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P10950 (ASMT_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 71. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Acetylserotonin O-methyltransferase

EC=2.1.1.4
Alternative name(s):
Hydroxyindole O-methyltransferase
Short name=HIOMT
Gene names
Name:ASMT
OrganismBos taurus (Bovine)
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length345 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Produces melatonin (N-acetyl-5-methoxytryptamine) from N-acetylserotonin.

Catalytic activity

S-adenosyl-L-methionine + N-acetylserotonin = S-adenosyl-L-homocysteine + N-acetyl-5-methoxytryptamine.

Pathway

Aromatic compound metabolism; melatonin biosynthesis; melatonin from serotonin: step 1/2.

Tissue specificity

Expressed in the pineal gland (at protein level). Not detectable in retina, nor in liver. Ref.1 Ref.3

Sequence similarities

Belongs to the methyltransferase superfamily.

Ontologies

Keywords
   Biological processMelatonin biosynthesis
   LigandS-adenosyl-L-methionine
   Molecular functionMethyltransferase
Transferase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processmelatonin biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionacetylserotonin O-methyltransferase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 345345Acetylserotonin O-methyltransferase
PRO_0000083980

Experimental info

Sequence conflict181G → A in AAA30565. Ref.1
Sequence conflict58 – 12164QGTEL…WRHLA → GDRAATEHLCVPEAAASRRE GRKSCVCKHGARQHLPGERQ PQVPAGHAAVRGQDRLRLLA PPG in AAA30565. Ref.1
Sequence conflict315 – 34531AEYRA…VLARK → GRSTARSVGPAASETCGDGG RGEPTMLSWPGNQACSV in AAA30565. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P10950 [UniParc].

Last modified November 1, 1997. Version 2.
Checksum: AA8EB84EB8D4A7E4

FASTA34537,924
        10         20         30         40         50         60 
MCSQEGEGYS LLKEYANGFM VSQVLFAACE LGVFELLAEA LEPLDSAAVS SHLGSSPQGT 

        70         80         90        100        110        120 
ELLLNTCVSL KLLQADVRGG KAVYANTELA STYLVRGSPR SQRDMLLYAG RTAYVCWRHL 

       130        140        150        160        170        180 
AEAVREGRNQ YLKAFGIPSE ELFSAIYRSE DERLQFMQGL QDVWRLEGAT VLAAFDLSPF 

       190        200        210        220        230        240 
PLICDLGGGS GALAKACVSL YPGCRAIVFD IPGVVQIAKR HFSASEDERI SFHEGDFFKD 

       250        260        270        280        290        300 
ALPEADLYIL ARVLHDWTDA KCSHLLQRVY RACRTGGGIL VIESLLDTDG RGPLTTLLYS 

       310        320        330        340 
LNMLVQTEGR ERTPAEYRAL LGPAGFRDVR CRRTGGTYDA VLARK 

« Hide

References

[1]"Molecular cloning and nucleotide sequence of cDNA encoding hydroxyindole O-methyltransferase of bovine pineal glands."
Ishida I., Obinata M., Deguchi T.
J. Biol. Chem. 262:2895-2899(1987) [PubMed: 3818627] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
Tissue: Pineal gland.
[2]"Bovine hydroxyindole-O-methyltransferase. Significant sequence revision."
Donohue S.J., Roseboom P.H., Klein D.C.
J. Biol. Chem. 267:5184-5185(1992) [PubMed: 1544900] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], SEQUENCE REVISION.
[3]"Human hydroxyindole-O-methyltransferase in pineal gland, retina and Y79 retinoblastoma cells."
Bernard M., Donohue S.J., Klein D.C.
Brain Res. 696:37-48(1995) [PubMed: 8574683] [Abstract]
Cited for: TISSUE SPECIFICITY.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J02671 mRNA. Translation: AAA30565.1.
M81862 mRNA. Translation: AAA30570.1.
IPIIPI00691900.
PIRA42106.
RefSeqNP_803459.1. NM_177493.2.
UniGeneBt.3930.

3D structure databases

ProteinModelPortalP10950.
ModBaseSearch...

Proteomic databases

PRIDEP10950.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID281013.
KEGGbta:281013.

Organism-specific databases

CTD438.

Phylogenomic databases

HOVERGENHBG001526.

Family and domain databases

InterProIPR016461. O-MeTrfase_COMT_euk.
IPR001077. O_MeTrfase_2.
IPR011991. WHTH_trsnscrt_rep_DNA-bd.
[Graphical view]
Gene3DG3DSA:1.10.10.10. Wing_hlx_DNA_bd. 1 hit.
KOK00543.
PfamPF00891. Methyltransf_2. 1 hit.
[Graphical view]
PIRSFPIRSF005739. O-mtase. 1 hit.
ProtoNetSearch...

Entry information

Entry nameASMT_BOVIN
AccessionPrimary (citable) accession number: P10950
Secondary accession number(s): Q28123
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: November 1, 1997
Last modified: January 25, 2012
This is version 71 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families