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Serotonin N-acetyltransferase (Serotonin acetylase) (EC 2.3.1.87) (Aralkylamine N-acetyltransferase) (AA-NAT)

 SNAT_SHEEP              Reviewed;         207 AA.
Q29495;
01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
10-MAY-2017, entry version 110.
RecName: Full=Serotonin N-acetyltransferase;
Short=Serotonin acetylase;
EC=2.3.1.87 {ECO:0000269|PubMed:10319816, ECO:0000269|PubMed:11884405, ECO:0000269|PubMed:11902838, ECO:0000269|PubMed:18362150};
AltName: Full=Aralkylamine N-acetyltransferase;
Short=AA-NAT;
Name=AANAT; Synonyms=SNAT;
Ovis aries (Sheep).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
Pecora; Bovidae; Caprinae; Ovis.
NCBI_TaxID=9940;
[1]
NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND INDUCTION.
STRAIN=Dorsett X Rambouillet; TISSUE=Pineal gland;
PubMed=7502081; DOI=10.1126/science.270.5242.1681;
Coon S.L., Roseboom P.H., Baler R., Weller J.L., Namboodiri M.A.A.,
Koonin E.V., Klein D.C.;
"Pineal serotonin N-acetyltransferase: expression cloning and
molecular analysis.";
Science 270:1681-1683(1995).
[2]
INDUCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=11313340; DOI=10.1074/jbc.M011298200;
Coon S.L., Weller J.L., Korf H.-W., Namboodiri M.A., Rollag M.,
Klein D.C.;
"cAMP regulation of arylalkylamine N-acetyltransferase (AANAT, EC
2.3.1.87): a new cell line (1E7) provides evidence of intracellular
AANAT activation.";
J. Biol. Chem. 276:24097-24107(2001).
[3]
PHOSPHORYLATION AT THR-31, INTERACTION WITH 14-3-3 PROTEINS, AND
IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=11427721; DOI=10.1073/pnas.141118798;
Ganguly S., Gastel J.A., Weller J.L., Schwartz C., Jaffe H.,
Namboodiri M.A., Coon S.L., Hickman A.B., Rollag M., Obsil T.,
Beauverger P., Ferry G., Boutin J.A., Klein D.C.;
"Role of a pineal cAMP-operated arylalkylamine N-acetyltransferase/14-
3-3-binding switch in melatonin synthesis.";
Proc. Natl. Acad. Sci. U.S.A. 98:8083-8088(2001).
[4]
ERRATUM.
Ganguly S., Gastel J.A., Weller J.L., Schwartz C., Jaffe H.,
Namboodiri M.A., Coon S.L., Hickman A.B., Rollag M., Obsil T.,
Beauverger P., Ferry G., Boutin J.A., Klein D.C.;
Proc. Natl. Acad. Sci. U.S.A. 98:14186-14186(2001).
[5]
PHOSPHORYLATION AT THR-31, INTERACTION WITH YWHAZ, AND IDENTIFICATION
BY MASS SPECTROMETRY.
PubMed=14578935; DOI=10.1038/nsb1005;
Zheng W., Zhang Z., Ganguly S., Weller J.L., Klein D.C., Cole P.A.;
"Cellular stabilization of the melatonin rhythm enzyme induced by
nonhydrolyzable phosphonate incorporation.";
Nat. Struct. Biol. 10:1054-1057(2003).
[6]
FUNCTION, PHOSPHORYLATION AT THR-31 AND SER-205, INDUCTION,
INTERACTION WITH YWHAZ, AND MUTAGENESIS OF THR-31 AND SER-205.
PubMed=15644438; DOI=10.1073/pnas.0406871102;
Ganguly S., Weller J.L., Ho A., Chemineau P., Malpaux B., Klein D.C.;
"Melatonin synthesis: 14-3-3-dependent activation and inhibition of
arylalkylamine N-acetyltransferase mediated by phosphoserine-205.";
Proc. Natl. Acad. Sci. U.S.A. 102:1222-1227(2005).
