ID A0A384BWD1_URSMA Unreviewed; 471 AA.
AC A0A384BWD1;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=NAD-dependent protein deacetylase sirtuin-2 {ECO:0000256|ARBA:ARBA00040697};
DE EC=2.3.1.286 {ECO:0000256|ARBA:ARBA00012928};
DE AltName: Full=NAD-dependent protein defatty-acylase sirtuin-2 {ECO:0000256|ARBA:ARBA00042077};
DE AltName: Full=Regulatory protein SIR2 homolog 2 {ECO:0000256|ARBA:ARBA00043039};
DE AltName: Full=SIR2-like protein 2 {ECO:0000256|ARBA:ARBA00041829};
GN Name=LOC103661014 {ECO:0000313|RefSeq:XP_008686901.1};
GN Synonyms=SIRT2 {ECO:0000313|Ensembl:ENSUMAP00000026386};
OS Ursus maritimus (Polar bear) (Thalarctos maritimus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ursus.
OX NCBI_TaxID=29073 {ECO:0000313|Proteomes:UP000261680, ECO:0000313|RefSeq:XP_008686901.1};
RN [1] {ECO:0000313|Ensembl:ENSUMAP00000026386}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (MAR-2019) to UniProtKB.
RN [2] {ECO:0000313|RefSeq:XP_008686901.1}
RP IDENTIFICATION.
RC TISSUE=Whole blood {ECO:0000313|RefSeq:XP_008686901.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N(6)-hexadecanoyl-L-lysyl-[protein] + NAD(+) = 2''-O-
CC hexadecanoyl-ADP-D-ribose + L-lysyl-[protein] + nicotinamide;
CC Xref=Rhea:RHEA:70563, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:14175,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:17154, ChEBI:CHEBI:29969,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:138936, ChEBI:CHEBI:189673;
CC Evidence={ECO:0000256|ARBA:ARBA00036899};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70564;
CC Evidence={ECO:0000256|ARBA:ARBA00036899};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N(6)-tetradecanoyl-L-lysyl-[protein] + NAD(+) = 2''-O-
CC tetradecanoyl-ADP-D-ribose + L-lysyl-[protein] + nicotinamide;
CC Xref=Rhea:RHEA:70567, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:15437,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:17154, ChEBI:CHEBI:29969,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:141129, ChEBI:CHEBI:189674;
CC Evidence={ECO:0000256|ARBA:ARBA00036729};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70568;
CC Evidence={ECO:0000256|ARBA:ARBA00036729};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PIRSR:PIRSR037938-3};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR037938-3};
CC -!- SUBCELLULAR LOCATION: Myelin membrane {ECO:0000256|ARBA:ARBA00037844}.
CC -!- SIMILARITY: Belongs to the sirtuin family. Class I subfamily.
CC {ECO:0000256|ARBA:ARBA00006924}.
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DR RefSeq; XP_008686901.1; XM_008688679.2.
DR STRING; 29073.ENSUMAP00000026386; -.
DR Ensembl; ENSUMAT00000031235.1; ENSUMAP00000026386.1; ENSUMAG00000019203.1.
DR GeneID; 103661014; -.
DR KEGG; umr:103661014; -.
DR OrthoDB; 10545at2759; -.
DR Proteomes; UP000261680; Unplaced.
DR GO; GO:0005814; C:centriole; IEA:Ensembl.
DR GO; GO:0005813; C:centrosome; IEA:Ensembl.
DR GO; GO:0005694; C:chromosome; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0072687; C:meiotic spindle; IEA:Ensembl.
DR GO; GO:0005874; C:microtubule; IEA:Ensembl.
DR GO; GO:0030496; C:midbody; IEA:Ensembl.
DR GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
DR GO; GO:0072686; C:mitotic spindle; IEA:Ensembl.
DR GO; GO:0005730; C:nucleolus; IEA:Ensembl.
DR GO; GO:0033010; C:paranodal junction; IEA:Ensembl.
DR GO; GO:0043204; C:perikaryon; IEA:Ensembl.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0043220; C:Schmidt-Lanterman incisure; IEA:Ensembl.
DR GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; IEA:Ensembl.
DR GO; GO:0035035; F:histone acetyltransferase binding; IEA:Ensembl.
DR GO; GO:0042826; F:histone deacetylase binding; IEA:Ensembl.
DR GO; GO:0003950; F:NAD+ ADP-ribosyltransferase activity; IEA:Ensembl.
DR GO; GO:0070403; F:NAD+ binding; IEA:Ensembl.
DR GO; GO:0046970; F:NAD-dependent histone H4K16 deacetylase activity; IEA:Ensembl.
DR GO; GO:0140773; F:NAD-dependent protein demyristoylase activity; IEA:Ensembl.
DR GO; GO:0140774; F:NAD-dependent protein depalmitoylase activity; IEA:Ensembl.
DR GO; GO:0042903; F:tubulin deacetylase activity; IEA:Ensembl.
DR GO; GO:0043130; F:ubiquitin binding; IEA:Ensembl.
DR GO; GO:0008270; F:zinc ion binding; IEA:Ensembl.
DR GO; GO:0044242; P:cellular lipid catabolic process; IEA:Ensembl.
DR GO; GO:0061433; P:cellular response to caloric restriction; IEA:Ensembl.
DR GO; GO:0071872; P:cellular response to epinephrine stimulus; IEA:Ensembl.
