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NAD-dependent protein deacetylase sirtuin-2 (EC 3.5.1.-) (Regulatory protein SIR2 homolog 2) (SIR2-like protein 2) (mSIR2L2)

 SIR2_MOUSE              Reviewed;         389 AA.
Q8VDQ8; E9PXF5; Q9CXS5; Q9EQ18; Q9ERJ9; U5TP50;
31-OCT-2003, integrated into UniProtKB/Swiss-Prot.
31-OCT-2003, sequence version 2.
30-AUG-2017, entry version 156.
RecName: Full=NAD-dependent protein deacetylase sirtuin-2;
EC=3.5.1.-;
AltName: Full=Regulatory protein SIR2 homolog 2;
AltName: Full=SIR2-like protein 2;
Short=mSIR2L2;
Name=Sirt2; Synonyms=Sir2l2;
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 [GENOMIC DNA / MRNA] (ISOFORM 1), AND SUBCELLULAR
LOCATION.
STRAIN=129/Ola;
PubMed=11056054; DOI=10.1006/geno.2000.6360;
Yang Y.H., Chen Y.H., Zhang C.Y., Nimmakayalu M.A., Ward D.C.,
Weissman S.;
"Cloning and characterization of two mouse genes with homology to the
yeast sir2 gene.";
Genomics 69:355-369(2000).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
STRAIN=C57BL/6J; TISSUE=Embryo;
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).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), AND ALTERNATIVE SPLICING
(ISOFORMS 1 AND 2).
TISSUE=Brain;
PubMed=24177535; DOI=10.1016/j.jmb.2013.10.027;
Rack J.G., Vanlinden M.R., Lutter T., Aasland R., Ziegler M.;
"Constitutive nuclear localization of an alternatively spliced
sirtuin-2 isoform.";
J. Mol. Biol. 426:1677-1691(2014).
[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] (ISOFORM 1).
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]
PROTEIN SEQUENCE OF 43-55; 58-69; 79-125; 137-153; 164-174; 213-253;
276-282 AND 348-371, AND IDENTIFICATION BY MASS SPECTROMETRY.
STRAIN=C57BL/6J, and OF1; TISSUE=Brain, and Hippocampus;
Lubec G., Klug S., Kang S.U., Sunyer B., Chen W.-Q.;
Submitted (JAN-2009) to UniProtKB.
[7]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic brain;
PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
"Phosphoproteomic analysis of the developing mouse brain.";
Mol. Cell. Proteomics 3:1093-1101(2004).
[8]
FUNCTION IN DEACETYLATION OF FOXO3, FUNCTION IN REGULATION OF FOXO3
ACTIVITY, INTERACTION WITH FOXO3, SUBCELLULAR LOCATION, MUTAGENESIS OF
HIS-187, AND INDUCTION BY CALORIC RESTRICTION AND OXIDATIVE STRESS.
PubMed=17521387; DOI=10.1111/j.1474-9726.2007.00304.x;
Wang F., Nguyen M., Qin F.X., Tong Q.;
"SIRT2 deacetylates FOXO3a in response to oxidative stress and caloric
restriction.";
Aging Cell 6:505-514(2007).
[9]
FUNCTION IN DEACETYLATION OF FOXO1, FUNCTION IN INHIBITION OF
ADIPOCYTE DIFFERENTIATION, INTERACTION WITH FOXO1, INDUCTION, AND
TISSUE SPECIFICITY.
PubMed=17681146; DOI=10.1016/j.cmet.2007.07.003;
Jing E., Gesta S., Kahn C.R.;
"SIRT2 regulates adipocyte differentiation through FoxO1
acetylation/deacetylation.";
Cell Metab. 6:105-114(2007).
[10]
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=17634366; DOI=10.1523/JNEUROSCI.1254-07.2007;
Werner H.B., Kuhlmann K., Shen S., Uecker M., Schardt A., Dimova K.,
Orfaniotou F., Dhaunchak A., Brinkmann B.G., Mobius W., Guarente L.,
Casaccia-Bonnefil P., Jahn O., Nave K.A.;
"Proteolipid protein is required for transport of sirtuin 2 into CNS
myelin.";
J. Neurosci. 27:7717-7730(2007).
[11]
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=16933150; DOI=10.1007/s11064-006-9127-6;
Southwood C.M., Peppi M., Dryden S., Tainsky M.A., Gow A.;
"Microtubule deacetylases, SirT2 and HDAC6, in the nervous system.";
Neurochem. Res. 32:187-195(2007).
[12]
FUNCTION IN DEACETYLATION OF TUBULIN, FUNCTION IN AXONAL DEGENERATION,
AND SUBCELLULAR LOCATION.
PubMed=17574768; DOI=10.1016/j.neuroscience.2007.04.059;
Suzuki K., Koike T.;
"Mammalian Sir2-related protein (SIRT) 2-mediated modulation of
resistance to axonal degeneration in slow Wallerian degeneration mice:
a crucial role of tubulin deacetylation.";
Neuroscience 147:599-612(2007).
[13]
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).
