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Protein

Pyrethroid hydrolase Ces2a

Gene

Ces2a

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Carboxylesterases that catalyzes the hydrolysis of pyrethroids pesticides. Hydrolyzes permethrin faster than cypermethrin.1 Publication

Catalytic activityi

Trans-permethrin + H2O = (3-phenoxyphenyl)methanol + (1S,3R)-3-(2,2-dichloroethenyl)-2,2-dimethylcyclopropanecarboxylate.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei227 – 2271Acyl-ester intermediatePROSITE-ProRule annotation
Active sitei344 – 3441Charge relay systemBy similarity
Active sitei456 – 4561Charge relay systemBy similarity

GO - Molecular functioni

  • carboxylic ester hydrolase activity Source: MGI

GO - Biological processi

  • protein glycosylation Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Serine esterase

Enzyme and pathway databases

ReactomeiR-MMU-211945. Phase 1 - Functionalization of compounds.

Protein family/group databases

ESTHERimouse-Ces2a. Carb_B_Chordata.
MEROPSiS09.997.

Names & Taxonomyi

Protein namesi
Recommended name:
Pyrethroid hydrolase Ces2a (EC:3.1.1.88)
Alternative name(s):
carboxylesterase 2A
Gene namesi
Name:Ces2a
Synonyms:Ces6
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 8

Organism-specific databases

MGIiMGI:2142491. Ces2a.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2626Sequence analysisAdd
BLAST
Chaini27 – 558532Pyrethroid hydrolase Ces2aPRO_0000424210Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei27 – 271Pyrrolidone carboxylic acidBy similarity
Disulfide bondi95 ↔ 122By similarity
Modified residuei209 – 2091N6-succinyllysineCombined sources
Glycosylationi275 – 2751N-linked (GlcNAc...)Sequence analysis
Disulfide bondi279 ↔ 290By similarity
Modified residuei296 – 2961N6-succinyllysineCombined sources
Glycosylationi361 – 3611N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Disulfide bond, Glycoprotein, Pyrrolidone carboxylic acid

Proteomic databases

EPDiQ8QZR3.
MaxQBiQ8QZR3.
PaxDbiQ8QZR3.
PRIDEiQ8QZR3.

PTM databases

iPTMnetiQ8QZR3.

Expressioni

Gene expression databases

GenevisibleiQ8QZR3. MM.

Interactioni

Protein-protein interaction databases

IntActiQ8QZR3. 3 interactions.
MINTiMINT-4118069.
STRINGi10090.ENSMUSP00000034346.

Structurei

3D structure databases

ProteinModelPortaliQ8QZR3.
SMRiQ8QZR3. Positions 32-538.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG1516. Eukaryota.
COG2272. LUCA.
GeneTreeiENSGT00760000118946.
HOGENOMiHOG000091866.
HOVERGENiHBG008839.
InParanoidiQ8QZR3.
KOiK03927.
OMAiVIVAIQY.
OrthoDBiEOG7RBZ7R.
PhylomeDBiQ8QZR3.
TreeFamiTF315470.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR002018. CarbesteraseB.
IPR019826. Carboxylesterase_B_AS.
IPR019819. Carboxylesterase_B_CS.
[Graphical view]
PfamiPF00135. COesterase. 1 hit.
[Graphical view]
SUPFAMiSSF53474. SSF53474. 1 hit.
PROSITEiPS00122. CARBOXYLESTERASE_B_1. 1 hit.
PS00941. CARBOXYLESTERASE_B_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q8QZR3-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MPLARLPGWL CVVACGLLLL LQHVHGQDSA SPIRNTHRGQ VRGSFVHVKD
60 70 80 90 100
TKSGVHAFLG IPFAKPPVGL LRFAPPEDPE PWSGVRDGTS QPAMCLQPDI
110 120 130 140 150
MNLEDAKEMN LILPPISMSE DCLYLNIYTP THAQEGSNLP VMVWIHGGGL
160 170 180 190 200
VVGSASMNDV SKLAATEEIV IVAIQYRLGV LGFFSTGDQH ARGNWGYLDQ
210 220 230 240 250
VAALRWVQKN IAYFGGNRDR VTIFGVSAGG TSVSSHILSP MSKGLFHGAI
260 270 280 290 300
MQSGVALLPD LISDTSEVVY KTVANLSGCE ATDSEALIHC LRAKSKQEIL
310 320 330 340 350
AINQVFKMIP AVVDGEFLPK HPQELLTSMD FHPVPSIIGV NTDECGWGVP
360 370 380 390 400
MFMGLDHIIK NITRETLPAV LKNTAARMML PPECSHLLVE EYMGDTEDPE
410 420 430 440 450
TLQAQFREML GDFMFVIPAL QVAHFQRSQA PVYFYEFQHL SSFIKHVRPS
460 470 480 490 500
HVKADHGDDV AFVFGSYLWD MNLDLTEEEE LLKRMMMKYW ANFARNGNPN
510 520 530 540 550
SEGLPSWPVL DHDEQYLQLD TQPAVGRALK ARRLQFWTKT LPQKIQELKG

SQDKHAEL
Length:558
Mass (Da):61,940
Last modified:June 1, 2002 - v1
Checksum:i961AD6BDC892E3FD
GO
Isoform 2 (identifier: Q8QZR3-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     272-304: Missing.

