ID   DESI2_PONAB             Reviewed;         194 AA.
AC   Q5R456;
DT   13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 55.
DE   RecName: Full=Deubiquitinase DESI2 {ECO:0000250|UniProtKB:Q9BSY9};
DE            EC=3.4.19.12 {ECO:0000250|UniProtKB:Q9BSY9};
DE   AltName: Full=Desumoylating isopeptidase 2;
DE            Short=DeSI-2;
DE   AltName: Full=PPPDE peptidase domain-containing protein 1;
DE   AltName: Full=Protein FAM152A;
GN   Name=DESI2; Synonyms=FAM152A, PPPDE1;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Has deubiquitinating activity towards 'Lys-48'- and 'Lys-63'-
CC       linked polyubiquitin chains. Deubiquitinates 'Lys-48'-linked
CC       polyubiquitination of RPS7 leading to its stabilization.
CC       {ECO:0000250|UniProtKB:Q9BSY9}.
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:Q9BSY9};
CC   -!- SUBUNIT: Interacts with RPS7. {ECO:0000250|UniProtKB:Q9BSY9}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9D291}.
CC   -!- SIMILARITY: Belongs to the DeSI family. {ECO:0000305}.
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DR   EMBL; CR861402; CAH93460.1; -; mRNA.
DR   RefSeq; NP_001127027.1; NM_001133555.1.
DR   AlphaFoldDB; Q5R456; -.
DR   SMR; Q5R456; -.
DR   STRING; 9601.ENSPPYP00000000052; -.
DR   MEROPS; C97.002; -.
DR   Ensembl; ENSPPYT00000046807; ENSPPYP00000042933; ENSPPYG00000000055.
DR   GeneID; 100174052; -.
DR   KEGG; pon:100174052; -.
DR   CTD; 51029; -.
DR   eggNOG; KOG0324; Eukaryota.
DR   GeneTree; ENSGT00730000111005; -.
DR   HOGENOM; CLU_069001_5_1_1; -.
DR   InParanoid; Q5R456; -.
DR   OrthoDB; 1300278at2759; -.
DR   Proteomes; UP000001595; Chromosome 1.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR   GO; GO:1990380; F:Lys48-specific deubiquitinase activity; ISS:UniProtKB.
DR   GO; GO:0061578; F:Lys63-specific deubiquitinase activity; ISS:UniProtKB.
DR   Gene3D; 3.90.1720.30; -; 1.
DR   InterPro; IPR008580; PPPDE_dom.
DR   InterPro; IPR042266; PPPDE_sf.
DR   PANTHER; PTHR12378; PTHR12378; 1.
DR   Pfam; PF05903; Peptidase_C97; 1.
DR   SMART; SM01179; DUF862; 1.
DR   PROSITE; PS51858; PPPDE; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Hydrolase; Protease; Reference proteome;
KW   Ubl conjugation pathway.
FT   CHAIN           1..194
FT                   /note="Deubiquitinase DESI2"
FT                   /id="PRO_0000221632"
FT   DOMAIN          5..149
FT                   /note="PPPDE"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01205"
FT   REGION          162..194
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        30
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01205"
FT   ACT_SITE        108
FT                   /evidence="ECO:0000250|UniProtKB:Q9BSY9,
FT                   ECO:0000255|PROSITE-ProRule:PRU01205"
SQ   SEQUENCE   194 AA;  21416 MW;  49FDC1A33642EFED CRC64;
     MGANQLVVLN VYDMYWMNEY TSSIGIGVFH SGIEVYGREF AYGGHPYPFS GIFEISPGNA
     SELGETFKFK EAVVLGSTDF LEDDIEKIVE ELGKEYKGNA YHLMHKNCNH FSSALSEILC
     GKEIPRWINR LAYFSSCIPF LQSCLPKEWL TPAALQSSVS QELQDELEEA EDAAASASAA
     STAAGSRPGR HTKL