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Q8R104 (SIR3_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 96. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
NAD-dependent protein deacetylase sirtuin-3
EC=3.5.1.-
Alternative name(s):
Regulatory protein SIR2 homolog 3
SIR2-like protein 3
Short name=mSIR2L3
Gene names
Name:Sirt3
Synonyms:Sir2l3
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length257 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

NAD-dependent protein deacetylase. Activates mitochondrial target proteins, including ACSS1, IDH2 and GDH by deacetylating key lysine residues By similarity. Contributes to the regulation of the cellular energy metabolism. Important for regulating tissue-specific ATP levels. Ref.4 Ref.5 Ref.6

Catalytic activity

NAD+ + an acetylprotein = nicotinamide + O-acetyl-ADP-ribose + a protein.

Cofactor

Binds 1 zinc ion per subunit By similarity.

Subunit structure

Interacts with NDUFA9, ACSS1, IDH2 and GDH By similarity.

Subcellular location

Cytoplasm. Mitochondrion matrix Probable Ref.1.

Tissue specificity

Strongly expressed in liver and kidney. Weakly expressed in lung. Ref.1

Disruption phenotype

No visible phenotype, but in vivo ATP levels are reduced by 50 % in organs that normally express high levels of this protein. ATP levels are unchanged in organs that normally express low levels of this protein. Leads to increased mitochondrial protein acetylation. Ref.6

Miscellaneous

Has some ability to deacetylate histones in vitro, but seeing its subcellular location, this is unlikely in vivo By similarity.

Sequence similarities

Belongs to the sirtuin family. Class I subfamily.

Contains 1 deacetylase sirtuin-type domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 257257NAD-dependent protein deacetylase sirtuin-3
PRO_0000110263

Regions

Domain1 – 240240Deacetylase sirtuin-type
Nucleotide binding3 – 2321NAD By similarity
Nucleotide binding86 – 894NAD By similarity
Nucleotide binding177 – 1793NAD By similarity
Nucleotide binding202 – 2043NAD By similarity

Sites

Active site1061Proton acceptor By similarity
Metal binding1141Zinc By similarity
Metal binding1171Zinc By similarity
Metal binding1381Zinc By similarity
Metal binding1411Zinc By similarity
Binding site2241NAD; via amide nitrogen By similarity

Experimental info

Sequence conflict1391P → A in AAG39258. Ref.1
Sequence conflict1391P → A in AAG33227. Ref.1
Sequence conflict1391P → A in AAG39257. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q8R104 [UniParc].

Last modified June 1, 2002. Version 1.
Checksum: F756041FBC9B985E

FASTA25728,822
        10         20         30         40         50         60 
MVGAGISTPS GIPDFRSPGS GLYSNLQQYD IPYPEAIFEL GFFFHNPKPF FMLAKELYPG 

        70         80         90        100        110        120 
HYRPNVTHYF LRLLHDKELL LRLYTQNIDG LERASGIPAS KLVEAHGTFV TATCTVCRRS 

       130        140        150        160        170        180 
FPGEDIWADV MADRVPRCPV CTGVVKPDIV FFGEQLPARF LLHMADFALA DLLLILGTSL 

       190        200        210        220        230        240 
EVEPFASLSE AVQKSVPRLL INRDLVGPFV LSPRRKDVVQ LGDVVHGVER LVDLLGWTQE 

       250 
LLDLMQRERG KLDGQDR

« Hide

References

« Hide 'large scale' references
[1]"Cloning and characterization of two mouse genes with homology to the yeast sir2 gene."
Yang Y.H., Chen Y.H., Zhang C.Y., Nimmakayalu M.A., Ward D.C., Weissman S.
Genomics 69:355-369(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
Strain: 129/Ola.
[2]"The transcriptional landscape of the mammalian genome."
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. expand/collapse author list , 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.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Tongue.
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Mammary tumor.
[4]"Sirtuins deacetylate and activate mammalian acetyl-CoA synthetases."
Hallows W.C., Lee S., Denu J.M.
Proc. Natl. Acad. Sci. U.S.A. 103:10230-10235(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[5]"Mammalian Sir2 homolog SIRT3 regulates global mitochondrial lysine acetylation."
Lombard D.B., Alt F.W., Cheng H.L., Bunkenborg J., Streeper R.S., Mostoslavsky R., Kim J., Yancopoulos G., Valenzuela D., Murphy A., Yang Y., Chen Y., Hirschey M.D., Bronson R.T., Haigis M., Guarente L.P., Farese R.V. Jr., Weissman S., Verdin E., Schwer B.
Mol. Cell. Biol. 27:8807-8814(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[6]"A role for the mitochondrial deacetylase Sirt3 in regulating energy homeostasis."
Ahn B.-H., Kim H.-S., Song S., Lee I.H., Liu J., Vassilopoulos A., Deng C.-X., Finkel T.
Proc. Natl. Acad. Sci. U.S.A. 105:14447-14452(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE, FUNCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF299339 mRNA. Translation: AAG39258.1.
AF302278 expand/collapse EMBL AC list , AF302274, AF302275, AF302276, AF302277 Genomic DNA. Translation: AAG33227.1.
AF299338 mRNA. Translation: AAG39257.1.
AK075861 mRNA. Translation: BAC36012.1.
BC025878 mRNA. Translation: AAH25878.1.
IPIIPI00317989.
RefSeqNP_001120823.1. NM_001127351.1.
NP_001171275.1. NM_001177804.1.
NP_071878.2. NM_022433.2.
UniGeneMm.244216.

3D structure databases

ProteinModelPortalQ8R104.
SMRQ8R104. Positions 1-252.
ModBaseSearch...

Proteomic databases

PaxDbQ8R104.
PRIDEQ8R104.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000026559; ENSMUSP00000026559; ENSMUSG00000025486.
ENSMUST00000106048; ENSMUSP00000101663; ENSMUSG00000025486.
GeneID64384.
KEGGmmu:64384.

Organism-specific databases

CTD23410.
MGIMGI:1927665. Sirt3.

Phylogenomic databases

eggNOGCOG0846.
GeneTreeENSGT00680000099776.
HOVERGENHBG057095.
InParanoidQ8R104.
KOK11413.
OMAAHYFLRL.
OrthoDBEOG4MKNH4.

Gene expression databases

ArrayExpressQ8R104.
BgeeQ8R104.
GenevestigatorQ8R104.
GermOnlineENSMUSG00000025486. Mus musculus.

Family and domain databases

Gene3D3.30.1600.10. 2 hits.
InterProIPR017328. NAD-dep_deAcase_SIR2_class_I.
IPR003000. Sirtuin.
IPR026591. Sirtuin_cat_small_dom.
IPR026590. Ssirtuin_cat_dom.
[Graphical view]
PANTHERPTHR11085. PTHR11085. 1 hit.
PfamPF02146. SIR2. 1 hit.
[Graphical view]
PIRSFPIRSF037938. SIR2_euk. 1 hit.
PROSITEPS50305. SIRTUIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSSIRT3. mouse.
NextBio320063.
SOURCESearch...

Entry information

Entry nameSIR3_MOUSE
AccessionPrimary (citable) accession number: Q8R104
Secondary accession number(s): Q9EPA8
Entry history
Integrated into UniProtKB/Swiss-Prot: October 31, 2003
Last sequence update: June 1, 2002
Last modified: April 3, 2013
This is version 96 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents