Reviewed, UniProtKB/Swiss-Prot P55159 (PON1_RAT)

Names and origin

Protein names

Recommended name:
    Serum paraoxonase/arylesterase 1
      Short name=PON 1
    EC=3.1.1.2
    EC=3.1.8.1
Alternative name(s):
    Serum aryldialkylphosphatase 1
    Aromatic esterase 1
      Short name=A-esterase 1

Gene names

Name:	Pon1
Synonyms:	Pon

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	355 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Hydrolyzes the toxic metabolites of a variety of organophosphorus insecticides. Capable of hydrolyzing a broad spectrum of organophosphate substrates and a number of aromatic carboxylic acid esters.
Catalytic activity	A phenyl acetate + H2O = a phenol + acetate. An aryl dialkyl phosphate + H2O = dialkyl phosphate + an aryl alcohol.
Cofactor	Binds 2 calcium ions per subunit By similarity.
Subunit structure	Interacts with CLU By similarity.
Subcellular location	Secreted › extracellular space.
Tissue specificity	Plasma. Associated with HDL.
Post-translational modification	Glycosylated By similarity. The signal sequence is not cleaved.
Miscellaneous	The preferential association of PON1 with HDL is mediated in part by its signal peptide, by binding phospholipids directly, rather than binding apo AI. The retained signal peptide may allow transfer of the protein between phospholipid surfaces By similarity.
Sequence similarities	Belongs to the paraoxonase family.

Ontologies

Keywords
Cellular component	HDL Secreted
Domain	Signal
Ligand	Calcium Metal-binding
Molecular function	Hydrolase
PTM	Disulfide bond Glycoprotein Phosphoprotein
Technical term	Direct protein sequencing
Gene Ontology (GO)
Cellular component	microsome Inferred from direct assay. Source: RGD
Molecular function	aryldialkylphosphatase activity Inferred from sequence or structural similarity. Source: UniProtKB arylesterase activity Inferred from sequence or structural similarity. Source: UniProtKB calcium ion binding Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – ?		Not cleaved
	Initiator methionine	1	1	Removed Ref.1 Ref.2
	Chain	2 – 355	354	Serum paraoxonase/arylesterase 1		PRO_0000223284
Sites
	Active site	115	1	Proton acceptor By similarity
	Metal binding	53	1	Calcium 1; catalytic By similarity
	Metal binding	54	1	Calcium 2 By similarity
	Metal binding	117	1	Calcium 2; via carbonyl oxygen By similarity
	Metal binding	168	1	Calcium 1; catalytic By similarity
	Metal binding	169	1	Calcium 2 By similarity
	Metal binding	224	1	Calcium 1; catalytic By similarity
	Metal binding	269	1	Calcium 1; catalytic By similarity
	Metal binding	270	1	Calcium 1; catalytic By similarity
Amino acid modifications
	Modified residue	76	1	Phosphoserine Ref.4
	Modified residue	80	1	Phosphoserine Ref.4
	Glycosylation	253	1	N-linked (GlcNAc...) Potential
	Glycosylation	270	1	N-linked (GlcNAc...) Potential
	Glycosylation	324	1	N-linked (GlcNAc...) Potential
	Disulfide bond	42 ↔ 353		By similarity
Experimental info
	Sequence conflict	20 – 26	7	HRSSYQT → PLXDWYR AA sequence Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P55159-1 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: 93F8AAF7A75E402D	FASTA	355	39,496
	10 20 30 40 50 60 MAKLLGLTLV GLVLALYKNH RSSYQTRLNA FREVTPVDLP NCTLVKGIEA GAEDLEILPN 70 80 90 100 110 120 GLTFFSTFLK YPGIKSFDPS KPGKILLMDL NEKEPAVSEL AIMGNTLDMS SFNPHGISTF 130 140 150 160 170 180 IDEDNTVYLL VVSHPDSSST VEVFKFQEEE RSLLHLKTIT HELLPSINDI AAVGPESFYA 190 200 210 220 230 240 TNDHYFADPY LRSWEMYLGL SWSNVVYYSP DKVRVVADGF DFANGIGISL DGKYVYIAEL 250 260 270 280 290 300 LAHKIHVYEK HANWTLTPLK VLSFDTLVDN ISVDPVTGDL WVGCHPNGMR IFFYDSENPP 310 320 330 340 350 GSEVLRIQSI LSEDPKVTVV YAENGTVLQG TTVAAVYKGK LLIGTVFHRA LCCYL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Purification and characterization of paraoxon hydrolase from rat liver." Rodrigo L., Gil F., Hernandez A.F., Marina A., Vazquez J., Pla A. Biochem. J. 321:595-601(1997) [PubMed: 9032442] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-11; 47-56 AND 307-316. Strain: Wistar. Tissue: Liver.
[2]	Blatter M.-C. Submitted (JAN-1995) to UniProtKB Cited for: PROTEIN SEQUENCE OF 2-26.
[3]	"Rat paraoxonase partial mRNA sequence." Leviev I.G., Blatter M.-C., James R.W. Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 11-355.
[4]	"Quantitative phosphoproteomics of vasopressin-sensitive renal cells: regulation of aquaporin-2 phosphorylation at two sites." Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A. Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006) [PubMed: 16641100] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-76 AND SER-80, MASS SPECTROMETRY. Tissue: Kidney.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U94856 mRNA. Translation: AAB53441.1.
IPI	IPI00231264.
PIR	PT0088.
RefSeq	NP_114466.1.
UniGene	Rn.20732
3D structure databases
SMR	P55159. Positions 16-355.
ModBase	Search...
Protein-protein interaction databases
STRING	P55159.
Proteomic databases
PRIDE	P55159.
Genome annotation databases
Ensembl	ENSRNOT00000011823; ENSRNOP00000011823; ENSRNOG00000008902; Rattus norvegicus. [Genome view]
GeneID	84024.
KEGG	rno:84024.
UCSC	NM_032077. rat.
Organism-specific databases
CTD	84024.
RGD	620062. Pon1.
Phylogenomic databases
eggNOG	roNOG04341.
HOVERGEN	P55159.
InParanoid	P55159.
Enzyme and pathway databases
BRENDA	3.1.1.2. 248. 3.1.8.1. 248.
Gene expression databases
ArrayExpress	P55159.
Genevestigator	P55159.
GermOnline	ENSRNOG00000008902. Rattus norvegicus.
Family and domain databases
InterPro	IPR011042. 6-blade_b-propeller_TolB-like. IPR002640. Arylesterase. IPR008363. Paraoxonase1. [Graphical view]
Gene3D	G3DSA:2.120.10.30. 6-blade_b-propeller_TolB-like. 1 hit.
Pfam	PF01731. Arylesterase. 1 hit. [Graphical view]
PRINTS	PR01785. PARAOXONASE. PR01786. PARAOXONASE1.
ProtoNet	Search...
Other Resources
NextBio	616593.

Entry information

Entry name

PON1_RAT

Accession

Primary (citable) accession number: P55159
Secondary accession number(s): O08682

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	January 23, 2007
Last modified:	February 9, 2010
This is version 80 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)