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 02-SEP-2026, entry version 121. 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=an alkane-alpha,omega-diamine + acetyl-CoA = 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=spermidine + acetyl-CoA = N(1)-acetylspermidine + CoA + H(+); 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=spermine + acetyl-CoA = N(1)-acetylspermine + CoA + H(+); 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 (7 CC dpc) to early differentiation (10 dpc). SSAT was found in Muller glial CC cells and its distribution pattern in these cells closely followed the CC three differentiation axis of the developing retina, with a central- CC dorsal-temporal preference. {ECO:0000269|PubMed:12076082}. CC -!- SIMILARITY: Belongs to the acetyltransferase family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF402003; AAN76653.1; -; mRNA. DR RefSeq; NP_989517.1; NM_204186.2. DR AlphaFoldDB; Q8AXL1; -. DR SMR; Q8AXL1; -. DR FunCoup; Q8AXL1; 483. DR STRING; 9031.ENSGALP00000035846; -. DR PaxDb; 9031-ENSGALP00000035846; -. DR Ensembl; ENSGALT00010007306.1; ENSGALP00010004384.1; ENSGALG00010003133.1. 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; IAVKCRC; -. DR OrthoDB; 7305308at2759; -. DR PhylomeDB; Q8AXL1; -. DR Reactome; R-GGA-351200; Interconversion of polyamines. DR UniPathway; UPA00188; UER00363. DR PRO; PR:Q8AXL1; -. DR Proteomes; UP000000539; Chromosome 1. DR Bgee; ENSGALG00000016348; Expressed in ovary and 14 other cell types or tissues. DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB. 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 CDD; cd04301; NAT_SF; 1. DR FunFam; 3.40.630.30:FF:000011; Diamine acetyltransferase 1; 1. DR Gene3D; 3.40.630.30; -; 1. DR InterPro; IPR016181; Acyl_CoA_acyltransferase. DR InterPro; IPR051016; Diverse_Substrate_AcTransf. DR InterPro; IPR000182; GNAT_dom. DR PANTHER; PTHR10545:SF36; DIAMINE ACETYLTRANSFERASE 1; 1. DR PANTHER; PTHR10545; DIAMINE N-ACETYLTRANSFERASE; 1. DR Pfam; PF00583; Acetyltransf_1; 1. DR SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 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 //