GenomeNet

Database: UniProt
Entry: A0A2Y9PKW1_DELLE
LinkDB: A0A2Y9PKW1_DELLE
Original site: A0A2Y9PKW1_DELLE 
ID   A0A2Y9PKW1_DELLE        Unreviewed;       735 AA.
AC   A0A2Y9PKW1;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=NAD-dependent protein deacetylase sirtuin-1 isoform X1 {ECO:0000313|RefSeq:XP_022446410.1};
GN   Name=SIRT1 {ECO:0000313|RefSeq:XP_022446410.1};
OS   Delphinapterus leucas (Beluga whale).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC   Monodontidae; Delphinapterus.
OX   NCBI_TaxID=9749 {ECO:0000313|Proteomes:UP000248483, ECO:0000313|RefSeq:XP_022446410.1};
RN   [1] {ECO:0000313|RefSeq:XP_022446410.1}
RP   IDENTIFICATION.
RC   TISSUE=Blood {ECO:0000313|RefSeq:XP_022446410.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
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DR   RefSeq; XP_022446410.1; XM_022590702.2.
DR   AlphaFoldDB; A0A2Y9PKW1; -.
DR   STRING; 9749.A0A2Y9PKW1; -.
DR   Ensembl; ENSDLET00000018290; ENSDLEP00000016581; ENSDLEG00000011987.
DR   KEGG; dle:111183434; -.
DR   InParanoid; A0A2Y9PKW1; -.
DR   OrthoDB; 10545at2759; -.
DR   Proteomes; UP000248483; Unplaced.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0061773; C:eNoSc complex; IEA:Ensembl.
DR   GO; GO:0035098; C:ESC/E(Z) complex; IEA:Ensembl.
DR   GO; GO:0000791; C:euchromatin; IEA:Ensembl.
DR   GO; GO:0001650; C:fibrillar center; IEA:Ensembl.
DR   GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
DR   GO; GO:0005637; C:nuclear inner membrane; IEA:Ensembl.
DR   GO; GO:0016605; C:PML body; IEA:Ensembl.
DR   GO; GO:0033553; C:rDNA heterochromatin; IEA:Ensembl.
DR   GO; GO:0043425; F:bHLH transcription factor binding; IEA:Ensembl.
DR   GO; GO:0140937; F:histone H4K12 deacetylase activity; IEA:Ensembl.
DR   GO; GO:0043398; F:HLH domain binding; IEA:Ensembl.
DR   GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR   GO; GO:1990254; F:keratin filament binding; IEA:Ensembl.
DR   GO; GO:0070577; F:lysine-acetylated histone binding; IEA:Ensembl.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0051019; F:mitogen-activated protein kinase binding; IEA:Ensembl.
DR   GO; GO:0070403; F:NAD+ binding; IEA:InterPro.
DR   GO; GO:0160012; F:NAD-dependent histone decrotonylase activity; IEA:Ensembl.
DR   GO; GO:0032041; F:NAD-dependent histone H3K14 deacetylase activity; IEA:Ensembl.
DR   GO; GO:0046969; F:NAD-dependent histone H3K9 deacetylase activity; IEA:Ensembl.
DR   GO; GO:0046970; F:NAD-dependent histone H4K16 deacetylase activity; IEA:Ensembl.
DR   GO; GO:0016922; F:nuclear receptor binding; IEA:Ensembl.
DR   GO; GO:0002039; F:p53 binding; IEA:Ensembl.
DR   GO; GO:1990841; F:promoter-specific chromatin binding; IEA:Ensembl.
DR   GO; GO:0106231; F:protein-propionyllysine depropionylase activity; IEA:Ensembl.
DR   GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IEA:Ensembl.
DR   GO; GO:0003713; F:transcription coactivator activity; IEA:Ensembl.
DR   GO; GO:0003714; F:transcription corepressor activity; IEA:Ensembl.
DR   GO; GO:0001525; P:angiogenesis; IEA:Ensembl.
DR   GO; GO:0042595; P:behavioral response to starvation; IEA:Ensembl.
DR   GO; GO:0042149; P:cellular response to glucose starvation; IEA:Ensembl.
DR   GO; GO:0070301; P:cellular response to hydrogen peroxide; IEA:Ensembl.
DR   GO; GO:0071456; P:cellular response to hypoxia; IEA:Ensembl.
DR   GO; GO:0071479; P:cellular response to ionizing radiation; IEA:Ensembl.
DR   GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEA:Ensembl.
DR   GO; GO:0071356; P:cellular response to tumor necrosis factor; IEA:Ensembl.
DR   GO; GO:0042632; P:cholesterol homeostasis; IEA:Ensembl.
DR   GO; GO:0032922; P:circadian regulation of gene expression; IEA:Ensembl.
DR   GO; GO:0140861; P:DNA repair-dependent chromatin remodeling; IEA:Ensembl.