[14]
INTERACTION WITH CDK5, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=18332217; DOI=10.1083/jcb.200707126;
Pandithage R., Lilischkis R., Harting K., Wolf A., Jedamzik B.,
Luscher-Firzlaff J., Vervoorts J., Lasonder E., Kremmer E., Knoll B.,
Luscher B.;
"The regulation of SIRT2 function by cyclin-dependent kinases affects
cell motility.";
J. Cell Biol. 180:915-929(2008).
[15]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
Thibault P.;
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Immunity 30:143-154(2009).
[16]
FUNCTION IN DEACETYLATION OF FOXO1, FUNCTION IN INHIBITION OF
ADIPOCYTE DIFFERENTIATION, INTERACTION WITH FOXO1, SUBCELLULAR
LOCATION, AND INDUCTION BY CALORIC RESTRICTION.
PubMed=19037106; DOI=10.1091/mbc.E08-06-0647;
Wang F., Tong Q.;
"SIRT2 suppresses adipocyte differentiation by deacetylating FOXO1 and
enhancing FOXO1's repressive interaction with PPARgamma.";
Mol. Biol. Cell 20:801-808(2009).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23; SER-25; THR-27;
SER-368 AND SER-372, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, 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).
[18]
FUNCTION IN DEACETYLATION OF CDC20 AND FZR1, POSSIBLE FUNCTION AS A
TUMOR SUPPRESSOR, INTERACTION WITH AURKA; CDC20 AND FZR1, DISRUPTION
PHENOTYPE, AND SUBCELLULAR LOCATION.
PubMed=22014574; DOI=10.1016/j.ccr.2011.09.004;
Kim H.S., Vassilopoulos A., Wang R.H., Lahusen T., Xiao Z., Xu X.,
Li C., Veenstra T.D., Li B., Yu H., Ji J., Wang X.W., Park S.H.,
Cha Y.I., Gius D., Deng C.X.;
"SIRT2 maintains genome integrity and suppresses tumorigenesis through
regulating APC/C activity.";
Cancer Cell 20:487-499(2011).
[19]
ALTERNATIVE SPLICING (ISOFORMS 1; 2 AND 4), FUNCTION IN DEACETYLATION
OF ALPHA-TUBULIN (ISOFORMS 1; 2 AND 4), ASSOCIATION WITH ALPHA-TUBULIN
(ISOFORMS 2 AND 4), SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
INDUCTION.
PubMed=21791548; DOI=10.1093/hmg/ddr326;
Maxwell M.M., Tomkinson E.M., Nobles J., Wizeman J.W., Amore A.M.,
Quinti L., Chopra V., Hersch S.M., Kazantsev A.G.;
"The Sirtuin 2 microtubule deacetylase is an abundant neuronal protein
that accumulates in the aging CNS.";
Hum. Mol. Genet. 20:3986-3996(2011).
[20]
FUNCTION IN REGULATION OF PERIPHERAL MYELINATION, CONDITIONAL KNOCKOUT
IN SCHWANN CELL, TISSUE SPECIFICITY, AND INDUCTION.
PubMed=21949390; DOI=10.1073/pnas.1104969108;
Beirowski B., Gustin J., Armour S.M., Yamamoto H., Viader A.,
North B.J., Michan S., Baloh R.H., Golden J.P., Schmidt R.E.,
Sinclair D.A., Auwerx J., Milbrandt J.;
"Sir-two-homolog 2 (Sirt2) modulates peripheral myelination through
polarity protein Par-3/atypical protein kinase C (aPKC) signaling.";
Proc. Natl. Acad. Sci. U.S.A. 108:E952-961(2011).
[21]
FUNCTION IN DEACETYLATION OF FOXO3, FUNCTION IN REGULATION OF FOXO3
ACTIVITY, AND MUTAGENESIS OF HIS-187.
PubMed=21841822; DOI=10.1038/onc.2011.347;
Wang F., Chan C.H., Chen K., Guan X., Lin H.K., Tong Q.;
"Deacetylation of FOXO3 by SIRT1 or SIRT2 leads to Skp2-mediated FOXO3
ubiquitination and degradation.";
Oncogene 31:1546-1557(2012).
[22]
REVIEW, AND FUNCTION AS A TUMOR SUPPRESSOR.
PubMed=22943040;
Park S.H., Zhu Y., Ozden O., Kim H.S., Jiang H., Deng C.X., Gius D.,
Vassilopoulos A.;
"SIRT2 is a tumor suppressor that connects aging, acetylome, cell
cycle signaling, and carcinogenesis.";
Transl. Cancer Res. 1:15-21(2012).
[23]
FUNCTION AS A TUMOR SUPPRESSOR, DISRUPTION PHENOTYPE, AND SUBCELLULAR
LOCATION.
PubMed=23468428; DOI=10.1101/gad.211342.112;
Serrano L., Martinez-Redondo P., Marazuela-Duque A., Vazquez B.N.,
Dooley S.J., Voigt P., Beck D.B., Kane-Goldsmith N., Tong Q.,
Rabanal R.M., Fondevila D., Munoz P., Kruger M., Tischfield J.A.,
Vaquero A.;
"The tumor suppressor SirT2 regulates cell cycle progression and
genome stability by modulating the mitotic deposition of H4K20
methylation.";
Genes Dev. 27:639-653(2013).
