ID   DESI2_DANRE             Reviewed;         196 AA.
AC   Q6DC39; Q1L8W2;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   03-AUG-2022, entry version 92.
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;
GN   ORFNames=si:ch211-132e22.3, zgc:100860;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tuebingen;
RX   PubMed=23594743; DOI=10.1038/nature12111;
RA   Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA   Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA   Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA   White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA   Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA   Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA   Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA   Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA   Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA   Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA   Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA   Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA   Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA   Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA   Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA   McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA   Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA   Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA   Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA   Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA   Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA   Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA   Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA   Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA   Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA   Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA   Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA   Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA   de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA   Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT   "The zebrafish reference genome sequence and its relationship to the human
RT   genome.";
RL   Nature 496:498-503(2013).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (JUL-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; BX957248; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CR556710; CAK04091.1; -; Genomic_DNA.
DR   EMBL; BC078248; AAH78248.1; -; mRNA.
DR   RefSeq; NP_001003532.1; NM_001003532.1.
DR   AlphaFoldDB; Q6DC39; -.
DR   SMR; Q6DC39; -.
DR   BioGRID; 92312; 1.
DR   STRING; 7955.ENSDARP00000033545; -.
DR   MEROPS; C97.002; -.
DR   PaxDb; Q6DC39; -.
DR   Ensembl; ENSDART00000034935; ENSDARP00000033545; ENSDARG00000004460.
DR   GeneID; 445138; -.
DR   KEGG; dre:445138; -.
DR   CTD; 51029; -.
DR   ZFIN; ZDB-GENE-040801-39; desi2.
DR   eggNOG; KOG0324; Eukaryota.
DR   GeneTree; ENSGT00730000111005; -.
DR   HOGENOM; CLU_069001_5_1_1; -.
DR   InParanoid; Q6DC39; -.
DR   OMA; GVYWTRP; -.
DR   OrthoDB; 1300278at2759; -.
DR   PhylomeDB; Q6DC39; -.
DR   TreeFam; TF313188; -.
DR   PRO; PR:Q6DC39; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Chromosome 13.
DR   Bgee; ENSDARG00000004460; Expressed in mature ovarian follicle and 39 other tissues.
DR   ExpressionAtlas; Q6DC39; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0101005; F:deubiquitinase activity; IBA:GO_Central.
DR   GO; GO:0060027; P:convergent extension involved in gastrulation; IMP:ZFIN.
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..196
FT                   /note="Deubiquitinase DESI2"
FT                   /id="PRO_0000317727"
FT   DOMAIN          4..148
FT                   /note="PPPDE"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01205"
FT   REGION          159..196
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   196 AA;  21859 MW;  D75BAF8AB15923B5 CRC64;
     MANEPVILNV YDMYWINEFT SSLGIGVFHS GIEIYGREFA YGGHPYPFSG IFEITPGDAT
     ELGETFKFKE AIVLGSTDFT EEDVERIVEE MGKEYKGNAY HLMHKNCNHF SSALSEILCG
     REIPRWVNRL AYFSSCVPFL QSCLPKEWLT PAALQSSVSQ ELQGELEEAE DAAASASTPT
     CAVAPAPRPA RHQPRR