[7]
CATALYTIC ACTIVITY, AND MUTAGENESIS OF ILE-57; VAL-59; PRO-64 AND
63-CYS--LEU-65.
PubMed=18362150; DOI=10.1074/jbc.M800593200;
Pavlicek J., Coon S.L., Ganguly S., Weller J.L., Hassan S.A.,
Sackett D.L., Klein D.C.;
"Evidence that proline focuses movement of the floppy loop of
arylalkylamine N-acetyltransferase (EC 2.3.1.87).";
J. Biol. Chem. 283:14552-14558(2008).
[8]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 30-195 IN COMPLEX WITH
COA-S-ACETYLTRYPTAMINE, IDENTIFICATION BY MASS SPECTROMETRY, CATALYTIC
ACTIVITY, AND MUTAGENESIS OF HIS-120; HIS-122 AND TYR-168.
PubMed=10319816; DOI=10.1016/S0092-8674(00)80745-X;
Hickman A.B., Namboodiri M.A., Klein D.C., Dyda F.;
"The structural basis of ordered substrate binding by serotonin N-
acetyltransferase: enzyme complex at 1.8 A resolution with a
bisubstrate analog.";
Cell 97:361-369(1999).
[9]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 28-201, IDENTIFICATION BY
MASS SPECTROMETRY, AND MUTAGENESIS OF CYS-160.
PubMed=10024876; DOI=10.1016/S1097-2765(00)80171-9;
Hickman A.B., Klein D.C., Dyda F.;
"Melatonin biosynthesis: the structure of serotonin N-
acetyltransferase at 2.5 A resolution suggests a catalytic
mechanism.";
Mol. Cell 3:23-32(1999).
[10]
X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 1-201 IN COMPLEX WITH THE
ACETYL-COA AND SUBSTRATE ANALOG COA-S-ACETYLTRYPTAMINE AND YWHAZ, AND
AFFINITY FOR ACETYL-COA AND SEROTONIN.
PubMed=11336675; DOI=10.1016/S0092-8674(01)00316-6;
Obsil T., Ghirlando R., Klein D.C., Ganguly S., Dyda F.;
"Crystal structure of the 14-3-3zeta:serotonin N-acetyltransferase
complex. a role for scaffolding in enzyme regulation.";
Cell 105:257-267(2001).
[11]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF MUTANT PHE-168 IN COMPLEX
WITH SUBSTRATE ANALOG, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
PROPERTIES, AND MUTAGENESIS OF HIS-120; HIS-122 AND TYR-168.
PubMed=11884405; DOI=10.1074/jbc.M200595200;
Scheibner K.A., De Angelis J., Burley S.K., Cole P.A.;
"Investigation of the roles of catalytic residues in serotonin N-
acetyltransferase.";
J. Biol. Chem. 277:18118-18126(2002).
[12]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEXES WITH ACETYL-COA AND
SUBSTRATE ANALOGS, CATALYTIC ACTIVITY, AND MUTAGENESIS OF CYS-160 AND
GLU-161.
PubMed=11902838; DOI=10.1006/jmbi.2001.5371;
Wolf E., De Angelis J., Khalil E.M., Cole P.A., Burley S.K.;
"X-ray crystallographic studies of serotonin N-acetyltransferase
catalysis and inhibition.";
J. Mol. Biol. 317:215-224(2002).
-!- FUNCTION: Controls the night/day rhythm of melatonin production in
the pineal gland. Catalyzes the N-acetylation of serotonin into N-
acetylserotonin, the penultimate step in the synthesis of
melatonin. {ECO:0000269|PubMed:15644438}.
