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P27170 (PON1_RABIT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 101. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended 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
OrganismOryctolagus cuniculus (Rabbit) [Reference proteome]
Taxonomic identifier9986 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Lagomorpha › Leporidae › Oryctolagus

Protein attributes

Sequence length359 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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. Ref.3

Catalytic activity

A phenyl acetate + H2O = a phenol + acetate. Ref.4

An aryl dialkyl phosphate + H2O = dialkyl phosphate + an aryl alcohol. Ref.4

An N-acyl-L-homoserine lactone + H2O = an N-acyl-L-homoserine. Ref.4

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.

The signal sequence is not cleaved.

Polymorphism

There are two allelic forms, allozyme A and B, which differ in their substrate specificity. Both forms have similar arylesterase activity but allozyme B possesses greater paraoxonase activity. Allozyme A is better at protecting LDL from oxidation.

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.

Sequence caution

The sequence AAK06398.1 differs from that shown. Reason: Erroneous termination at position 356. Translated as Ser.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.4
Chain2 – 359358Serum paraoxonase/arylesterase 1
PRO_0000223283
Signal peptide2 – ?Not cleaved

Sites

Active site1151Proton acceptor By similarity
Metal binding531Calcium 1; catalytic By similarity
Metal binding541Calcium 2 By similarity
Metal binding1171Calcium 2; via carbonyl oxygen By similarity
Metal binding1681Calcium 1; catalytic By similarity
Metal binding1691Calcium 2 By similarity
Metal binding2241Calcium 1; catalytic By similarity
Metal binding2691Calcium 1; catalytic By similarity
Metal binding2701Calcium 1; catalytic By similarity

Amino acid modifications

Modified residue761Phosphoserine By similarity
Glycosylation501N-linked (GlcNAc...) Potential
Glycosylation2271N-linked (GlcNAc...) Potential
Glycosylation2531N-linked (GlcNAc...) Potential
Glycosylation2701N-linked (GlcNAc...) Potential
Glycosylation3241N-linked (GlcNAc...) Potential
Disulfide bond42 ↔ 353 By similarity

Natural variations

Natural variant821P → S in allele A. Ref.3
Natural variant931K → E in allele A. Ref.3
Natural variant1011S → G in allele A. Ref.3

Experimental info

Sequence conflict671A → S in AAK06398. Ref.3
Sequence conflict671A → S in AAK06399. Ref.3
Sequence conflict671A → S in AAK06400. Ref.3
Sequence conflict3201A → V in AAK06398. Ref.3

Sequences

Sequence LengthMass (Da)Tools
P27170 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 535124A736EE312A

FASTA35940,010
        10         20         30         40         50         60 
MAKLTALTLL GLGLALFDGQ KSSFQTRFNV HREVTPVELP NCNLVKGIDN GSEDLEILPN 

        70         80         90        100        110        120 
GLAFISAGLK YPGIMSFDPD KPGKILLMDL NEKDPVVLEL SITGSTFDLS SFNPHGISTF 

       130        140        150        160        170        180 
TDEDNIVYLM VVNHPDSKST VELFKFQEKE KSLLHLKTIR HKLLPSVNDI VAVGPEHFYA 

       190        200        210        220        230        240 
TNDHYFIDPY LKSWEMHLGL AWSFVTYYSP NDVRVVAEGF DFANGINISP DGKYVYIAEL 

       250        260        270        280        290        300 
LAHKIHVYEK HANWTLTPLK SLDFNTLVDN ISVDPVTGDL WVGCHPNGMR IFYYDPKNPP 

       310        320        330        340        350 
ASEVLRIQDI LSKEPKVTVA YAENGTVLQG STVAAVYKGK MLVGTVFHKA LYCELSQAN

« Hide

References

[1]"Characterization of cDNA clones encoding rabbit and human serum paraoxonase: the mature protein retains its signal sequence."
Hassett C., Richter R.J., Humbert R., Chapline C., Crabb J.W., Omiecinski C.J., Furlong C.E.
Biochemistry 30:10141-10149(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
Tissue: Liver.
[2]"Human and rabbit paraoxonases: purification, cloning, sequencing, mapping and role of polymorphism in organophosphate detoxification."
Furlong C.E., Costa L.G., Hassett C., Richter R.J., Sundstrom J.A., Adler D.A., Disteche C.M., Omiecinski C.J., Chapline C., Crabb J.W.
Chem. Biol. Interact. 87:35-48(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION.
Tissue: Liver.
[3]"Rabbits possess a serum paraoxonase polymorphism similar to the human Q192R."
Watson C.E., Draganov D.I., Billecke S.S., Bisgaier C.L., La Du B.N.
Pharmacogenetics 11:123-134(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, VARIANTS SER-82; GLU-93 AND GLY-101.
Strain: New Zealand white.
Tissue: Liver.
[4]"Purification of rabbit and human serum paraoxonase."
Furlong C.E., Richter R.J., Chapline C., Crabb J.W.
Biochemistry 30:10133-10140(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-21, CATALYTIC ACTIVITY.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		M63011 mRNA. Translation: AAA31452.1.
S64616 mRNA. Translation: AAB27713.2.
AF220941 mRNA. Translation: AAK06398.1. Sequence problems.
AF220942 mRNA. Translation: AAK06399.1.
AF220943 mRNA. Translation: AAK06400.1.
PIRB40354.
RefSeqNP_001075766.1. NM_001082297.1.
UniGeneOcu.1952.

3D structure databases

ProteinModelPortalP27170.
SMRP27170. Positions 16-355.
ModBaseSearch...

Protein-protein interaction databases

STRING9986.ENSOCUP00000004445.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID100009133.

Organism-specific databases

CTD5444.

Phylogenomic databases

eggNOGNOG68009.
HOGENOMHOG000252960.
HOVERGENHBG003604.
OrthoDBEOG4XD3RN.

Family and domain databases

Gene3D2.120.10.30. 1 hit.
InterProIPR011042. 6-blade_b-propeller_TolB-like.
IPR002640. Arylesterase.
IPR008363. Paraoxonase1.
[Graphical view]
PfamPF01731. Arylesterase. 1 hit.
[Graphical view]
PRINTSPR01785. PARAOXONASE.
PR01786. PARAOXONASE1.
ProtoNetSearch...

Entry information

Entry namePON1_RABIT
AccessionPrimary (citable) accession number: P27170
Secondary accession number(s): Q9BGN1, Q9BGN2, Q9BGN3
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: January 23, 2007
Last modified: April 3, 2013
This is version 101 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

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