UBP20_PONAB
ID UBP20_PONAB Reviewed; 913 AA.
AC Q5R5Z6;
DT 15-DEC-2009, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 88.
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 Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex;
RG The German cDNA consortium;
RL Submitted (NOV-2004) 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. Upon dissociation, it is
CC probably transferred to the translocated beta-arrestins, possibly
CC leading to beta-arrestins deubiquitination and disengagement from
CC ADRB2. This suggests the existence of a dynamic exchange between the
CC ADRB2 and beta-arrestins. Deubiquitinates DIO2, thereby regulating
CC thyroid hormone regulation. Deubiquitinates HIF1A, leading to stabilize
CC HIF1A and enhance HIF1A-mediated activity. 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 -!- SUBUNIT: Interacts with VHL, leading to its ubiquitination and
CC subsequent degradation (By similarity). Interacts with CCP110 (By
CC similarity). Interacts with DIO2 (By similarity). Interacts with HIF1A
CC (By similarity). Interacts with ADRB2 (By similarity).
CC {ECO:0000250|UniProtKB:Q9Y2K6}.
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 -!- PTM: Ubiquitinated via a VHL-dependent pathway for proteasomal
CC degradation. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase C19 family. USP20/USP33 subfamily.
CC {ECO:0000305}.
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DR EMBL; CR860704; CAH92820.1; -; mRNA.
DR RefSeq; NP_001126647.1; NM_001133175.1.
DR AlphaFoldDB; Q5R5Z6; -.
DR STRING; 9601.ENSPPYP00000022065; -.
DR MEROPS; C19.025; -.
DR GeneID; 100173645; -.
DR KEGG; pon:100173645; -.
DR CTD; 10868; -.
DR eggNOG; KOG1870; Eukaryota.
DR InParanoid; Q5R5Z6; -.
DR OrthoDB; 147564at2759; -.
DR Proteomes; UP000001595; Unplaced.
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 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;
KW Phosphoprotein; Protease; Reference proteome; Repeat; Thiol protease;
KW Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..913
FT /note="Ubiquitin carboxyl-terminal hydrolase 20"
FT /id="PRO_0000390419"
FT DOMAIN 144..684
FT /note="USP"
FT DOMAIN 686..779
FT /note="DUSP 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00613"
FT DOMAIN 788..891
FT /note="DUSP 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00613"
FT ZN_FING 6..111
FT /note="UBP-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT REGION 256..414
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 261..288
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 316..334
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 374..388
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 153
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT ACT_SITE 642
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"
FT MOD_RES 111
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2K6"
FT MOD_RES 131
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2K6"
FT MOD_RES 133
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2K6"
FT MOD_RES 257
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2K6"
FT MOD_RES 304
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2K6"
FT MOD_RES 367
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8C6M1"
FT MOD_RES 376
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2K6"
FT MOD_RES 407
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2K6"
FT MOD_RES 412
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2K6"
SQ SEQUENCE 913 AA; 101851 MW; 54CA311FD1D3E626 CRC64;
MGDSRDLCPH LDSIGEVTKE DLLLKSMGTC QSCGVTGPNL WACLQVACPY VGCGESFADH
STIHAQAKKH NLTVNLTTFR LWCYACEKEV FLEQRLAAPL LGSSKFSEQD SPPPSHPLKA
VPIAVADEGE SESEDDDLKP RGLTGMKNLG NSCYMNAALQ ALSNCPPLTQ FFLECGGLVR
TDKKPALCKS YQKLVSEVWH KKRPSYVVPT SLSHGIKLVN PMFRGYAQQD TQEFLRCLMD
QLHEELKEPV VATVALTEAR DSDSSDTDEK REGDRSPSED EFLSCDSSSD RGEGDGQGRG
GGSSQAETEL LIPDEASRAI SEKERMKDRK FSWGQQRTNS EQVDEDADVD TTMAALDDQP
AEAQPPSPRS SSPCRTPEPD NDAHLCSSSR PCSPVHHHEG HAKLSSSPPR ASPVRMAPSY
VLKKAQVLSA GSRRRKEQRY RSVISDIFDG SILSLVQCLT CDRVSATVET FQDLSLPIPG
KEDLAKLHSA IYQNVPAKPG TCGDSYAAQG WLAFIVEYIR RFVVSCTPSW FWGPVVTLED
CLAAFFAADE LKGDNMYSCE RCKKLRNGVK YCKVLRLPEI LCIHLKRFRH EVMYSFKINS
HVSFPLEGLD LRPFLAKECT SQITTYDLLS VICHHGTAGS GHYIAYCQNV INGQWYEFDD
QYVTEVHETV VQNAEGYVLF YRKSSEEAVR ERQQVVSLAA MREPSLLRFY VSREWLNKFN
TFAEPGPITN QTFLCSHGGI PPHKYHYIDD LVVILPQNVW EHLYNRFGGG PAVNHLYVCS
ICQVEIEALA KRRRIEIDTF IKLNKAFQAE ESPGIIYCIS MQWFREWEAF VKGKDNEPPG
PIDNSRIAQV KGSGHVQLKQ GADYGQISEE TWTYLNSLYG GGPEIAIRQS VAQPLGPESL
HGEQKIEAEA RAV
