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Protein

Diamine acetyltransferase 1

Gene

Sat1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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. 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 (By similarity).By similarity1 Publication

Catalytic activityi

Acetyl-CoA + an alkane-alpha,omega-diamine = CoA + an N-acetyldiamine.1 Publication

pH dependencei

Optimum pH is 8.5-9.5.1 Publication

Pathwayi: putrescine degradation

This protein is involved in step 1 of the subpathway that synthesizes N-acetylputrescine from putrescine.
Proteins known to be involved in this subpathway in this organism are:
  1. Diamine acetyltransferase 2 (Sat2), Diamine acetyltransferase 1 (Sat1)
This subpathway is part of the pathway putrescine degradation, which is itself part of Amine and polyamine degradation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes N-acetylputrescine from putrescine, the pathway putrescine degradation and in Amine and polyamine degradation.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei92Substrate; via carbonyl oxygen1
Binding sitei152SubstrateBy similarity1

GO - Molecular functioni

GO - Biological processi

  • angiogenesis Source: Ensembl
  • nor-spermidine metabolic process Source: GO_Central
  • putrescine acetylation Source: GO_Central
  • putrescine catabolic process Source: UniProtKB-UniPathway
  • regulation of cell proliferation Source: MGI
  • spermidine acetylation Source: GO_Central
  • spermine acetylation Source: GO_Central
  • spermine catabolic process Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Enzyme and pathway databases

BRENDAi2.3.1.57. 3474.
ReactomeiR-MMU-351200. Interconversion of polyamines.
SABIO-RKP48026.
UniPathwayiUPA00188; UER00363.

Names & Taxonomyi

Protein namesi
Recommended name:
Diamine acetyltransferase 1 (EC:2.3.1.571 Publication)
Alternative name(s):
Polyamine N-acetyltransferase 1
Putrescine acetyltransferase
Spermidine/spermine N(1)-acetyltransferase 1
Short name:
SSAT
Short name:
SSAT-1
Gene namesi
Name:Sat1
Synonyms:Sat
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome X

Organism-specific databases

MGIiMGI:98233. Sat1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi92E → Q: Reduced activity. 1 Publication1
Mutagenesisi93D → N: Reduced activity. 1 Publication1

Chemistry databases

ChEMBLiCHEMBL4775.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000745931 – 171Diamine acetyltransferase 1Add BLAST171

Proteomic databases

PaxDbiP48026.
PRIDEiP48026.

PTM databases

iPTMnetiP48026.
PhosphoSitePlusiP48026.

Expressioni

Gene expression databases

BgeeiENSMUSG00000025283.
CleanExiMM_SAT1.
ExpressionAtlasiP48026. baseline and differential.
GenevisibleiP48026. MM.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

BioGridi203076. 1 interactor.
DIPiDIP-46096N.
STRINGi10090.ENSMUSP00000026318.

Structurei

Secondary structure

1171
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi5 – 8Combined sources4
Helixi11 – 13Combined sources3
Helixi14 – 27Combined sources14
Helixi31 – 33Combined sources3
Helixi38 – 46Combined sources9
Beta strandi47 – 49Combined sources3
Beta strandi53 – 58Combined sources6
Helixi61 – 63Combined sources3
Beta strandi70 – 82Combined sources13
Turni83 – 85Combined sources3
Beta strandi86 – 96Combined sources11
Helixi98 – 100Combined sources3
Helixi105 – 119Combined sources15
Beta strandi123 – 129Combined sources7
Helixi134 – 141Combined sources8
Turni142 – 144Combined sources3
Helixi149 – 151Combined sources3
Beta strandi157 – 160Combined sources4
Helixi161 – 168Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3BJ7X-ray2.20A/B/C/D1-171[»]
3BJ8X-ray2.30A/B/C/D1-171[»]
ProteinModelPortaliP48026.
SMRiP48026.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP48026.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini4 – 170N-acetyltransferasePROSITE-ProRule annotationAdd BLAST167

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni27 – 28Substrate bindingBy similarity2
Regioni94 – 96Acetyl-CoA binding1 Publication3
Regioni102 – 107Acetyl-CoA binding1 Publication6
Regioni126 – 128Substrate binding3
Regioni133 – 136Acetyl-CoA binding1 Publication4
Regioni140 – 143Acetyl-CoA binding1 Publication4

Sequence similaritiesi

Belongs to the acetyltransferase family.Curated
Contains 1 N-acetyltransferase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG3216. Eukaryota.
COG0454. LUCA.
GeneTreeiENSGT00440000039972.
HOGENOMiHOG000078521.
HOVERGENiHBG063175.
InParanoidiP48026.
KOiK00657.
PhylomeDBiP48026.
TreeFamiTF319736.

