AANAT

Functionⁱ

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.

1 Publication

Catalytic activityⁱ

2-arylethylamine
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Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
+
acetyl-CoA
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Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
=
CoA
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Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
+
H⁺
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See the description of this molecule in ChEBI.
+
N-acetyl-2-arylethylamine
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Search chemical reactions in Rhea for this molecule.
See the description of this molecule in ChEBI.
4 Publications
Manual assertion based on experiment inⁱ
- Ref.7
  "Evidence that proline focuses movement of the floppy loop of arylalkylamine N-acetyltransferase (EC 2.3.1.87)."
  Pavlicek J., Coon S.L., Ganguly S., Weller J.L., Hassan S.A., Sackett D.L., Klein D.C.
  J. Biol. Chem. 283:14552-14558(2008) [PubMed] [Europe PMC] [Abstract]
  Cited for: CATALYTIC ACTIVITY, MUTAGENESIS OF ILE-57; VAL-59; PRO-64 AND 63-CYS--LEU-65.
- Ref.8
  "The structural basis of ordered substrate binding by serotonin N-acetyltransferase: enzyme complex at 1.8 A resolution with a bisubstrate analog."
  Hickman A.B., Namboodiri M.A., Klein D.C., Dyda F.
  Cell 97:361-369(1999) [PubMed] [Europe PMC] [Abstract]
  Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 30-195 IN COMPLEX WITH COA-S-ACETYLTRYPTAMINE, IDENTIFICATION BY MASS SPECTROMETRY, CATALYTIC ACTIVITY, MUTAGENESIS OF HIS-120; HIS-122 AND TYR-168.
- Ref.11
  "Investigation of the roles of catalytic residues in serotonin N-acetyltransferase."
  Scheibner K.A., De Angelis J., Burley S.K., Cole P.A.
  J. Biol. Chem. 277:18118-18126(2002) [PubMed] [Europe PMC] [Abstract]
  Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF MUTANT PHE-168 IN COMPLEX WITH SUBSTRATE ANALOG, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF HIS-120; HIS-122 AND TYR-168.
- Ref.12
  "X-ray crystallographic studies of serotonin N-acetyltransferase catalysis and inhibition."
  Wolf E., De Angelis J., Khalil E.M., Cole P.A., Burley S.K.
  J. Mol. Biol. 317:215-224(2002) [PubMed] [Europe PMC] [Abstract]
  Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEXES WITH ACETYL-COA AND SUBSTRATE ANALOGS, CATALYTIC ACTIVITY, MUTAGENESIS OF CYS-160 AND GLU-161.
EC:
2.3.1.87
- Search proteins in UniProtKB for this EC number.
- See the description of this EC number in ENZYME.
- Search reactions for this EC number in Rhea.
4 Publications
Manual assertion based on experiment inⁱ
- Ref.7
  "Evidence that proline focuses movement of the floppy loop of arylalkylamine N-acetyltransferase (EC 2.3.1.87)."
  Pavlicek J., Coon S.L., Ganguly S., Weller J.L., Hassan S.A., Sackett D.L., Klein D.C.
  J. Biol. Chem. 283:14552-14558(2008) [PubMed] [Europe PMC] [Abstract]
  Cited for: CATALYTIC ACTIVITY, MUTAGENESIS OF ILE-57; VAL-59; PRO-64 AND 63-CYS--LEU-65.
- Ref.8
  "The structural basis of ordered substrate binding by serotonin N-acetyltransferase: enzyme complex at 1.8 A resolution with a bisubstrate analog."
  Hickman A.B., Namboodiri M.A., Klein D.C., Dyda F.
  Cell 97:361-369(1999) [PubMed] [Europe PMC] [Abstract]
  Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 30-195 IN COMPLEX WITH COA-S-ACETYLTRYPTAMINE, IDENTIFICATION BY MASS SPECTROMETRY, CATALYTIC ACTIVITY, MUTAGENESIS OF HIS-120; HIS-122 AND TYR-168.
- Ref.11
  "Investigation of the roles of catalytic residues in serotonin N-acetyltransferase."
  Scheibner K.A., De Angelis J., Burley S.K., Cole P.A.
  J. Biol. Chem. 277:18118-18126(2002) [PubMed] [Europe PMC] [Abstract]
  Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF MUTANT PHE-168 IN COMPLEX WITH SUBSTRATE ANALOG, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF HIS-120; HIS-122 AND TYR-168.
- Ref.12
  "X-ray crystallographic studies of serotonin N-acetyltransferase catalysis and inhibition."
  Wolf E., De Angelis J., Khalil E.M., Cole P.A., Burley S.K.
  J. Mol. Biol. 317:215-224(2002) [PubMed] [Europe PMC] [Abstract]
  Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEXES WITH ACETYL-COA AND SUBSTRATE ANALOGS, CATALYTIC ACTIVITY, MUTAGENESIS OF CYS-160 AND GLU-161.
Source:
Rhea
Search for this reaction in UniProtKB.
See the description of this reaction in Rhea.
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2-arylethylamine
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+
acetyl-CoA
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=
CoA
+
H⁺
+
N-acetyl-2-arylethylamine
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Kineticsⁱ

Pathwayⁱ: melatonin biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes melatonin from serotonin.Curated This subpathway is part of the pathway melatonin biosynthesis, which is itself part of Aromatic compound metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes melatonin from serotonin, the pathway melatonin biosynthesis and in Aromatic compound metabolism.