DR   GO; GO:0000731; P:DNA synthesis involved in DNA repair; IEA:Ensembl.
DR   GO; GO:0097009; P:energy homeostasis; IEA:Ensembl.
DR   GO; GO:0055089; P:fatty acid homeostasis; IEA:Ensembl.
DR   GO; GO:0001678; P:intracellular glucose homeostasis; IEA:Ensembl.
DR   GO; GO:0035356; P:intracellular triglyceride homeostasis; IEA:Ensembl.
DR   GO; GO:0042771; P:intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator; IEA:Ensembl.
DR   GO; GO:0033210; P:leptin-mediated signaling pathway; IEA:Ensembl.
DR   GO; GO:0030225; P:macrophage differentiation; IEA:Ensembl.
DR   GO; GO:0051658; P:maintenance of nucleus location; IEA:Ensembl.
DR   GO; GO:0060766; P:negative regulation of androgen receptor signaling pathway; IEA:Ensembl.
DR   GO; GO:0043124; P:negative regulation of canonical NF-kappaB signal transduction; IEA:Ensembl.
DR   GO; GO:0045786; P:negative regulation of cell cycle; IEA:Ensembl.
DR   GO; GO:2000655; P:negative regulation of cellular response to testosterone stimulus; IEA:Ensembl.
DR   GO; GO:2000773; P:negative regulation of cellular senescence; IEA:Ensembl.
DR   GO; GO:0043518; P:negative regulation of DNA damage response, signal transduction by p53 class mediator; IEA:Ensembl.
DR   GO; GO:0045599; P:negative regulation of fat cell differentiation; IEA:Ensembl.
DR   GO; GO:1902166; P:negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator; IEA:Ensembl.
DR   GO; GO:0043524; P:negative regulation of neuron apoptotic process; IEA:Ensembl.
DR   GO; GO:1902176; P:negative regulation of oxidative stress-induced intrinsic apoptotic signaling pathway; IEA:Ensembl.
DR   GO; GO:2000757; P:negative regulation of peptidyl-lysine acetylation; IEA:Ensembl.
DR   GO; GO:0051898; P:negative regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction; IEA:Ensembl.
DR   GO; GO:0042326; P:negative regulation of phosphorylation; IEA:Ensembl.
DR   GO; GO:0031393; P:negative regulation of prostaglandin biosynthetic process; IEA:Ensembl.
DR   GO; GO:0032007; P:negative regulation of TOR signaling; IEA:Ensembl.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR   GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; IEA:Ensembl.
DR   GO; GO:0010868; P:negative regulation of triglyceride biosynthetic process; IEA:Ensembl.
DR   GO; GO:0001542; P:ovulation from ovarian follicle; IEA:Ensembl.
DR   GO; GO:0002821; P:positive regulation of adaptive immune response; IEA:Ensembl.
DR   GO; GO:1904179; P:positive regulation of adipose tissue development; IEA:Ensembl.
DR   GO; GO:0045766; P:positive regulation of angiogenesis; IEA:Ensembl.
DR   GO; GO:0043536; P:positive regulation of blood vessel endothelial cell migration; IEA:Ensembl.
DR   GO; GO:2000774; P:positive regulation of cellular senescence; IEA:Ensembl.
DR   GO; GO:0010875; P:positive regulation of cholesterol efflux; IEA:Ensembl.
DR   GO; GO:2000781; P:positive regulation of double-strand break repair; IEA:Ensembl.
DR   GO; GO:1902237; P:positive regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway; IEA:Ensembl.
DR   GO; GO:0001938; P:positive regulation of endothelial cell proliferation; IEA:Ensembl.
DR   GO; GO:0045722; P:positive regulation of gluconeogenesis; IEA:Ensembl.
DR   GO; GO:0031065; P:positive regulation of histone deacetylation; IEA:Ensembl.
DR   GO; GO:0046628; P:positive regulation of insulin receptor signaling pathway; IEA:Ensembl.
DR   GO; GO:0016239; P:positive regulation of macroautophagy; IEA:Ensembl.
DR   GO; GO:2000111; P:positive regulation of macrophage apoptotic process; IEA:Ensembl.
DR   GO; GO:0060907; P:positive regulation of macrophage cytokine production; IEA:Ensembl.
DR   GO; GO:0045348; P:positive regulation of MHC class II biosynthetic process; IEA:Ensembl.
DR   GO; GO:0051897; P:positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction; IEA:Ensembl.
DR   GO; GO:0001934; P:positive regulation of protein phosphorylation; IEA:Ensembl.
DR   GO; GO:0051152; P:positive regulation of smooth muscle cell differentiation; 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:0031648; P:protein destabilization; IEA:Ensembl.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:Ensembl.
DR   GO; GO:0000720; P:pyrimidine dimer repair by nucleotide-excision repair; IEA:Ensembl.
