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Protein

Phenylethanolamine N-methyltransferase

Gene

Pnmt

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

Converts noradrenaline to adrenaline.

Catalytic activityi

S-adenosyl-L-methionine + phenylethanolamine = S-adenosyl-L-homocysteine + N-methylphenylethanolamine.

Pathwayi: (R)-adrenaline biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes (R)-adrenaline from (R)-noradrenaline.
Proteins known to be involved in this subpathway in this organism are:
  1. Phenylethanolamine N-methyltransferase (Pnmt)
This subpathway is part of the pathway (R)-adrenaline biosynthesis, which is itself part of Catecholamine biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes (R)-adrenaline from (R)-noradrenaline, the pathway (R)-adrenaline biosynthesis and in Catecholamine biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei36 – 361S-adenosyl-L-methionineBy similarity
Binding sitei41 – 411S-adenosyl-L-methionineBy similarity
Binding sitei86 – 861S-adenosyl-L-methionineBy similarity
Binding sitei102 – 1021S-adenosyl-L-methionineBy similarity
Binding sitei107 – 1071S-adenosyl-L-methionineBy similarity
Binding sitei182 – 1821S-adenosyl-L-methionine; via carbonyl oxygenBy similarity
Binding sitei220 – 2201SubstrateBy similarity

GO - Molecular functioni

  • methyltransferase activity Source: RGD
  • phenylethanolamine N-methyltransferase activity Source: RGD
  • S-adenosylmethionine-dependent methyltransferase activity Source: RGD
  • transferase activity Source: RGD

GO - Biological processi

  • adrenal gland development Source: RGD
  • cellular response to dexamethasone stimulus Source: RGD
  • cellular response to growth factor stimulus Source: RGD
  • cellular response to peptide hormone stimulus Source: RGD
  • epinephrine biosynthetic process Source: RGD
  • norepinephrine metabolic process Source: RGD
  • response to activity Source: RGD
  • response to cold Source: RGD
  • response to corticosteroid Source: RGD
  • response to ethanol Source: RGD
  • response to ether Source: RGD
  • response to hypoxia Source: RGD
  • response to immobilization stress Source: RGD
  • response to insulin Source: RGD
  • response to isolation stress Source: RGD
  • response to peptide hormone Source: RGD
  • response to water deprivation Source: RGD
  • S-adenosylhomocysteine metabolic process Source: RGD
  • S-adenosylmethionine metabolic process Source: RGD
  • sensory perception of taste Source: RGD
  • social behavior Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Transferase

Keywords - Biological processi

Catecholamine biosynthesis

Keywords - Ligandi

S-adenosyl-L-methionine

Enzyme and pathway databases

UniPathwayiUPA00749; UER00736.

Names & Taxonomyi

Protein namesi
Recommended name:
Phenylethanolamine N-methyltransferase (EC:2.1.1.28)
Short name:
PNMTase
Alternative name(s):
Noradrenaline N-methyltransferase
Gene namesi
Name:Pnmt
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi3361. Pnmt.

Subcellular locationi

GO - Cellular componenti

  • axon Source: RGD
  • cytoplasm Source: RGD
  • dendrite Source: RGD
  • neuronal cell body Source: RGD
  • perikaryon Source: RGD
  • terminal bouton Source: RGD
  • varicosity Source: RGD
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 285285Phenylethanolamine N-methyltransferasePRO_0000159711Add
BLAST

Proteomic databases

PaxDbiP10937.
PRIDEiP10937.

Interactioni

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000067392.

