DESI1_MOUSE
ID DESI1_MOUSE Reviewed; 168 AA.
AC Q9CQT7; Q3V2M9;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Desumoylating isopeptidase 1 {ECO:0000303|PubMed:22370726};
DE Short=DeSI-1 {ECO:0000303|PubMed:22370726};
DE EC=3.4.-.- {ECO:0000269|PubMed:22370726, ECO:0000269|PubMed:22498933};
DE AltName: Full=PPPDE peptidase domain-containing protein 2;
GN Name=Desi1 {ECO:0000303|PubMed:22370726, ECO:0000312|MGI:MGI:106313};
GN Synonyms=D15Wsu75e {ECO:0000312|MGI:MGI:106313}, Fam152b, Pppde2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and DBA/2J; TISSUE=Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and FVB/N-3; TISSUE=Brain, and Mammary tumor;
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).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Liver, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [4]
RP FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=22370726; DOI=10.1038/embor.2012.3;
RA Shin E.J., Shin H.M., Nam E., Kim W.S., Kim J.H., Oh B.H., Yun Y.;
RT "DeSUMOylating isopeptidase: a second class of SUMO protease.";
RL EMBO Rep. 13:339-346(2012).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS), FUNCTION, SUBUNIT, AND ACTIVE SITE.
RX PubMed=22498933; DOI=10.1002/prot.24093;
RA Suh H.Y., Kim J.H., Woo J.S., Ku B., Shin E.J., Yun Y., Oh B.H.;
RT "Crystal structure of DeSI-1, a novel deSUMOylase belonging to a putative
RT isopeptidase superfamily.";
RL Proteins 80:2099-2104(2012).
CC -!- FUNCTION: Protease which deconjugates SUMO1, SUMO2 and SUMO3 from some
CC substrate proteins (PubMed:22370726, PubMed:22498933). Has isopeptidase
CC but not SUMO-processing activity (PubMed:22370726, PubMed:22498933).
CC Desumoylates ZBTB46 (PubMed:22370726). 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:0000269|PubMed:22370726, ECO:0000269|PubMed:22498933}.
CC -!- SUBUNIT: Homodimer (PubMed:22370726, PubMed:22498933). Interacts with
CC UBQLN4; leading to the export of UBQLN4 from the nucleus (By
CC similarity). {ECO:0000250|UniProtKB:Q6ICB0,
CC ECO:0000269|PubMed:22370726, ECO:0000269|PubMed:22498933}.
CC -!- INTERACTION:
CC Q9CQT7; Q9CQT7: Desi1; NbExp=3; IntAct=EBI-7768710, EBI-7768710;
CC Q9CQT7; Q8BID6: Zbtb46; NbExp=2; IntAct=EBI-7768710, EBI-7768990;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22370726}. Nucleus
CC {ECO:0000269|PubMed:22370726}. Note=Shuttles between the nucleus and
CC the cytoplasm; exported from the nucleus in a XPO1/CRM1-dependent
CC manner via its nuclear export signal motifs.
CC {ECO:0000250|UniProtKB:Q6ICB0}.
CC -!- SIMILARITY: Belongs to the DeSI family. {ECO:0000305}.
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DR EMBL; AK005706; BAB24198.1; -; mRNA.
DR EMBL; AK005963; BAB24342.1; -; mRNA.
DR EMBL; AK131703; BAE20768.1; -; mRNA.
DR EMBL; AK146155; BAE26939.1; -; mRNA.
DR EMBL; BC056972; AAH56972.1; -; mRNA.
DR EMBL; BC071205; AAH71205.1; -; mRNA.
DR EMBL; BC131979; AAI31980.1; -; mRNA.
DR EMBL; BC132642; AAI32643.1; -; mRNA.
DR CCDS; CCDS27681.1; -.
DR RefSeq; NP_598856.1; NM_134095.2.
DR PDB; 2WP7; X-ray; 1.90 A; A=1-168.
DR PDBsum; 2WP7; -.
DR AlphaFoldDB; Q9CQT7; -.
DR SMR; Q9CQT7; -.
DR IntAct; Q9CQT7; 29.
DR MINT; Q9CQT7; -.
DR STRING; 10090.ENSMUSP00000121504; -.
DR MEROPS; C97.001; -.
DR iPTMnet; Q9CQT7; -.
DR PhosphoSitePlus; Q9CQT7; -.
DR EPD; Q9CQT7; -.
DR MaxQB; Q9CQT7; -.
DR PaxDb; Q9CQT7; -.
DR PRIDE; Q9CQT7; -.
DR ProteomicsDB; 279628; -.
