SENP3_MOUSE
ID SENP3_MOUSE Reviewed; 568 AA.
AC Q9EP97; Q5F2A5; Q8BRD5; Q8C2H5;
DT 28-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Sentrin-specific protease 3;
DE EC=3.4.22.-;
DE AltName: Full=SUMO-1-specific protease 3;
DE AltName: Full=Sentrin/SUMO-specific protease SENP3;
DE AltName: Full=Smt3-specific isopeptidase 1 {ECO:0000303|PubMed:11029585};
DE Short=Smt3ip1 {ECO:0000303|PubMed:11029585};
GN Name=Senp3; Synonyms=Smt3ip, Smt3ip1 {ECO:0000303|PubMed:11029585};
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 [MRNA], SUBCELLULAR LOCATION, AND FUNCTION.
RC TISSUE=T-cell lymphoma;
RX PubMed=11029585; DOI=10.1046/j.1432-1327.2000.01729.x;
RA Nishida T., Tanaka H., Yasuda H.;
RT "A novel mammalian Smt3-specific isopeptidase 1 (SMT3IP1) localized in the
RT nucleolus at interphase.";
RL Eur. J. Biochem. 267:6423-6427(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J;
RX PubMed=10806345; DOI=10.1016/s0378-1119(00)00139-6;
RA Yeh E.T.H., Gong L., Kamitani T.;
RT "Ubiquitin-like proteins: new wines in new bottles.";
RL Gene 248:1-14(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=NOD; TISSUE=Embryo, and Thymus;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-175, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-71; SER-73; SER-163; THR-170;
RP SER-175; SER-182; SER-206 AND SER-226, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Liver, Lung, Pancreas, Spleen,
RC 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 [8]
RP FUNCTION, IDENTIFICATION IN THE 5FMC COMPLEX, INTERACTION OF THE 5FMC
RP COMPLEX WITH CHTOP AND ZNF148, INTERACTION WITH NOL9, AND SUBCELLULAR
RP LOCATION.
RX PubMed=22872859; DOI=10.1074/mcp.m112.017194;
RA Fanis P., Gillemans N., Aghajanirefah A., Pourfarzad F., Demmers J.,
RA Esteghamat F., Vadlamudi R.K., Grosveld F., Philipsen S., van Dijk T.B.;
RT "Five friends of methylated chromatin target of protein-arginine-
RT methyltransferase[prmt]-1 (chtop), a complex linking arginine methylation
RT to desumoylation.";
RL Mol. Cell. Proteomics 11:1263-1273(2012).
CC -!- FUNCTION: Protease that releases SUMO2 and SUMO3 monomers from
CC sumoylated substrates, but has only weak activity against SUMO1
CC conjugates (PubMed:11029585). Deconjugates SUMO2 from MEF2D, which
CC increases its transcriptional activation capability (By similarity).
CC Deconjugates SUMO2 and SUMO3 from CDCA8 (By similarity). Redox sensor
CC that, when redistributed into nucleoplasm, can act as an effector to
CC enhance HIF1A transcriptional activity by desumoylating EP300 (By
CC similarity). Required for rRNA processing through deconjugation of
CC SUMO2 and SUMO3 from nucleophosmin, NPM1 (By similarity). Plays a role
CC in the regulation of sumoylation status of ZNF148 (By similarity).
CC Functions as a component of the Five Friends of Methylated CHTOP (5FMC)
CC complex; the 5FMC complex is recruited to ZNF148 by methylated CHTOP,
CC leading to desumoylation of ZNF148 and subsequent transactivation of
CC ZNF148 target genes (PubMed:22872859). Deconjugates SUMO2 from KAT5 (By
CC similarity). {ECO:0000250|UniProtKB:Q9H4L4,
CC ECO:0000269|PubMed:11029585, ECO:0000269|PubMed:22872859}.
CC -!- ACTIVITY REGULATION: On oxidative stress, SENP3 degradation is blocked
CC by inhibition of its ubiquitination, which stabilizes it as it
CC accumulates in the nucleoplasm. {ECO:0000250|UniProtKB:Q9H4L4}.
