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Protein

Serum paraoxonase/arylesterase 2

Gene

Pon2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Capable of hydrolyzing lactones and a number of aromatic carboxylic acid esters.By similarity

Catalytic activityi

A phenyl acetate + H2O = a phenol + acetate.1 Publication
An N-acyl-L-homoserine lactone + H2O = an N-acyl-L-homoserine.1 Publication

Cofactori

Ca2+By similarityNote: Binds 2 calcium ions per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi53 – 531Calcium 1; catalyticBy similarity
Metal bindingi54 – 541Calcium 2By similarity
Active sitei114 – 1141Proton acceptorBy similarity
Metal bindingi116 – 1161Calcium 2; via carbonyl oxygenBy similarity
Metal bindingi167 – 1671Calcium 1; catalyticBy similarity
Metal bindingi168 – 1681Calcium 2By similarity
Metal bindingi223 – 2231Calcium 1; catalyticBy similarity
Metal bindingi268 – 2681Calcium 1; catalyticBy similarity
Metal bindingi269 – 2691Calcium 1; catalyticBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

BRENDAi3.1.8.1. 3474.

Names & Taxonomyi

Protein namesi
Recommended name:
Serum paraoxonase/arylesterase 2 (EC:3.1.1.2, EC:3.1.1.81)
Short name:
PON 2
Alternative name(s):
Aromatic esterase 2
Short name:
A-esterase 2
Serum aryldialkylphosphatase 2
Gene namesi
Name:Pon2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 6

Organism-specific databases

MGIiMGI:106687. Pon2.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 354354Serum paraoxonase/arylesterase 2PRO_0000223288Add
BLAST
Signal peptidei1 – ?Not cleavedSequence analysis

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi42 ↔ 352By similarity
Glycosylationi254 – 2541N-linked (GlcNAc...)Sequence analysis
Glycosylationi269 – 2691N-linked (GlcNAc...)Sequence analysis
Glycosylationi323 – 3231N-linked (GlcNAc...)Sequence analysis

Post-translational modificationi

Glycosylated.By similarity
The signal sequence is not cleaved.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

EPDiQ62086.
MaxQBiQ62086.
PaxDbiQ62086.
PeptideAtlasiQ62086.
PRIDEiQ62086.

PTM databases

PhosphoSiteiQ62086.

Expressioni

Gene expression databases

BgeeiQ62086.
CleanExiMM_PON2.
GenevisibleiQ62086. MM.

Interactioni

Subunit structurei

Homotrimer.By similarity

GO - Molecular functioni

Protein-protein interaction databases

IntActiQ62086. 3 interactions.
MINTiMINT-4115570.
STRINGi10090.ENSMUSP00000062670.

Structurei

3D structure databases

ProteinModelPortaliQ62086.
SMRiQ62086. Positions 23-354.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the paraoxonase family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG410IHDV. Eukaryota.
ENOG4111QK7. LUCA.
GeneTreeiENSGT00390000008932.
HOGENOMiHOG000252960.
HOVERGENiHBG003604.
InParanoidiQ62086.
KOiK01045.
OMAiTWSNVVY.
OrthoDBiEOG7GN2N3.
PhylomeDBiQ62086.
TreeFamiTF322436.

Family and domain databases

Gene3Di2.120.10.30. 1 hit.
InterProiIPR011042. 6-blade_b-propeller_TolB-like.
IPR002640. Arylesterase.
IPR008364. Paraoxonase2.
[Graphical view]
PfamiPF01731. Arylesterase. 1 hit.
[Graphical view]
PRINTSiPR01785. PARAOXONASE.
PR01787. PARAOXONASE2.

Sequencei

Sequence statusi: Complete.

Q62086-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGRMVALSLL GIGLALLGER FLALRSRLKA SREVESVDLP NCHLIKGIET
60 70 80 90 100
GAEDIDILPN GLAFFSVGLK FPGLHSFAPD KPGGILMMDL KDERPRALEL
110 120 130 140 150
RVSWGFDLAS FNPHGISTFI DDDDTVYLFV VNHPQFKSTV EIFKFQEEEN
160 170 180 190 200
SLLHLKTIKH ELLPSVNDII AVGPTHFYAT NDHYFSDPFL KYLETYLNLH
210 220 230 240 250
WANVVYYSPE EVKLVAEGFD SANGINISPD KKYVYVADIL AHEIHVLEKQ
260 270 280 290 300
PNMNLTQLKV LQLGTLVDNL SIDPSSGDIW VGCHPNGQRL FVYHPNHPPA
310 320 330 340 350
SEVLRIQNIL SEKPSVTTVY INNGSVLQGS SVATIYDRKL LVGTLYQKAL

