SAT1_CHICK
ID SAT1_CHICK Reviewed; 171 AA.
AC Q8AXL1;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 106.
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:12076082};
DE Short=SSAT {ECO:0000303|PubMed:12076082};
DE Short=SSAT-1;
GN Name=SAT1; Synonyms=SAT, SSAT;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE.
RC TISSUE=Retina;
RX PubMed=12076082; DOI=10.1006/exer.2002.1167;
RA Witte R.L., Godbout R.;
RT "Expression of spermidine/spermine N(1)-acetyltransferase in the Muller
RT glial cells of the developing chick retina.";
RL Exp. Eye Res. 74:605-613(2002).
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.
CC {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 {ECO:0000250|UniProtKB:P21673}.
CC -!- DEVELOPMENTAL STAGE: Preferentially expressed in the dorsal-temporal
CC quadrant of the developing retina. There was a sharp increase in
CC retinal SSAT levels during the transition stage from proliferation (E7)
CC to early differentiation (E10). SSAT was found in Muller glial cells
CC and its distribution pattern in these cells closely followed the three
CC differentiation axis of the developing retina, with a central-dorsal-
CC temporal preference. {ECO:0000269|PubMed:12076082}.
CC -!- SIMILARITY: Belongs to the acetyltransferase family. {ECO:0000305}.
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DR EMBL; AF402003; AAN76653.1; -; mRNA.
DR RefSeq; NP_989517.1; NM_204186.1.
DR AlphaFoldDB; Q8AXL1; -.
DR SMR; Q8AXL1; -.
DR STRING; 9031.ENSGALP00000035846; -.
DR PaxDb; Q8AXL1; -.
DR Ensembl; ENSGALT00000036635; ENSGALP00000035846; ENSGALG00000016348.
DR GeneID; 374006; -.
DR KEGG; gga:374006; -.
DR CTD; 6303; -.
DR VEuPathDB; HostDB:geneid_374006; -.
DR eggNOG; KOG3216; Eukaryota.
DR GeneTree; ENSGT00950000183121; -.
DR HOGENOM; CLU_013985_41_1_1; -.
DR InParanoid; Q8AXL1; -.
DR OMA; AVERQCG; -.
DR OrthoDB; 1228251at2759; -.
DR PhylomeDB; Q8AXL1; -.
DR UniPathway; UPA00188; UER00363.
DR PRO; PR:Q8AXL1; -.
DR Proteomes; UP000000539; Chromosome 1.
DR Bgee; ENSGALG00000016348; Expressed in ovary and 14 other tissues.
DR ExpressionAtlas; Q8AXL1; baseline and differential.
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; IEA:Ensembl.
DR GO; GO:0008080; F:N-acetyltransferase activity; ISS:UniProtKB.
DR GO; GO:0019809; F:spermidine binding; IBA:GO_Central.
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; Reference proteome; Transferase.
FT CHAIN 1..171
FT /note="Diamine acetyltransferase 1"
FT /id="PRO_0000074596"
FT DOMAIN 4..171
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"
SQ SEQUENCE 171 AA; 19965 MW; 884F62EE071A368F CRC64;
MASFSIRAAR PEDCSDLLRL IKELAKYEDM EDQVVLTEKE LLEDGFGEHP FYHCLVAEVP
KEQWSSEGHS IVGFAMYYFT YDPWIGKLLY LEDFYVMAEY RGLGIGSEIL KNLSQVAVKC
RCSSMHFLVA EWNEPSIRFY KRRGASDLST EEGWRLFKID KEYLLKMATE E
