Q62086 (PON2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Serum paraoxonase/arylesterase 2
Short name=PON 2
EC=3.1.1.2
EC=3.1.1.81

Alternative name(s):
Aromatic esterase 2
Short name=A-esterase 2
Serum aryldialkylphosphatase 2

Gene names

Name:

Pon2

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	354 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Capable of hydrolyzing lactones and a number of aromatic carboxylic acid esters By similarity.
Catalytic activity	A phenyl acetate + H2O = a phenol + acetate. 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	Homotrimer By similarity.
Subcellular location	Membrane; Peripheral membrane protein By similarity.
Post-translational modification	Glycosylated By similarity. The signal sequence is not cleaved By similarity.
Sequence similarities	Belongs to the paraoxonase family.

Ontologies

Keywords
Cellular component	Membrane
Domain	Signal
Ligand	Calcium Metal-binding
Molecular function	Hydrolase
PTM	Disulfide bond Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Cellular component	extracellular region Inferred from electronic annotation. Source: InterPro
Molecular function	arylesterase activity Inferred from electronic annotation. Source: EC metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 354	354	Serum paraoxonase/arylesterase 2		PRO_0000223288
	Signal peptide	1 – ?		Not cleaved Potential
Sites
	Active site	114	1	Proton acceptor By similarity
	Metal binding	53	1	Calcium 1; catalytic By similarity
	Metal binding	54	1	Calcium 2 By similarity
	Metal binding	116	1	Calcium 2; via carbonyl oxygen By similarity
	Metal binding	167	1	Calcium 1; catalytic By similarity
	Metal binding	168	1	Calcium 2 By similarity
	Metal binding	223	1	Calcium 1; catalytic By similarity
	Metal binding	268	1	Calcium 1; catalytic By similarity
	Metal binding	269	1	Calcium 1; catalytic By similarity
Amino acid modifications
	Glycosylation	254	1	N-linked (GlcNAc...) Potential
	Glycosylation	269	1	N-linked (GlcNAc...) Potential
	Glycosylation	323	1	N-linked (GlcNAc...) Potential
	Disulfide bond	42 ↔ 352		By similarity
Experimental info
	Sequence conflict	8 – 14	7	SLLGIGL → GFAGHRV in AAC42089. Ref.1
	Sequence conflict	25	1	R → S in AAC42089. Ref.1
	Sequence conflict	30	1	A → G in AAC42089. Ref.1
	Sequence conflict	91 – 98	8	KDERPRAL → DERPPSLE in AAC42089. Ref.1
	Sequence conflict	137 – 138	2	KS → SN in AAC42089. Ref.1
	Sequence conflict	148	1	E → A in AAC42089. Ref.1
	Sequence conflict	175	1	T → A in AAC42089. Ref.1
	Sequence conflict	300	1	A → T in AAC42089. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q62086 [UniParc]. Last modified July 19, 2005. Version 2. Checksum: D16C3F3C9D853CD2	FASTA	354	39,617
	10 20 30 40 50 60 MGRMVALSLL GIGLALLGER FLALRSRLKA SREVESVDLP NCHLIKGIET GAEDIDILPN 70 80 90 100 110 120 GLAFFSVGLK FPGLHSFAPD KPGGILMMDL KDERPRALEL RVSWGFDLAS FNPHGISTFI 130 140 150 160 170 180 DDDDTVYLFV VNHPQFKSTV EIFKFQEEEN SLLHLKTIKH ELLPSVNDII AVGPTHFYAT 190 200 210 220 230 240 NDHYFSDPFL KYLETYLNLH WANVVYYSPE EVKLVAEGFD SANGINISPD KKYVYVADIL 250 260 270 280 290 300 AHEIHVLEKQ PNMNLTQLKV LQLGTLVDNL SIDPSSGDIW VGCHPNGQRL FVYHPNHPPA 310 320 330 340 350 SEVLRIQNIL SEKPSVTTVY INNGSVLQGS SVATIYDRKL LVGTLYQKAL YCEL

References

	« Hide 'large scale' referencesShow '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: 8661009] [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. , 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: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: BALB/c 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: 15489334] [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: 15963993] [Abstract] Cited for: CATALYTIC ACTIVITY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	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.
IPI	IPI00310567.
RefSeq	NP_899131.1. NM_183308.2.
UniGene	Mm.126984. Mm.460999.
3D structure databases
ProteinModelPortal	Q62086.
SMR	Q62086. Positions 23-354.
ModBase	Search...
Protein-protein interaction databases
STRING	Q62086.
Proteomic databases
PRIDE	Q62086.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000057792; ENSMUSP00000062670; ENSMUSG00000032667.
GeneID	330260.
KEGG	mmu:330260.
UCSC	uc009awf.1. mouse.
Organism-specific databases
CTD	5445.
MGI	MGI:106687. Pon2.
Phylogenomic databases
GeneTree	ENSGT00390000008932.
HOGENOM	HBG613410.
HOVERGEN	HBG003604.
InParanoid	Q62086.
OMA	HTIEIFE.
OrthoDB	EOG4XD3RN.
PhylomeDB	Q62086.
Gene expression databases
ArrayExpress	Q62086.
Bgee	Q62086.
CleanEx	MM_PON2.
Genevestigator	Q62086.
GermOnline	ENSMUSG00000032667. Mus musculus.
Family and domain databases
InterPro	IPR011042. 6-blade_b-propeller_TolB-like. IPR002640. Arylesterase. IPR008364. Paraoxonase2. [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. PR01787. PARAOXONASE2.
ProtoNet	Search...
Other
NextBio	399259.
SOURCE	Search...

Entry information

Entry name

PON2_MOUSE

Accession

Primary (citable) accession number: Q62086
Secondary accession number(s): Q3TAD3, Q8CFK3

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	July 19, 2005
Last modified:	November 16, 2011
This is version 90 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program