SAT1_CRIGR
ID SAT1_CRIGR Reviewed; 171 AA.
AC Q9JHW6;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Diamine acetyltransferase 1;
DE EC=2.3.1.57 {ECO:0000250|UniProtKB:P21673};
DE AltName: Full=Polyamine N-acetyltransferase 1;
DE AltName: Full=Putrescine acetyltransferase;
DE AltName: Full=Spermidine/spermine N(1)-acetyltransferase 1 {ECO:0000303|PubMed:10887189};
DE Short=SSAT {ECO:0000303|PubMed:10887189};
DE Short=SSAT-1;
GN Name=SAT1 {ECO:0000250|UniProtKB:P21673}; Synonyms=SAT;
OS Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Cricetulus.
OX NCBI_TaxID=10029;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT PHE-156.
RC TISSUE=Ovarian carcinoma;
RX PubMed=10887189; DOI=10.1074/jbc.m004120200;
RA McCloskey D.E., Pegg A.E.;
RT "Altered spermidine/spermine N1-acetyltransferase activity as a mechanism
RT of cellular resistance to bis(ethyl)polyamine analogues.";
RL J. Biol. Chem. 275:28708-28714(2000).
CC -!- FUNCTION: Enzyme which catalyzes the acetylation of polyamines.
CC Substrate specificity: norspermidine = spermidine >> spermine > N(1)-
CC acetylspermine. This highly regulated enzyme allows a fine attenuation
CC of the intracellular concentration of polyamines. Also involved in the
CC regulation of polyamine transport out of cells. Also acts on 1,3-
CC diaminopropane and 1,5-diaminopentane. {ECO:0000250|UniProtKB:P21673}.
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:P21673};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11117;
CC Evidence={ECO:0000250|UniProtKB:P21673};
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:0000250|UniProtKB:P21673};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:28151;
CC Evidence={ECO:0000250|UniProtKB:P21673};
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 -!- PATHWAY: Amine and polyamine degradation; putrescine degradation; N-
CC acetylputrescine from putrescine: step 1/1.
CC {ECO:0000250|UniProtKB:P21673}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P21673}.
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; AF281149; AAF86286.1; -; mRNA.
DR RefSeq; NP_001233618.1; NM_001246689.1.
DR AlphaFoldDB; Q9JHW6; -.
DR SMR; Q9JHW6; -.
DR STRING; 10029.NP_001233618.1; -.
DR Ensembl; ENSCGRT00001028331; ENSCGRP00001024085; ENSCGRG00001022103.
DR GeneID; 100689427; -.
DR KEGG; cge:100689427; -.
DR CTD; 6303; -.
DR eggNOG; KOG3216; Eukaryota.
DR GeneTree; ENSGT00950000183121; -.
DR OrthoDB; 1228251at2759; -.
DR UniPathway; UPA00188; UER00363.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0004145; F:diamine N-acetyltransferase activity; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0008080; F:N-acetyltransferase activity; ISS:UniProtKB.
DR GO; GO:0001525; P:angiogenesis; IEA:Ensembl.
DR GO; GO:0006596; P:polyamine biosynthetic process; ISS:UniProtKB.
DR GO; GO:0009447; P:putrescine catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0032918; P:spermidine acetylation; ISS:UniProtKB.
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 2: Evidence at transcript level;
KW Acyltransferase; Cytoplasm; Transferase.
FT CHAIN 1..171
FT /note="Diamine acetyltransferase 1"
FT /id="PRO_0000074590"
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:0000250|UniProtKB:P21673"
FT BINDING 94..96
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:P21673"
FT BINDING 102..107
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:P21673"
FT BINDING 126..128
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P21673"
FT BINDING 133..136
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:P21673"
FT BINDING 140..143
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:P21673"
FT BINDING 152
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P21673"
FT VARIANT 156
FT /note="L -> F (in N(1),N(12)-bis(ethyl)spermine-resistant
FT cell line C55.7Res)"
FT /evidence="ECO:0000269|PubMed:10887189"
SQ SEQUENCE 171 AA; 20029 MW; C2749F8366CEC6F1 CRC64;
MAKFKIRPAT ASDCSDILRL IKELAKYEYM EDQVMLTEKD LLEDGFGEHP FYHCLIAEVP
KEHWTPEGHS IVGFAMYYFT YDPWIGKLLY LEDFFVMSDY RGFGIGSEIL KNLSQVAMKC
RCSSMHFLVA EWNEPSINFY KRRGASDLSS EEGWRLFKID KEYLLKMAAE E