CC -!- SUBUNIT: Component of some MLL1/MLL complex, at least composed of the
CC core components KMT2A/MLL1, ASH2L, HCFC1/HCF1, WDR5 and RBBP5, as well
CC as the facultative components BAP18, CHD8, E2F6, HSP70, INO80C, KANSL1,
CC LAS1L, MAX, MCRS1, MGA, MYST1/MOF, PELP1, PHF20, PRP31, RING2,
CC RUVB1/TIP49A, RUVB2/TIP49B, SENP3, TAF1, TAF4, TAF6, TAF7, TAF9 and
CC TEX10 (By similarity). Interacts with EP300, NPM1 and CDCA8 (By
CC similarity). Component of the 5FMC complex, at least composed of PELP1,
CC LAS1L, TEX10, WDR18 and SENP3; the complex interacts with methylated
CC CHTOP and ZNF148 (PubMed:22872859). Interacts with NOL9
CC (PubMed:22872859). Interacts with CCAR2 (By similarity).
CC {ECO:0000250|UniProtKB:Q9H4L4, ECO:0000269|PubMed:22872859}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:11029585}.
CC Nucleus, nucleoplasm {ECO:0000269|PubMed:22872859}. Cytoplasm
CC {ECO:0000269|PubMed:22872859}. Note=Redistributes between the nucleolus
CC and the nucleoplasm in response to mild oxidative stress (By
CC similarity). Mainly found in the nucleoplasm, with low levels detected
CC in the cytoplasmic and chromatin fractions (PubMed:22872859).
CC {ECO:0000250|UniProtKB:Q9H4L4, ECO:0000269|PubMed:22872859}.
CC -!- SIMILARITY: Belongs to the peptidase C48 family. {ECO:0000305}.
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DR EMBL; AF194031; AAG28418.1; -; mRNA.
DR EMBL; AY008764; AAG33253.1; -; mRNA.
DR EMBL; AK045071; BAC32209.1; -; mRNA.
DR EMBL; AK088608; BAC40451.1; -; mRNA.
DR EMBL; AL603707; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC037014; AAH37014.1; -; mRNA.
DR CCDS; CCDS24905.1; -.
DR RefSeq; NP_001157043.1; NM_001163571.1.
DR RefSeq; NP_109627.3; NM_030702.4.
DR AlphaFoldDB; Q9EP97; -.
DR SMR; Q9EP97; -.
DR BioGRID; 219830; 6.
DR DIP; DIP-59204N; -.
DR IntAct; Q9EP97; 2.
DR STRING; 10090.ENSMUSP00000005336; -.
DR MEROPS; C48.003; -.
DR iPTMnet; Q9EP97; -.
DR PhosphoSitePlus; Q9EP97; -.
DR EPD; Q9EP97; -.
DR jPOST; Q9EP97; -.
DR MaxQB; Q9EP97; -.
DR PaxDb; Q9EP97; -.
DR PeptideAtlas; Q9EP97; -.
DR PRIDE; Q9EP97; -.
DR ProteomicsDB; 256960; -.
DR DNASU; 80886; -.
DR Ensembl; ENSMUST00000005336; ENSMUSP00000005336; ENSMUSG00000005204.
DR Ensembl; ENSMUST00000066760; ENSMUSP00000066581; ENSMUSG00000005204.
DR GeneID; 80886; -.
DR KEGG; mmu:80886; -.
DR UCSC; uc007jrb.2; mouse.
DR CTD; 26168; -.
DR MGI; MGI:2158736; Senp3.
DR VEuPathDB; HostDB:ENSMUSG00000005204; -.
DR eggNOG; KOG0778; Eukaryota.
DR GeneTree; ENSGT00940000156309; -.
DR HOGENOM; CLU_035238_0_0_1; -.
DR InParanoid; Q9EP97; -.
DR OMA; YCKYLAL; -.