Sites

Feature key	Position(s)	DescriptionActions	Length
Siteⁱ	120	Important for the catalytic mechanism; involved in substrate deprotonation2 Publications	1
Siteⁱ	122	Important for the catalytic mechanism; involved in substrate deprotonation2 Publications	1
Binding siteⁱ	124	Substrate; via amide nitrogen3 Publications	1
Binding siteⁱ	159	Substrate; via carbonyl oxygen3 Publications	1

GO - Molecular functionⁱ

aralkylamine N-acetyltransferase activity
Source: UniProtKB
Inferred from direct assayⁱ
- Ref.2
  "cAMP regulation of arylalkylamine N-acetyltransferase (AANAT, EC 2.3.1.87): a new cell line (1E7) provides evidence of intracellular AANAT activation."
  Coon S.L., Weller J.L., Korf H.-W., Namboodiri M.A., Rollag M., Klein D.C.
  J. Biol. Chem. 276:24097-24107(2001) [PubMed] [Europe PMC] [Abstract]
  Cited for: INDUCTION, BIOPHYSICOCHEMICAL PROPERTIES.

Complete GO annotation on QuickGO ...

GO - Biological processⁱ

Complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Acyltransferase, Transferase
Biological process	Biological rhythms, Melatonin biosynthesis

Enzyme and pathway databases

BRENDAⁱ	2.3.1.87, 2668
SABIO-RKⁱ	Q29495
UniPathwayⁱ	UPA00837;UER00815

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Serotonin N-acetyltransferase (EC:2.3.1.874 Publications) Short name: Serotonin acetylase Alternative name(s): Aralkylamine N-acetyltransferase Short name: AA-NAT
Gene namesⁱ	Name:AANAT Synonyms:SNAT
Organismⁱ	Ovis aries (Sheep)
Taxonomic identifierⁱ	9940 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Laurasiatheria › Artiodactyla › Ruminantia › Pecora › Bovidae › Caprinae › Ovis
Proteomesⁱ	UP000002356 Componentⁱ: Unplaced

Keywords - Cellular componentⁱ

Cytoplasm

Pathology & Biotechⁱ

Mutagenesis

Feature key	Position(s)	DescriptionActions	Length
Mutagenesisⁱ	31	T → A: Loss of PKA-promoted YWHAZ-binding; when associated with G-205. 1 Publication	1
Mutagenesisⁱ	57	I → A: No effect on enzymatic activity; when associated with A-59. 1 Publication	1
Mutagenesisⁱ	59	V → A: No effect on enzymatic activity; when associated with A-57. 1 Publication	1
Mutagenesisⁱ	63 – 65	Missing : Drastic loss of enzymatic activity. 1 Publication	3
Mutagenesisⁱ	64	P → A, G or W: Drastic loss of enzymatic activity. 1 Publication	1
Mutagenesisⁱ	120	H → A: Reduces catalytic activity 270-fold and decreases affinity for acetyl-coenzyme A; when associated with A-122. 2 Publications	1
Mutagenesisⁱ	120	H → Q: Decreases affinity for acetyl-coenzyme A and for substrate. 2 Publications	1
Mutagenesisⁱ	122	H → A: Reduces catalytic activity 270-fold and decreases affinity for acetyl-coenzyme A; when associated with A-120. 2 Publications	1
Mutagenesisⁱ	122	H → Q: Decreases affinity for acetyl-coenzyme A and for substrate. 2 Publications	1
Mutagenesisⁱ	160	C → A: No effect on catalytic activity. 2 Publications	1
Mutagenesisⁱ	160	C → S: Reduces catalytic activity. 2 Publications	1
Mutagenesisⁱ	161	E → A: No effect. 1 Publication	1
Mutagenesisⁱ	168	Y → F: Reduces catalytic activity 30-fold. 2 Publications	1
Mutagenesisⁱ	205	S → G: Loss of PKA-promoted YWHAZ-binding; when associated with A-31. 1 Publication	1

Chemistry databases

ChEMBLⁱ	CHEMBL5452

ChEMBLⁱ

CHEMBL5452

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000074586	1 – 207	Serotonin N-acetyltransferaseAdd BLAST		207

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Modified residueⁱ	31	Phosphothreonine; by PKA3 Publications		1
Modified residueⁱ	205	Phosphoserine; by PKA1 Publication		1

Post-translational modificationⁱ

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.By similarity

Keywords - PTMⁱ

Phosphoprotein

PTM databases

iPTMnetⁱ	Q29495

iPTMnetⁱ

Q29495

Expressionⁱ

Tissue specificityⁱ

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.1 Publication

Inductionⁱ

Exhibits night/day variations with a 7-fold increased activity at night. At the mRNA level, the nocturnal increase is lower than 2-fold.3 Publications

Interactionⁱ

Subunit structureⁱ

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).

