UBP30_XENTR
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 03-AUG-2022, entry version 80.
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.ENSXETP00000048254; -.
DR PaxDb; A4QNN3; -.
DR Ensembl; ENSXETT00000048254; ENSXETP00000048254; ENSXETG00000022301.
DR GeneID; 733894; -.
DR KEGG; xtr:733894; -.
DR CTD; 84749; -.
DR Xenbase; XB-GENE-981069; usp30.
DR eggNOG; KOG1867; Eukaryota.
DR HOGENOM; CLU_008279_14_0_1; -.
DR InParanoid; A4QNN3; -.
DR OMA; TTWDEEL; -.
DR OrthoDB; 1437269at2759; -.
DR TreeFam; TF105781; -.
DR Reactome; R-XTR-5689880; Ub-specific processing proteases.
DR Proteomes; UP000008143; Chromosome 1.
DR Proteomes; UP000790000; Unplaced.
DR Bgee; ENSXETG00000022301; Expressed in egg cell and 14 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; 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: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 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