[24]
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=24460154; DOI=10.3109/00016489.2013.861928;
Takumida M., Takumida H., Anniko M.;
"Localization of sirtuins in the mouse inner ear.";
Acta Oto-Laryngol. 134:331-338(2014).
[25]
FUNCTION IN DEACETYLATION OF HISTONE H4 AND ALPHA-TUBULIN, FUNCTION IN
OOCYTE MEIOSIS, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=24334550; DOI=10.1096/fj.13-244111;
Zhang L., Hou X., Ma R., Moley K., Schedl T., Wang Q.;
"Sirt2 functions in spindle organization and chromosome alignment in
mouse oocyte meiosis.";
FASEB J. 28:1435-1445(2014).
-!- FUNCTION: NAD-dependent protein deacetylase, which deacetylates
internal lysines on histone and alpha-tubulin as well as many
other proteins such as key transcription factors. Participates in
the modulation of multiple and diverse biological processes such
as cell cycle control, genomic integrity, microtubule dynamics,
cell differentiation, metabolic networks, and autophagy. Plays a
major role in the control of cell cycle progression and genomic
stability. Functions in the antephase checkpoint preventing
precocious mitotic entry in response to microtubule stress agents,
and hence allowing proper inheritance of chromosomes. Positively
regulates the anaphase promoting complex/cyclosome (APC/C)
ubiquitin ligase complex activity by deacetylating CDC20 and FZR1,
then allowing progression through mitosis. Associates with both
chromatin at transcriptional start sites (TSSs) and enhancers of
active genes. Plays a role in cell cycle and chromatin compaction
through epigenetic modulation of the regulation of histone H4
'Lys-20' methylation (H4K20me1) during early mitosis. Specifically
deacetylates histone H4 at 'Lys-16' (H4K16ac) between the G2/M
transition and metaphase enabling H4K20me1 deposition by KMT5A
leading to ulterior levels of H4K20me2 and H4K20me3 deposition
throughout cell cycle, and mitotic S-phase progression.
Deacetylates KMT5A modulating KMT5A chromatin localization during
the mitotic stress response. Deacetylates also histone H3 at 'Lys-
57' (H3K56ac) during the mitotic G2/M transition. During oocyte
meiosis progression, may deacetylate histone H4 at 'Lys-16'
(H4K16ac) and alpha-tubulin, regulating spindle assembly and
chromosome alignment by influencing microtubule dynamics and
kinetochore function. Deacetylates alpha-tubulin at 'Lys-40' and
hence controls neuronal motility, oligodendroglial cell arbor
projection processes and proliferation of non-neuronal cells.
Phosphorylation at Ser-368 by a G1/S-specific cyclin E-CDK2
complex inactivates SIRT2-mediated alpha-tubulin deacetylation,
negatively regulating cell adhesion, cell migration and neurite
outgrowth during neuronal differentiation. Deacetylates PARD3 and
participates in the regulation of Schwann cell peripheral
myelination formation during early postnatal development and
during postinjury remyelination. Involved in several cellular
metabolic pathways. Plays a role in the regulation of blood
glucose homeostasis by deacetylating and stabilizing
phosphoenolpyruvate carboxykinase PCK1 activity in response to low
nutrient availability. Acts as a key regulator in the pentose
phosphate pathway (PPP) by deacetylating and activating the
glucose-6-phosphate G6PD enzyme, and therefore, stimulates the
production of cytosolic NADPH to counteract oxidative damage.
Maintains energy homeostasis in response to nutrient deprivation
as well as energy expenditure by inhibiting adipogenesis and
promoting lipolysis. Attenuates adipocyte differentiation by
deacetylating and promoting FOXO1 interaction to PPARG and
subsequent repression of PPARG-dependent transcriptional activity.
Plays a role in the regulation of lysosome-mediated degradation of
protein aggregates by autophagy in neuronal cells. Deacetylates
FOXO1 in response to oxidative stress or serum deprivation,
thereby negatively regulating FOXO1-mediated autophagy.
Deacetylates a broad range of transcription factors and co-
regulators regulating target gene expression. Deacetylates
transcriptional factor FOXO3 stimulating the ubiquitin ligase
SCF(SKP2)-mediated FOXO3 ubiquitination and degradation.
Deacetylates HIF1A, and therefore promotes HIF1A degradation and
inhibition of HIF1A transcriptional activity in tumor cells in
response to hypoxia. Deacetylates RELA in the cytoplasm inhibiting
NF-kappaB-dependent transcription activation upon TNF-alpha
stimulation. Inhibits transcriptional activation by deacetylating
p53/TP53 and EP300. Deacetylates also EIF5A. Functions as a
negative regulator on oxidative stress-tolerance in response to
anoxia-reoxygenation conditions. Plays a role as tumor suppressor.
-!- FUNCTION: Isoform 1: Deacetylates alpha-tubulin.
-!- FUNCTION: Isoform 2: Deacetylates alpha-tubulin.
-!- FUNCTION: Isoform 4: Deacetylates alpha-tubulin.
