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   27-MAR-2024, entry version 93.
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}.
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; 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; 7955-ENSDARP00000073858; -.
DR   GeneID; 559099; -.
DR   KEGG; dre:559099; -.
DR   AGR; ZFIN:ZDB-GENE-060526-335; -.
DR   CTD; 84749; -.
DR   ZFIN; ZDB-GENE-060526-335; usp30.
DR   eggNOG; KOG1867; Eukaryota.
DR   InParanoid; A2BGT0; -.
DR   OMA; CEREGND; -.
DR   OrthoDB; 227085at2759; -.
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; Chromosome 5.
DR   Bgee; ENSDARG00000056842; Expressed in mature ovarian follicle and 19 other cell types or tissues.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
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; ISS:UniProtKB.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd02662; Peptidase_C19F; 1.
DR   Gene3D; 3.90.70.10; Cysteine proteinases; 1.
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   PANTHER; PTHR24006; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR   PANTHER; PTHR24006:SF650; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 30; 1.
DR   Pfam; PF00443; UCH; 1.
DR   SUPFAM; SSF54001; Cysteine proteinases; 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
//