SAT1_MOUSE
ID SAT1_MOUSE Reviewed; 171 AA.
AC P48026; Q3U444;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Diamine acetyltransferase 1 {ECO:0000305};
DE EC=2.3.1.57 {ECO:0000269|PubMed:18690703};
DE AltName: Full=Polyamine N-acetyltransferase 1;
DE AltName: Full=Putrescine acetyltransferase;
DE AltName: Full=Spermidine/spermine N(1)-acetyltransferase 1 {ECO:0000303|PubMed:8241266};
DE Short=SSAT {ECO:0000303|PubMed:8241266};
DE Short=SSAT-1;
GN Name=Sat1 {ECO:0000312|MGI:MGI:98233}; Synonyms=Sat;
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 [MRNA].
RC STRAIN=BALB/cJ; TISSUE=Liver;
RX PubMed=8241266; DOI=10.1016/0167-4781(93)90152-4;
RA Fogel-Petrovic M., Kramer D.L., Ganis B., Casero R.A. Jr., Porter C.W.;
RT "Cloning and sequence analysis of the gene and cDNA encoding mouse
RT spermidine/spermine N1-acetyltransferase -- a gene uniquely regulated by
RT polyamines and their analogs.";
RL Biochim. Biophys. Acta 1216:255-264(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Kidney;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [4]
RP PROTEIN SEQUENCE OF 20-26, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH THE ACETYL-COA ANALOG
RP COENZYME A AND THE SUBSTRATE SPERMINE, MUTAGENESIS OF GLU-92 AND ASP-93,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND CATALYTIC ACTIVITY.
RX PubMed=18690703; DOI=10.1021/bi8009357;
RA Montemayor E.J., Hoffman D.W.;
RT "The crystal structure of spermidine/spermine N1-acetyltransferase in
RT complex with spermine provides insights into substrate binding and
RT catalysis.";
RL Biochemistry 47:9145-9153(2008).
CC -!- FUNCTION: Enzyme which catalyzes the acetylation of polyamines
CC (PubMed:18690703). Substrate specificity: norspermidine = spermidine >>
CC spermine > N(1)-acetylspermine (By similarity). This highly regulated
CC enzyme allows a fine attenuation of the intracellular concentration of
CC polyamines (By similarity). Also involved in the regulation of
CC polyamine transport out of cells (By similarity). Also acts on 1,3-
CC diaminopropane and 1,5-diaminopentane (By similarity).
CC {ECO:0000250|UniProtKB:P21673, ECO:0000305|PubMed:18690703}.
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:0000269|PubMed:18690703};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11117;
CC Evidence={ECO:0000269|PubMed:18690703};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + spermidine = CoA + H(+) + N(1)-acetylspermidine;
CC Xref=Rhea:RHEA:28150, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:57288, ChEBI:CHEBI:57834, ChEBI:CHEBI:58324; EC=2.3.1.57;
CC Evidence={ECO:0000269|PubMed:18690703};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:28151;
CC Evidence={ECO:0000269|PubMed:18690703};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + spermine = CoA + H(+) + N(1)-acetylspermine;
CC Xref=Rhea:RHEA:33099, ChEBI:CHEBI:15378, ChEBI:CHEBI:45725,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:58101; EC=2.3.1.57;
CC Evidence={ECO:0000250|UniProtKB:P21673};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33100;
CC Evidence={ECO:0000250|UniProtKB:P21673};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 8.5-9.5. {ECO:0000269|PubMed:18690703};
CC -!- PATHWAY: Amine and polyamine degradation; putrescine degradation; N-
CC acetylputrescine from putrescine: step 1/1.
CC {ECO:0000305|PubMed:18690703}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:18690703}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:P21673}.
CC -!- SIMILARITY: Belongs to the acetyltransferase family. {ECO:0000305}.
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DR EMBL; L10244; AAA16566.1; -; mRNA.
DR EMBL; AK002531; BAB22167.1; -; mRNA.
DR EMBL; AK154445; BAE32591.1; -; mRNA.
DR EMBL; BC058696; AAH58696.1; -; mRNA.
DR CCDS; CCDS30495.1; -.
DR PIR; S43429; S43429.
DR RefSeq; NP_001278794.1; NM_001291865.1.
DR RefSeq; NP_033147.1; NM_009121.4.
DR PDB; 3BJ7; X-ray; 2.20 A; A/B/C/D=1-171.
DR PDB; 3BJ8; X-ray; 2.30 A; A/B/C/D=1-171.
DR PDBsum; 3BJ7; -.
DR PDBsum; 3BJ8; -.
DR AlphaFoldDB; P48026; -.
DR SMR; P48026; -.
DR BioGRID; 203076; 1.
DR DIP; DIP-46096N; -.
DR IntAct; P48026; 1.
DR STRING; 10090.ENSMUSP00000026318; -.
DR ChEMBL; CHEMBL4775; -.
DR iPTMnet; P48026; -.
DR PhosphoSitePlus; P48026; -.
DR PaxDb; P48026; -.
DR PRIDE; P48026; -.
DR ProteomicsDB; 256705; -.
DR Antibodypedia; 24525; 259 antibodies from 22 providers.
DR DNASU; 20229; -.
DR Ensembl; ENSMUST00000026318; ENSMUSP00000026318; ENSMUSG00000025283.
