UBP20_BOVIN
ID UBP20_BOVIN Reviewed; 912 AA.
AC A7Z056;
DT 15-DEC-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 1.
DT 03-AUG-2022, entry version 95.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Uterus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2007) 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; BC153254; AAI53255.1; -; mRNA.
DR RefSeq; NP_001098803.1; NM_001105333.1.
DR AlphaFoldDB; A7Z056; -.
DR STRING; 9913.ENSBTAP00000027070; -.
DR PaxDb; A7Z056; -.
DR Ensembl; ENSBTAT00000027070; ENSBTAP00000027070; ENSBTAG00000020311.
DR GeneID; 505839; -.
DR KEGG; bta:505839; -.
DR CTD; 10868; -.
DR VEuPathDB; HostDB:ENSBTAG00000020311; -.
DR VGNC; VGNC:36715; USP20.
DR eggNOG; KOG1870; Eukaryota.
DR GeneTree; ENSGT00940000158829; -.
DR HOGENOM; CLU_004896_0_0_1; -.
DR InParanoid; A7Z056; -.
DR OMA; IFECEIC; -.
DR OrthoDB; 147564at2759; -.
DR TreeFam; TF352179; -.
DR Proteomes; UP000009136; Chromosome 11.
DR Bgee; ENSBTAG00000020311; Expressed in thyroid gland and 105 other tissues.
DR ExpressionAtlas; A7Z056; baseline and differential.
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:0001664; F:G protein-coupled receptor binding; IEA:Ensembl.
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..912
FT /note="Ubiquitin carboxyl-terminal hydrolase 20"
FT /id="PRO_0000390417"
FT DOMAIN 145..683
FT /note="USP"
FT DOMAIN 685..778
FT /note="DUSP 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00613"
FT DOMAIN 787..890
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 101..120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 258..308
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 322..415
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 263..290
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 322..336
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 381..406
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 641
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 112
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2K6"
FT MOD_RES 132
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2K6"
FT MOD_RES 134
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2K6"
FT MOD_RES 259
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2K6"
FT MOD_RES 306
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2K6"
FT MOD_RES 369
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8C6M1"
FT MOD_RES 378
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2K6"
FT MOD_RES 408
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2K6"
FT MOD_RES 413
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y2K6"
SQ SEQUENCE 912 AA; 101815 MW; A2E4A254D3C95EDF CRC64;
MGDSRDLCPH LDSIGEVTKE DLLLKSKSTC QSCGVSGPNL WACLQVSCSY VGCGESFADH
STLHAQAKKH NLTVNLTTFR VWCYACEKEV FLEPRLAAHP PGPAPKFSEQ DSPPPSHPLK
AVPIAVADEG ESESEDDDLK PRGLTGMKNL GNSCYMNAAL QALSNCPPLT QFFLECGGLV
RTDKKPALCK SYQKLVSEVW HRKRPSYVVP TSLSHGIKLV NPMFRGYAQQ DTQEFLRCLM
DQLHEELKEP VVATAAALTE ARDSDSSDTD EKREGDRSPS EDEFLSCDSS SDRGEGDGQG
RSGGGSQAEA ELLMADEAGR AISEKERMKD RKFSWGQQRT NSEQVDEDAD VDTAMAALEQ
QPPETQPPSP RSTSPCRTPE PDNEAHMRSS RPCSPVHHHE GHAKLASSPH RASPVRMGPA
YVLKKAQVPG SRRRKEQSYR SVISDIFDGS VLSLVQCLTC DRVSTTVETF QDLSLPIPGK
EDLAKLHSAI YQNVPAKPGA CGDSYVAQGW LAFIVEYIRR FVVSCTPSWF WGPVVTLEDC
LAAFFAADEL KGDNMYSCER CKKLRNGVKY CKVLRLPEIL CIHLKRFRHE VMYSFKISSH
VSFPLEGLDL RPFLAKECTS QITTYDLLSV ICHHGTAGSG HYIAYCQNVI NGQWYEFDDQ
YVTEVHETVV QNAEAYVLFY RKSSEEAVRE RQQVVSLAAM REPSLLRFYV SREWLNKFNT
FAEPGPITNH TFLCSHGGIP PNKYHYIDDL VVILPQNVWE HLYSRFGGGP AVNHLYVCSI
CQVEIEALAK RRRVEIDTFI KLNKAFQAEE SPSVIYCISM QWFREWEAFV KGKDNEPPGP
IDNSRIAQVK GSGHIQLKPG ADYGQISEET WVYLNNLYGG GPEIAIRQSV AQLPDPESLH
GEQKIEAETR AL