-!- CATALYTIC ACTIVITY: NAD(+) + an acetylprotein = nicotinamide + O-
acetyl-ADP-ribose + a protein. {ECO:0000255|PROSITE-
ProRule:PRU00236}.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
Note=Binds 1 zinc ion per subunit. {ECO:0000250};
-!- ENZYME REGULATION: Inhibited by Sirtinol, A3 and M15 small
molecules. Inhibited by nicotinamide. Inhibited by a macrocyclic
peptide inhibitor S2iL5. Inhibited by EP300-induced acetylation
(By similarity). {ECO:0000250}.
-!- SUBUNIT: Homotrimer. Interacts (via both phosphorylated,
unphosphorylated, active or inactive forms) with HDAC6; the
interaction is necessary for the complex to interact with alpha-
tubulin, suggesting that these proteins belong to a large complex
that deacetylates the cytoskeleton. Interacts with RELA; the
interaction occurs in the cytoplasm and is increased in a TNF-
alpha-dependent manner. Interacts with HOXA10; the interaction is
direct. Interacts with YWHAB and YWHAG; the interactions occur in
a AKT-dependent manner and increase SIRT2-dependent TP53
deacetylation. Interacts with MAPK1/ERK2 and MAPK3/ERK1; the
interactions increase SIRT2 stability and deacetylation activity.
Interacts (phosphorylated form) with KMT5A; the interaction is
direct, stimulates KMT5A-mediated methyltransferase activity on
histone at 'Lys-20' (H4K20me1) and is increased in a H(2)O(2)-
induced oxidative stress-dependent manner. Interacts with G6PD;
the interaction is enhanced by H(2)O(2) treatment. Interacts (via
C-terminus region) with EP300. Interacts with HIF1A. Interacts
with a G1/S-specific cyclin E-CDK2 complex (By similarity).
Interacts with FOXO1; the interaction is disrupted upon serum-
starvation or oxidative stress, leading to increased level of
acetylated FOXO1 and induction of autophagy. Interacts with AURKA,
CDC20, CDK5 (p35 form), FOXO3 and FZR1. Isoform 2 and isoform 4
associate with microtubule in primary cortical mature neurons.
{ECO:0000250, ECO:0000269|PubMed:17521387,
ECO:0000269|PubMed:17681146, ECO:0000269|PubMed:18332217,
ECO:0000269|PubMed:19037106, ECO:0000269|PubMed:22014574}.
-!- INTERACTION:
O14965:AURKA (xeno); NbExp=5; IntAct=EBI-911012, EBI-448680;
Q9JJ66:Cdc20; NbExp=2; IntAct=EBI-911012, EBI-2551389;
Q9R1K5:Fzr1; NbExp=2; IntAct=EBI-911012, EBI-5238560;
-!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Cytoplasm, perinuclear
region. Perikaryon. Cytoplasm, cytoskeleton. Cell projection. Cell
projection, growth cone. Myelin membrane. Cytoplasm, cytoskeleton,
microtubule organizing center, centrosome. Cytoplasm,
cytoskeleton, spindle. Chromosome. Midbody. Cytoplasm,
cytoskeleton, microtubule organizing center, centrosome, centriole
{ECO:0000250}. Note=Localizes in the cytoplasm during most of the
cell cycle except in the G2/M transition and during mitosis, where
it is localized in association with chromatin and induces
deacetylation of histone at 'Lys-16' (H4K16ac). Colocalizes with
CDK1 at centrosome during prophase and splindle fibers during
metaphase. Colocalizes with Aurora kinase AURKA in centrioles
during early prophase and growing mitotic spindle throughout
metaphase. Colocalizes with Aurora kinase AURKB during cytokinesis
with the midbody. Detected in perinuclear foci that may be
aggresomes containing misfolded, ubiquitinated proteins. Shuttles
between the cytoplasm and the nucleus through the CRM1 export
pathway. Colocalizes with EP300 in the nucleus. Colocalizes with
PARD3 in internodal region of axons. Colocalizes with acetylated
alpha-tubulin in cell projection processes during primary
oligodendrocyte precursor (OLP) differentiation (By similarity).
Deacetylates FOXO3 in the cytoplasm. Colocalizes with Aurora
kinase AURKA at centrosome. Colocalizes with microtubules.
Colocalizes with PLP1 in internodal regions of myelin sheat, at
paranodal axoglial junction and Schmidt-Lanterman incisures.
Colocalizes with CDK5R1 in the perikaryon, neurites and growth
cone of hippocampal neurons. Colocalizes with alpha-tubulin in
neuronal growth cone. Colocalizes with KMT5A at mitotic foci.
Localizes in the cytoplasm and nucleus of germinal vesicle (GV)
stage oocytes. Colocalizes with alpha-tubulin on the meiotic
spindle as the oocytes enter into metaphase, and also during
meiotic anaphase and telophase, especially with the midbody.
{ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1; Synonyms=SIRT2.1;
IsoId=Q8VDQ8-1; Sequence=Displayed;
Name=2; Synonyms=SIRT2.2;
IsoId=Q8VDQ8-2; Sequence=VSP_008729;
Name=3;
IsoId=Q8VDQ8-3; Sequence=VSP_055330;
Name=4; Synonyms=SIRT2.3;
IsoId=Q8VDQ8-4; Sequence=VSP_055329;
Note=Gene prediction based on EST data.;
-!- TISSUE SPECIFICITY: Isoform 1 is weakly expressed in the cortex at
postnatal(P) days P1, P3 and P7, and increases progressively
between P17 and older adult cortex. Isoform 1 is also expressed in
heart, liver and skeletal muscle, weakly expressed in the striatum
and spinal cord. Isoform 2 is not expressed in the cortex at P1,
P3 and P7, and increases strongly and progressively between P17
and older adult cortex. Isoform 2 is also expressed in the heart,
liver, striatum and spinal cord. Isoform 4 is weakly expressed in
older adult cortex and spinal cords. Expressed in the cortex.
Expressed in postnatal sciatic nerves during myelination and
during remyelination after nerve injury. Expressed in neurons,
oligodendrocytes, Schwann cells, Purkinje cells and in astrocytes
of white matter. Strongly expressed in preadipocytes compared with
differentiated adipocytes. Expressed in cerebellar granule cells.
Expressed in the inner ear: in the cochlea, expressed in types I
and V fibrocytes in the spiral ligament (SL) and slightly in stria
vascularis (SV); in the organ of Corti, expressed in some
supporting cells; in the crista ampullaris, expressed in spiral
ganglion cells; also expressed in the endolymphatic sac (ES)
epithelial cells (at protein level). Expressed in the brain,
spinal cord, optic nerve and hippocampus. Strongly expressed in 6-
8 week-old ovulated meiosis II oocytes and weakly expressed in 45-
58 week-old ovulated meiosis II oocytes. Expressed in the cochlea,
vestibule and acoustic nerve of the inner ear.
{ECO:0000269|PubMed:16933150, ECO:0000269|PubMed:17634366,
ECO:0000269|PubMed:17681146, ECO:0000269|PubMed:18332217,
ECO:0000269|PubMed:21791548, ECO:0000269|PubMed:21949390,
ECO:0000269|PubMed:24334550, ECO:0000269|PubMed:24460154}.
-!- DEVELOPMENTAL STAGE: Isoform 1 is expressed in the cortex at 15.5
dpc. Isoform 2 is not detected in the cortex at 15.5 dpc (at
protein level).
-!- INDUCTION: Up-regulated in response to caloric restriction in
white and brown adipose tissues. Up-regulated during cold exposure
and down-regulated in higher ambient temperature in brown adipose
tissue. Up-regulated after beta-adrenergic agonist (isoproterenol)
treatment in white adipose tissue (at protein level). Up-regulated
in response to caloric restriction in adipose tissue and kidney.
Up-regulated in response to oxidative stress. Up-regulated during
postnatal sciatic nerve myelination development and axonal
regeneration. Down-regulated during preadipocyte differentiation.
Down-regulated in Schwann dedifferentiated cells during Wallerian
degeneration. Isoform 1 is up-regulated upon differentiation to a
neuron-like phenotype. {ECO:0000269|PubMed:17521387,
ECO:0000269|PubMed:17681146, ECO:0000269|PubMed:19037106,
ECO:0000269|PubMed:21791548, ECO:0000269|PubMed:21949390}.
-!- PTM: Phosphorylated at phosphoserine and phosphothreonine.
Phosphorylated at Ser-368 by a mitotic kinase CDK1/cyclin B at the
G2/M transition; phosphorylation regulates the delay in cell-cycle
progression. Phosphorylated at Ser-368 by a mitotic kinase G1/S-
specific cyclin E/Cdk2 complex; phosphorylation inactivates SIRT2-
mediated alpha-tubulin deacetylation and thereby negatively
regulates cell adhesion, cell migration and neurite outgrowth
during neuronal differentiation. Phosphorylated by cyclin A/Cdk2
and p35-Cdk5 complexes and to a lesser extent by the cyclin
D3/Cdk4 and cyclin B/Cdk1, in vitro. Dephosphorylated at Ser-368
by CDC14A and CDC14B around early anaphase (By similarity).
{ECO:0000250}.
-!- PTM: Acetylated by EP300; acetylation leads both to the decreased
of SIRT2-mediated alpha-tubulin deacetylase activity and SIRT2-
mediated down-regulation of TP53 transcriptional activity.
{ECO:0000250}.
-!- PTM: Ubiquitinated. {ECO:0000250}.
-!- DISRUPTION PHENOTYPE: Tissue-specific knockout of SIRT2 in Schwann
cells of early postnatal mice leads to a transient delay in
myelination, a reduction in the nerve conduction velocity and
hyperacetylation of PARD3. The number of dividing Schwann cells in
the developing nerve and alpha-tubulin acetylation are normal
(PubMed:21949390). Mutant mice embryo grow normally and new born
are healthy. Embryonic fibroblasts (MEFs) display reduced cell
proliferation capacity, centrosome amplification and mitotic cell
death. Nude mice inoculated with immortalized MEFs from mutant
mice developed tumors. Adult mutant mice exhibit genomic
instability and chromosomal aberrations, such as double-strand
breaks (DSBs), with a gender-specific spectrum of tumorigenesis;
females develop primarily mammary tumors and males develop tumors
in several organs, including the liver, lung, pancreas, stomach,
duodenum and prostate. Drastic increases of histone H4K16
acetylation and decreases of both histone methylation (H4K20me1)
in metaphasic chromosomes and histone methylations (H4K20me2/3) in
late M/early G1 but also throughout all phases of the cell cycle
(PubMed:23468428). {ECO:0000269|PubMed:21949390,
ECO:0000269|PubMed:22014574, ECO:0000269|PubMed:23468428}.
