Serum paraoxonase/arylesterase 1 - Rattus norvegicus (Rat)

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P55159 (PON1_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 94. History...

Clusters with 100%, 90%, 50% identity |

Documents (1) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Serum paraoxonase/arylesterase 1
Short name=PON 1
EC=3.1.1.2
EC=3.1.1.81
EC=3.1.8.1

Alternative name(s):
Aromatic esterase 1
Short name=A-esterase 1
Serum aryldialkylphosphatase 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 lactones, and a number of aromatic carboxylic acid esters. Mediates an enzymatic protection of low density lipoproteins against oxidative modification By similarity.
Catalytic activity	A phenyl acetate + H₂O = a phenol + acetate. An aryl dialkyl phosphate + H₂O = dialkyl phosphate + an aryl alcohol. An N-acyl-L-homoserine lactone + H₂O = an N-acyl-L-homoserine.
Cofactor	Binds 2 calcium ions per subunit By similarity.
Subunit structure	Homodimer. 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	Complete proteome Direct protein sequencing Reference proteome
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

Initiator methionine

Removed Ref.3 Ref.4

Chain

2 – 355

354

Serum paraoxonase/arylesterase 1

PRO_0000223284

Signal peptide

2 – ?

Not cleaved

Sites

Active site

115

Proton acceptor By similarity

Metal binding

Calcium 1; catalytic By similarity

Metal binding

Calcium 2 By similarity

Metal binding

117

Calcium 2; via carbonyl oxygen By similarity

Metal binding

168

Calcium 1; catalytic By similarity

Metal binding

169

Calcium 2 By similarity

Metal binding

224

Calcium 1; catalytic By similarity

Metal binding

269

Calcium 1; catalytic By similarity

Metal binding

270

Calcium 1; catalytic By similarity

Amino acid modifications

Modified residue

Phosphoserine Ref.6

Modified residue

Phosphoserine Ref.6

Glycosylation

253

N-linked (GlcNAc...) Potential

Glycosylation

270

N-linked (GlcNAc...) Potential

Glycosylation

324

N-linked (GlcNAc...) Potential

Disulfide bond

42 ↔ 353

By similarity

Experimental info

Sequence conflict

20 – 26

HRSSYQT → PLXDWYR AA sequence Ref.4

Sequence conflict

G → F in AAB53441. Ref.5

Sequence conflict

354

D → Y in AAB53441. Ref.5

Sequences

Sequence

Length

Mass (Da)

Tools

P55159 [UniParc].

Last modified October 5, 2010. Version 3.
Checksum: FE2886875D01E52D
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FASTA

355

39,358

        10         20         30         40         50         60 
MAKLLGLTLV GLVLALYKNH RSSYQTRLNA FREVTPVDLP NCTLVKGIEA GAEDLEILPN 

        70         80         90        100        110        120 
GLTFFSTGLK 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 LCCDL

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C. Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[2]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Liver.
[3]	"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.
[4]	Blatter M.-C. Submitted (JAN-1995) to UniProtKB Cited for: PROTEIN SEQUENCE OF 2-26.
[5]	"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.
[6]	"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: Renal collecting duct.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CH473959 Genomic DNA. Translation: EDM15017.1. BC091403 mRNA. Translation: AAH91403.1. U94856 mRNA. Translation: AAB53441.1.
IPI	IPI00231264.
PIR	PT0088.
RefSeq	NP_114466.1. NM_032077.1.
UniGene	Rn.20732.
3D structure databases
ProteinModelPortal	P55159.
SMR	P55159. Positions 16-355.
ModBase	Search...
Protein-protein interaction databases
STRING	P55159.
PTM databases
PhosphoSite	P55159.
Proteomic databases
PRIDE	P55159.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSRNOT00000011823; ENSRNOP00000011823; ENSRNOG00000008902.
GeneID	84024.
KEGG	rno:84024.
UCSC	NM_032077. rat.
Organism-specific databases
CTD	5444.
RGD	620062. Pon1.
Phylogenomic databases
eggNOG	roNOG04341.
GeneTree	ENSGT00390000008932.
HOVERGEN	HBG003604.
InParanoid	P55159.
OMA	FFYDSEN.
OrthoDB	EOG4XD3RN.
PhylomeDB	P55159.
Enzyme and pathway databases
BRENDA	3.1.8.1. 5301.
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.
KO	K01045.
Pfam	PF01731. Arylesterase. 1 hit. [Graphical view]
PRINTS	PR01785. PARAOXONASE. PR01786. PARAOXONASE1.
ProtoNet	Search...
Other
NextBio	616593.

Entry information

Entry name

PON1_RAT

Accession

Primary (citable) accession number: P55159
Secondary accession number(s): O08682, Q5BJN6

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	October 5, 2010
Last modified:	December 14, 2011
This is version 94 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents