ID   DESI2_RAT               Reviewed;         194 AA.
AC   Q5XIT6;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 90.
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   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Testis;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BC083584; AAH83584.1; -; mRNA.
DR   RefSeq; NP_001013895.1; NM_001013873.1.
DR   AlphaFoldDB; Q5XIT6; -.
DR   SMR; Q5XIT6; -.
DR   STRING; 10116.ENSRNOP00000005967; -.
DR   MEROPS; C97.002; -.
DR   PaxDb; Q5XIT6; -.
DR   Ensembl; ENSRNOT00000005967; ENSRNOP00000005967; ENSRNOG00000004524.
DR   GeneID; 289277; -.
DR   KEGG; rno:289277; -.
DR   UCSC; RGD:1359392; rat.
DR   CTD; 51029; -.
DR   RGD; 1359392; Desi2.
DR   eggNOG; KOG0324; Eukaryota.
DR   GeneTree; ENSGT00730000111005; -.
DR   HOGENOM; CLU_069001_5_1_1; -.
DR   InParanoid; Q5XIT6; -.
DR   OMA; GVYWTRP; -.
DR   OrthoDB; 1300278at2759; -.
DR   PhylomeDB; Q5XIT6; -.
DR   PRO; PR:Q5XIT6; -.
DR   Proteomes; UP000002494; Chromosome 13.
DR   Bgee; ENSRNOG00000004524; Expressed in testis and 19 other tissues.
DR   ExpressionAtlas; Q5XIT6; baseline and differential.
DR   Genevisible; Q5XIT6; RN.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0004843; F:cysteine-type deubiquitinase activity; ISO:RGD.
DR   GO; GO:0101005; F:deubiquitinase activity; IBA:GO_Central.
DR   GO; GO:1990380; F:Lys48-specific deubiquitinase activity; ISS:UniProtKB.
DR   GO; GO:0061578; F:Lys63-specific deubiquitinase activity; ISS:UniProtKB.
DR   GO; GO:0016579; P:protein deubiquitination; IBA:GO_Central.
DR   GO; GO:0070646; P:protein modification by small protein removal; IBA:GO_Central.
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_0000317725"
FT   DOMAIN          5..149
FT                   /note="PPPDE"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01205"
FT   REGION          166..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;  21418 MW;  3AE32005FC4D533A CRC64;
     MGANQLVVLN VYDMYWMNEY TSSIGIGVFH SGIEVYGREF AYGGHPYPFS GIFEISPGNA
     AELGETFKFK EAVVLGSTDF LEDDIEKIVE ELGKEYKGNA YHLMHKNCNH FSSALSEILC
     GKEIPRWINR LAYFSSCIPF LQSCLPKEWL TPAALQSSVS QELQDELEEA EDAAASTAMA
     SAAAGGRTGR HTKL