6 Publications

Binary interactionsⁱ

Q29495

With	#Exp.	IntAct
YWHAZ [P63104] from Homo sapiens.	3	EBI-446413,EBI-347088

Protein-protein interaction databases

IntActⁱ	Q29495, 1 interactor
Molecular INTeraction database More...MINTⁱ	Q29495
STRINGⁱ	9940.ENSOARP00000007675

Chemistry databases

BindingDBⁱ

Q29495

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Beta strandⁱ	34 – 38	Combined sources	5
Helixⁱ	42 – 44	Combined sources	3
Helixⁱ	45 – 55	Combined sources	11
Helixⁱ	57 – 60	Combined sources	4
Helixⁱ	67 – 76	Combined sources	10
Helixⁱ	78 – 80	Combined sources	3
Beta strandⁱ	81 – 86	Combined sources	6
Beta strandⁱ	89 – 99	Combined sources	11
Beta strandⁱ	101 – 103	Combined sources	3
Helixⁱ	106 – 110	Combined sources	5
Beta strandⁱ	118 – 126	Combined sources	9
Helixⁱ	128 – 130	Combined sources	3
Beta strandⁱ	132 – 134	Combined sources	3
Helixⁱ	135 – 148	Combined sources	14
Beta strandⁱ	150 – 152	Combined sources	3
Beta strandⁱ	155 – 160	Combined sources	6
Helixⁱ	162 – 164	Combined sources	3
Helixⁱ	165 – 169	Combined sources	5
Turnⁱ	170 – 172	Combined sources	3
Beta strandⁱ	173 – 178	Combined sources	6
Beta strandⁱ	189 – 194	Combined sources	6

Show more details

3D structure databases

AlphaFoldDBⁱ	Q29495
SMRⁱ	Q29495
ModBaseⁱ	Search...
PDBe-KBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ

Q29495

Family & Domainsⁱ

Domains and Repeats

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Domainⁱ	35 – 196	N-acetyltransferasePROSITE-ProRule annotationAdd BLAST		162

Region

Feature key	Position(s)	DescriptionActions	Length
Regionⁱ	1 – 29	DisorderedSequence analysisAdd BLAST	29
Regionⁱ	28 – 35	YWHAZ-binding	8
Regionⁱ	124 – 126	Acetyl-CoA binding3 Publications	3
Regionⁱ	132 – 137	Acetyl-CoA binding3 Publications	6
Regionⁱ	168 – 170	Acetyl-CoA binding3 Publications	3

Sequence similaritiesⁱ

Belongs to the acetyltransferase family. AANAT subfamily.Curated

Phylogenomic databases

eggNOGⁱ	KOG4144, Eukaryota
Database of Orthologous Groups More...OrthoDBⁱ	1528352at2759

Family and domain databases

IDEALⁱ	IID50013
InterProⁱ	View protein in InterPro IPR016181, Acyl_CoA_acyltransferase IPR000182, GNAT_dom
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF00583, Acetyltransf_1, 1 hit
SUPFAMⁱ	SSF55729, SSF55729, 1 hit
PROSITEⁱ	View protein in PROSITE PS51186, GNAT, 1 hit

Sequenceⁱ

Sequence statusⁱ: Complete.

Q29495-1 [UniParc]FASTA Add to basket

« Hide

        10         20         30         40         50
MSTPSVHCLK PSPLHLPSGI PGSPGRQRRH TLPANEFRCL TPEDAAGVFE 
        60         70         80         90        100
IEREAFISVS GNCPLNLDEV QHFLTLCPEL SLGWFVEGRL VAFIIGSLWD 
       110        120        130        140        150
EERLTQESLA LHRPRGHSAH LHALAVHRSF RQQGKGSVLL WRYLHHVGAQ 
       160        170        180        190        200
PAVRRAVLMC EDALVPFYQR FGFHPAGPCA IVVGSLTFTE MHCSLRGHAA 

LRRNSDR

Length:207

Mass (Da):23,077

Last modified:November 1, 1996 - v1

Checksum:ⁱF6752A872F436DF9

GO

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	U29663 mRNA Translation: AAC48690.1
NCBI Reference Sequences More...RefSeqⁱ	NP_001009461.1, NM_001009461.1

