SAT2_MOUSE
ID SAT2_MOUSE Reviewed; 170 AA.
AC Q6P8J2; Q5F299;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Thialysine N-epsilon-acetyltransferase {ECO:0000305};
DE EC=2.3.1.- {ECO:0000250|UniProtKB:Q96F10};
DE AltName: Full=Diamine acetyltransferase 2 {ECO:0000250|UniProtKB:Q96F10};
DE EC=2.3.1.57 {ECO:0000250|UniProtKB:Q96F10};
DE AltName: Full=Spermidine/spermine N(1)-acetyltransferase 2 {ECO:0000250|UniProtKB:Q96F10};
DE Short=SSAT-2 {ECO:0000250|UniProtKB:Q96F10};
GN Name=Sat2 {ECO:0000312|MGI:MGI:1916465};
GN Synonyms=Ssat2 {ECO:0000250|UniProtKB:Q96F10};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, Liver, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [4]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-29, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
CC -!- FUNCTION: Catalyzes the N-acetylation of the amino acid thialysine (S-
CC (2-aminoethyl)-L-cysteine), a L-lysine analog with the 4-methylene
CC group substituted with a sulfur. May also catalyze acetylation of
CC polyamines, such as norspermidine, spermidine or spermine. However,
CC ability to acetylate polyamines is weak, suggesting that it does not
CC act as a diamine acetyltransferase in vivo.
CC {ECO:0000250|UniProtKB:Q96F10}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + S-(2-aminoethyl)-L-cysteine = CoA + H(+) + S-(2-
CC acetamidoethyl)-L-cysteine; Xref=Rhea:RHEA:64804, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:156132,
CC ChEBI:CHEBI:156134; Evidence={ECO:0000250|UniProtKB:Q96F10};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64805;
CC Evidence={ECO:0000250|UniProtKB:Q96F10};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + an alkane-alpha,omega-diamine = an N-
CC acetylalkane-alpha,omega-diamine + CoA + H(+); Xref=Rhea:RHEA:11116,
CC Rhea:RHEA-COMP:9766, Rhea:RHEA-COMP:9767, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:70977,
CC ChEBI:CHEBI:70988; EC=2.3.1.57;
CC Evidence={ECO:0000250|UniProtKB:Q96F10};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q96F10}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q96F10}.
CC Note=Intracellular organelles. {ECO:0000250|UniProtKB:Q96F10}.
CC -!- SIMILARITY: Belongs to the acetyltransferase family. {ECO:0000305}.
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DR EMBL; AL603707; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL731687; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC061227; AAH61227.1; -; mRNA.
DR CCDS; CCDS36194.1; -.
DR RefSeq; NP_081267.1; NM_026991.2.
DR RefSeq; XP_006534175.1; XM_006534112.3.
DR AlphaFoldDB; Q6P8J2; -.
DR SMR; Q6P8J2; -.
DR BioGRID; 213297; 2.
DR STRING; 10090.ENSMUSP00000104296; -.
DR ChEMBL; CHEMBL3794; -.
DR iPTMnet; Q6P8J2; -.
DR PhosphoSitePlus; Q6P8J2; -.
DR jPOST; Q6P8J2; -.
DR MaxQB; Q6P8J2; -.
DR PaxDb; Q6P8J2; -.
DR PRIDE; Q6P8J2; -.
DR ProteomicsDB; 253398; -.
DR Antibodypedia; 12120; 155 antibodies from 21 providers.
DR Ensembl; ENSMUST00000092969; ENSMUSP00000090647; ENSMUSG00000069835.
DR Ensembl; ENSMUST00000108656; ENSMUSP00000104296; ENSMUSG00000069835.
DR GeneID; 69215; -.
DR KEGG; mmu:69215; -.
DR UCSC; uc007jqq.1; mouse.
DR CTD; 112483; -.
DR MGI; MGI:1916465; Sat2.
DR VEuPathDB; HostDB:ENSMUSG00000069835; -.
DR eggNOG; KOG3216; Eukaryota.
DR GeneTree; ENSGT00950000183121; -.
DR HOGENOM; CLU_013985_41_1_1; -.
DR InParanoid; Q6P8J2; -.
DR OMA; RYSTWKG; -.
DR OrthoDB; 1228251at2759; -.
DR PhylomeDB; Q6P8J2; -.
DR TreeFam; TF319736; -.
DR BioGRID-ORCS; 69215; 2 hits in 70 CRISPR screens.
DR ChiTaRS; Sat2; mouse.
DR PRO; PR:Q6P8J2; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q6P8J2; protein.
DR Bgee; ENSMUSG00000069835; Expressed in otolith organ and 200 other tissues.
DR ExpressionAtlas; Q6P8J2; baseline and differential.
DR Genevisible; Q6P8J2; MM.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004145; F:diamine N-acetyltransferase activity; ISA:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0008080; F:N-acetyltransferase activity; ISS:UniProtKB.
DR GO; GO:0019809; F:spermidine binding; IBA:GO_Central.
DR GO; GO:0046204; P:nor-spermidine metabolic process; ISO:MGI.
DR GO; GO:0032920; P:putrescine acetylation; ISO:MGI.
DR GO; GO:0032918; P:spermidine acetylation; IBA:GO_Central.
DR GO; GO:0008216; P:spermidine metabolic process; ISA:MGI.
DR GO; GO:0032919; P:spermine acetylation; ISO:MGI.
DR GO; GO:0008215; P:spermine metabolic process; ISA:MGI.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR000182; GNAT_dom.
DR InterPro; IPR032959; SAT2.
DR PANTHER; PTHR10545:SF51; PTHR10545:SF51; 1.
DR Pfam; PF00583; Acetyltransf_1; 1.
DR SUPFAM; SSF55729; SSF55729; 1.
DR PROSITE; PS51186; GNAT; 1.
PE 1: Evidence at protein level;
KW Acetylation; Acyltransferase; Cytoplasm; Reference proteome; Transferase.
FT CHAIN 1..170
FT /note="Thialysine N-epsilon-acetyltransferase"
FT /id="PRO_0000074599"
FT DOMAIN 4..166
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT ACT_SITE 140
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P0A951"
FT BINDING 27..28
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P21673"
FT BINDING 92
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P21673"
FT BINDING 94..96
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q96F10"
FT BINDING 102..107
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q96F10"
FT BINDING 133..135
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q96F10"
FT BINDING 140
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q96F10"
FT BINDING 152
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P21673"
FT MOD_RES 29
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
SQ SEQUENCE 170 AA; 19305 MW; 5D82F98DAD0619AA CRC64;
MASTRIREAR ESDCGDIMRM IRELAEFEKL SHQVKISEEA LRADGFGENP FFHCLVAEII
PAPGESQGSL VVGYGLYYFI YSTWTGRNVY LEDIYVMPQY RGQGIGTKII KKVAEVALNK
GCSQFRLAVL DWNKKAVNLY KFLGAQDLTE SEGWLSFRFE GEAMRELAGR
