ID   DESI2_XENLA             Reviewed;         192 AA.
AC   Q5PQ09;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, 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   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Has deubiquitinating activity towards 'Lys-48'- and 'Lys-63'-
CC       linked polyubiquitin chains. {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   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9D291}.
CC   -!- SIMILARITY: Belongs to the DeSI family. {ECO:0000305}.
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DR   EMBL; BC087412; AAH87412.1; -; mRNA.
DR   RefSeq; NP_001088756.1; NM_001095287.1.
DR   AlphaFoldDB; Q5PQ09; -.
DR   SMR; Q5PQ09; -.
DR   MEROPS; C97.002; -.
DR   MaxQB; Q5PQ09; -.
DR   DNASU; 496020; -.
DR   GeneID; 496020; -.
DR   KEGG; xla:496020; -.
DR   CTD; 496020; -.
DR   Xenbase; XB-GENE-1014049; desi2.L.
DR   OMA; QRIWAQI; -.
DR   OrthoDB; 1300278at2759; -.
DR   Proteomes; UP000186698; Chromosome 5L.
DR   Bgee; 496020; Expressed in testis and 19 other tissues.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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..192
FT                   /note="Deubiquitinase DESI2"
FT                   /id="PRO_0000317728"
FT   DOMAIN          4..148
FT                   /note="PPPDE"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01205"
FT   REGION          160..192
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        29
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01205"
FT   ACT_SITE        107
FT                   /evidence="ECO:0000250|UniProtKB:Q9BSY9,
FT                   ECO:0000255|PROSITE-ProRule:PRU01205"
SQ   SEQUENCE   192 AA;  21415 MW;  73407DBA4D017A78 CRC64;
     MANQPIILNV YDMYWINEYT SSLGIGVFHS GIQVYGREFA YGGHPYPFSG VFEISPGDST
     ELGDTFKFKE AIALGSTDFT ENDIEKIIEE LGKEYKGNAY HLMHKNCNHF SSALSEILCG
     KEIPRWVNRL AYFSTCVPFL QSCLPKEWLT PAALQSSISQ ELQDELEEAE DAAASASTST
     TAMPRPGRHT KL