Show »
Length:525
Mass (Da):58,430
Checksum:i6A7BFF2F1FF75C6B
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti200 – 2001Q → K in BAE38379 (PubMed:16141072).Curated
Sequence conflicti223 – 2231I → V in BAE38379 (PubMed:16141072).Curated
Sequence conflicti371 – 3733LKN → VKD in BAE38379 (PubMed:16141072).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei272 – 30433Missing in isoform 2. 1 PublicationVSP_053352Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK078953 mRNA. Translation: BAC37476.1.
AK165784 mRNA. Translation: BAE38379.1.
AC156564 Genomic DNA. No translation available.
CH466525 Genomic DNA. Translation: EDL11232.1.
BC024082 mRNA. Translation: AAH24082.1.
BC024491 mRNA. Translation: AAH24491.1.
BC024517 mRNA. Translation: AAH24517.1.
BC025537 mRNA. Translation: AAH25537.1.
BC025812 mRNA. Translation: AAH25812.1.
BC026643 mRNA. Translation: AAH26643.1.
BC031295 mRNA. Translation: AAH31295.1.
CCDSiCCDS22585.1. [Q8QZR3-1]
CCDS52650.1. [Q8QZR3-2]
RefSeqiNP_001177259.1. NM_001190330.1. [Q8QZR3-2]
NP_598721.1. NM_133960.5. [Q8QZR3-1]
UniGeneiMm.212983.

Genome annotation databases

EnsembliENSMUST00000034346; ENSMUSP00000034346; ENSMUSG00000055730. [Q8QZR3-1]
ENSMUST00000164182; ENSMUSP00000127346; ENSMUSG00000055730. [Q8QZR3-2]
GeneIDi102022.
KEGGimmu:102022.
UCSCiuc009nbc.2. mouse. [Q8QZR3-1]
uc012giz.1. mouse. [Q8QZR3-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK078953 mRNA. Translation: BAC37476.1.
AK165784 mRNA. Translation: BAE38379.1.
AC156564 Genomic DNA. No translation available.
CH466525 Genomic DNA. Translation: EDL11232.1.
BC024082 mRNA. Translation: AAH24082.1.
BC024491 mRNA. Translation: AAH24491.1.
BC024517 mRNA. Translation: AAH24517.1.
BC025537 mRNA. Translation: AAH25537.1.
BC025812 mRNA. Translation: AAH25812.1.
BC026643 mRNA. Translation: AAH26643.1.
BC031295 mRNA. Translation: AAH31295.1.
CCDSiCCDS22585.1. [Q8QZR3-1]
CCDS52650.1. [Q8QZR3-2]
RefSeqiNP_001177259.1. NM_001190330.1. [Q8QZR3-2]
NP_598721.1. NM_133960.5. [Q8QZR3-1]
UniGeneiMm.212983.

3D structure databases

ProteinModelPortaliQ8QZR3.
SMRiQ8QZR3. Positions 32-538.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ8QZR3. 3 interactions.
MINTiMINT-4118069.
STRINGi10090.ENSMUSP00000034346.

Protein family/group databases

ESTHERimouse-Ces2a. Carb_B_Chordata.
MEROPSiS09.997.

PTM databases

iPTMnetiQ8QZR3.

Proteomic databases

EPDiQ8QZR3.
MaxQBiQ8QZR3.
PaxDbiQ8QZR3.
PRIDEiQ8QZR3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000034346; ENSMUSP00000034346; ENSMUSG00000055730. [Q8QZR3-1]
ENSMUST00000164182; ENSMUSP00000127346; ENSMUSG00000055730. [Q8QZR3-2]
GeneIDi102022.
KEGGimmu:102022.
UCSCiuc009nbc.2. mouse. [Q8QZR3-1]
uc012giz.1. mouse. [Q8QZR3-2]

Organism-specific databases

CTDi102022.
MGIiMGI:2142491. Ces2a.

Phylogenomic databases

eggNOGiKOG1516. Eukaryota.
COG2272. LUCA.
GeneTreeiENSGT00760000118946.
HOGENOMiHOG000091866.
HOVERGENiHBG008839.
InParanoidiQ8QZR3.
KOiK03927.
OMAiVIVAIQY.
OrthoDBiEOG7RBZ7R.
PhylomeDBiQ8QZR3.
TreeFamiTF315470.

Enzyme and pathway databases

ReactomeiR-MMU-211945. Phase 1 - Functionalization of compounds.

Miscellaneous databases

NextBioi355236.
PROiQ8QZR3.
SOURCEiSearch...

Gene expression databases

GenevisibleiQ8QZR3. MM.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR002018. CarbesteraseB.
IPR019826. Carboxylesterase_B_AS.
IPR019819. Carboxylesterase_B_CS.
[Graphical view]
PfamiPF00135. COesterase. 1 hit.
[Graphical view]
SUPFAMiSSF53474. SSF53474. 1 hit.
PROSITEiPS00122. CARBOXYLESTERASE_B_1. 1 hit.
PS00941. CARBOXYLESTERASE_B_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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] (ISOFORMS 1 AND 2).
    Strain: C57BL/6J.
    Tissue: Cecum and Intestinal mucosa.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  3. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-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] (ISOFORM 1).
    Strain: FVB/N.
    Tissue: Colon and Liver.
  5. "Identification, expression, and purification of a pyrethroid-hydrolyzing carboxylesterase from mouse liver microsomes."
    Stok J.E., Huang H., Jones P.D., Wheelock C.E., Morisseau C., Hammock B.D.
    J. Biol. Chem. 279:29863-29869(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  7. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-209 AND LYS-296, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiEST2A_MOUSE
AccessioniPrimary (citable) accession number: Q8QZR3
Secondary accession number(s): E9Q3D0, Q3TMR2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 16, 2013
Last sequence update: June 1, 2002
Last modified: May 11, 2016
This is version 121 of the entry and version 1 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.