DR OrthoDB; 1480705at2759; -.
DR PhylomeDB; Q9EP97; -.
DR TreeFam; TF316289; -.
DR BRENDA; 3.4.22.B72; 3474.
DR Reactome; R-MMU-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR BioGRID-ORCS; 80886; 7 hits in 73 CRISPR screens.
DR ChiTaRS; Senp3; mouse.
DR PRO; PR:Q9EP97; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q9EP97; protein.
DR Bgee; ENSMUSG00000005204; Expressed in retinal neural layer and 264 other tissues.
DR ExpressionAtlas; Q9EP97; baseline and differential.
DR Genevisible; Q9EP97; MM.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0071339; C:MLL1 complex; ISS:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IDA:MGI.
DR GO; GO:0008234; F:cysteine-type peptidase activity; ISO:MGI.
DR GO; GO:0016929; F:deSUMOylase activity; ISO:MGI.
DR GO; GO:0016926; P:protein desumoylation; ISS:UniProtKB.
DR GO; GO:0019538; P:protein metabolic process; IDA:MGI.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR003653; Peptidase_C48_C.
DR InterPro; IPR037945; SENP3.
DR InterPro; IPR045577; SENP3_5_cons_dom.
DR PANTHER; PTHR12606:SF16; PTHR12606:SF16; 1.
DR Pfam; PF02902; Peptidase_C48; 1.
DR Pfam; PF19722; SENP3_5_N; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR PROSITE; PS50600; ULP_PROTEASE; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Hydrolase; Nucleus; Phosphoprotein; Protease;
KW Reference proteome; Thiol protease; Ubl conjugation pathway.
FT CHAIN 1..568
FT /note="Sentrin-specific protease 3"
FT /id="PRO_0000101722"
FT REGION 1..119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 155..174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 380..537
FT /note="Protease"
FT MOTIF 119..122
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT MOTIF 147..153
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 72..87
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 459
FT /evidence="ECO:0000250|UniProtKB:Q9HC62"
FT ACT_SITE 476
FT /evidence="ECO:0000250|UniProtKB:Q9HC62"
FT ACT_SITE 526
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q9HC62"
FT MOD_RES 52
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H4L4"
FT MOD_RES 71
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 73
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 163
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 170
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 175
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 182
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 206
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 226
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 229
FT /note="D -> G (in Ref. 3; BAC32209)"
FT /evidence="ECO:0000305"
FT CONFLICT 440
FT /note="K -> E (in Ref. 3; BAC40451)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 568 AA; 64403 MW; 655F1FAB1AB62EA8 CRC64;
MKETIQGTGS WGPEPPGPGT TYSNPRRERL RWPLPPKPRL KSGGGFGPDP GSGTTVPTRR
LPAPRPSFDA SASEEEEEEE EEDEEEVAAW RLPPRWGQLG ASQRSRALRP SHRKTCSQRR
RRAMRAFQML LYSKSTSLTF HWKLWGRHRG RRRNLAHPKN HLSPQEGGAT PQVPSPCCRF
DSPRGLPPPR LGLLGALMAE DGMRGSPPVP SGPPMEEDGL RWTPKSPLDP DSGLLSCTLP
NGFGGLSGPE GERSLAPPDA SILISNVCSI GDHVAQELFQ SSDLGIAEEA DRTGEKAGQH
SPLREEHVTC VQSILDEFLQ TYGSLIPLST DEVVEKLEDI FQQEFSTPSR KSLVLQLIQS
YQRMPGNAMV RGFRVSYKRH VLTMDDLGTL YGQNWLNDQV MNMYGDLVMD TVPEKVHFFN
SFFYDKLRTK GYDGVKRWTK NVDIFNKELL LIPIHLEVHW SLISVDVRRR TITYFDSQRT
LNRRCPKHIA KYLQAEAVKK DRLDFHQGWK GYFKMNVARQ NNDSDCGAFV LQYCKHLALS
QPFSFTQQDM PKLRRQIYKE LCHCKLTV
