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Sestrin-3

 SESN3_MOUSE             Reviewed;         492 AA.
Q9CYP7; Q3U2A0;
27-APR-2001, integrated into UniProtKB/Swiss-Prot.
27-APR-2001, sequence version 1.
05-JUL-2017, entry version 104.
RecName: Full=Sestrin-3 {ECO:0000305};
Name=Sesn3 {ECO:0000312|MGI:MGI:1922997};
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 [LARGE SCALE MRNA].
STRAIN=C57BL/6J, and NOD; 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).
[2]
DISRUPTION PHENOTYPE.
PubMed=22958918; DOI=10.1016/j.cmet.2012.08.004;
Lee J.H., Budanov A.V., Talukdar S., Park E.J., Park H.L., Park H.W.,
Bandyopadhyay G., Li N., Aghajan M., Jang I., Wolfe A.M.,
Perkins G.A., Ellisman M.H., Bier E., Scadeng M., Foretz M.,
Viollet B., Olefsky J., Karin M.;
"Maintenance of metabolic homeostasis by Sestrin2 and Sestrin3.";
Cell Metab. 16:311-321(2012).
[3]
FUNCTION, INTERACTION WITH RRAGA; RRAGB; RRAGC AND RRAGD, TISSUE
SPECIFICITY, AND DISRUPTION PHENOTYPE.
PubMed=25259925; DOI=10.1016/j.cell.2014.08.038;
Peng M., Yin N., Li M.O.;
"Sestrins function as guanine nucleotide dissociation inhibitors for
Rag GTPases to control mTORC1 signaling.";
Cell 159:122-133(2014).
[4]
FUNCTION, INTERACTION WITH TORC2 COMPLEX, SUBCELLULAR LOCATION, AND
DISRUPTION PHENOTYPE.
PubMed=25377878; DOI=10.2337/db14-0539;
Tao R., Xiong X., Liangpunsakul S., Dong X.C.;
"Sestrin 3 protein enhances hepatic insulin sensitivity by direct
activation of the mTORC2-Akt signaling.";
Diabetes 64:1211-1223(2015).
-!- FUNCTION: May function as an intracellular leucine sensor that
negatively regulates the TORC1 signaling pathway
(PubMed:25259925). May also regulate the insulin-receptor
signaling pathway through activation of TORC2 (PubMed:25377878).
This metabolic regulator may also play a role in protection
against oxidative and genotoxic stresses (By similarity).
{ECO:0000250|UniProtKB:P58004, ECO:0000269|PubMed:25259925,
ECO:0000269|PubMed:25377878}.
-!- SUBUNIT: Interacts with the GATOR2 complex which is composed of
MIOS, SEC13, SEH1L, WDR24 and WDR59; the interaction is not
regulated by leucine (By similarity). Interacts with RRAGA, RRAGB,
RRAGC and RRAGD; may function as a guanine nucleotide dissociation
inhibitor for RRAGs and regulate them (PubMed:25259925). Interacts
with the TORC2 complex; through RICTOR (PubMed:25377878).
{ECO:0000250|UniProtKB:P58005, ECO:0000269|PubMed:25259925,
ECO:0000269|PubMed:25377878}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:25377878}.
-!- TISSUE SPECIFICITY: Detected in liver and skeletal muscles.
{ECO:0000269|PubMed:25259925}.
-!- DOMAIN: The C-terminal domain may mediate interaction with GATOR2
and regulation of TORC1 signaling. {ECO:0000250|UniProtKB:P58004}.
-!- DISRUPTION PHENOTYPE: Liver-specific Sesn3 knockout mice display
insulin resistance and glucose intolerance (PubMed:25377878).
Sesn2 and Sesn3 double knockout mice display insulin resistance
and glucose intolerance (PubMed:22958918). Triple knockout mice
lacking Sesn1, Sesn2 and Sesn3 do not display an embryonic lethal
phenotype since they are born at an expected Mendelian ratio.
Moreover, they are not distinguishable from their wild-type
littermate. However, their survival at 10 days is dramatically
affected. This is associated with a constitutive activation of
TORC1 signaling in the liver, heart and skeletal muscle during
postnatal fasting, that occurs between birth and suckling
(PubMed:25259925). {ECO:0000269|PubMed:22958918,
ECO:0000269|PubMed:25259925, ECO:0000269|PubMed:25377878}.
-!- SIMILARITY: Belongs to the sestrin family. {ECO:0000305}.
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EMBL; AK017464; BAB30755.1; -; mRNA.
EMBL; AK155398; BAE33242.1; -; mRNA.
CCDS; CCDS22820.1; -.
RefSeq; NP_084537.2; NM_030261.4.
UniGene; Mm.325126; -.
UniGene; Mm.439776; -.
ProteinModelPortal; Q9CYP7; -.
SMR; Q9CYP7; -.
STRING; 10090.ENSMUSP00000034507; -.
iPTMnet; Q9CYP7; -.
PhosphoSitePlus; Q9CYP7; -.
MaxQB; Q9CYP7; -.
PaxDb; Q9CYP7; -.
PRIDE; Q9CYP7; -.
Ensembl; ENSMUST00000208222; ENSMUSP00000146362; ENSMUSG00000032009.
GeneID; 75747; -.
KEGG; mmu:75747; -.
UCSC; uc009oej.1; mouse.
CTD; 143686; -.
MGI; MGI:1922997; Sesn3.
eggNOG; KOG3746; Eukaryota.
eggNOG; ENOG410XP7Z; LUCA.
GeneTree; ENSGT00440000040103; -.
HOGENOM; HOG000232949; -.
HOVERGEN; HBG054648; -.
InParanoid; Q9CYP7; -.
KO; K10141; -.
OMA; HRHYIAI; -.
OrthoDB; EOG091G0IVA; -.
PhylomeDB; Q9CYP7; -.
TreeFam; TF314230; -.
ChiTaRS; Sesn3; mouse.
PRO; PR:Q9CYP7; -.
Proteomes; UP000000589; Chromosome 9.
Bgee; ENSMUSG00000032009; -.
CleanEx; MM_SESN3; -.
ExpressionAtlas; Q9CYP7; baseline and differential.
Genevisible; Q9CYP7; MM.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0061700; C:GATOR2 complex; IEA:Ensembl.
GO; GO:0005634; C:nucleus; IEA:InterPro.
GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
GO; GO:0034198; P:cellular response to amino acid starvation; ISS:UniProtKB.
GO; GO:0071230; P:cellular response to amino acid stimulus; IMP:UniProtKB.
GO; GO:0042149; P:cellular response to glucose starvation; ISO:MGI.
GO; GO:0042593; P:glucose homeostasis; IMP:UniProtKB.
GO; GO:1904262; P:negative regulation of TORC1 signaling; IMP:UniProtKB.
GO; GO:0046626; P:regulation of insulin receptor signaling pathway; IMP:UniProtKB.
GO; GO:0051896; P:regulation of protein kinase B signaling; IDA:MGI.
GO; GO:1901031; P:regulation of response to reactive oxygen species; IEA:InterPro.
GO; GO:0032868; P:response to insulin; IMP:UniProtKB.
GO; GO:0038203; P:TORC2 signaling; IMP:UniProtKB.
Gene3D; 1.20.1290.10; -; 1.
InterPro; IPR029032; AhpD-like.
InterPro; IPR006730; Sestrin.
Pfam; PF04636; PA26; 1.
SUPFAM; SSF69118; SSF69118; 1.
1: Evidence at protein level;
Complete proteome; Cytoplasm; Oxidoreductase; Reference proteome.
CHAIN 1 492 Sestrin-3.
/FTId=PRO_0000221184.
REGION 310 492 C-terminal domain; mediates TORC1
regulation.
{ECO:0000250|UniProtKB:P58004}.
REGION 386 389 Leucine-binding.
{ECO:0000250|UniProtKB:P58004}.
BINDING 398 398 Leucine; via carbonyl oxygen.
{ECO:0000250|UniProtKB:P58004}.
BINDING 463 463 Leucine. {ECO:0000250|UniProtKB:P58004}.
SEQUENCE 492 AA; 57021 MW; 8E8AD9CB45656827 CRC64;
MNRGGSSASA SANYLLCTNC RKVLRKDKRI RVSQPLTRGP SAFIPEKEVV QANTADERTN
FLVEEYSTSG RLDNITQVMS LHTQYLESFL RSQFYMLRMD GPLPLPDRHY IAIMAAARHQ
CSYLINMHVD EFLKTGGIAE WLNGLEYVPQ RLRNLNEINK LLAHRPWLIT KEHIQKLVKT
GENNWSLPEL VHAVVLLAHY HALASFVFGS GINPERDPGI ANGFRLISVS SFCVCDLAND
NSIENTSLAG SNFGIVDSLG ELEALMERMK RLQEDREDDE TTREEMTTRF EKEKKESLFV
VPGETLHAFP HSDFEDDVIV TADVSRYIED PSFGYEDFAR RGEEHLPTFR AQDYTWENHG
FSLVNRLYSD IGHLLDEKFR MVYNLTYNTM ATHEDVDTTT LRRALFNYVH CMFGIRYDDY
DYGEVNQLLE RSLKVYIKTV TCYPERTTKR MYDSYWRQFT HSEKVHVNLL LMEARMQAEL
LYALRAITRH LT


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