Structurei

3D structure databases

ProteinModelPortaliP10937.
SMRiP10937. Positions 16-281.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni80 – 812S-adenosyl-L-methionine bindingBy similarity
Regioni159 – 1602S-adenosyl-L-methionine bindingBy similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG410IJGY. Eukaryota.
ENOG4111F9R. LUCA.
HOVERGENiHBG000797.
InParanoidiP10937.
KOiK00553.
PhylomeDBiP10937.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
InterProiIPR025820. NNMT/PNMT/TEMT_CS.
IPR000940. NNMT_TEMT_trans.
IPR029063. SAM-dependent_MTases.
[Graphical view]
PANTHERiPTHR10867. PTHR10867. 1 hit.
PfamiPF01234. NNMT_PNMT_TEMT. 1 hit.
[Graphical view]
PIRSFiPIRSF000384. PNMTase. 1 hit.
SUPFAMiSSF53335. SSF53335. 1 hit.
PROSITEiPS01100. NNMT_PNMT_TEMT. 1 hit.
PS51681. SAM_MT_NNMT_PNMT_TEMT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P10937-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDRGSDPKHT AGMDSDSDPG QAEVALAYQR FEPRAYLRNN YAPPRGDLSN
60 70 80 90 100
PDGVGPWKLR CMAQVFATGE VSGQVLIDIG SGPTIYQLLS ACAHFEDITM
110 120 130 140 150
TDFLEVNRQE LGLWLREEPG AFDWSVYSQH VCLIEDKGES WQEKERQLRA
160 170 180 190 200
RVKRVLPIDV HKPQPLGASG LAPLPADALV SAFCLEAVSP DLPSFRQALY
210 220 230 240 250
HITTLLRPGG NLLFIGALEE SWYLAGEARL SVVPVSEEEV REALVCSGYE
260 270 280
VRDLRTYIMP AHLRTGVDDV KGIFFAWAQK IEVQV
Length:285
Mass (Da):31,670
Last modified:October 1, 1996 - v3
Checksum:i28A239A5411AD2F6
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti16 – 172DS → LA (PubMed:2575695).Curated
Sequence conflicti52 – 521D → H in CAA32428 (PubMed:2928117).Curated
Sequence conflicti204 – 2041T → A in CAA32428 (PubMed:2928117).Curated
Sequence conflicti211 – 2111N → H (PubMed:7558218).Curated
Sequence conflicti211 – 2111N → H (PubMed:2575695).Curated
Sequence conflicti214 – 2141F → L (PubMed:7558218).Curated
Sequence conflicti214 – 2141F → L (PubMed:2575695).Curated
Sequence conflicti285 – 2851V → A in AAA91779 (PubMed:7558218).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X75333 Genomic DNA. Translation: CAA53082.1.
U11694, U11275 Genomic DNA. Translation: AAA91779.1.
X14211 mRNA. Translation: CAA32428.1.
PIRiS38567.
RefSeqiNP_113714.1. NM_031526.1.
UniGeneiRn.202604.

Genome annotation databases

GeneIDi24661.
KEGGirno:24661.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X75333 Genomic DNA. Translation: CAA53082.1.
U11694, U11275 Genomic DNA. Translation: AAA91779.1.
X14211 mRNA. Translation: CAA32428.1.
PIRiS38567.
RefSeqiNP_113714.1. NM_031526.1.
UniGeneiRn.202604.

3D structure databases

ProteinModelPortaliP10937.
SMRiP10937. Positions 16-281.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000067392.

Proteomic databases

PaxDbiP10937.
PRIDEiP10937.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi24661.
KEGGirno:24661.

Organism-specific databases

CTDi5409.
RGDi3361. Pnmt.

Phylogenomic databases

eggNOGiENOG410IJGY. Eukaryota.
ENOG4111F9R. LUCA.
HOVERGENiHBG000797.
InParanoidiP10937.
KOiK00553.
PhylomeDBiP10937.

Enzyme and pathway databases

UniPathwayiUPA00749; UER00736.

Miscellaneous databases

NextBioi604018.
PROiP10937.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
InterProiIPR025820. NNMT/PNMT/TEMT_CS.
IPR000940. NNMT_TEMT_trans.
IPR029063. SAM-dependent_MTases.
[Graphical view]
PANTHERiPTHR10867. PTHR10867. 1 hit.
PfamiPF01234. NNMT_PNMT_TEMT. 1 hit.
[Graphical view]
PIRSFiPIRSF000384. PNMTase. 1 hit.
SUPFAMiSSF53335. SSF53335. 1 hit.
PROSITEiPS01100. NNMT_PNMT_TEMT. 1 hit.
PS51681. SAM_MT_NNMT_PNMT_TEMT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Complete nucleotide sequence and tissue-specific expression of the rat phenylethanolamine N-methyltransferase gene."
    Suh Y.H., Chun Y.S., Lee I.S., Kim S.S., Choi W., Chong Y.H., Hong L., Kim S.H., Park C.W., Kim C.G.
    J. Neurochem. 63:1603-1608(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: Sprague-Dawley.
  2. "Investigation of the phenylethanolamine N-methyltransferase gene as a candidate gene for hypertension."
    Koike G., Jacob H.J., Krieger J.E., Szpirer C., Hoehe M.R., Horiuchi M., Dzau V.J.
    Hypertension 26:595-601(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: Wistar.
    Tissue: Spleen.
  3. "Isolation of a rat adrenal cDNA clone encoding phenylethanolamine N-methyltransferase and cold-induced alterations in adrenal PNMT mRNA and protein."
    Weisberg E.P., Baruchin A., Stachowiak M.K., Stricker E.M., Zigmond M.J., Kaplan B.B.
    Brain Res. Mol. Brain Res. 6:159-166(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 16-285.
    Tissue: Adrenal gland.
  4. "Cloning of the rat adrenal medullary phenylethanolamine-N-methyltransferase."
    Mezey E.
    Nucleic Acids Res. 17:2125-2125(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 26-285.
    Strain: Sprague-Dawley.

Entry informationi

Entry nameiPNMT_RAT
AccessioniPrimary (citable) accession number: P10937
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: October 1, 1996
Last modified: November 11, 2015
This is version 104 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.