ID A0A7J8E0Q4_ROUAE Unreviewed; 258 AA.
AC A0A7J8E0Q4;
DT 07-APR-2021, integrated into UniProtKB/TrEMBL.
DT 07-APR-2021, sequence version 1.
DT 18-JUN-2025, entry version 19.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000256|RuleBase:RU361215};
DE EC=3.4.19.12 {ECO:0000256|RuleBase:RU361215};
GN ORFNames=HJG63_020257 {ECO:0000313|EMBL:KAF6428712.1};
OS Rousettus aegyptiacus (Egyptian fruit bat) (Pteropus aegyptiacus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Yinpterochiroptera; Pteropodoidea;
OC Pteropodidae; Rousettinae; Rousettus.
OX NCBI_TaxID=9407 {ECO:0000313|EMBL:KAF6428712.1, ECO:0000313|Proteomes:UP000593571};
RN [1] {ECO:0000313|EMBL:KAF6428712.1, ECO:0000313|Proteomes:UP000593571}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MRouAeg1 {ECO:0000313|EMBL:KAF6428712.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:KAF6428712.1};
RX PubMed=32699395;
RA Jebb D., Huang Z., Pippel M., Hughes G.M., Lavrichenko K., Devanna P.,
RA Winkler S., Jermiin L.S., Skirmuntt E.C., Katzourakis A., Burkitt-Gray L.,
RA Ray D.A., Sullivan K.A.M., Roscito J.G., Kirilenko B.M., Davalos L.M.,
RA Corthals A.P., Power M.L., Jones G., Ransome R.D., Dechmann D.K.N.,
RA Locatelli A.G., Puechmaille S.J., Fedrigo O., Jarvis E.D., Hiller M.,
RA Vernes S.C., Myers E.W., Teeling E.C.;
RT "Six reference-quality genomes reveal evolution of bat adaptations.";
RL Nature 583:578-584(2020).
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:0000256|ARBA:ARBA00000707,
CC ECO:0000256|PROSITE-ProRule:PRU01393, ECO:0000256|RuleBase:RU361215};
CC -!- SUBUNIT: Preferentially binds diubiquitin; the interaction does not
CC hydrolyze diubiquitin but, in vitro, inhibits the hydrolyzing activity
CC on other substrates. {ECO:0000256|ARBA:ARBA00062672}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the peptidase C12 family.
CC {ECO:0000256|ARBA:ARBA00009326, ECO:0000256|PROSITE-ProRule:PRU01393,
CC ECO:0000256|RuleBase:RU361215}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KAF6428712.1}.
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DR EMBL; JACASE010000011; KAF6428712.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A7J8E0Q4; -.
DR Proteomes; UP000593571; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR GO; GO:0016579; P:protein deubiquitination; IEA:TreeGrafter.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd09616; Peptidase_C12_UCH_L1_L3; 1.
DR Gene3D; 3.40.532.10; Peptidase C12, ubiquitin carboxyl-terminal hydrolase; 1.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001578; Peptidase_C12_UCH.
DR InterPro; IPR036959; Peptidase_C12_UCH_sf.
DR InterPro; IPR057254; UCH_AS.
DR PANTHER; PTHR10589; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR PANTHER; PTHR10589:SF24; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE ISOZYME L3; 1.
DR Pfam; PF01088; Peptidase_C12; 1.
DR PRINTS; PR00707; UBCTHYDRLASE.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR PROSITE; PS00140; UCH_1; 1.
DR PROSITE; PS52048; UCH_DOMAIN; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU01393};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW ProRule:PRU01393}; Reference proteome {ECO:0000313|Proteomes:UP000593571};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807, ECO:0000256|PROSITE-
KW ProRule:PRU01393};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU01393}.
FT DOMAIN 1..257
FT /note="UCH catalytic"
FT /evidence="ECO:0000259|PROSITE:PS52048"
FT REGION 114..135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 123..133
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 59
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01393"
FT ACT_SITE 197
FT /note="Proton donor"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01393"
FT SITE 53
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01393"
FT SITE 212
FT /note="Important for enzyme activity"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01393"
SQ SEQUENCE 258 AA; 29109 MW; 3C4029A1F0684B9E CRC64;
MDPELLSMVP RPVCAVLLLF PITEKYEIFR TEEEEKIKSQ GQDVTSSVYF MKQTISNACG
TIGLIHAIAN NKDKMHFESG STLKKFLEES VSMSPEERAR FLENYDAIRV THETSAHEGQ
TESSSPSSSQ PHCSHCRTKA SSLCHHASLP WVKRNHVDPA KATSPSLRLR RWRPFLRLPS
MGLHSVTPSI DEKVDLHFIA LVHVDGHLYE LDGRKPFPIN HGETSDDTLL EDAIEVCKKF
MERDPDELRF NAIALSAA
//