-!- SIMILARITY: Belongs to the sirtuin family. Class I subfamily.
{ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AF299337; AAG39256.1; -; mRNA.
EMBL; AF302272; AAG32038.1; -; Genomic_DNA.
EMBL; AF302265; AAG32038.1; JOINED; Genomic_DNA.
EMBL; AF302266; AAG32038.1; JOINED; Genomic_DNA.
EMBL; AF302267; AAG32038.1; JOINED; Genomic_DNA.
EMBL; AF302268; AAG32038.1; JOINED; Genomic_DNA.
EMBL; AF302269; AAG32038.1; JOINED; Genomic_DNA.
EMBL; AF302270; AAG32038.1; JOINED; Genomic_DNA.
EMBL; AF302271; AAG32038.1; JOINED; Genomic_DNA.
EMBL; AK014042; BAB29128.1; -; mRNA.
EMBL; KF032392; AGZ02590.1; -; mRNA.
EMBL; AC171210; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC021439; AAH21439.1; -; mRNA.
CCDS; CCDS21055.1; -. [Q8VDQ8-1]
CCDS; CCDS52165.1; -. [Q8VDQ8-4]
CCDS; CCDS85253.1; -. [Q8VDQ8-2]
RefSeq; NP_001116237.1; NM_001122765.1. [Q8VDQ8-2]
RefSeq; NP_001116238.1; NM_001122766.1. [Q8VDQ8-4]
RefSeq; NP_071877.3; NM_022432.4. [Q8VDQ8-1]
UniGene; Mm.272443; -.
ProteinModelPortal; Q8VDQ8; -.
SMR; Q8VDQ8; -.
BioGrid; 211070; 23.
IntAct; Q8VDQ8; 15.
MINT; MINT-4134698; -.
STRING; 10090.ENSMUSP00000072732; -.
ChEMBL; CHEMBL3232691; -.
iPTMnet; Q8VDQ8; -.
PhosphoSitePlus; Q8VDQ8; -.
PaxDb; Q8VDQ8; -.
PeptideAtlas; Q8VDQ8; -.
PRIDE; Q8VDQ8; -.
Ensembl; ENSMUST00000072965; ENSMUSP00000072732; ENSMUSG00000015149. [Q8VDQ8-1]
Ensembl; ENSMUST00000122915; ENSMUSP00000147217; ENSMUSG00000015149. [Q8VDQ8-2]
Ensembl; ENSMUST00000170068; ENSMUSP00000132783; ENSMUSG00000015149. [Q8VDQ8-4]
GeneID; 64383; -.
KEGG; mmu:64383; -.
UCSC; uc009fzt.2; mouse. [Q8VDQ8-1]
UCSC; uc012fgx.1; mouse. [Q8VDQ8-4]
CTD; 22933; -.
MGI; MGI:1927664; Sirt2.
eggNOG; KOG2682; Eukaryota.
eggNOG; COG0846; LUCA.
GeneTree; ENSGT00870000136486; -.
HOGENOM; HOG000085952; -.
HOVERGEN; HBG057095; -.
InParanoid; Q8VDQ8; -.
KO; K11412; -.
OMA; LYPGSFI; -.
OrthoDB; EOG091G07CT; -.
PhylomeDB; Q8VDQ8; -.
TreeFam; TF106181; -.
ChiTaRS; Sirt2; mouse.
PRO; PR:Q8VDQ8; -.
Proteomes; UP000000589; Chromosome 7.
Bgee; ENSMUSG00000015149; -.
ExpressionAtlas; Q8VDQ8; baseline and differential.
Genevisible; Q8VDQ8; MM.
GO; GO:0005814; C:centriole; ISS:UniProtKB.
GO; GO:0005813; C:centrosome; ISS:UniProtKB.
GO; GO:0005694; C:chromosome; ISS:UniProtKB.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; ISS:UniProtKB.
GO; GO:0097386; C:glial cell projection; ISS:UniProtKB.
GO; GO:0030426; C:growth cone; IEA:UniProtKB-SubCell.
GO; GO:0044224; C:juxtaparanode region of axon; ISS:UniProtKB.
GO; GO:0043219; C:lateral loop; ISS:UniProtKB.
GO; GO:0072687; C:meiotic spindle; IDA:UniProtKB.
GO; GO:0005874; C:microtubule; ISS:UniProtKB.
GO; GO:0030496; C:midbody; IDA:UniProtKB.
GO; GO:0005739; C:mitochondrion; IDA:MGI.
GO; GO:0072686; C:mitotic spindle; ISS:UniProtKB.
GO; GO:0043209; C:myelin sheath; IDA:UniProtKB.
GO; GO:0005720; C:nuclear heterochromatin; ISS:UniProtKB.
