DESI2_PIG
ID DESI2_PIG Reviewed; 194 AA.
AC A3QRX8;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 1.
DT 03-AUG-2022, entry version 58.
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 Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Skeletal muscle;
RA Zhu Z., Mo D., Li X., Zhao S., Li K.;
RL Submitted (FEB-2006) 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; DQ435075; ABD76387.1; -; mRNA.
DR RefSeq; NP_001090888.1; NM_001097419.1.
DR AlphaFoldDB; A3QRX8; -.
DR SMR; A3QRX8; -.
DR STRING; 9823.ENSSSCP00000011594; -.
DR MEROPS; C97.002; -.
DR PaxDb; A3QRX8; -.
DR Ensembl; ENSSSCT00070011638; ENSSSCP00070009590; ENSSSCG00070006105.
DR GeneID; 100037270; -.
DR KEGG; ssc:100037270; -.
DR CTD; 51029; -.
DR eggNOG; KOG0324; Eukaryota.
DR HOGENOM; CLU_069001_5_1_1; -.
DR InParanoid; A3QRX8; -.
DR OMA; GVYWTRP; -.
DR OrthoDB; 1300278at2759; -.
DR TreeFam; TF313188; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Chromosome 10.
DR Genevisible; A3QRX8; SS.
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: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_0000317724"
FT DOMAIN 5..149
FT /note="PPPDE"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01205"
FT REGION 161..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; 21448 MW; 6FBDC1B5FC43E87C CRC64;
MGANQLVVLN VYDMYWMNEY TSSIGIGVFH SGIEVYGREF AYGGHPYPFS GIFEISPGNA
SELGETFKFK EAVVLGSTDF LEDDIEKIVE ELGKEYKGNA YHLMHKNCNH FSSALSEILC
GKEIPRWINR LAYFSSCIPF LQSCLPKEWL TPAALQSSVS QELQDELEEA EDAAASASMG
SASAGSRPGR HTKL