Genome annotation databases

GeneIDⁱ	443531
KEGGⁱ	oas:443531

Similar proteinsⁱ

100% Identity
90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length	Source
Q29495	Aralkylamine N-acetyltransferase		SHEEP		207	UniRef100_Q29495
+3

Protein	Similar proteins		Species	Score	Length	Source
Q29495	Serotonin N-acetyltransferase		BOVIN		207	UniRef90_Q29495
Aralkylamine N-acetyltransferase		SHEEP		207
Aralkylamine N-acetyltransferase		CAPHI		207
Serotonin N-acetyltransferase		BOBOX		207
Arylalkylamine-N-acetyltransferase		BOSMU		207
+21

Protein	Similar proteins		Species	Score	Length	Source
Q29495	Serotonin N-acetyltransferase	)	HUMAN		207	UniRef50_Q16613
Serotonin N-acetyltransferase		BOVIN		207
Aralkylamine N-acetyltransferase		Equus asinus asinus		207
N-acetyltransferase domain-containing protein		DICBM		246
serotonin N-acetyltransferase isoform X1		ERIEU		264
+81

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	U29663 mRNA Translation: AAC48690.1
RefSeqⁱ	NP_001009461.1, NM_001009461.1

3D structure databases

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...PDBjⁱ Links Updated	PDB entry	Method	Resolution (Å)	Chain	Positions	PDBsum
	1B6B	X-ray	2.50	A/B	28-201	[»]
	1CJW	X-ray	1.80	A	30-195	[»]
	1IB1	X-ray	2.70	E/F/G/H	2-201	[»]
	1KUV	X-ray	2.00	A	1-207	[»]
	1KUX	X-ray	1.80	A	1-207	[»]
	1KUY	X-ray	2.40	A	1-207	[»]
	1L0C	X-ray	2.30	A	1-207	[»]
AlphaFoldDBⁱ	Q29495
SMRⁱ	Q29495
ModBaseⁱ	Search...
PDBe-KBⁱ	Search...

Protein-protein interaction databases

IntActⁱ	Q29495, 1 interactor
MINTⁱ	Q29495
STRINGⁱ	9940.ENSOARP00000007675

Chemistry databases

BindingDBⁱ	Q29495
ChEMBLⁱ	CHEMBL5452

PTM databases

iPTMnetⁱ	Q29495

iPTMnetⁱ

Q29495

Genome annotation databases

GeneIDⁱ	443531
KEGGⁱ	oas:443531

Organism-specific databases

CTDⁱ	15

CTDⁱ

15

Phylogenomic databases

eggNOGⁱ	KOG4144, Eukaryota
OrthoDBⁱ	1528352at2759

Enzyme and pathway databases

UniPathwayⁱ	UPA00837;UER00815
BRENDAⁱ	2.3.1.87, 2668
SABIO-RKⁱ	Q29495

Miscellaneous databases

EvolutionaryTraceⁱ	Q29495
Protein Ontology More...PROⁱ	PR:Q29495

Family and domain databases

IDEALⁱ	IID50013
InterProⁱ	View protein in InterPro IPR016181, Acyl_CoA_acyltransferase IPR000182, GNAT_dom
Pfamⁱ	View protein in Pfam PF00583, Acetyltransf_1, 1 hit
SUPFAMⁱ	SSF55729, SSF55729, 1 hit
PROSITEⁱ	View protein in PROSITE PS51186, GNAT, 1 hit
MobiDBⁱ	Search...

Entry informationⁱ

Entry nameⁱ	SNAT_SHEEP
Accessionⁱ	Q29495Primary (citable) accession number: Q29495
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
	Last sequence update:	November 1, 1996
	Last modified:	May 25, 2022
	This is version 127 of the entry and version 1 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Chordata Protein Annotation Program

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UniProtKB - Q29495 (SNAT_SHEEP)

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Serotonin N-acetyltransferase

Select a section on the left to see content.

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: melatonin biosynthesis

Sites

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

Enzyme and pathway databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Cytoplasm and Cytosol

Other locations

Keywords - Cellular componenti

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Chemistry databases

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Amino acid modifications

Keywords - PTMi

PTM databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

Q29495

Protein-protein interaction databases

Chemistry databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

3D structure databases

Miscellaneous databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Region

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Phylogenomic databases

Family and domain databases

Sequence databases

Genome annotation databases

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

3D structure databases

Protein-protein interaction databases

Chemistry databases

PTM databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

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Functionⁱ

Catalytic activityⁱ

Kineticsⁱ

Pathwayⁱ: melatonin biosynthesis

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Keywords - PTMⁱ

Expressionⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