DR Antibodypedia; 55491; 33 antibodies from 13 providers.
DR DNASU; 28075; -.
DR Ensembl; ENSMUST00000152227; ENSMUSP00000121504; ENSMUSG00000022472.
DR GeneID; 28075; -.
DR KEGG; mmu:28075; -.
DR UCSC; uc007wxw.1; mouse.
DR CTD; 27351; -.
DR MGI; MGI:106313; Desi1.
DR VEuPathDB; HostDB:ENSMUSG00000022472; -.
DR eggNOG; KOG0324; Eukaryota.
DR GeneTree; ENSGT00730000111100; -.
DR HOGENOM; CLU_101028_0_0_1; -.
DR InParanoid; Q9CQT7; -.
DR OMA; LFDNNCN; -.
DR PhylomeDB; Q9CQT7; -.
DR TreeFam; TF328492; -.
DR BioGRID-ORCS; 28075; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Desi1; mouse.
DR EvolutionaryTrace; Q9CQT7; -.
DR PRO; PR:Q9CQT7; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q9CQT7; protein.
DR Bgee; ENSMUSG00000022472; Expressed in seminiferous tubule of testis and 252 other tissues.
DR ExpressionAtlas; Q9CQT7; baseline and differential.
DR Genevisible; Q9CQT7; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0016929; F:deSUMOylase activity; IDA:FlyBase.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0061676; F:importin-alpha family protein binding; ISO:MGI.
DR GO; GO:0016926; P:protein desumoylation; IDA:FlyBase.
DR GO; GO:0006611; P:protein export from nucleus; ISO:MGI.
DR GO; GO:0070646; P:protein modification by small protein removal; IBA:GO_Central.
DR GO; GO:0032434; P:regulation of proteasomal ubiquitin-dependent protein catabolic process; ISO:MGI.
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 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Hydrolase; Nucleus; Protease; Reference proteome.
FT CHAIN 1..168
FT /note="Desumoylating isopeptidase 1"
FT /id="PRO_0000318151"
FT DOMAIN 7..149
FT /note="PPPDE"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01205"
FT MOTIF 83..91
FT /note="Nuclear export signal 1"
FT /evidence="ECO:0000250|UniProtKB:Q6ICB0"
FT MOTIF 139..153
FT /note="Nuclear export signal 2"
FT /evidence="ECO:0000250|UniProtKB:Q6ICB0"
FT ACT_SITE 38
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01205,
FT ECO:0000269|PubMed:22498933"
FT ACT_SITE 108
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01205,
FT ECO:0000269|PubMed:22498933"
FT CONFLICT 54
FT /note="G -> S (in Ref. 1; BAE20768)"
FT /evidence="ECO:0000305"
FT STRAND 7..15
FT /evidence="ECO:0007829|PDB:2WP7"
FT TURN 16..19
FT /evidence="ECO:0007829|PDB:2WP7"
FT HELIX 20..28
FT /evidence="ECO:0007829|PDB:2WP7"
FT STRAND 37..43
FT /evidence="ECO:0007829|PDB:2WP7"
FT STRAND 46..51
FT /evidence="ECO:0007829|PDB:2WP7"
FT STRAND 54..59
FT /evidence="ECO:0007829|PDB:2WP7"
FT STRAND 69..77
FT /evidence="ECO:0007829|PDB:2WP7"
FT HELIX 81..92
FT /evidence="ECO:0007829|PDB:2WP7"
FT TURN 93..95
FT /evidence="ECO:0007829|PDB:2WP7"
FT HELIX 98..100
FT /evidence="ECO:0007829|PDB:2WP7"
FT TURN 103..105
FT /evidence="ECO:0007829|PDB:2WP7"
FT HELIX 108..120
FT /evidence="ECO:0007829|PDB:2WP7"
FT HELIX 126..129
FT /evidence="ECO:0007829|PDB:2WP7"
FT HELIX 131..136
FT /evidence="ECO:0007829|PDB:2WP7"
FT HELIX 139..148
FT /evidence="ECO:0007829|PDB:2WP7"
SQ SEQUENCE 168 AA; 18385 MW; 5C81CE4CE5752421 CRC64;
MEPPNLYPVK LYVYDLSKGL ARRLSPIMLG KQLEGIWHTS IVVHKDEFFF GSSGISSCTP
GGTLLGPPDS VVDVGNTEVT EEIFLEYLSS LGESLFRGEA YNLFEHNCNT FSNEVAQFLT
GRKIPSYITD LPSEVLSTPF GQALRPFLDS IQIQPPGGNS VGRPNGQS