GO; GO:0005730; C:nucleolus; ISO:MGI.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0033010; C:paranodal junction; IDA:UniProtKB.
GO; GO:0033270; C:paranode region of axon; ISS:UniProtKB.
GO; GO:0043204; C:perikaryon; IDA:UniProtKB.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; ISO:MGI.
GO; GO:0043220; C:Schmidt-Lanterman incisure; IDA:UniProtKB.
GO; GO:0005819; C:spindle; ISS:UniProtKB.
GO; GO:0048487; F:beta-tubulin binding; IDA:MGI.
GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
GO; GO:0035035; F:histone acetyltransferase binding; ISS:UniProtKB.
GO; GO:0004407; F:histone deacetylase activity; IMP:UniProtKB.
GO; GO:0042826; F:histone deacetylase binding; ISS:UniProtKB.
GO; GO:0070403; F:NAD+ binding; ISO:MGI.
GO; GO:0017136; F:NAD-dependent histone deacetylase activity; ISS:UniProtKB.
GO; GO:0046970; F:NAD-dependent histone deacetylase activity (H4-K16 specific); ISS:UniProtKB.
GO; GO:0034979; F:NAD-dependent protein deacetylase activity; ISS:UniProtKB.
GO; GO:0033558; F:protein deacetylase activity; IDA:UniProtKB.
GO; GO:0008134; F:transcription factor binding; IPI:UniProtKB.
GO; GO:0042903; F:tubulin deacetylase activity; IMP:UniProtKB.
GO; GO:0043130; F:ubiquitin binding; ISS:UniProtKB.
GO; GO:0008270; F:zinc ion binding; ISO:MGI.
GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
GO; GO:0044242; P:cellular lipid catabolic process; IMP:UniProtKB.
GO; GO:0061433; P:cellular response to caloric restriction; IDA:UniProtKB.
GO; GO:0071872; P:cellular response to epinephrine stimulus; IDA:UniProtKB.
GO; GO:0035729; P:cellular response to hepatocyte growth factor stimulus; ISS:UniProtKB.
GO; GO:0071456; P:cellular response to hypoxia; ISS:UniProtKB.
GO; GO:0071219; P:cellular response to molecule of bacterial origin; ISS:UniProtKB.
GO; GO:0034599; P:cellular response to oxidative stress; IDA:UniProtKB.
GO; GO:0048012; P:hepatocyte growth factor receptor signaling pathway; ISS:UniProtKB.
GO; GO:0016575; P:histone deacetylation; IGI:MGI.
GO; GO:0070932; P:histone H3 deacetylation; IMP:UniProtKB.
GO; GO:0070933; P:histone H4 deacetylation; IMP:UniProtKB.
GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
GO; GO:0022011; P:myelination in peripheral nervous system; IMP:UniProtKB.
GO; GO:0010507; P:negative regulation of autophagy; ISS:UniProtKB.
GO; GO:0008285; P:negative regulation of cell proliferation; IMP:UniProtKB.
GO; GO:1900425; P:negative regulation of defense response to bacterium; IMP:UniProtKB.
GO; GO:0045599; P:negative regulation of fat cell differentiation; IMP:UniProtKB.
GO; GO:1900226; P:negative regulation of NLRP3 inflammasome complex assembly; IMP:MGI.
GO; GO:0070446; P:negative regulation of oligodendrocyte progenitor proliferation; ISS:UniProtKB.
GO; GO:0010801; P:negative regulation of peptidyl-threonine phosphorylation; IMP:UniProtKB.
GO; GO:0042177; P:negative regulation of protein catabolic process; ISS:UniProtKB.
GO; GO:2000378; P:negative regulation of reactive oxygen species metabolic process; IMP:UniProtKB.
GO; GO:0045843; P:negative regulation of striated muscle tissue development; ISS:UniProtKB.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IMP:UniProtKB.
GO; GO:0061428; P:negative regulation of transcription from RNA polymerase II promoter in response to hypoxia; ISS:UniProtKB.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
GO; GO:0034983; P:peptidyl-lysine deacetylation; ISS:UniProtKB.
GO; GO:0014065; P:phosphatidylinositol 3-kinase signaling; ISS:UniProtKB.
GO; GO:0051987; P:positive regulation of attachment of spindle microtubules to kinetochore; IMP:UniProtKB.
GO; GO:0051781; P:positive regulation of cell division; IMP:UniProtKB.
GO; GO:0043388; P:positive regulation of DNA binding; IDA:UniProtKB.
GO; GO:1900119; P:positive regulation of execution phase of apoptosis; IMP:UniProtKB.
GO; GO:0045836; P:positive regulation of meiotic nuclear division; IMP:UniProtKB.
GO; GO:1900195; P:positive regulation of oocyte maturation; IMP:UniProtKB.
GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IMP:UniProtKB.
GO; GO:2000777; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process involved in cellular response to hypoxia; ISS:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IMP:UniProtKB.
GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
GO; GO:0006476; P:protein deacetylation; IDA:UniProtKB.
GO; GO:0043491; P:protein kinase B signaling; ISS:UniProtKB.
GO; GO:0051726; P:regulation of cell cycle; ISS:UniProtKB.
GO; GO:0045598; P:regulation of fat cell differentiation; IMP:MGI.
