Reviewed, UniProtKB/Swiss-Prot P48026 (SAT1_MOUSE)

Names and origin

Protein names

Recommended name:
    Diamine acetyltransferase 1
    EC=2.3.1.57
Alternative name(s):
    Spermidine/spermine N(1)-acetyltransferase 1
      Short name=SSAT-1
      Short name=SSAT
    Putrescine acetyltransferase
    Polyamine N-acetyltransferase 1

Gene names

Name:	Sat1
Synonyms:	Sat

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	171 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Enzyme which catalyzes the acetylation of polyamines. Substrate specificity: norspermidine = spermidine >> spermine > N(1)-acetylspermine > putrescine. This highly regulated enzyme allows a fine attenuation of the intracellular concentration of polyamines. Also involved in the regulation of polyamine transport out of cells By similarity.
Catalytic activity	Acetyl-CoA + an alkane-alpha,omega-diamine = CoA + an N-acetyldiamine.
Pathway	Amine and polyamine degradation; putrescine degradation; N-acetylputrescine from putrescine: step 1/1.
Subunit structure	Homodimer. Ref.5
Subcellular location	Cytoplasm.
Miscellaneous	Acts on 1,3-diaminopropane, 1,5-diaminopentane, putrescine, spermidine (forming N(1)- and N(8)-acetylspermidine), spermine, N(1)-acetylspermidine and N(8)-acetylspermidine.
Sequence similarities	Belongs to the acetyltransferase family. Contains 1 N-acetyltransferase domain.
Biophysicochemical properties	pH dependence: Optimum pH is 8.5-9.5.

Ontologies

Keywords
Cellular component	Cytoplasm
Molecular function	Acyltransferase Transferase
PTM	Acetylation
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	regulation of cell proliferation Inferred from genetic interaction. Source: MGI spermine catabolic process Traceable author statement. Source: MGI
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	diamine N-acetyltransferase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 171

171

Diamine acetyltransferase 1

PRO_0000074593

Regions

Domain

4 – 170

167

N-acetyltransferase

Region

27 – 28

2

Substrate binding By similarity

Region

94 – 96

3

Acetyl-CoA binding

Region

102 – 107

6

Acetyl-CoA binding

Region

126 – 128

3

Substrate binding

Region

133 – 136

4

Acetyl-CoA binding

Region

140 – 143

4

Acetyl-CoA binding

Sites

Binding site

92

1

Substrate; via carbonyl oxygen

Binding site

152

1

Substrate By similarity

Amino acid modifications

Modified residue

26

1

N6-acetyllysine By similarity

Experimental info

Mutagenesis

92

1

E → Q: Reduced activity. Ref.5

Mutagenesis

93

1

D → N: Reduced activity. Ref.5

Secondary structure

1

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171

Helix Strand Turn

Details...

Beta strand

5 – 8

4

Helix

11 – 13

3

Helix

14 – 27

14

Helix

31 – 33

3

Helix

38 – 43

6

Beta strand

53 – 58

6

Beta strand

75 – 80

6

Beta strand

88 – 94

7

Helix

98 – 100

3

Helix

108 – 119

12

Beta strand

123 – 129

7

Helix

134 – 141

8

Helix

149 – 151

3

Beta strand

157 – 160

4

Helix

161 – 168

8

Sequences

	Sequence		Length	Mass (Da)
	P48026-1 [UniParc]. Last modified February 1, 1996. Version 1. Checksum: A919838E8AA81899	FASTA	171	20,012
	10 20 30 40 50 60 MAKFKIRPAT ASDCSDILRL IKELAKYEYM EDQVILTEKD LQEDGFGEHP FYHCLVAEVP 70 80 90 100 110 120 KEHWTPEGHS IVGFAMYYFT YDPWIGKLLY LEDFFVMSDY RGFGIGSEIL KNLSQVAMKC 130 140 150 160 170 RCSSMHFLVA EWNEPSINFY KRRGASDLSS EEGWRLFKID KEYLLKMAAE E

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and sequence analysis of the gene and cDNA encoding mouse spermidine/spermine N1-acetyltransferase -- a gene uniquely regulated by polyamines and their analogs." Fogel-Petrovic M., Kramer D.L., Ganis B., Casero R.A. Jr., Porter C.W. Biochim. Biophys. Acta 1216:255-264(1993) [PubMed: 8241266] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: BALB/c. Tissue: Liver.
[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. , 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: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J and NOD. Tissue: Kidney.
[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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6. Tissue: Brain.
[4]	Lubec G., Kang S.U. Submitted (APR-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 20-26, MASS SPECTROMETRY. Strain: C57BL/6. Tissue: Brain.
[5]	"The crystal structure of spermidine/spermine N1-acetyltransferase in complex with spermine provides insights into substrate binding and catalysis." Montemayor E.J., Hoffman D.W. Biochemistry 47:9145-9153(2008) [PubMed: 18690703] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH COENZYME A AND SPERMINE, MUTAGENESIS OF GLU-92 AND ASP-93, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

L10244 mRNA. Translation: AAA16566.1.
AK002531 mRNA. Translation: BAB22167.1.
AK154445 mRNA. Translation: BAE32591.1.
BC058696 mRNA. Translation: AAH58696.1.

IPI

IPI00137937.

PIR

S43429.

RefSeq

NP_033147.1.

UniGene

Mm.2734
Mm.474481

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3BJ7	X-ray	2.20	A/B/C/D	1-171	[»]
3BJ8	X-ray	2.30	A/B/C/D	1-171	[»]

SMR

P48026. Positions 2-171.

ModBase

Search...

Protein-protein interaction databases

STRING

P48026.

PTM databases

PhosphoSite

P48026.

Proteomic databases

PRIDE

P48026.

Genome annotation databases

Ensembl

ENSMUST00000026318; ENSMUSP00000026318; ENSMUSG00000025283; Mus musculus. [Genome view]
ENSMUST00000112551; ENSMUSP00000108170; ENSMUSG00000025283; Mus musculus. [Genome view]

GeneID

20229.

KEGG

mmu:20229.

UCSC

uc009urq.1. mouse.

Organism-specific databases

CTD

20229.

MGI

MGI:98233. Sat1.

Phylogenomic databases

HOGENOM

P48026.

HOVERGEN

P48026.

Enzyme and pathway databases

BRENDA

2.3.1.57. 244.

Gene expression databases

ArrayExpress

P48026.

Bgee

P48026.

CleanEx

MM_SAT1.

Genevestigator

P48026.

GermOnline

ENSMUSG00000025283. Mus musculus.

Family and domain databases

InterPro

IPR016181. Acyl_CoA_acyltransferase.
IPR000182. GCN5-rel_AcTrfase.
[Graphical view]

Gene3D

G3DSA:3.40.630.30. Acyl_CoA_acyltransferase. 1 hit.

Pfam

PF00583. Acetyltransf_1. 1 hit.
[Graphical view]

PROSITE

PS51186. GNAT. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

297857.

SOURCE

Search...

Entry information

Entry name

SAT1_MOUSE

Accession

Primary (citable) accession number: P48026
Secondary accession number(s): Q3U444

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1996
Last sequence update:	February 1, 1996
Last modified:	October 13, 2009
This is version 75 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)