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Sentrin-specific protease 3 (EC 3.4.22.68) (SUMO-1-specific protease 3) (Sentrin/SUMO-specific protease SENP3) (Smt3-specific isopeptidase 1) (Smt3ip1)

 SENP3_MOUSE             Reviewed;         568 AA.
Q9EP97; Q5F2A5; Q8BRD5; Q8C2H5;
28-NOV-2002, integrated into UniProtKB/Swiss-Prot.
01-MAR-2001, sequence version 1.
25-OCT-2017, entry version 126.
RecName: Full=Sentrin-specific protease 3;
EC=3.4.22.-;
AltName: Full=SUMO-1-specific protease 3;
AltName: Full=Sentrin/SUMO-specific protease SENP3;
AltName: Full=Smt3-specific isopeptidase 1;
Short=Smt3ip1;
Name=Senp3; Synonyms=Smt3ip, Smt3ip1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND FUNCTION.
TISSUE=T-cell lymphoma;
PubMed=11029585; DOI=10.1046/j.1432-1327.2000.01729.x;
Nishida T., Tanaka H., Yasuda H.;
"A novel mammalian Smt3-specific isopeptidase 1 (SMT3IP1) localized in
the nucleolus at interphase.";
Eur. J. Biochem. 267:6423-6427(2000).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=C57BL/6J;
PubMed=10806345; DOI=10.1016/S0378-1119(00)00139-6;
Yeh E.T.H., Gong L., Kamitani T.;
"Ubiquitin-like proteins: new wines in new bottles.";
Gene 248:1-14(2000).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=NOD; TISSUE=Embryo, and Thymus;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Mammary tumor;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-175, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=17242355; DOI=10.1073/pnas.0609836104;
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
"Large-scale phosphorylation analysis of mouse liver.";
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-71; SER-73; SER-163;
THR-170; SER-175; SER-182; SER-206 AND SER-226, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Kidney, Liver, Lung, Pancreas,
Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[8]
FUNCTION, IDENTIFICATION IN THE 5FMC COMPLEX, INTERACTION OF THE 5FMC
COMPLEX WITH CHTOP AND ZNF148, INTERACTION WITH NOL9, AND SUBCELLULAR
LOCATION.
PubMed=22872859; DOI=10.1074/mcp.M112.017194;
Fanis P., Gillemans N., Aghajanirefah A., Pourfarzad F., Demmers J.,
Esteghamat F., Vadlamudi R.K., Grosveld F., Philipsen S.,
van Dijk T.B.;
"Five friends of methylated chromatin target of protein-arginine-
methyltransferase[prmt]-1 (chtop), a complex linking arginine
methylation to desumoylation.";
Mol. Cell. Proteomics 11:1263-1273(2012).
-!- FUNCTION: Protease that releases SUMO2 and SUMO3 monomers from
sumoylated substrates, but has only weak activity against SUMO1
conjugates. Deconjugates SUMO2 from MEF2D, which increases its
transcriptional activation capability. Deconjugates SUMO2 and
SUMO3 from CDCA8. Redox sensor that, when redistributed into
nucleoplasm, can act as an effector to enhance HIF1A
transcriptional activity by desumoylating EP300. Required for rRNA
processing through deconjugation of SUMO2 and SUMO3 from
nucleophosmin. Plays a role in the regulation of sumoylation
status of ZNF148. Functions as a component of the Five Friends of
Methylated CHTOP (5FMC) complex; the 5FMC complex is recruited to
ZNF148 by methylated CHTOP, leading to desumoylation of ZNF148 and
subsequent transactivation of ZNF148 target genes.
{ECO:0000269|PubMed:11029585, ECO:0000269|PubMed:22872859}.
-!- ENZYME REGULATION: On oxidative stress, SENP3 degradation is
blocked by inhibition of its ubiquitination, which stabilizes it
as it accumulates in the nucleoplasm. {ECO:0000250}.
-!- SUBUNIT: Binds to SUMO1 and SUMO3. Component of some MLL1/MLL
complex, at least composed of the core components KMT2A/MLL1,
ASH2L, HCFC1/HCF1, WDR5 and RBBP5, as well as the facultative
components BAP18, CHD8, E2F6, HSP70, INO80C, KANSL1, LAS1L, MAX,
MCRS1, MGA, MYST1/MOF, PELP1, PHF20, PRP31, RING2, RUVB1/TIP49A,
RUVB2/TIP49B, SENP3, TAF1, TAF4, TAF6, TAF7, TAF9 and TEX10.
Interacts with EP300, NPM1 and CDCA8 (By similarity). Component of
the 5FMC complex, at least composed of PELP1, LAS1L, TEX10, WDR18
and SENP3; the complex interacts with methylated CHTOP and ZNF148.
Interacts with NOL9. Interacts with CCAR2 (By similarity).
{ECO:0000250|UniProtKB:Q9H4L4, ECO:0000269|PubMed:22872859}.
