ID   UBP20_DANRE             Reviewed;         911 AA.
AC   A5PN09; A5PM59;
DT   15-DEC-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 1.
DT   27-MAR-2024, entry version 98.
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; ORFNames=dkey-125i20.3;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tuebingen;
RX   PubMed=23594743; DOI=10.1038/nature12111;
RA   Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA   Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA   Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA   White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA   Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA   Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA   Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA   Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA   Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA   Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA   Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA   Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA   Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA   Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA   Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA   McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA   Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA   Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA   Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA   Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA   Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA   Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA   Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA   Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA   Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA   Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA   Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA   Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA   de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA   Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT   "The zebrafish reference genome sequence and its relationship to the human
RT   genome.";
RL   Nature 496:498-503(2013).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAN88765.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; BX927184; CAN88489.1; -; Genomic_DNA.
DR   EMBL; BX005029; CAN88088.1; -; Genomic_DNA.
DR   EMBL; CR382323; CAN88088.1; JOINED; Genomic_DNA.
DR   EMBL; CR382323; CAN88765.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; BX005029; CAN88765.1; JOINED; Genomic_DNA.
DR   RefSeq; NP_957281.2; NM_200987.2.
DR   RefSeq; XP_009299733.1; XM_009301458.2.
DR   AlphaFoldDB; A5PN09; -.
DR   STRING; 7955.ENSDARP00000014964; -.
DR   MEROPS; C19.025; -.
DR   PaxDb; 7955-ENSDARP00000014964; -.
DR   GeneID; 393962; -.
DR   KEGG; dre:393962; -.
DR   AGR; ZFIN:ZDB-GENE-040426-1219; -.
DR   CTD; 10868; -.
DR   ZFIN; ZDB-GENE-040426-1219; usp20.
DR   eggNOG; KOG1870; Eukaryota.
DR   InParanoid; A5PN09; -.
DR   OMA; IDQDDEC; -.
DR   OrthoDB; 227085at2759; -.
DR   PhylomeDB; A5PN09; -.
DR   Reactome; R-DRE-5689880; Ub-specific processing proteases.
DR   PRO; PR:A5PN09; -.
DR   Proteomes; UP000000437; Alternate scaffold 5.
DR   Proteomes; UP000000437; Chromosome 5.
DR   Bgee; ENSDARG00000027501; Expressed in mature ovarian follicle and 24 other cell types or tissues.
DR   ExpressionAtlas; A5PN09; baseline and differential.
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:0021551; P:central nervous system morphogenesis; IMP:ZFIN.
DR   GO; GO:1904888; P:cranial skeletal system development; IMP:ZFIN.
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:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   GO; GO:0008277; P:regulation of G protein-coupled receptor signaling pathway; ISS:UniProtKB.
DR   CDD; cd02674; Peptidase_C19R; 1.
DR   Gene3D; 3.90.70.10; Cysteine proteinases; 2.
DR   Gene3D; 3.30.2230.10; DUSP-like; 2.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 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   PANTHER; PTHR21646; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR   PANTHER; PTHR21646:SF13; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 20; 1.
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; SSF54001; Cysteine proteinases; 1.
DR   SUPFAM; SSF143791; DUSP-like; 2.
DR   SUPFAM; SSF57850; RING/U-box; 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   3: Inferred from homology;
KW   Cytoplasm; Cytoskeleton; Endocytosis; Hydrolase; Metal-binding; Protease;
KW   Reference proteome; Repeat; Thiol protease; Ubl conjugation pathway; Zinc;
KW   Zinc-finger.
FT   CHAIN           1..911
FT                   /note="Ubiquitin carboxyl-terminal hydrolase 20"
FT                   /id="PRO_0000390420"
FT   DOMAIN          148..685
FT                   /note="USP"
FT   DOMAIN          687..780
FT                   /note="DUSP 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00613"
FT   DOMAIN          789..891
FT                   /note="DUSP 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00613"
FT   ZN_FING         6..108
FT                   /note="UBP-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT   REGION          279..309
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          327..420
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        327..357
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        382..420
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        157
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT                   ECO:0000255|PROSITE-ProRule:PRU10093"
FT   ACT_SITE        643
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   CONFLICT        115
FT                   /note="S -> L (in Ref. 1; CAN88765/CAN88088)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        429
FT                   /note="M -> I (in Ref. 1; CAN88765/CAN88088)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   911 AA;  101984 MW;  EB98B978FAE7FA4D CRC64;
     MTDSGDLCPH LDSIGEVTKE ELIQKSKGTC QSCGVGGPNL WACLQCDCPY VGCGESYSDH
     STIHAQAKKH NLTVNLTTFR VWCYVCEREV FLEPKPVTPV SSAHRCKPHD QDPVSQTTCY
     PLKAVPIAVA DEEGSESEED ELKPRGLTGM KNIGNSCYMN AALQALSNCP PLTQFFQDCS
     GLVRTDKKPA LCKSYQKLIS ELWHKKRPSY VVPTTLFHGI KLVNPMFRGY AQQDTQEFLR
     CLMDQLHEEL KEPLFDCSGG ISEVEPDLSL DSCNLVDGDR SPSEDEFLSC DSGSGSERGD
     GERAGGEAEL LIQDECVAVR GTGGISEKER LKERRGEERT REMDEDADVD TAAQDGQAER
     ETETATPATA VPAPGNTEPD NEASMHCPSS RPCSPAHSVQ ELHSRLSSNP PRSSPLRTGP
     TYTFKKAQML LSTKKKKQSR FRSVISDIFD GSILSLVQCL TCDRVSTTVE TFQDLSLPIP
     GKEDLAKLHS SIHQSAPVKA GVCTDGYAAQ GWISYIMDSI RRFVVSCIPS WFWGPMVTLE
     DCLAAFFAAD ELKGDNMYSC ERCKKLRNGV KYCKVLRLPE ILCIHLKRFR HEVMYSFKIN
     SHVSFPLEGL DLKPFLAKES PSQITTYDLL SVICHHGTAG SGHYIAYCQN VINGQWYEFD
     DQYVTEVHET VVQNAEAYVL FYRKSSEESV RERQRVVALA NLKEPSLLQF YISREWLNKF
     NTFTEPGPIT NHTFLCQHGG IPPTKYHYVD DLVVILPQNV WEYLYNRFGG GPAVNHLYVC
     AICQVEIETL AKRRKLEIDT FIKLNKEFQA EEAPTVILCI SMQWFREWEN FVKGKDNEPP
     GPIDNSKIAV MKGGHIQLKQ GADYGQISEE TWQYLLSIYG GGPEIAVRQT ISPPDTDTHG
     ERKIEAETRA L
//