Reviewed, UniProtKB/Swiss-Prot P10937 (PNMT_RAT)

Names and origin

Protein names

Recommended name:
    Phenylethanolamine N-methyltransferase
      Short name=PNMTase
    EC=2.1.1.28
Alternative name(s):
    Noradrenaline N-methyltransferase

Gene names

Name:

Pnmt

Organism

Rattus norvegicus (Rat)

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	285 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Function	Converts noradrenaline to adrenaline.
Catalytic activity	S-adenosyl-L-methionine + phenylethanolamine = S-adenosyl-L-homocysteine + N-methylphenylethanolamine.
Pathway	Catecholamine biosynthesis; epinephrine biosynthesis; epinephrine from norepinephrine: step 1/1.
Sequence similarities	Belongs to the NNMT/PNMT/TEMT family.

Ontologies

Keywords
Biological process	Catecholamine biosynthesis
Ligand	S-adenosyl-L-methionine
Molecular function	Methyltransferase Transferase
Gene Ontology (GO)
Biological process	S-adenosylhomocysteine metabolic process Traceable author statement. Source: RGD S-adenosylmethionine metabolic process Traceable author statement. Source: RGD epinephrine biosynthetic process Traceable author statement. Source: RGD
Molecular function	phenylethanolamine N-methyltransferase activity Traceable author statement. Source: RGD
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 285	285	Phenylethanolamine N-methyltransferase		PRO_0000159711
Regions
	Region	80 – 81	2	S-adenosyl-L-methionine binding By similarity
	Region	159 – 160	2	S-adenosyl-L-methionine binding By similarity
Sites
	Binding site	36	1	S-adenosyl-L-methionine By similarity
	Binding site	41	1	S-adenosyl-L-methionine By similarity
	Binding site	86	1	S-adenosyl-L-methionine By similarity
	Binding site	102	1	S-adenosyl-L-methionine By similarity
	Binding site	107	1	S-adenosyl-L-methionine By similarity
	Binding site	182	1	S-adenosyl-L-methionine; via carbonyl oxygen By similarity
	Binding site	220	1	Substrate By similarity
Experimental info
	Sequence conflict	16 – 17	2	DS → LA Ref.3
	Sequence conflict	52	1	D → H in CAA32428. Ref.4
	Sequence conflict	204	1	T → A in CAA32428. Ref.4
	Sequence conflict	211	1	N → H Ref.2
	Sequence conflict	211	1	N → H Ref.3
	Sequence conflict	214	1	F → L Ref.2
	Sequence conflict	214	1	F → L Ref.3
	Sequence conflict	285	1	V → A in AAA91779. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P10937-1 [UniParc]. Last modified October 1, 1996. Version 3. Checksum: 28A239A5411AD2F6	FASTA	285	31,670
	10 20 30 40 50 60 MDRGSDPKHT AGMDSDSDPG QAEVALAYQR FEPRAYLRNN YAPPRGDLSN PDGVGPWKLR 70 80 90 100 110 120 CMAQVFATGE VSGQVLIDIG SGPTIYQLLS ACAHFEDITM TDFLEVNRQE LGLWLREEPG 130 140 150 160 170 180 AFDWSVYSQH VCLIEDKGES WQEKERQLRA RVKRVLPIDV HKPQPLGASG LAPLPADALV 190 200 210 220 230 240 SAFCLEAVSP DLPSFRQALY HITTLLRPGG NLLFIGALEE SWYLAGEARL SVVPVSEEEV 250 260 270 280 REALVCSGYE VRDLRTYIMP AHLRTGVDDV KGIFFAWAQK IEVQV

References

[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: 7931317] [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: 7558218] [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: 2575695] [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: 2928117] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 26-285. Strain: Sprague-Dawley.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X75333 Genomic DNA. Translation: CAA53082.1. U11694, U11275 Genomic DNA. Translation: AAA91779.1. X14211 mRNA. Translation: CAA32428.1.
IPI	IPI00876607.
PIR	S38567.
RefSeq	NP_113714.1.
UniGene	Rn.202604
3D structure databases
HSSP	HSSP built from PDB template 1HNN based on UniProtKB P11086.
SMR	P10937. Positions 16-281.
ModBase	Search...
Genome annotation databases
GeneID	24661.
KEGG	rno:24661.
Organism-specific databases
RGD	3361. Pnmt.
Phylogenomic databases
HOVERGEN	P10937.
Enzyme and pathway databases
BRENDA	2.1.1.28. 248.
Family and domain databases
InterPro	IPR000940. NNMT_TEMT_trans. [Graphical view]
PANTHER	PTHR10867. NNMT_TEMT_trans. 1 hit.
Pfam	PF01234. NNMT_PNMT_TEMT. 1 hit. [Graphical view]
PIRSF	PIRSF000384. PNMTase. 1 hit.
PROSITE	PS01100. NNMT_PNMT_TEMT. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	604018.

Entry information

Entry name

PNMT_RAT

Accession

Primary (citable) accession number: P10937

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	October 1, 1996
Last modified:	June 16, 2009
This is version 71 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)