DR GeneID; 20229; -.
DR KEGG; mmu:20229; -.
DR UCSC; uc009urq.2; mouse.
DR CTD; 6303; -.
DR MGI; MGI:98233; Sat1.
DR VEuPathDB; HostDB:ENSMUSG00000025283; -.
DR eggNOG; KOG3216; Eukaryota.
DR GeneTree; ENSGT00950000183121; -.
DR HOGENOM; CLU_013985_41_1_1; -.
DR InParanoid; P48026; -.
DR OMA; AVERQCG; -.
DR OrthoDB; 1228251at2759; -.
DR PhylomeDB; P48026; -.
DR TreeFam; TF319736; -.
DR BRENDA; 2.3.1.57; 3474.
DR Reactome; R-MMU-351200; Interconversion of polyamines.
DR SABIO-RK; P48026; -.
DR UniPathway; UPA00188; UER00363.
DR BioGRID-ORCS; 20229; 1 hit in 76 CRISPR screens.
DR ChiTaRS; Sat1; mouse.
DR EvolutionaryTrace; P48026; -.
DR PRO; PR:P48026; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; P48026; protein.
DR Bgee; ENSMUSG00000025283; Expressed in granulocyte and 120 other tissues.
DR ExpressionAtlas; P48026; baseline and differential.
DR Genevisible; P48026; MM.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0004145; F:diamine N-acetyltransferase activity; ISS:UniProtKB.
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:0006596; P:polyamine biosynthetic process; ISS:UniProtKB.
DR GO; GO:0009447; P:putrescine catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0042127; P:regulation of cell population proliferation; IGI:MGI.
DR GO; GO:0032918; P:spermidine acetylation; ISS:UniProtKB.
DR GO; GO:0046208; P:spermine catabolic process; TAS:MGI.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR000182; GNAT_dom.
DR InterPro; IPR032957; SAT1.
DR PANTHER; PTHR10545:SF36; PTHR10545:SF36; 1.
DR Pfam; PF00583; Acetyltransf_1; 1.
DR SUPFAM; SSF55729; SSF55729; 1.
DR PROSITE; PS51186; GNAT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acyltransferase; Cytoplasm; Direct protein sequencing;
KW Reference proteome; Transferase.
FT CHAIN 1..171
FT /note="Diamine acetyltransferase 1"
FT /id="PRO_0000074593"
FT DOMAIN 4..170
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:0000305|PubMed:18690703"
FT BINDING 94..96
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000305|PubMed:18690703"
FT BINDING 102..107
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000305|PubMed:18690703"
FT BINDING 126..128
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:18690703"
FT BINDING 133..136
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000305|PubMed:18690703"
FT BINDING 140..143
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000305|PubMed:18690703"
FT BINDING 152
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P21673"
FT MUTAGEN 92
FT /note="E->Q: Reduced activity."
FT /evidence="ECO:0000269|PubMed:18690703"
FT MUTAGEN 93
FT /note="D->N: Reduced activity."
FT /evidence="ECO:0000269|PubMed:18690703"
FT STRAND 5..8
FT /evidence="ECO:0007829|PDB:3BJ7"
FT HELIX 11..13
FT /evidence="ECO:0007829|PDB:3BJ7"
FT HELIX 14..27
FT /evidence="ECO:0007829|PDB:3BJ7"
FT HELIX 31..33
FT /evidence="ECO:0007829|PDB:3BJ7"
FT HELIX 38..46
FT /evidence="ECO:0007829|PDB:3BJ7"
FT STRAND 47..49
FT /evidence="ECO:0007829|PDB:3BJ7"
FT STRAND 53..58
FT /evidence="ECO:0007829|PDB:3BJ7"
FT HELIX 61..63
FT /evidence="ECO:0007829|PDB:3BJ7"
FT STRAND 70..82
FT /evidence="ECO:0007829|PDB:3BJ7"
FT TURN 83..85
FT /evidence="ECO:0007829|PDB:3BJ7"
FT STRAND 86..96
FT /evidence="ECO:0007829|PDB:3BJ7"
FT HELIX 98..100
FT /evidence="ECO:0007829|PDB:3BJ7"
FT HELIX 105..119
FT /evidence="ECO:0007829|PDB:3BJ7"
FT STRAND 123..129
FT /evidence="ECO:0007829|PDB:3BJ7"
FT HELIX 134..141
FT /evidence="ECO:0007829|PDB:3BJ7"
FT TURN 142..144
FT /evidence="ECO:0007829|PDB:3BJ7"
FT HELIX 149..151
FT /evidence="ECO:0007829|PDB:3BJ7"
FT STRAND 157..160
FT /evidence="ECO:0007829|PDB:3BJ7"
FT HELIX 161..168
FT /evidence="ECO:0007829|PDB:3BJ7"
SQ SEQUENCE 171 AA; 20012 MW; A919838E8AA81899 CRC64;
MAKFKIRPAT ASDCSDILRL IKELAKYEYM EDQVILTEKD LQEDGFGEHP FYHCLVAEVP
KEHWTPEGHS IVGFAMYYFT YDPWIGKLLY LEDFFVMSDY RGFGIGSEIL KNLSQVAMKC
RCSSMHFLVA EWNEPSINFY KRRGASDLSS EEGWRLFKID KEYLLKMAAE E