GO; GO:0031641; P:regulation of myelination; IMP:UniProtKB.
GO; GO:1901026; P:ripoptosome assembly involved in necroptotic process; IMP:MGI.
GO; GO:0021762; P:substantia nigra development; IEA:Ensembl.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0090042; P:tubulin deacetylation; IMP:UniProtKB.
Gene3D; 3.30.1600.10; -; 1.
Gene3D; 3.40.50.1220; -; 1.
InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
InterPro; IPR003000; Sirtuin.
InterPro; IPR026591; Sirtuin_cat_small_dom.
InterPro; IPR017328; Sirtuin_class_I.
InterPro; IPR026590; Ssirtuin_cat_dom.
Pfam; PF02146; SIR2; 1.
PIRSF; PIRSF037938; SIR2_euk; 1.
SUPFAM; SSF52467; SSF52467; 1.
PROSITE; PS50305; SIRTUIN; 1.
1: Evidence at protein level;
Acetylation; Alternative splicing; Autophagy; Cell cycle;
Cell division; Cell membrane; Cell projection; Chromosome;
Complete proteome; Cytoplasm; Cytoskeleton; Differentiation;
Direct protein sequencing; Hydrolase; Meiosis; Membrane;
Metal-binding; Microtubule; Mitosis; NAD; Neurogenesis; Nucleus;
Phosphoprotein; Reference proteome; Transcription;
Transcription regulation; Ubl conjugation; Zinc.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:Q8IXJ6}.
CHAIN 2 389 NAD-dependent protein deacetylase
sirtuin-2.
/FTId=PRO_0000110259.
DOMAIN 65 340 Deacetylase sirtuin-type.
{ECO:0000255|PROSITE-ProRule:PRU00236}.
NP_BIND 84 104 NAD. {ECO:0000250}.
NP_BIND 167 170 NAD. {ECO:0000250}.
NP_BIND 261 263 NAD. {ECO:0000250}.
NP_BIND 286 288 NAD. {ECO:0000250}.
REGION 116 120 Peptide inhibitor binding. {ECO:0000250}.
REGION 232 301 Peptide inhibitor binding. {ECO:0000250}.
MOTIF 41 51 Nuclear export signal. {ECO:0000250}.
ACT_SITE 187 187 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00236}.
METAL 195 195 Zinc. {ECO:0000255|PROSITE-
ProRule:PRU00236}.
METAL 200 200 Zinc. {ECO:0000255|PROSITE-
ProRule:PRU00236}.
METAL 221 221 Zinc. {ECO:0000255|PROSITE-
ProRule:PRU00236}.
METAL 224 224 Zinc. {ECO:0000255|PROSITE-
ProRule:PRU00236}.
BINDING 324 324 NAD; via amide nitrogen. {ECO:0000250}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000250|UniProtKB:Q8IXJ6}.
MOD_RES 23 23 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 25 25 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 27 27 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 53 53 Phosphoserine.
{ECO:0000250|UniProtKB:Q5RJQ4}.
MOD_RES 100 100 Phosphoserine.
{ECO:0000250|UniProtKB:Q5RJQ4}.
MOD_RES 368 368 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 372 372 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
VAR_SEQ 1 37 Missing (in isoform 2).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_008729.
VAR_SEQ 6 76 PSDPLETQAGKVQEAQDSDSDTEGGATGGEAEMDFLRNLFT
QTLGLGSQKERLLDELTLEGVTRYMQSERC -> R (in
isoform 4). {ECO:0000305}.
/FTId=VSP_055329.
VAR_SEQ 236 389 Missing (in isoform 3).
{ECO:0000303|PubMed:24177535}.
/FTId=VSP_055330.
MUTAGEN 187 187 H->A: Abolishes deacetylation of FOXO3.
Does not inhibit interaction with FOXO3.
{ECO:0000269|PubMed:17521387,
ECO:0000269|PubMed:21841822}.
CONFLICT 230 230 P -> L (in Ref. 1; AAG32038).
{ECO:0000305}.
CONFLICT 241 241 S -> P (in Ref. 5; AAH21439).
{ECO:0000305}.
SEQUENCE 389 AA; 43256 MW; 15F96635445A1BC0 CRC64;
MAEPDPSDPL ETQAGKVQEA QDSDSDTEGG ATGGEAEMDF LRNLFTQTLG LGSQKERLLD
ELTLEGVTRY MQSERCRKVI CLVGAGISTS AGIPDFRSPS TGLYANLEKY HLPYPEAIFE
ISYFKKHPEP FFALAKELYP GQFKPTICHY FIRLLKEKGL LLRCYTQNID TLERVAGLEP
QDLVEAHGTF YTSHCVNTSC RKEYTMGWMK EKIFSEATPR CEQCQSVVKP DIVFFGENLP
SRFFSCMQSD FSKVDLLIIM GTSLQVQPFA SLISKAPLAT PRLLINKEKT GQTDPFLGMM
MGLGGGMDFD SKKAYRDVAW LGDCDQGCLA LADLLGWKKE LEDLVRREHA NIDAQSGSQA
PNPSTTISPG KSPPPAKEAA RTKEKEEQQ


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