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 25-OCT-2017, entry version 73. 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; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; 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 CC coupled receptor (GPCR) signaling by mediating the CC deubiquitination beta-2 adrenergic receptor (ADRB2). Plays a CC central role in ADRB2 recycling and resensitization after CC prolonged agonist stimulation by constitutively binding ADRB2, CC mediating deubiquitination of ADRB2 and inhibiting lysosomal CC trafficking of ADRB2. Upon dissociation, it is probably CC transferred to the translocated beta-arrestins, possibly leading CC to beta-arrestins deubiquitination and disengagement from ADRB2. CC 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 CC stabilize HIF1A and enhance HIF1A-mediated activity. Mediates CC deubiquitination of both 'Lys-48'- and 'Lys-63'-linked CC polyubiquitin chains (By similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Thiol-dependent hydrolysis of ester, CC thioester, amide, peptide and isopeptide bonds formed by the C- CC terminal Gly of ubiquitin (a 76-residue protein attached to CC proteins as an intracellular targeting signal). CC -!- SUBUNIT: Interacts with VHL, leading to its ubiquitination and CC subsequent degradation. Interacts with CCP110, DIO2 and HIF1A (By CC similarity). {ECO:0000250}. 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 CC does not bind ubiquitin, probably because the conserved Arg in CC position 55 is replaced by a Glu residue (By similarity). CC {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 CC subfamily. {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; CR860704; CAH92820.1; -; mRNA. DR RefSeq; NP_001126647.1; NM_001133175.1. DR ProteinModelPortal; Q5R5Z6; -. DR STRING; 9601.ENSPPYP00000022065; -. DR MEROPS; C19.025; -. DR GeneID; 100173645; -. DR KEGG; pon:100173645; -. DR CTD; 10868; -. DR eggNOG; KOG1870; Eukaryota. DR eggNOG; COG5560; LUCA. DR HOGENOM; HOG000286031; -. DR HOVERGEN; HBG054196; -. DR InParanoid; Q5R5Z6; -. DR KO; K11848; -. 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:0004197; F:cysteine-type endopeptidase activity; ISS:UniProtKB. DR GO; GO:0004843; F:thiol-dependent ubiquitin-specific protease activity; IEA:InterPro. DR GO; GO:0036459; F:thiol-dependent ubiquitinyl hydrolase 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 protein 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; 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; 1. DR Pfam; PF02148; zf-UBP; 1. DR SMART; SM00695; DUSP; 2. DR SMART; SM00290; ZnF_UBP; 1. DR SUPFAM; SSF143791; SSF143791; 2. 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 Complete proteome; Cytoplasm; Cytoskeleton; Endocytosis; Hydrolase; KW Metal-binding; Phosphoprotein; Protease; Reference proteome; Repeat; KW Thiol protease; Ubl conjugation; Ubl conjugation pathway; Zinc; KW Zinc-finger. FT CHAIN 1 913 Ubiquitin carboxyl-terminal hydrolase 20. FT /FTId=PRO_0000390419. FT DOMAIN 144 684 USP. FT DOMAIN 686 779 DUSP 1. {ECO:0000255|PROSITE- FT ProRule:PRU00613}. FT DOMAIN 788 891 DUSP 2. {ECO:0000255|PROSITE- FT ProRule:PRU00613}. FT ZN_FING 28 92 UBP-type. {ECO:0000255|PROSITE- FT ProRule:PRU00502}. FT ACT_SITE 153 153 Nucleophile. {ECO:0000255|PROSITE- FT ProRule:PRU10092, ECO:0000255|PROSITE- FT ProRule:PRU10093}. FT ACT_SITE 642 642 Proton acceptor. {ECO:0000255|PROSITE- FT ProRule:PRU10092, ECO:0000255|PROSITE- FT ProRule:PRU10093}. FT MOD_RES 111 111 Phosphoserine. FT {ECO:0000250|UniProtKB:Q9Y2K6}. FT MOD_RES 131 131 Phosphoserine. FT {ECO:0000250|UniProtKB:Q9Y2K6}. FT MOD_RES 133 133 Phosphoserine. FT {ECO:0000250|UniProtKB:Q9Y2K6}. FT MOD_RES 257 257 Phosphothreonine. FT {ECO:0000250|UniProtKB:Q9Y2K6}. FT MOD_RES 304 304 Phosphoserine. FT {ECO:0000250|UniProtKB:Q9Y2K6}. FT MOD_RES 367 367 Phosphoserine. FT {ECO:0000250|UniProtKB:Q8C6M1}. FT MOD_RES 376 376 Phosphothreonine. FT {ECO:0000250|UniProtKB:Q9Y2K6}. FT MOD_RES 407 407 Phosphoserine. FT {ECO:0000250|UniProtKB:Q9Y2K6}. FT MOD_RES 412 412 Phosphoserine. FT {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 //