DR GO; GO:0071456; P:cellular response to hypoxia; IEA:Ensembl.
DR GO; GO:0034599; P:cellular response to oxidative stress; IEA:Ensembl.
DR GO; GO:0040029; P:epigenetic regulation of gene expression; IEA:Ensembl.
DR GO; GO:0022011; P:myelination in peripheral nervous system; IEA:Ensembl.
DR GO; GO:0010507; P:negative regulation of autophagy; IEA:Ensembl.
DR GO; GO:0045599; P:negative regulation of fat cell differentiation; IEA:Ensembl.
DR GO; GO:1900226; P:negative regulation of NLRP3 inflammasome complex assembly; IEA:Ensembl.
DR GO; GO:0010801; P:negative regulation of peptidyl-threonine phosphorylation; IEA:Ensembl.
DR GO; GO:0042177; P:negative regulation of protein catabolic process; IEA:Ensembl.
DR GO; GO:2000378; P:negative regulation of reactive oxygen species metabolic process; IEA:Ensembl.
DR GO; GO:0045843; P:negative regulation of striated muscle tissue development; IEA:Ensembl.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0044546; P:NLRP3 inflammasome complex assembly; IEA:Ensembl.
DR GO; GO:0051987; P:positive regulation of attachment of spindle microtubules to kinetochore; IEA:Ensembl.
DR GO; GO:0051781; P:positive regulation of cell division; IEA:Ensembl.
DR GO; GO:1900119; P:positive regulation of execution phase of apoptosis; IEA:Ensembl.
DR GO; GO:0045723; P:positive regulation of fatty acid biosynthetic process; IEA:Ensembl.
DR GO; GO:0045836; P:positive regulation of meiotic nuclear division; IEA:Ensembl.
DR GO; GO:1900195; P:positive regulation of oocyte maturation; IEA:Ensembl.
DR GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IEA:Ensembl.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IEA:Ensembl.
DR GO; GO:0031641; P:regulation of myelination; IEA:Ensembl.
DR CDD; cd01408; SIRT1; 1.
DR Gene3D; 3.30.1600.10; SIR2/SIRT2 'Small Domain; 2.
DR Gene3D; 3.40.50.1220; TPP-binding domain; 1.
DR InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
DR InterPro; IPR003000; Sirtuin.
DR InterPro; IPR026591; Sirtuin_cat_small_dom_sf.
DR InterPro; IPR017328; Sirtuin_class_I.
DR InterPro; IPR026590; Ssirtuin_cat_dom.
DR PANTHER; PTHR11085:SF10; NAD-DEPENDENT PROTEIN DEACETYLASE SIRTUIN-2; 1.
DR PANTHER; PTHR11085; NAD-DEPENDENT PROTEIN DEACYLASE SIRTUIN-5, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF02146; SIR2; 2.
DR PIRSF; PIRSF037938; SIR2_euk; 2.
DR SUPFAM; SSF52467; DHS-like NAD/FAD-binding domain; 1.
DR PROSITE; PS50305; SIRTUIN; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|PIRSR:PIRSR037938-3, ECO:0000256|PROSITE-
KW ProRule:PRU00236};
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|PIRSR:PIRSR037938-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000261680};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR037938-3}.
FT DOMAIN 57..420
FT /note="Deacetylase sirtuin-type"
FT /evidence="ECO:0000259|PROSITE:PS50305"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 434..471
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 456..471
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 187
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR037938-1,
FT ECO:0000256|PROSITE-ProRule:PRU00236"
FT BINDING 85..89
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR037938-2"
FT BINDING 95..97
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR037938-2"
FT BINDING 167..170
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR037938-2"
FT BINDING 195
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR037938-3,
FT ECO:0000256|PROSITE-ProRule:PRU00236"
FT BINDING 200
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR037938-3,
FT ECO:0000256|PROSITE-ProRule:PRU00236"
FT BINDING 303
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR037938-3,
FT ECO:0000256|PROSITE-ProRule:PRU00236"
FT BINDING 306
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR037938-3,
FT ECO:0000256|PROSITE-ProRule:PRU00236"
FT BINDING 344..345
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR037938-2"
FT BINDING 368..370
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR037938-2"
FT BINDING 406
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR037938-2"
SQ SEQUENCE 471 AA; 52943 MW; 814842D871B34B72 CRC64;
MAEPDPSDPL ETQAGKVQEA QDSDSDTEEG AAGGEAEMDF LRNFFSQTLG LGTQKERLLD
ELTLEGVTRY MQSERCRRVI CLVGAGISTS AGIPDFRSPS TGLYANLEKY RLPYPEAIFE
IGYFKKHPEP FFALAKELYP GQFKPTVCHY FIRLLKEKGL LLRCYTQNID TLERVAGLES
EDLVEAHGTF HTSHCTSPLC RREYTLSWMK GGLRRKQAPR PIQPRAEPRV GTEAARWSRG
LFCEVVRPQL FVLRGAHERK RNDIRIHVCA VQYSGHRHMW PSGTRRCEQW YQEKIFSEVT
PKCEKCHSVV KPDIVFFGEN LPARFFSCMQ SDFLKVDLLI IMGTSLQVQP FASLISKAPL
STPRLLINKE KTGQTDPFLG MMMGLGGGMD FDSKKAYRDV AWLGDCDQGC LALADLLGWK
KELEDLVRKE HANIDAQAGS GSPNPNTCAS PRKSPPPAKE EARSTEGEKP Q
//