-!- CATALYTIC ACTIVITY: Acetyl-CoA + a 2-arylethylamine = CoA + an N-
acetyl-2-arylethylamine. {ECO:0000269|PubMed:10319816,
ECO:0000269|PubMed:11884405, ECO:0000269|PubMed:11902838,
ECO:0000269|PubMed:18362150}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=0.29 mM for acetyl-CoA {ECO:0000269|PubMed:11313340,
ECO:0000269|PubMed:11884405};
KM=0.17 mM for tryptamine {ECO:0000269|PubMed:11313340,
ECO:0000269|PubMed:11884405};
KM=0.20 mM for tryptamine {ECO:0000269|PubMed:11313340,
ECO:0000269|PubMed:11884405};
KM=0.31 mM for 5-hydroxytryptamine {ECO:0000269|PubMed:11313340,
ECO:0000269|PubMed:11884405};
KM=3.4 mM for phenylethylamine {ECO:0000269|PubMed:11313340,
ECO:0000269|PubMed:11884405};
KM=3.4 mM for tyramine {ECO:0000269|PubMed:11313340,
ECO:0000269|PubMed:11884405};
-!- PATHWAY: Aromatic compound metabolism; melatonin biosynthesis;
melatonin from serotonin: step 1/2. {ECO:0000305}.
-!- SUBUNIT: Monomer. Interacts with several 14-3-3 proteins,
including YWHAB, YWHAE, YWHAG and YWHAZ, preferentially when
phosphorylated at Thr-31. Phosphorylation on Ser-205 also allows
binding to YWHAZ, but with a 10-fold lower affinity. The
interaction with YWHAZ considerably increases affinity for
arylalkylamines and acetyl-CoA and protects the enzyme from
dephosphorylation and proteasomal degradation. It may also prevent
thiol-dependent inactivation. The physiological stoichiometry of
the interaction is not clear. In vitro studies show either 1:2
(i.e. 1 AANAT molecule per YWHAZ dimer) (PubMed:11427721) or 2:2
(PubMed:11336675). {ECO:0000269|PubMed:10319816,
ECO:0000269|PubMed:11336675, ECO:0000269|PubMed:11427721,
ECO:0000269|PubMed:11884405, ECO:0000269|PubMed:14578935,
ECO:0000269|PubMed:15644438}.
-!- INTERACTION:
P63104:YWHAZ (xeno); NbExp=3; IntAct=EBI-446413, EBI-347088;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q16613}.
-!- TISSUE SPECIFICITY: Highest expression in the pineal gland,
followed by retina. Expressed at much lower levels in brainstem
and pituitary gland. AANAT activity also detected at low levels in
the olfactory lobe. {ECO:0000269|PubMed:7502081}.
-!- INDUCTION: Exhibits night/day variations with a 7-fold increased
activity at night. At the mRNA level, the nocturnal increase is
lower than 2-fold. {ECO:0000269|PubMed:11313340,
ECO:0000269|PubMed:15644438, ECO:0000269|PubMed:7502081}.
-!- PTM: cAMP-dependent phosphorylation on both N-terminal Thr-31 and
C-terminal Ser-205 regulates AANAT activity by promoting
interaction with 14-3-3 proteins. {ECO:0000250}.
-!- SIMILARITY: Belongs to the acetyltransferase family. AANAT
subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; U29663; AAC48690.1; -; mRNA.
RefSeq; NP_001009461.1; NM_001009461.1.
UniGene; Oar.638; -.
PDB; 1B6B; X-ray; 2.50 A; A/B=28-201.
PDB; 1CJW; X-ray; 1.80 A; A=30-195.
PDB; 1IB1; X-ray; 2.70 A; E/F/G/H=2-201.
PDB; 1KUV; X-ray; 2.00 A; A=1-207.
PDB; 1KUX; X-ray; 1.80 A; A=1-207.
PDB; 1KUY; X-ray; 2.40 A; A=1-207.
PDB; 1L0C; X-ray; 2.30 A; A=1-207.
PDBsum; 1B6B; -.
PDBsum; 1CJW; -.
PDBsum; 1IB1; -.
PDBsum; 1KUV; -.
PDBsum; 1KUX; -.
PDBsum; 1KUY; -.
PDBsum; 1L0C; -.
ProteinModelPortal; Q29495; -.
SMR; Q29495; -.
IntAct; Q29495; 1.
MINT; MINT-7997059; -.
