UBP30_DANRE
ID UBP30_DANRE Reviewed; 491 AA.
AC A2BGT0;
DT 16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase 30;
DE EC=3.4.19.12;
DE AltName: Full=Deubiquitinating enzyme 30;
DE AltName: Full=Ubiquitin thioesterase 30;
DE AltName: Full=Ubiquitin-specific-processing protease 30;
DE Short=Ub-specific protease 30;
GN Name=usp30; ORFNames=si:dkey-72n1.2;
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 that acts as a key inhibitor of
CC mitophagy by counteracting the action of parkin (PRKN).
CC {ECO:0000250|UniProtKB:Q70CQ3}.
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; Evidence={ECO:0000250|UniProtKB:Q70CQ3};
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC {ECO:0000250|UniProtKB:Q70CQ3}.
CC -!- SIMILARITY: Belongs to the peptidase C19 family. {ECO:0000305}.
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DR EMBL; BX511005; CAM16313.1; -; Genomic_DNA.
DR RefSeq; NP_001155956.1; NM_001162484.1.
DR AlphaFoldDB; A2BGT0; -.
DR SMR; A2BGT0; -.
DR BioGRID; 285302; 1.
DR STRING; 7955.ENSDARP00000073858; -.
DR PaxDb; A2BGT0; -.
DR Ensembl; ENSDART00000079402; ENSDARP00000073858; ENSDARG00000056842.
DR GeneID; 559099; -.
DR KEGG; dre:559099; -.
DR CTD; 84749; -.
DR ZFIN; ZDB-GENE-060526-335; usp30.
DR eggNOG; KOG1867; Eukaryota.
DR GeneTree; ENSGT00550000075075; -.
DR InParanoid; A2BGT0; -.
DR PhylomeDB; A2BGT0; -.
DR TreeFam; TF105781; -.
DR Reactome; R-DRE-5689880; Ub-specific processing proteases.
DR Reactome; R-DRE-9664873; Pexophagy.
DR PRO; PR:A2BGT0; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 5.
DR Bgee; ENSDARG00000056842; Expressed in mature ovarian follicle and 19 other tissues.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005741; C:mitochondrial outer membrane; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IDA:ZFIN.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; ISS:UniProtKB.
DR GO; GO:0000422; P:autophagy of mitochondrion; ISS:UniProtKB.
DR GO; GO:0008053; P:mitochondrial fusion; ISS:UniProtKB.
DR GO; GO:0016579; P:protein deubiquitination; ISS:UniProtKB.
DR GO; GO:0035871; P:protein K11-linked deubiquitination; ISS:UniProtKB.
DR GO; GO:0044313; P:protein K6-linked deubiquitination; IDA:ZFIN.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR Pfam; PF00443; UCH; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR PROSITE; PS00972; USP_1; 1.
DR PROSITE; PS00973; USP_2; 1.
DR PROSITE; PS50235; USP_3; 1.
PE 3: Inferred from homology;
KW Hydrolase; Membrane; Mitochondrion; Mitochondrion outer membrane; Protease;
KW Reference proteome; Thiol protease; Transmembrane; Transmembrane helix;
KW Ubl conjugation pathway.
FT CHAIN 1..491
FT /note="Ubiquitin carboxyl-terminal hydrolase 30"
FT /id="PRO_0000377538"
FT TOPO_DOM 1..31
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255"
FT TRANSMEM 32..52
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 53..491
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 64..482
FT /note="USP"
FT REGION 346..365
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 73
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT ACT_SITE 432
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
SQ SEQUENCE 491 AA; 55643 MW; 8F3FF87F855E4CC9 CRC64;
MPWCKQGTTD KLVREFLRTG AAARNKMMKN WGVIGGIAAA MAAGVYVLWG PISDRRKKRK
GMVPGLLNLG NTCFMNSLLQ GLAACPSFIR WLEDFTSQNS ADRERTERET QLSRSLMQLL
KALSSHDPGE DDVLDAGGLL EALRLYRWHI SSFEEQDAHE LFHVLTSSLE EEQERQPRVA
HLFDMQTLEK SVESKEKNIS CRSGGPLHPI PSLWRTRHPF HGRLTSYMAC KRCEQQSPVH
YDSFDSLSLS IPSIQWGRPV TLDQCLQHFI SSETIKEVEC ENCTKQQAGE LVNGEVLESQ
RTTFVKQLKL GKRLTWSKEG SPIKRQEHVQ FTEYLSLDRY KHCSAAQSQQ KTSRTNKAKA
SADPKDKAIA NGVDSEHCNN NKPQSNGTFP SVFLHSPGLS SQLNLTYDYS TSEYLFRLTA
VLVHHGDMHS GHFITYRRCP AAPRGTSPFS SQWLWVSDDS VRKASLQEVL SSSAYLLFYE
RMQRPGLRVE E