DR   GO; GO:0000183; P:rDNA heterochromatin formation; IEA:Ensembl.
DR   GO; GO:0070857; P:regulation of bile acid biosynthetic process; IEA:Ensembl.
DR   GO; GO:0090335; P:regulation of brown fat cell differentiation; IEA:Ensembl.
DR   GO; GO:0010824; P:regulation of centrosome duplication; IEA:Ensembl.
DR   GO; GO:0010883; P:regulation of lipid storage; IEA:Ensembl.
DR   GO; GO:0007346; P:regulation of mitotic cell cycle; IEA:Ensembl.
DR   GO; GO:0035358; P:regulation of peroxisome proliferator activated receptor signaling pathway; IEA:Ensembl.
DR   GO; GO:0034391; P:regulation of smooth muscle cell apoptotic process; IEA:Ensembl.
DR   GO; GO:0046015; P:regulation of transcription by glucose; IEA:Ensembl.
DR   GO; GO:0032868; P:response to insulin; IEA:Ensembl.
DR   GO; GO:0000012; P:single strand break repair; IEA:Ensembl.
DR   GO; GO:0007283; P:spermatogenesis; IEA:Ensembl.
DR   GO; GO:0090400; P:stress-induced premature senescence; IEA:Ensembl.
DR   GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IEA:Ensembl.
DR   GO; GO:0006642; P:triglyceride mobilization; IEA:Ensembl.
DR   GO; GO:0070914; P:UV-damage excision repair; IEA:Ensembl.
DR   GO; GO:0050872; P:white fat cell differentiation; IEA:Ensembl.
DR   CDD; cd01408; SIRT1; 1.
DR   Gene3D; 3.30.1600.10; SIR2/SIRT2 'Small Domain; 1.
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; IPR026590; Ssirtuin_cat_dom.
DR   PANTHER; PTHR11085:SF14; NAD-DEPENDENT PROTEIN DEACETYLASE SIRTUIN-1; 1.
DR   PANTHER; PTHR11085; NAD-DEPENDENT PROTEIN DEACYLASE SIRTUIN-5, MITOCHONDRIAL-RELATED; 1.
DR   Pfam; PF02146; SIR2; 1.
DR   SUPFAM; SSF52467; DHS-like NAD/FAD-binding domain; 1.
DR   PROSITE; PS50305; SIRTUIN; 1.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00236};
KW   NAD {ECO:0000256|ARBA:ARBA00023027};
KW   Reference proteome {ECO:0000313|Proteomes:UP000248483};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU00236}.
FT   DOMAIN          222..482
FT                   /note="Deacetylase sirtuin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50305"
FT   REGION          1..127
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          144..164
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          508..534
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          571..606
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          651..712
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        28..43
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        101..121
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        144..158
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        517..534
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        571..601
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        651..674
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        675..691
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        349
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
FT   BINDING         357
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
FT   BINDING         360
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
FT   BINDING         381
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
FT   BINDING         384
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00236"
SQ   SEQUENCE   735 AA;  80466 MW;  5F613F27CE4034F2 CRC64;
     MADEAALAFQ PGGSPSAVTA EREAPSPPAG EPLRKRPRRD GPGVGRSPGE PGGAAPEREL
     PAAAGGCPAA ALRREAQAAA AGEGDNGPGL QGLSREAPPA DDFYDDDDDD DDDDEGEEEE
     EAAAAIGYRD NLLFGDEIIT NGFHSCESDE DDRASHASSS DWTPRPRIGP YTFVQQHLMI
     GTDPRTILKD LLPETIPPPE LDDMTLWQIV INILSEPPKR KKRKDINTIE DAVKLLQECK
     KIIVLTGAGV SVSCGIPDFR SRDGIYARLA VDFPDLPDPQ AMFDIEYFRK DPRPFFKFAK
     EIYPGQFQPS LCHKFIALSD KEGKLLRNYT QNIDTLEQVA GIQRIIQCHG SFATASCLIC
     KYKVDCEAVR GDIFNQVVPR CPRCPADEPL AIMKPEIVFF GENLPEQFHR AMKYDKDEVD
     LLIVIGSSLK VRPVALIPSS IPHEVPQILI NREPLPHLHF DVELLGDCDV IINELCHRLG
     GEYAKLCCNP VKLSEITEKP PRTQKELAHL SELPPTPLNI SEGSSSPEGT SPADSSVIVT
     LLDQETKSNV DDPDASESKN CVEEKLQEVQ TSARSIESVN EQLESPDLKN VASNTGEKNE
     RTSVAETVRK CWPARLAKEQ ISKRLDGNQY LFLPPNRYIF HGAEVYSDSE DDVLSSSSCG
     SNSDSGTCQS PSLEEPMEDE SEIEEFYNGL EDDADVNERA GATGFGADGG DQEAVNEATS
     MKQEATCINY PSNKS
//
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