BindingDB; Q29495; -.
ChEMBL; CHEMBL5452; -.
iPTMnet; Q29495; -.
GeneID; 443531; -.
KEGG; oas:443531; -.
CTD; 15; -.
HOVERGEN; HBG016332; -.
KO; K00669; -.
BRENDA; 2.3.1.87; 2668.
UniPathway; UPA00837; UER00815.
EvolutionaryTrace; Q29495; -.
PRO; PR:Q29495; -.
Proteomes; UP000002356; Unplaced.
GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
GO; GO:0004059; F:aralkylamine N-acetyltransferase activity; IDA:UniProtKB.
GO; GO:0071320; P:cellular response to cAMP; ISS:UniProtKB.
GO; GO:0007623; P:circadian rhythm; ISS:UniProtKB.
GO; GO:0030187; P:melatonin biosynthetic process; IDA:UniProtKB.
GO; GO:0006474; P:N-terminal protein amino acid acetylation; ISS:UniProtKB.
InterPro; IPR016181; Acyl_CoA_acyltransferase.
InterPro; IPR000182; GNAT_dom.
Pfam; PF00583; Acetyltransf_1; 1.
SUPFAM; SSF55729; SSF55729; 1.
PROSITE; PS51186; GNAT; 1.
1: Evidence at protein level;
3D-structure; Acyltransferase; Biological rhythms; Complete proteome;
Cytoplasm; Melatonin biosynthesis; Phosphoprotein; Reference proteome;
Transferase.
CHAIN 1 207 Serotonin N-acetyltransferase.
/FTId=PRO_0000074586.
DOMAIN 35 196 N-acetyltransferase.
{ECO:0000255|PROSITE-ProRule:PRU00532}.
REGION 28 35 YWHAZ-binding.
REGION 124 126 Acetyl-CoA binding.
{ECO:0000269|PubMed:10319816,
ECO:0000269|PubMed:11336675,
ECO:0000269|PubMed:11902838}.
REGION 132 137 Acetyl-CoA binding.
{ECO:0000269|PubMed:10319816,
ECO:0000269|PubMed:11336675,
ECO:0000269|PubMed:11902838}.
REGION 168 170 Acetyl-CoA binding.
{ECO:0000269|PubMed:10319816,
ECO:0000269|PubMed:11336675,
ECO:0000269|PubMed:11902838}.
BINDING 124 124 Substrate; via amide nitrogen.
{ECO:0000269|PubMed:11336675,
ECO:0000269|PubMed:11884405,
ECO:0000269|PubMed:11902838}.
BINDING 159 159 Substrate; via carbonyl oxygen.
{ECO:0000269|PubMed:11336675,
ECO:0000269|PubMed:11884405,
ECO:0000269|PubMed:11902838}.
SITE 120 120 Important for the catalytic mechanism;
involved in substrate deprotonation.
{ECO:0000269|PubMed:10319816,
ECO:0000269|PubMed:11884405}.
SITE 122 122 Important for the catalytic mechanism;
involved in substrate deprotonation.
{ECO:0000269|PubMed:10319816,
ECO:0000269|PubMed:11884405}.
MOD_RES 31 31 Phosphothreonine; by PKA.
{ECO:0000269|PubMed:11427721,
ECO:0000269|PubMed:14578935,
ECO:0000269|PubMed:15644438}.
MOD_RES 205 205 Phosphoserine; by PKA.
{ECO:0000269|PubMed:15644438}.
MUTAGEN 31 31 T->A: Loss of PKA-promoted YWHAZ-binding;
when associated with G-205.
{ECO:0000269|PubMed:15644438}.
MUTAGEN 57 57 I->A: No effect on enzymatic activity;
when associated with A-59.
{ECO:0000269|PubMed:18362150}.
MUTAGEN 59 59 V->A: No effect on enzymatic activity;
when associated with A-57.
{ECO:0000269|PubMed:18362150}.
MUTAGEN 63 65 Missing: Drastic loss of enzymatic
activity. {ECO:0000269|PubMed:18362150}.
