ID   UBP30_XENTR             Reviewed;         519 AA.
AC   A4QNN3; Q28CN8;
DT   16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT   15-MAY-2007, sequence version 1.
DT   27-MAR-2024, entry version 87.
DE   RecName: Full=Ubiquitin carboxyl-terminal hydrolase 30;
DE            EC=3.4.19.12 {ECO:0000250|UniProtKB:Q70CQ3};
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=TEgg099b09.1;
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Egg;
RG   Sanger Xenopus tropicalis EST/cDNA project;
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Tadpole;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
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; CR926280; CAJ81380.1; -; mRNA.
DR   EMBL; BC135925; AAI35926.1; -; mRNA.
DR   RefSeq; NP_001039085.1; NM_001045620.1.
DR   AlphaFoldDB; A4QNN3; -.
DR   SMR; A4QNN3; -.
DR   STRING; 8364.ENSXETP00000038088; -.
DR   PaxDb; 8364-ENSXETP00000048254; -.
DR   GeneID; 733894; -.
DR   KEGG; xtr:733894; -.
DR   AGR; Xenbase:XB-GENE-981069; -.
DR   CTD; 84749; -.
DR   Xenbase; XB-GENE-981069; usp30.
DR   eggNOG; KOG1867; Eukaryota.
DR   HOGENOM; CLU_008279_14_0_1; -.
DR   InParanoid; A4QNN3; -.
DR   OrthoDB; 227085at2759; -.
DR   TreeFam; TF105781; -.
DR   Proteomes; UP000008143; Chromosome 1.
DR   Bgee; ENSXETG00000022301; Expressed in egg cell and 14 other cell types or tissues.
DR   ExpressionAtlas; A4QNN3; differential.
DR   GO; GO:0005741; C:mitochondrial outer membrane; ISS:UniProtKB.
DR   GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
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: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   2: Evidence at transcript level;
KW   Hydrolase; Membrane; Mitochondrion; Mitochondrion outer membrane; Protease;
KW   Reference proteome; Thiol protease; Transmembrane; Transmembrane helix;
KW   Ubl conjugation pathway.
FT   CHAIN           1..519
FT                   /note="Ubiquitin carboxyl-terminal hydrolase 30"
FT                   /id="PRO_0000377539"
FT   TOPO_DOM        1..52
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        53..73
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        74..519
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          85..504
FT                   /note="USP"
FT   REGION          379..405
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        379..400
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        94
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT                   ECO:0000255|PROSITE-ProRule:PRU10093"
FT   ACT_SITE        455
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT                   ECO:0000255|PROSITE-ProRule:PRU10093"
FT   CONFLICT        61
FT                   /note="A -> V (in Ref. 1; CAJ81380)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   519 AA;  58683 MW;  31FC4F6B8309D7E7 CRC64;
     MSWAPVSTWS RRTPLAACCS APELPPAGAW KACAAGSLRI GPQGRCKMMK NWGMIGGIAA
     ALAAGIYVLW GPISDRKKYR KGLVPGLLNL GNTCFMNSLL QGLASCPSFI RWLADFTSKY
     RQENNTTEHQ HLSVTLLHLL KALCNQEGTE DEVLDASPLL EVLRAHRWQI SSFEEQDAHE
     LFHVLTSSLE DERDRRPHVT HLFDLDSLEF PLEPQRQIHC RTQVPIYPIP SQWKSQHPFH
     GRLTSNMVCK HCQHQSPMRY DTFDSLSLSI PVATWGHPIT LDQCLQHFIS TESVKDVVCE
     NCTKIHAAQI PNSQSVENRK TTFVKQLKLG KLPQCLCIHL QRLSWSNQGS PLKRNEHVQF
     SEFLAMDRFK YRISGCSTSK QPANHLSAAE QETTDGKEGG AQNPTMPFLN GACSTSYISP
     PFTSPLPTNP EWTSSSYLFR LMAVVVHHGD MHSGHFVTYR RSPAAKNQKL TSQQWLWISD
     DTVRRTNFQE VLSSSAYLLF YERIQSNLHH PEDQRAAEK
//