Family and domain databases

Gene3Di3.40.630.30. 1 hit.
InterProiIPR016181. Acyl_CoA_acyltransferase.
IPR000182. GNAT_dom.
IPR032957. SAT1.
[Graphical view]
PANTHERiPTHR10545:SF36. PTHR10545:SF36. 1 hit.
PfamiPF00583. Acetyltransf_1. 1 hit.
[Graphical view]
SUPFAMiSSF55729. SSF55729. 1 hit.
PROSITEiPS51186. GNAT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P48026-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAKFKIRPAT ASDCSDILRL IKELAKYEYM EDQVILTEKD LQEDGFGEHP
60 70 80 90 100
FYHCLVAEVP KEHWTPEGHS IVGFAMYYFT YDPWIGKLLY LEDFFVMSDY
110 120 130 140 150
RGFGIGSEIL KNLSQVAMKC RCSSMHFLVA EWNEPSINFY KRRGASDLSS
160 170
EEGWRLFKID KEYLLKMAAE E
Length:171
Mass (Da):20,012
Last modified:February 1, 1996 - v1
Checksum:iA919838E8AA81899
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L10244 mRNA. Translation: AAA16566.1.
AK002531 mRNA. Translation: BAB22167.1.
AK154445 mRNA. Translation: BAE32591.1.
BC058696 mRNA. Translation: AAH58696.1.
CCDSiCCDS30495.1.
PIRiS43429.
RefSeqiNP_001278794.1. NM_001291865.1.
NP_033147.1. NM_009121.4.
UniGeneiMm.2734.
Mm.474481.

Genome annotation databases

EnsembliENSMUST00000026318; ENSMUSP00000026318; ENSMUSG00000025283.
GeneIDi20229.
KEGGimmu:20229.
UCSCiuc009urq.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L10244 mRNA. Translation: AAA16566.1.
AK002531 mRNA. Translation: BAB22167.1.
AK154445 mRNA. Translation: BAE32591.1.
BC058696 mRNA. Translation: AAH58696.1.
CCDSiCCDS30495.1.
PIRiS43429.
RefSeqiNP_001278794.1. NM_001291865.1.
NP_033147.1. NM_009121.4.
UniGeneiMm.2734.
Mm.474481.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3BJ7X-ray2.20A/B/C/D1-171[»]
3BJ8X-ray2.30A/B/C/D1-171[»]
ProteinModelPortaliP48026.
SMRiP48026.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi203076. 1 interactor.
DIPiDIP-46096N.
STRINGi10090.ENSMUSP00000026318.

Chemistry databases

ChEMBLiCHEMBL4775.

PTM databases

iPTMnetiP48026.
PhosphoSitePlusiP48026.

Proteomic databases

PaxDbiP48026.
PRIDEiP48026.

Protocols and materials databases

DNASUi20229.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000026318; ENSMUSP00000026318; ENSMUSG00000025283.
GeneIDi20229.
KEGGimmu:20229.
UCSCiuc009urq.2. mouse.

Organism-specific databases

CTDi6303.
MGIiMGI:98233. Sat1.

Phylogenomic databases

eggNOGiKOG3216. Eukaryota.
COG0454. LUCA.
GeneTreeiENSGT00440000039972.
HOGENOMiHOG000078521.
HOVERGENiHBG063175.
InParanoidiP48026.
KOiK00657.
PhylomeDBiP48026.
TreeFamiTF319736.

Enzyme and pathway databases

UniPathwayiUPA00188; UER00363.
BRENDAi2.3.1.57. 3474.
ReactomeiR-MMU-351200. Interconversion of polyamines.
SABIO-RKP48026.

Miscellaneous databases

EvolutionaryTraceiP48026.
PROiP48026.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000025283.
CleanExiMM_SAT1.
ExpressionAtlasiP48026. baseline and differential.
GenevisibleiP48026. MM.

Family and domain databases

Gene3Di3.40.630.30. 1 hit.
InterProiIPR016181. Acyl_CoA_acyltransferase.
IPR000182. GNAT_dom.
IPR032957. SAT1.
[Graphical view]
PANTHERiPTHR10545:SF36. PTHR10545:SF36. 1 hit.
PfamiPF00583. Acetyltransf_1. 1 hit.
[Graphical view]
SUPFAMiSSF55729. SSF55729. 1 hit.
PROSITEiPS51186. GNAT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiSAT1_MOUSE
AccessioniPrimary (citable) accession number: P48026
Secondary accession number(s): Q3U444
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: November 2, 2016
This is version 125 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.