Reviewed, UniProtKB/Swiss-Prot P10938 (PNMT_BOVIN)

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

Bos taurus (Bovine)

Taxonomic identifier

9913 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Protein attributes

Sequence length	283 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein 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.
Post-translational modification	The N-terminus is blocked.
Sequence similarities	Belongs to the NNMT/PNMT/TEMT family.

Ontologies

Keywords
Biological process	Catecholamine biosynthesis
Ligand	S-adenosyl-L-methionine
Molecular function	Methyltransferase Transferase
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	catecholamine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	phenylethanolamine N-methyltransferase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 283	283	Phenylethanolamine N-methyltransferase		PRO_0000159708
Regions
	Region	79 – 80	2	S-adenosyl-L-methionine binding By similarity
	Region	158 – 159	2	S-adenosyl-L-methionine binding By similarity
Sites
	Binding site	35	1	S-adenosyl-L-methionine By similarity
	Binding site	40	1	S-adenosyl-L-methionine By similarity
	Binding site	85	1	S-adenosyl-L-methionine By similarity
	Binding site	101	1	S-adenosyl-L-methionine By similarity
	Binding site	106	1	S-adenosyl-L-methionine By similarity
	Binding site	181	1	S-adenosyl-L-methionine; via carbonyl oxygen By similarity
Experimental info
	Sequence conflict	246 – 248	3	TAT → SAM in AAA30715. Ref.1
	Sequence conflict	255 – 276	22	RTPMP…IFFTR → LHLHHACPPSDRCRRCQGHL LHL in AAA30715. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P10938-1 [UniParc]. Last modified November 1, 1990. Version 2. Checksum: AE8B4C53E6C987E5	FASTA	283	30,918
	10 20 30 40 50 60 MSGTDRSQAA GAVPDSDPGL AAVSSAYQRF EPRAYLRNNY APPRGDLSCP DGVGPWKLRC 70 80 90 100 110 120 LAQTFATGEV SGRTLIDIGS GPTIYQLLSA CAHFEDITMT DFLEVNRQEL RLWLREEPGA 130 140 150 160 170 180 FDWSVYSQHV CLIEGKGESW QEKECQLRAR VKRILPIDVH RPQPLGAGGL APLPADALVS 190 200 210 220 230 240 AFCLEAVSPD LASFQRALDH ITTLLRPGGH LLLIGALEES WYLAGEARLA VVPVREEEVR 250 260 270 280 EALVRTATRC GICARTPMPA HLQTGVDDVK GIFFTRAQKK VGV

References

[1]	"Complete nucleotide and deduced amino acid sequence of bovine phenylethanolamine N-methyltransferase: partial amino acid homology with rat tyrosine hydroxylase." Baetge E.E., Suh Y.H., Joh T.H. Proc. Natl. Acad. Sci. U.S.A. 83:5454-5458(1986) [PubMed: 2874553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"The complete nucleotide sequence and structure of the gene encoding bovine phenylethanolamine N-methyltransferase." Batter D.K., D'Mello S.R., Turzai L.M., Hughes H.B. III, Gioio A.E., Kaplan B.B. J. Neurosci. Res. 19:367-376(1988) [PubMed: 3379652] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"Purification and partial amino acid sequence of bovine adrenal phenylethanolamine N-methyltransferase: a comparison of nucleic acid and protein sequence data." Weisberg E.P., Batter D.K., Brown W.E., Kaplan B.B. J. Neurosci. Res. 19:377-382(1988) [PubMed: 3379653] [Abstract] Cited for: PARTIAL PROTEIN SEQUENCE.
[4]	"Primary structure of bovine adrenal phenylethanolamine N-methyltransferase." Wong D.L., Yoo Y.S., Lau K., Schilling J.W. Neuropsychopharmacology 3:175-180(1990) [PubMed: 2363805] [Abstract] Cited for: PARTIAL PROTEIN SEQUENCE.

Cross-references

Sequence databases
EMBLGenBankDDBJ	M36706 Genomic DNA. Translation: AAA30716.1. M14318 mRNA. Translation: AAA30715.1.
IPI	IPI00701042.
PIR	A24313. I45962.
UniGene	Bt.451
3D structure databases
HSSP	HSSP built from PDB template 1HNN based on UniProtKB P11086.
SMR	P10938. Positions 14-279.
ModBase	Search...
Genome annotation databases
Ensembl	ENSBTAG00000011731. Bos taurus. [Contig view]
Phylogenomic databases
HOVERGEN	P10938.
Enzyme and pathway databases
BRENDA	2.1.1.28. 251.
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...

Entry information

Entry name

PNMT_BOVIN

Accession

Primary (citable) accession number: P10938

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	November 1, 1990
Last modified:	May 5, 2009
This is version 66 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)