-!- SUBCELLULAR LOCATION: Nucleus, nucleolus
{ECO:0000269|PubMed:11029585}. Nucleus, nucleoplasm
{ECO:0000269|PubMed:22872859}. Cytoplasm
{ECO:0000269|PubMed:22872859}. Note=Redistributes between the
nucleolus and the nucleoplasm in response to mild oxidative stress
(By similarity). Mainly found in the nucleoplasm, with low levels
detected in the cytoplasmic and chromatin fractions
(PubMed:22872859). {ECO:0000250|UniProtKB:Q9H4L4,
ECO:0000269|PubMed:22872859}.
-!- SIMILARITY: Belongs to the peptidase C48 family. {ECO:0000305}.
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EMBL; AF194031; AAG28418.1; -; mRNA.
EMBL; AY008764; AAG33253.1; -; mRNA.
EMBL; AK045071; BAC32209.1; -; mRNA.
EMBL; AK088608; BAC40451.1; -; mRNA.
EMBL; AL603707; CAI51945.1; -; Genomic_DNA.
EMBL; BC037014; AAH37014.1; -; mRNA.
CCDS; CCDS24905.1; -.
RefSeq; NP_001157043.1; NM_001163571.1.
RefSeq; NP_109627.3; NM_030702.4.
UniGene; Mm.284592; -.
UniGene; Mm.422171; -.
ProteinModelPortal; Q9EP97; -.
SMR; Q9EP97; -.
BioGrid; 219830; 3.
DIP; DIP-59204N; -.
IntAct; Q9EP97; 1.
STRING; 10090.ENSMUSP00000005336; -.
MEROPS; C48.003; -.
iPTMnet; Q9EP97; -.
PhosphoSitePlus; Q9EP97; -.
EPD; Q9EP97; -.
MaxQB; Q9EP97; -.
PaxDb; Q9EP97; -.
PeptideAtlas; Q9EP97; -.
PRIDE; Q9EP97; -.
Ensembl; ENSMUST00000005336; ENSMUSP00000005336; ENSMUSG00000005204.
Ensembl; ENSMUST00000066760; ENSMUSP00000066581; ENSMUSG00000005204.
GeneID; 80886; -.
KEGG; mmu:80886; -.
UCSC; uc007jrb.2; mouse.
CTD; 26168; -.
MGI; MGI:2158736; Senp3.
eggNOG; KOG0778; Eukaryota.
eggNOG; COG5160; LUCA.
GeneTree; ENSGT00530000062941; -.
HOGENOM; HOG000154287; -.
HOVERGEN; HBG059450; -.
InParanoid; Q9EP97; -.
KO; K08593; -.
OMA; FQMLLYS; -.
OrthoDB; EOG091G092N; -.
PhylomeDB; Q9EP97; -.
TreeFam; TF316289; -.
BRENDA; 3.4.22.B72; 3474.
Reactome; R-MMU-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
PRO; PR:Q9EP97; -.
Proteomes; UP000000589; Chromosome 11.
Bgee; ENSMUSG00000005204; -.
CleanEx; MM_SENP3; -.
ExpressionAtlas; Q9EP97; baseline and differential.
Genevisible; Q9EP97; MM.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0071339; C:MLL1 complex; ISS:UniProtKB.
GO; GO:0005730; C:nucleolus; IDA:MGI.
GO; GO:0005634; C:nucleus; ISO:MGI.
GO; GO:0004175; F:endopeptidase activity; IBA:GO_Central.
GO; GO:0004843; F:thiol-dependent ubiquitin-specific protease activity; IDA:MGI.
GO; GO:0016926; P:protein desumoylation; IBA:GO_Central.
GO; GO:0019538; P:protein metabolic process; IDA:MGI.
InterPro; IPR003653; Peptidase_C48_C.
Pfam; PF02902; Peptidase_C48; 1.
PROSITE; PS50600; ULP_PROTEASE; 1.
1: Evidence at protein level;
Complete proteome; Cytoplasm; Hydrolase; Nucleus; Phosphoprotein;
Protease; Reference proteome; Thiol protease; Ubl conjugation pathway.
CHAIN 1 568 Sentrin-specific protease 3.
/FTId=PRO_0000101722.
REGION 380 537 Protease.
MOTIF 119 122 Nuclear localization signal.
{ECO:0000255}.
MOTIF 147 153 Nuclear localization signal.
{ECO:0000255}.
COMPBIAS 13 66 Pro-rich.
COMPBIAS 70 86 Glu-rich.
ACT_SITE 459 459 {ECO:0000250}.
ACT_SITE 476 476 {ECO:0000250}.
ACT_SITE 526 526 {ECO:0000250}.
MOD_RES 52 52 Phosphoserine.
{ECO:0000250|UniProtKB:Q9H4L4}.
MOD_RES 71 71 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 73 73 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 163 163 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 170 170 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 175 175 Phosphoserine.
{ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:21183079}.
MOD_RES 182 182 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 206 206 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 226 226 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
CONFLICT 229 229 D -> G (in Ref. 3; BAC32209).
{ECO:0000305}.
CONFLICT 440 440 K -> E (in Ref. 3; BAC40451).
{ECO:0000305}.
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


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