ID   DESI1_XENLA             Reviewed;         169 AA.
AC   Q6GLM5;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 56.
DE   RecName: Full=Desumoylating isopeptidase 1 {ECO:0000250|UniProtKB:Q9CQT7};
DE            Short=DeSI-1 {ECO:0000250|UniProtKB:Q9CQT7};
DE            EC=3.4.-.- {ECO:0000250|UniProtKB:Q9CQT7};
DE   AltName: Full=PPPDE peptidase domain-containing protein 2;
GN   Name=desi1 {ECO:0000250|UniProtKB:Q9CQT7}; Synonyms=fam152b, pppde2;
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=Eye;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Protease which deconjugates SUMO1, SUMO2 and SUMO3 from some
CC       substrate proteins (By similarity). Has isopeptidase but not SUMO-
CC       processing activity (By similarity). Collaborates with ubqln4 in the
CC       export of ubiquitinated proteins from the nucleus to the cytoplasm (By
CC       similarity). {ECO:0000250|UniProtKB:Q6ICB0,
CC       ECO:0000250|UniProtKB:Q9CQT7}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q9CQT7}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9CQT7}. Nucleus
CC       {ECO:0000250|UniProtKB:Q9CQT7}.
CC   -!- SIMILARITY: Belongs to the DeSI family. {ECO:0000305}.
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DR   EMBL; BC074444; AAH74444.1; -; mRNA.
DR   RefSeq; NP_001086298.1; NM_001092829.1.
DR   AlphaFoldDB; Q6GLM5; -.
DR   SMR; Q6GLM5; -.
DR   MEROPS; C97.001; -.
DR   DNASU; 444727; -.
DR   GeneID; 444727; -.
DR   KEGG; xla:444727; -.
DR   CTD; 444727; -.
DR   Xenbase; XB-GENE-998986; desi1.L.
DR   OrthoDB; 1201769at2759; -.
DR   Proteomes; UP000186698; Chromosome 4L.
DR   Bgee; 444727; Expressed in egg cell and 19 other tissues.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
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; Nucleus; Protease; Reference proteome.
FT   CHAIN           1..169
FT                   /note="Desumoylating isopeptidase 1"
FT                   /id="PRO_0000318153"
FT   DOMAIN          8..150
FT                   /note="PPPDE"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01205"
FT   MOTIF           84..92
FT                   /note="Nuclear export signal 1"
FT                   /evidence="ECO:0000250|UniProtKB:Q6ICB0"
FT   MOTIF           140..154
FT                   /note="Nuclear export signal 2"
FT                   /evidence="ECO:0000250|UniProtKB:Q6ICB0"
FT   ACT_SITE        39
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01205"
FT   ACT_SITE        109
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01205"
SQ   SEQUENCE   169 AA;  18737 MW;  4FF28A24864F36EF CRC64;
     METAEGPHLV RLYVYDMSRG LARRLSPVML GKQLEGIWHT SIIVFDEEFF YGREGITSCL
     PGRTMLGEPD SVMELGITEV TEEIFLEYLS SLGESGFSGE SYHLFDHNCN TFSNEVAQFL
     TGKKIPSYIT ELPSEVLSTP LGQALRPLLD SVQIQPAGGN IFNRQSGPS