YCEL
Length:354
Mass (Da):39,617
Last modified:July 19, 2005 - v2
Checksum:iD16C3F3C9D853CD2
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti8 – 147SLLGIGL → GFAGHRV in AAC42089 (PubMed:8661009).Curated
Sequence conflicti25 – 251R → S in AAC42089 (PubMed:8661009).Curated
Sequence conflicti30 – 301A → G in AAC42089 (PubMed:8661009).Curated
Sequence conflicti91 – 988KDERPRAL → DERPPSLE in AAC42089 (PubMed:8661009).Curated
Sequence conflicti137 – 1382KS → SN in AAC42089 (PubMed:8661009).Curated
Sequence conflicti148 – 1481E → A in AAC42089 (PubMed:8661009).Curated
Sequence conflicti175 – 1751T → A in AAC42089 (PubMed:8661009).Curated
Sequence conflicti300 – 3001A → T in AAC42089 (PubMed:8661009).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L48514 mRNA. Translation: AAC42089.1.
AK146311 mRNA. Translation: BAE27066.1.
AK171926 mRNA. Translation: BAE42735.1.
CH466533 Genomic DNA. Translation: EDL13967.1.
BC037140 mRNA. Translation: AAH37140.1.
BC055896 mRNA. Translation: AAH55896.1.
BC062200 mRNA. Translation: AAH62200.1.
CCDSiCCDS19900.1.
RefSeqiNP_899131.1. NM_183308.2.
UniGeneiMm.126984.
Mm.460999.

Genome annotation databases

EnsembliENSMUST00000057792; ENSMUSP00000062670; ENSMUSG00000032667.
GeneIDi330260.
KEGGimmu:330260.
UCSCiuc009awf.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L48514 mRNA. Translation: AAC42089.1.
AK146311 mRNA. Translation: BAE27066.1.
AK171926 mRNA. Translation: BAE42735.1.
CH466533 Genomic DNA. Translation: EDL13967.1.
BC037140 mRNA. Translation: AAH37140.1.
BC055896 mRNA. Translation: AAH55896.1.
BC062200 mRNA. Translation: AAH62200.1.
CCDSiCCDS19900.1.
RefSeqiNP_899131.1. NM_183308.2.
UniGeneiMm.126984.
Mm.460999.

3D structure databases

ProteinModelPortaliQ62086.
SMRiQ62086. Positions 23-354.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ62086. 3 interactions.
MINTiMINT-4115570.
STRINGi10090.ENSMUSP00000062670.

PTM databases

PhosphoSiteiQ62086.

Proteomic databases

EPDiQ62086.
MaxQBiQ62086.
PaxDbiQ62086.
PeptideAtlasiQ62086.
PRIDEiQ62086.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000057792; ENSMUSP00000062670; ENSMUSG00000032667.
GeneIDi330260.
KEGGimmu:330260.
UCSCiuc009awf.1. mouse.

Organism-specific databases

CTDi5445.
MGIiMGI:106687. Pon2.

Phylogenomic databases

eggNOGiENOG410IHDV. Eukaryota.
ENOG4111QK7. LUCA.
GeneTreeiENSGT00390000008932.
HOGENOMiHOG000252960.
HOVERGENiHBG003604.
InParanoidiQ62086.
KOiK01045.
OMAiTWSNVVY.
OrthoDBiEOG7GN2N3.
PhylomeDBiQ62086.
TreeFamiTF322436.

Enzyme and pathway databases

BRENDAi3.1.8.1. 3474.

Miscellaneous databases

ChiTaRSiPon2. mouse.
PROiQ62086.
SOURCEiSearch...

Gene expression databases

BgeeiQ62086.
CleanExiMM_PON2.
GenevisibleiQ62086. MM.

Family and domain databases

Gene3Di2.120.10.30. 1 hit.
InterProiIPR011042. 6-blade_b-propeller_TolB-like.
IPR002640. Arylesterase.
IPR008364. Paraoxonase2.
[Graphical view]
PfamiPF01731. Arylesterase. 1 hit.
[Graphical view]
PRINTSiPR01785. PARAOXONASE.
PR01787. PARAOXONASE2.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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/cJ.
    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.
    , 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: BALB/cJ and NOD.
    Tissue: Spleen.
  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].
    Strain: FVB/N.
    Tissue: Colon and Mammary tumor.
  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.
  6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Heart, Liver, Lung, Pancreas and Spleen.

Entry informationi

Entry nameiPON2_MOUSE
AccessioniPrimary (citable) accession number: Q62086
Secondary accession number(s): Q3TAD3, Q8CFK3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: July 19, 2005
Last modified: July 6, 2016
This is version 121 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.