ID   UBP50_MACFA             Reviewed;         373 AA.
AC   Q4R6D3;
DT   19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   27-MAR-2024, entry version 72.
DE   RecName: Full=Ubiquitin carboxyl-terminal hydrolase 50;
DE            EC=3.4.19.12 {ECO:0000250|UniProtKB:Q70EL3};
DE   AltName: Full=Deubiquitinating enzyme 50;
DE   AltName: Full=Ubiquitin thioesterase 50;
DE   AltName: Full=Ubiquitin-specific-processing protease 50;
GN   Name=USP50; ORFNames=QtsA-18237;
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RG   International consortium for macaque cDNA sequencing and analysis;
RT   "DNA sequences of macaque genes expressed in brain or testis and its
RT   evolutionary implications.";
RL   Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Deubiquitinating enzyme that removes conjugated ubiquitin
CC       from specific proteins to regulate different cellular processes.
CC       Regulates the inflammasome signaling pathway by deubiquitinating 'Lys-
CC       63'-linked polyubiquitination of the PYCARD/ASC adapter protein.
CC       Regulates the ubiquitination and stability of the ACE2 protein. Acts as
CC       a negative regulator of the G2/M checkpoint pathway, by preventing
CC       serine/threonine kinase WEE1 degradation, thereby repressing entry into
CC       mitosis following activation of the G2/M DNA damage checkpoint.
CC       {ECO:0000250|UniProtKB:Q70EL3}.
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:Q70EL3};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q70EL3}.
CC       Cytoplasm, cytoskeleton, microtubule organizing center, centrosome
CC       {ECO:0000250|UniProtKB:Q70EL3}. Nucleus {ECO:0000250|UniProtKB:Q70EL3}.
CC       Note=Accumulates in the nucleus following DNA injury.
CC       {ECO:0000250|UniProtKB:Q70EL3}.
CC   -!- MISCELLANEOUS: The human ortholog is inactive.
CC   -!- SIMILARITY: Belongs to the peptidase C19 family. {ECO:0000305}.
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DR   EMBL; AB169252; BAE01342.1; -; mRNA.
DR   RefSeq; NP_001270928.1; NM_001283999.1.
DR   AlphaFoldDB; Q4R6D3; -.
DR   SMR; Q4R6D3; -.
DR   STRING; 9541.ENSMFAP00000024469; -.
DR   MEROPS; C19.058; -.
DR   VEuPathDB; HostDB:ENSMFAG00000043824; -.
DR   eggNOG; KOG1868; Eukaryota.
DR   OMA; ECTDHYD; -.
DR   OrthoDB; 227085at2759; -.
DR   Proteomes; UP000233100; Chromosome 7.
DR   GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0004843; F:cysteine-type deubiquitinase activity; ISS:UniProtKB.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   GO; GO:1902749; P:regulation of cell cycle G2/M phase transition; ISS:UniProtKB.
DR   CDD; cd02674; Peptidase_C19R; 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; PTHR21646:SF11; INACTIVE UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 50; 1.
DR   PANTHER; PTHR21646; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 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   Cell cycle; Cytoplasm; Cytoskeleton; Hydrolase; Nucleus; Protease;
KW   Reference proteome; Thiol protease; Ubl conjugation pathway.
FT   CHAIN           1..373
FT                   /note="Ubiquitin carboxyl-terminal hydrolase 50"
FT                   /id="PRO_0000249528"
FT   DOMAIN          44..364
FT                   /note="USP"
FT   ACT_SITE        53
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT                   ECO:0000255|PROSITE-ProRule:PRU10093"
FT   ACT_SITE        322
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT                   ECO:0000255|PROSITE-ProRule:PRU10093"
SQ   SEQUENCE   373 AA;  42752 MW;  09C80C792C8E4FE4 CRC64;
     MTSQRSLPAD DFGIYYVLAE CTDYYDTLPV KEADGSQPCS QGVTGLRNLG NTCYMNAILQ
     CLCSISPLVE YFLSGKYITA LQNDCSEVAT AFAYLMTDMW LGDSDCVSPE IFRSALGNLY
     PAFTKKTQQD AQEFLIYVLN ELHEALKKYH YPRRRSHEKG SAQRCCRKWI TTETSVITQL
     FEGQLNYSIV CLKCEKCTYK NEVFTVLSLP IPSEYECSLQ DCLQCFFQQD TLTWNNQIHC
     SFCETKQETA VRAGISKAPK IIIFHLKRFD IQGTTKRKLR TDIHYPLTNL DLTPYICPIF
     RKYPKYNLCA VVNHFGDLDG GHYTAFCKNS FTQAWYSFDD TRVSEIPDTS VQNATAYLLF
     YSCQPFSIPI QKH
//