PAA1_YEAST
ID PAA1_YEAST Reviewed; 191 AA.
AC Q12447; D6VS57;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Polyamine N-acetyltransferase 1;
DE EC=2.3.1.-;
DE AltName: Full=Arylalkylamine N-acetyltransferase homolog;
DE Short=scAANAT;
GN Name=PAA1; OrderedLocusNames=YDR071C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(1997).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [4]
RP FUNCTION.
RX PubMed=11559708; DOI=10.1074/jbc.m107222200;
RA Ganguly S., Mummaneni P., Steinbach P.J., Klein D.C., Coon S.L.;
RT "Characterization of the Saccharomyces cerevisiae homolog of the melatonin
RT rhythm enzyme arylalkylamine N-acetyltransferase (EC 2.3.1.87).";
RL J. Biol. Chem. 276:47239-47247(2001).
RN [5]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [6]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [7]
RP FUNCTION.
RX PubMed=15723835; DOI=10.1074/jbc.m414008200;
RA Liu B., Sutton A., Sternglanz R.;
RT "A yeast polyamine acetyltransferase.";
RL J. Biol. Chem. 280:16659-16664(2005).
CC -!- FUNCTION: Acetylates spermine and probably also other polyamines such
CC as putrescine or spermidine. May regulate the levels of polyamines on
CC chromosomal DNA, which would modify chromatin structure and affect
CC transcription or replication. Also able to acetylate arylalkylamines
CC such as tryptamine and serotonin in vitro.
CC {ECO:0000269|PubMed:11559708, ECO:0000269|PubMed:15723835}.
CC -!- INTERACTION:
CC Q12447; P39966: PTC2; NbExp=8; IntAct=EBI-33397, EBI-12795;
CC Q12447; P34221: PTC3; NbExp=6; IntAct=EBI-33397, EBI-12805;
CC Q12447; P38089: PTC4; NbExp=5; IntAct=EBI-33397, EBI-12814;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 8680 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the acetyltransferase family. AANAT subfamily.
CC {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; Z46796; CAA86793.1; -; Genomic_DNA.
DR EMBL; Z74367; CAA98889.1; -; Genomic_DNA.
DR EMBL; AY557672; AAS55998.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA11917.1; -; Genomic_DNA.
DR PIR; S49826; S49826.
DR RefSeq; NP_010356.1; NM_001180379.1.
DR AlphaFoldDB; Q12447; -.
DR SMR; Q12447; -.
DR BioGRID; 32126; 300.
DR DIP; DIP-1540N; -.
DR IntAct; Q12447; 17.
DR MINT; Q12447; -.
DR STRING; 4932.YDR071C; -.
DR iPTMnet; Q12447; -.
DR MaxQB; Q12447; -.
DR PaxDb; Q12447; -.
DR PRIDE; Q12447; -.
DR EnsemblFungi; YDR071C_mRNA; YDR071C; YDR071C.
DR GeneID; 851643; -.
DR KEGG; sce:YDR071C; -.
DR SGD; S000002478; PAA1.
DR VEuPathDB; FungiDB:YDR071C; -.
DR eggNOG; KOG4144; Eukaryota.
DR GeneTree; ENSGT00390000015579; -.
DR HOGENOM; CLU_061829_0_2_1; -.
DR InParanoid; Q12447; -.
DR OMA; IVIIAHE; -.
DR BioCyc; YEAST:G3O-29678-MON; -.
DR Reactome; R-SCE-209931; Serotonin and melatonin biosynthesis.
DR PRO; PR:Q12447; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q12447; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0004059; F:aralkylamine N-acetyltransferase activity; IDA:SGD.
DR GO; GO:0004145; F:diamine N-acetyltransferase activity; IDA:SGD.
DR GO; GO:0006325; P:chromatin organization; IMP:SGD.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR000182; GNAT_dom.
DR Pfam; PF00583; Acetyltransf_1; 1.
DR SUPFAM; SSF55729; SSF55729; 1.
DR PROSITE; PS51186; GNAT; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Cytoplasm; Reference proteome; Transferase.
FT CHAIN 1..191
FT /note="Polyamine N-acetyltransferase 1"
FT /id="PRO_0000245843"
FT DOMAIN 12..179
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
SQ SEQUENCE 191 AA; 21947 MW; 76AAC4EA2926660D CRC64;
MASSSSTLPL HMYIRPLIIE DLKQILNLES QGFPPNERAS EEIISFRLIN CPELCSGLFI
REIEGKEVKK ETLIGHIMGT KIPHEYITIE SMGKLQVESS NHIGIHSVVI KPEYQKKNLA
TLLLTDYIQK LSNQEIGNKI VLIAHEPLIP FYERVGFKII AENTNVAKDK NFAEQKWIDM
ERELIKEEYD N