MUTAGEN 64 64 P->A,G,W: Drastic loss of enzymatic
activity. {ECO:0000269|PubMed:18362150}.
MUTAGEN 120 120 H->A: Reduces catalytic activity 270-fold
and decreases affinity for acetyl-
coenzyme A; when associated with A-122.
{ECO:0000269|PubMed:10319816,
ECO:0000269|PubMed:11884405}.
MUTAGEN 120 120 H->Q: Decreases affinity for acetyl-
coenzyme A and for substrate.
{ECO:0000269|PubMed:10319816,
ECO:0000269|PubMed:11884405}.
MUTAGEN 122 122 H->A: Reduces catalytic activity 270-fold
and decreases affinity for acetyl-
coenzyme A; when associated with A-120.
{ECO:0000269|PubMed:10319816,
ECO:0000269|PubMed:11884405}.
MUTAGEN 122 122 H->Q: Decreases affinity for acetyl-
coenzyme A and for substrate.
{ECO:0000269|PubMed:10319816,
ECO:0000269|PubMed:11884405}.
MUTAGEN 160 160 C->A: No effect on catalytic activity.
{ECO:0000269|PubMed:10024876,
ECO:0000269|PubMed:11902838}.
MUTAGEN 160 160 C->S: Reduces catalytic activity.
{ECO:0000269|PubMed:10024876,
ECO:0000269|PubMed:11902838}.
MUTAGEN 161 161 E->A: No effect.
{ECO:0000269|PubMed:11902838}.
MUTAGEN 168 168 Y->F: Reduces catalytic activity 30-fold.
{ECO:0000269|PubMed:10319816,
ECO:0000269|PubMed:11884405}.
MUTAGEN 205 205 S->G: Loss of PKA-promoted YWHAZ-binding;
when associated with A-31.
{ECO:0000269|PubMed:15644438}.
STRAND 34 38 {ECO:0000244|PDB:1CJW}.
HELIX 42 44 {ECO:0000244|PDB:1CJW}.
HELIX 45 55 {ECO:0000244|PDB:1CJW}.
HELIX 57 60 {ECO:0000244|PDB:1CJW}.
HELIX 67 76 {ECO:0000244|PDB:1CJW}.
HELIX 78 80 {ECO:0000244|PDB:1CJW}.
STRAND 81 86 {ECO:0000244|PDB:1CJW}.
STRAND 89 99 {ECO:0000244|PDB:1CJW}.
STRAND 101 103 {ECO:0000244|PDB:1CJW}.
HELIX 106 110 {ECO:0000244|PDB:1CJW}.
STRAND 118 126 {ECO:0000244|PDB:1CJW}.
HELIX 128 130 {ECO:0000244|PDB:1KUX}.
STRAND 132 134 {ECO:0000244|PDB:1KUX}.
HELIX 135 148 {ECO:0000244|PDB:1CJW}.
STRAND 150 152 {ECO:0000244|PDB:1L0C}.
STRAND 155 160 {ECO:0000244|PDB:1CJW}.
HELIX 162 164 {ECO:0000244|PDB:1CJW}.
HELIX 165 169 {ECO:0000244|PDB:1CJW}.
TURN 170 172 {ECO:0000244|PDB:1CJW}.
STRAND 173 178 {ECO:0000244|PDB:1CJW}.
STRAND 189 194 {ECO:0000244|PDB:1CJW}.
SEQUENCE 207 AA; 23077 MW; F6752A872F436DF9 CRC64;
MSTPSVHCLK PSPLHLPSGI PGSPGRQRRH TLPANEFRCL TPEDAAGVFE IEREAFISVS
GNCPLNLDEV QHFLTLCPEL SLGWFVEGRL VAFIIGSLWD EERLTQESLA LHRPRGHSAH
LHALAVHRSF RQQGKGSVLL WRYLHHVGAQ PAVRRAVLMC EDALVPFYQR FGFHPAGPCA
IVVGSLTFTE MHCSLRGHAA LRRNSDR


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