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Q6PE15 (ABHDA_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 77. Feed History...

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

Names and origin

Protein namesRecommended name:
Mycophenolic acid acyl-glucuronide esterase, mitochondrial

EC=3.1.1.93
Alternative name(s):
Alpha/beta hydrolase domain-containing protein 10
Short name=Abhydrolase domain-containing protein 10
Gene names
Name:Abhd10
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length297 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Catalytic activity

Mycophenolic acid O-acyl-glucuronide + H2O = mycophenolate + D-glucuronate.

Subcellular location

Mitochondrion Potential.

Sequence similarities

Belongs to the AB hydrolase superfamily.

Ontologies

Keywords
   Cellular componentMitochondrion
   Coding sequence diversityAlternative splicing
   DomainTransit peptide
   Molecular functionHydrolase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processglucuronoside catabolic process

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcytosol

Inferred from electronic annotation. Source: Ensembl

mitochondrion

Inferred from direct assay PubMed 18614015. Source: MGI

   Molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q6PE15-1)

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.
Isoform 2 (identifier: Q6PE15-2)

The sequence of this isoform differs from the canonical sequence as follows:
     269-269: D → AQSVDICGAATPSEWSSKPLGTDS
     270-297: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 4343Mitochondrion Potential
Chain44 – 297254Mycophenolic acid acyl-glucuronide esterase, mitochondrial
PRO_0000280734

Sites

Active site1431Charge relay system By similarity
Active site2401Charge relay system By similarity
Active site2701Charge relay system By similarity

Natural variations

Alternative sequence2691D → AQSVDICGAATPSEWSSKPL GTDS in isoform 2.
VSP_023893
Alternative sequence270 – 29728Missing in isoform 2.
VSP_023894

Experimental info

Sequence conflict2671Q → R in BAC35091. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 7AE4AEBD214ED6CE

FASTA29733,040
        10         20         30         40         50         60 
MAAWAPCRRW GWAAVSFGRH PGLSASLARK PPRAWWLSAC RQKASLSFLN RSELPNLAYK 

        70         80         90        100        110        120 
RLKGKTPGII FIPGYLSNMN GIKAVAVEEF CKSLGHAFIR FDYSGIGSSD GNLAECTVGK 

       130        140        150        160        170        180 
WRKDVLSILD DVAEGPQILV GSSLGGWLML HAAIARPEKV IALIGIATAA DGLVTQYHAL 

       190        200        210        220        230        240 
PVETQKEIEM KGEWTLPSRY NKEGYFRIPY SFIKEAEHHC LLHSPIPVTC PVRLLHGMKD 

       250        260        270        280        290 
EIVPWQRSLQ VADRIVSPDV DVILRKQGDH RMKEKADIHL LICTIDDLID KLSTVVP 

« Hide

Isoform 2 [UniParc].

Checksum: 03B5FC190A05C96F
Show »

FASTA29232,115

References

[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. 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] (ISOFORMS 1 AND 2).
Strain: C57BL/6J.
Tissue: Kidney and Lung.
[2]"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: C57BL/6 and C57BL/6J.
Tissue: Brain and Thymus.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK052670 mRNA. Translation: BAC35091.1.
AK084998 mRNA. Translation: BAC39335.1.
AK166025 mRNA. Translation: BAE38528.1.
BC027656 mRNA. Translation: AAH27656.1.
BC058347 mRNA. Translation: AAH58347.1.
CCDSCCDS28201.1. [Q6PE15-1]
RefSeqNP_001258999.1. NM_001272070.1. [Q6PE15-2]
NP_766099.3. NM_172511.4. [Q6PE15-1]
UniGeneMm.247453.

3D structure databases

ProteinModelPortalQ6PE15.
SMRQ6PE15. Positions 67-290.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ6PE15. 1 interaction.
MINTMINT-4114279.

Chemistry

ChEMBLCHEMBL2146294.

Protein family/group databases

MEROPSS09.023.

PTM databases

PhosphoSiteQ6PE15.

Proteomic databases

MaxQBQ6PE15.
PaxDbQ6PE15.
PRIDEQ6PE15.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000066983; ENSMUSP00000065282; ENSMUSG00000033157. [Q6PE15-1]
GeneID213012.
KEGGmmu:213012.
UCSCuc007zix.2. mouse. [Q6PE15-2]
uc007ziy.2. mouse. [Q6PE15-1]

Organism-specific databases

CTD55347.
MGIMGI:2442422. Abhd10.

Phylogenomic databases

eggNOGCOG0596.
GeneTreeENSGT00390000017765.
HOGENOMHOG000139902.
HOVERGENHBG080562.
InParanoidQ6PE15.
KOK13702.
OMAIEDGRNH.
OrthoDBEOG7673B6.
PhylomeDBQ6PE15.
TreeFamTF329757.

Gene expression databases

BgeeQ6PE15.
CleanExMM_ABHD10.
GenevestigatorQ6PE15.

Family and domain databases

Gene3D3.40.50.1820. 2 hits.
InterProIPR029058. AB_hydrolase.
[Graphical view]
SUPFAMSSF53474. SSF53474. 1 hit.
ProtoNetSearch...

Other

NextBio373814.
PROQ6PE15.
SOURCESearch...

Entry information

Entry nameABHDA_MOUSE
AccessionPrimary (citable) accession number: Q6PE15
Secondary accession number(s): Q3TMB4 expand/collapse secondary AC list , Q8C3S8, Q8C724, Q8K188
Entry history
Integrated into UniProtKB/Swiss-Prot: March 20, 2007
Last sequence update: July 5, 2004
Last modified: July 9, 2014
This is version 77 of the entry and version 1 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

MGD cross-references

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