UBP20_XENTR
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 03-AUG-2022, entry version 76.
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}.
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DR EMBL; BC125749; AAI25750.1; -; mRNA.
DR RefSeq; NP_001090641.1; NM_001097172.1.
DR AlphaFoldDB; A0JM59; -.
DR STRING; 8364.ENSXETP00000028068; -.
DR MEROPS; C19.025; -.
DR PaxDb; A0JM59; -.
DR DNASU; 100036606; -.
DR GeneID; 100036606; -.
DR KEGG; xtr:100036606; -.
DR CTD; 10868; -.
DR Xenbase; XB-GENE-966528; usp20.
DR eggNOG; KOG1870; Eukaryota.
DR InParanoid; A0JM59; -.
DR OrthoDB; 147564at2759; -.
DR Reactome; R-XTR-5689880; Ub-specific processing proteases.
DR Proteomes; UP000008143; Chromosome 8.
DR Proteomes; UP000790000; Unplaced.
DR GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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 SMART; SM00290; ZnF_UBP; 1.
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..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
