ID UBP20_XENLA Reviewed; 840 AA. AC B1WBD7; DT 15-DEC-2009, integrated into UniProtKB/Swiss-Prot. DT 20-MAY-2008, sequence version 1. DT 27-MAR-2024, entry version 71. 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 laevis (African clawed frog). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia; OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus. OX NCBI_TaxID=8355; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Ovary; RG NIH - Xenopus Gene Collection (XGC) project; RL Submitted (APR-2008) 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; BC161716; AAI61716.1; -; mRNA. DR RefSeq; NP_001121345.1; NM_001127873.1. DR AlphaFoldDB; B1WBD7; -. DR GeneID; 100158436; -. DR KEGG; xla:100158436; -. DR AGR; Xenbase:XB-GENE-966533; -. DR CTD; 100158436; -. DR Xenbase; XB-GENE-966533; usp20.L. DR OrthoDB; 227085at2759; -. DR Proteomes; UP000186698; Chromosome 8L. DR Bgee; 100158436; Expressed in brain and 20 other cell types or tissues. 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 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..840 FT /note="Ubiquitin carboxyl-terminal hydrolase 20" FT /id="PRO_0000390421" FT DOMAIN 101..611 FT /note="USP" FT DOMAIN 613..706 FT /note="DUSP 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00613" FT DOMAIN 715..818 FT /note="DUSP 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00613" FT ZN_FING 6..117 FT /note="UBP-type; degenerate" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502" FT REGION 205..254 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 315..342 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 110 FT /note="Nucleophile" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092, FT ECO:0000255|PROSITE-ProRule:PRU10093" FT ACT_SITE 569 FT /note="Proton acceptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092, FT ECO:0000255|PROSITE-ProRule:PRU10093" FT BINDING 30 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502" FT BINDING 33 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502" FT BINDING 53 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502" FT BINDING 60 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502" SQ SEQUENCE 840 AA; 94092 MW; C75C9C8E2A85C350 CRC64; MADAEDFCPH LDSIGEVTKE DLILKSKGTC ESCGVGGPNL WACLQDGCQS VGCGESYADH STLHAQDFPS PAHPLKSVPI AVGDDGESES DEDDIKPRGL TGMKNIGNSC YMNAALQALS NCPPLTQFFL ECGGLVRTDK KPALCKSYQK LVSELWHKKR PSYVVPSSLY HGIKLINPLF RGYSQQDTQE FLRCLMDQLH EELKEPILPE NQEQEEEERD DQREGERGGT TEEDFLSCDS GGEMGDGEGG GGVGTLSEME LLIREEVGRG LSEKEKLKER KLSYCHRRTS SEQADEDADV DTAMIPEPDN DAYMHCSSRS CSPHPVESIS KHSSTPPRSS PLRTAHSYVL KKAQVLSGGK KRSEVRYRSV ISDIFDGSIL SLVQCLTCDR VSTTIETFQD LSLPIPGKED LAKLHSTIHQ STVIKAGTCG DSYAAQGWLA FVMDYIRRFV VSCIPSWFWG PMITLEDCLA AFFAADELKG DNMYSCERCK KLRNGVKYCK VLRLPEVLCI HLKRFRHEVM YSFKIGSHVS FPLEGLNLRP FLAKECVSRI TTYDLLAVIC HHGSASSGHY ISYCQNVING QWYEFDDQYV TEVHETVVQN AEAYVLFYRK SSEEAERERQ KVVSLAAMKE SGLLQFYISR EWLNKFNTFA EPGPISNQSF LCAHGGIPPN KYHYIDDLVV ILPQSVWEYL YNRFGGGPAV NHLYVCSICQ VEIEALAKRR KTEIDTFIKL NKAFQAEEAP SVIYCISMQW FREWEAFVKA KDSDPPGPID NSKVALTKSS GHVQLKQGAD YGQISEETWN YLLNIYGGGP EIAIRQTVAQ YQDPEHLHGE QKIEAETRAG //