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Q62087 (PON3_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 92. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Serum paraoxonase/lactonase 3
EC=3.1.1.2
EC=3.1.1.81
EC=3.1.8.1
Gene names
Name:Pon3
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length354 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Has low activity towards the organophosphate paraxon and aromatic carboxylic acid esters. Rapidly hydrolyzes lactones such as statin prodrugs (e.g. lovastatin). Hydrolyzes aromatic lactones and 5- or 6-member ring lactones with aliphatic substituents but not simple lactones or those with polar substituents By similarity.

Catalytic activity

A phenyl acetate + H2O = a phenol + acetate. Ref.5

An aryl dialkyl phosphate + H2O = dialkyl phosphate + an aryl alcohol. Ref.5

An N-acyl-L-homoserine lactone + H2O = an N-acyl-L-homoserine. Ref.5

Cofactor

Binds 2 calcium ions per subunit By similarity.

Subunit structure

Homodimer By similarity.

Subcellular location

Secreted › extracellular space By similarity.

Post-translational modification

Glycosylated By similarity.

The signal sequence is not cleaved By similarity.

Sequence similarities

Belongs to the paraoxonase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 354353Serum paraoxonase/lactonase 3
PRO_0000223291
Signal peptide2 – ?Not cleaved Potential

Sites

Active site1141Proton acceptor By similarity
Metal binding531Calcium 1; catalytic By similarity
Metal binding541Calcium 2 By similarity
Metal binding1161Calcium 2; via carbonyl oxygen By similarity
Metal binding1671Calcium 1; catalytic By similarity
Metal binding1681Calcium 2 By similarity
Metal binding2231Calcium 1; catalytic By similarity
Metal binding2681Calcium 1; catalytic By similarity
Metal binding2691Calcium 1; catalytic By similarity

Amino acid modifications

Modified residue1651Phosphoserine By similarity
Glycosylation501N-linked (GlcNAc...) Potential
Glycosylation2691N-linked (GlcNAc...) Potential
Glycosylation3231N-linked (GlcNAc...) Potential
Disulfide bond42 ↔ 352 By similarity

Experimental info

Sequence conflict31K → H in AAC42090. Ref.1
Sequence conflict81T → P in AAC42090. Ref.1
Sequence conflict2481K → E in AAC42090. Ref.1
Sequence conflict2731D → A in AAC42090. Ref.1
Sequence conflict2971D → G in AAC42090. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q62087 [UniParc].

Last modified July 19, 2004. Version 2.
Checksum: D66534EAA4EB10F2

FASTA35439,351
        10         20         30         40         50         60 
MGKLVALTLL GACLALIGER LLNFRERVST TREIKATEPQ NCHLIEGLEN GSEDIDILPS 

        70         80         90        100        110        120 
GLAFISTGLK YPGMPAFAPD KPGRIFLMDL NEQNPEAQAL EISGGLDQES LNPHGISTFI 

       130        140        150        160        170        180 
DKDNTAYLYV VNHPNMDSTV EIFKFEEQQR SLIHLKTLKH ELLKSVNDIV VLGPEQFYAT 

       190        200        210        220        230        240 
RDHYFTSYFL VLLEMILDPH WTSVVFYSPK EVKVVAQGFS SANGITVSLD QKFVYVADVT 

       250        260        270        280        290        300 
AKNIHIMKKH DNWDLTPVKV IQLGTLVDNL TVDPATGDIL AGCHPNPMKL LIYNPEDPPG 

       310        320        330        340        350 
SEVLRIQDSL SDKPRVSTLY ANNGSVLQGS TVASVYHKRM LIGTIFHKAL YCDL

« Hide

References

« Hide 'large scale' references
[1]"The human serum paraoxonase/arylesterase gene (PON1) is one member of a multigene family."
Primo-Parmo S.L., Sorenson R.C., Teiber J., La Du B.N.
Genomics 33:498-507(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: BALB/c.
Tissue: Liver.
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: NOD.
Tissue: Thymus.
[3]Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Thyroid.
[5]"Quorum quenching enzyme activity is widely conserved in the sera of mammalian species."
Yang F., Wang L.H., Wang J., Dong Y.H., Hu J.Y., Zhang L.H.
FEBS Lett. 579:3713-3717(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: CATALYTIC ACTIVITY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		L76193 mRNA. Translation: AAC42090.1.
AK088572 mRNA. Translation: BAC40430.1.
CH466533 Genomic DNA. Translation: EDL13970.1.
BC099416 mRNA. Translation: AAH99416.1.
IPIIPI00121114.
RefSeqNP_766594.1. NM_173006.1.
UniGeneMm.9122.

3D structure databases

ProteinModelPortalQ62087.
SMRQ62087. Positions 23-354.
ModBaseSearch...

PTM databases

PhosphoSiteQ62087.

Proteomic databases

PaxDbQ62087.
PRIDEQ62087.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000031773; ENSMUSP00000031773; ENSMUSG00000029759.
GeneID269823.
KEGGmmu:269823.
UCSCuc009awe.1. mouse.

Organism-specific databases

CTD5446.
MGIMGI:106686. Pon3.

Phylogenomic databases

eggNOGNOG68009.
GeneTreeENSGT00390000008932.
HOGENOMHOG000252960.
HOVERGENHBG003604.
InParanoidQ4FZK0.
KOK01045.
OMAQKYVYVA.
OrthoDBEOG4XD3RN.

Gene expression databases

ArrayExpressQ62087.
BgeeQ62087.
CleanExMM_PON3.
GenevestigatorQ62087.
GermOnlineENSMUSG00000029759. Mus musculus.

Family and domain databases

Gene3D2.120.10.30. 1 hit.
InterProIPR011042. 6-blade_b-propeller_TolB-like.
IPR002640. Arylesterase.
IPR008364. Paraoxonase2.
[Graphical view]
PfamPF01731. Arylesterase. 1 hit.
[Graphical view]
PRINTSPR01785. PARAOXONASE.
PR01787. PARAOXONASE2.
ProtoNetSearch...

Other

NextBio393049.
SOURCESearch...

Entry information

Entry namePON3_MOUSE
AccessionPrimary (citable) accession number: Q62087
Secondary accession number(s): Q4FZK0, Q8C2I7
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: July 19, 2004
Last modified: April 3, 2013
This is version 92 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents