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   03-AUG-2022, entry version 66.
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}.
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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   CTD; 100158436; -.
DR   Xenbase; XB-GENE-966533; usp20.L.
DR   OrthoDB; 147564at2759; -.
DR   Proteomes; UP000186698; Chromosome 8L.
DR   Bgee; 100158436; Expressed in brain and 20 other 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:0008277; P:regulation of G protein-coupled receptor signaling pathway; ISS:UniProtKB.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR   Gene3D; 3.30.2230.10; -; 2.
DR   Gene3D; 3.30.40.10; -; 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   Pfam; PF06337; DUSP; 2.
DR   Pfam; PF00443; UCH; 2.
DR   Pfam; PF02148; zf-UBP; 1.
DR   SMART; SM00695; DUSP; 2.
DR   SUPFAM; SSF143791; SSF143791; 2.
DR   SUPFAM; SSF54001; SSF54001; 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