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502" SQ SEQUENCE 884 AA; 99135 MW; DA651CCD8694FFF1 CRC64; MGDAEDFCPH LDSIGEVTKE DLILKSKGTC ESCGVGGPNL WACLQDGCQS VGCGESYVDH STLHAQAKKH NLTVNLTTFR VWCYACEKEV FLDPRGPPAS QTTSPRLSHR DFPTSAHPLK SVPIAVGDDG ESESDEDDIK PRGLTGMKNI GNSCYMNAAL QALSNCPPLT QFFLECGGLV RTDKKPALCK SYQKLISELW HKKRPSYVVP SSLYHGIKLI NPLFRGYSQQ DTQEFLRCLM DQLHEELKEP VPLETQEREE EDRDDQREGE RGGTVEEDFL SCDSGGEMGD GEGGGGVGTL SEMELLIREE VGRGLSEKEK LKERKLSYCH RRTSSEQADE DADVDTAMIP EPDNDAYVHC SSRSCSPHPV ESISKHSSTP PRSSPLRTSH SYVLKKAQVL SGGKKRSEVR YRSVISDIFD GSILSLVQCL TCDRVSTTIE TFQDLSLPIP GKEDLAKLHS TIHQSAVSKA GTCGDSYAAQ GWLSFFMDYI RRFVVSCIPS WFWGPMITLE DCLAAFFAAD ELKGDNMYSC ERCKKLRNGV KYCKVLRLPE ILCIHLKRFR HEVMYSFKIG SHVSFPLEGL NLRPFLAKEC VSRITTYDLL AVICHHGSAS SGHYISYCQN VINGQWYEFD DQYVTEVHET VVQNAEAYVL FYRKSSEEAE RERQKVVSLA AMKESGLLQF YISREWLNKF NTFAEPGPIS NQSFLCSHGG IPPNKYHYID DLVVILPQSV WEYLYNRFGG GPAVNHLYVC SICQVEIEAL AKRRKTEIDT FIKLNKAFQA EEAPSVIYCI SMQWFREWEA FVKAKDSDPP GPIDNSKVAL TKSSGQVQLK QGADYGQISE ETWNYLLNVY GGGPEIAIRQ TVAQYQEAEH LHGEQKIEAE TRAG //