Q6P8J2 (SAT2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Diamine acetyltransferase 2
EC=2.3.1.57

Alternative name(s):
Polyamine N-acetyltransferase 2
Spermidine/spermine N(1)-acetyltransferase 2

Gene names

Name:	Sat2
Synonyms:	Ssat2

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	170 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Enzyme which catalyzes the acetylation of polyamines. Substrate specificity: norspermidine > spermidine = spermine >> N1acetylspermine = putrescine 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 By similarity.
Subcellular location	Cytoplasm By similarity. Note: Intracellular organelles By similarity.
Sequence similarities	Belongs to the acetyltransferase family. Contains 1 N-acetyltransferase domain.

Ontologies

Keywords
Cellular component	Cytoplasm
Molecular function	Acyltransferase Transferase
PTM	Acetylation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	putrescine catabolic process Inferred from electronic annotation. Source: UniProtKB-UniPathway spermidine metabolic process Inferred from sequence alignment PubMed 12803540. Source: MGI spermine metabolic process Inferred from sequence alignment PubMed 12803540. Source: MGI
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	diamine N-acetyltransferase activity Inferred from sequence alignment PubMed 12803540. Source: MGI
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 170	170	Diamine acetyltransferase 2		PRO_0000074599
Regions
	Domain	4 – 166	163	N-acetyltransferase
	Region	27 – 28	2	Substrate binding By similarity
	Region	94 – 96	3	Acetyl-CoA binding By similarity
	Region	102 – 107	6	Acetyl-CoA binding By similarity
	Region	133 – 135	3	Acetyl-CoA binding By similarity
Sites
	Binding site	92	1	Substrate; via carbonyl oxygen By similarity
	Binding site	140	1	Acetyl-CoA By similarity
	Binding site	152	1	Substrate By similarity
Amino acid modifications
	Modified residue	29	1	N6-acetyllysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q6P8J2 [UniParc]. Last modified July 5, 2004. Version 1. Checksum: 5D82F98DAD0619AA	FASTA	170	19,305
	10 20 30 40 50 60 MASTRIREAR ESDCGDIMRM IRELAEFEKL SHQVKISEEA LRADGFGENP FFHCLVAEII 70 80 90 100 110 120 PAPGESQGSL VVGYGLYYFI YSTWTGRNVY LEDIYVMPQY RGQGIGTKII KKVAEVALNK 130 140 150 160 170 GCSQFRLAVL DWNKKAVNLY KFLGAQDLTE SEGWLSFRFE GEAMRELAGR

References

[1]	"Lineage-specific biology revealed by a finished genome assembly of the mouse." Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P. PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: C57BL/6J.
[2]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Kidney.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AL603707, AL731687 Genomic DNA. Translation: CAI51952.1. BC061227 mRNA. Translation: AAH61227.1.
IPI	IPI00347376.
RefSeq	NP_081267.1. NM_026991.2.
UniGene	Mm.340410.
3D structure databases
ProteinModelPortal	Q6P8J2.
SMR	Q6P8J2. Positions 2-170.
ModBase	Search...
PTM databases
PhosphoSite	Q6P8J2.
Proteomic databases
PaxDb	Q6P8J2.
PRIDE	Q6P8J2.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000092969; ENSMUSP00000090647; ENSMUSG00000069835. ENSMUST00000108656; ENSMUSP00000104296; ENSMUSG00000069835.
GeneID	69215.
KEGG	mmu:69215.
UCSC	uc007jqq.1. mouse.
Organism-specific databases
CTD	112483.
MGI	MGI:1916465. Sat2.
Phylogenomic databases
eggNOG	COG0454.
GeneTree	ENSGT00440000039972.
HOGENOM	HOG000078521.
HOVERGEN	HBG063175.
InParanoid	Q5F299.
KO	K00657.
OMA	LDWNPAR.
OrthoDB	EOG47SSG0.
Enzyme and pathway databases
UniPathway	UPA00188; UER00363.
Gene expression databases
Bgee	Q6P8J2.
CleanEx	MM_SAT2.
Genevestigator	Q6P8J2.
GermOnline	ENSMUSG00000069835. Mus musculus.
Family and domain databases
Gene3D	3.40.630.30. 1 hit.
InterPro	IPR016181. Acyl_CoA_acyltransferase. IPR000182. GNAT_dom. [Graphical view]
Pfam	PF00583. Acetyltransf_1. 1 hit. [Graphical view]
SUPFAM	SSF55729. Acyl_CoA_acyltransferase. 1 hit.
PROSITE	PS51186. GNAT. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChEMBL	CHEMBL3794.
NextBio	328895.
SOURCE	Search...

Entry information

Entry name

SAT2_MOUSE

Accession

Primary (citable) accession number: Q6P8J2
Secondary accession number(s): Q5F299

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 16, 2004
Last sequence update:	July 5, 2004
Last modified:	May 1, 2013
This is version 68 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program