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Q9QXM0 (ABHD2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 93. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Abhydrolase domain-containing protein 2

EC=3.1.1.-
Alternative name(s):
Lung alpha/beta hydrolase 2
Short name=MmLABH2
Gene names
Name:Abhd2
Synonyms:Labh-2, Labh2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length425 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

May play a role in smooth muscle cells migration. Ref.5

Subcellular location

Membrane; Single-pass type II membrane protein Potential.

Tissue specificity

Widely expressed with higher expression in testis. Expressed by vascular smooth muscle cells, non vascular smooth muscle cells and heart. Ref.1 Ref.5

Developmental stage

Detected in embryos from E7 to E17. Weakly expressed in heart at E9.5. Expression is detected in endothelial cells of the dorsal aorta at E10.5 and disappear at E12.5. Expression in smooth muscle cells is first detected at E11.5. Strongly expressed in vitelline vessels at E12.5. Expressed in all smooth muscle cells at E16.5. Ref.1 Ref.5

Disruption phenotype

Neointimal hyperplasia. Ref.5

Sequence similarities

Belongs to the AB hydrolase superfamily. AB hydrolase 4 family.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 425425Abhydrolase domain-containing protein 2
PRO_0000280782

Regions

Transmembrane10 – 3021Helical; Signal-anchor for type II membrane protein; Potential

Sites

Active site2071Charge relay system By similarity
Active site3451Charge relay system By similarity
Active site3761Charge relay system By similarity

Experimental info

Sequence conflict211A → V in BAB25836. Ref.3
Sequence conflict631T → A in AAH89477. Ref.4
Sequence conflict3381M → L in BAE32131. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q9QXM0 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 82CC000D4A90004F

FASTA42548,378
        10         20         30         40         50         60 
MNAMLETPEL PAVFDGVKLA AVAAVLYVIV RCLNLKSPTA PPDLYFQDSG LSRFLLKSCP 

        70         80         90        100        110        120 
LLTKEYIPPL IWGKSGHIQT ALYGKMGRVR SPHPYGHRKF ITMSDGATST FDLFEPLAEH 

       130        140        150        160        170        180 
CVGDDITMVI CPGIANHSEK QYIRTFVDYA QKNGYRCAVL NHLGALPNIE LTSPRMFTYG 

       190        200        210        220        230        240 
CTWEFGAMVN YIKRTYPQTQ LVVVGFSLGG NIVCKYLGET QANQEKVLCC VSVCQGYSAL 

       250        260        270        280        290        300 
RAQETFMQWD QCRRFYNFLM ADNMKKIILS HRQALFGDHV KKPQSLEDTD LSRLYTATSL 

       310        320        330        340        350        360 
MQIDDNVMRK FHGYNSLKEY YEEESCMRYL HRIYVPLMLV NAADDPLVHE SLLTIPKSLS 

       370        380        390        400        410        420 
EKRENVMFVL PLHGGHLGFF EGSVLFPEPL TWMDKLVVEY ANAICQWERN KSQCSDTEQM 


EAELE 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and tissue distribution of three murine alpha/beta hydrolase fold protein cDNAs."
Edgar A.J., Polak J.M.
Biochem. Biophys. Res. Commun. 292:617-625(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
Tissue: Lung.
[2]"Cloning of an androgen-regulated a/b hydrolase."
Utleg A., White J., Lin B.
Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"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: C57BL/6J.
Tissue: Egg, Stomach and Thymus.
[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: Mammary tumor and Testis.
[5]"Increase of smooth muscle cell migration and of intimal hyperplasia in mice lacking the alpha/beta hydrolase domain containing 2 gene."
Miyata K., Oike Y., Hoshii T., Maekawa H., Ogawa H., Suda T., Araki K., Yamamura K.
Biochem. Biophys. Res. Commun. 329:296-304(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF201730 mRNA. Translation: AAF17566.1.
AF546701 mRNA. Translation: AAQ12022.1.
AK008690 mRNA. Translation: BAB25836.1.
AK139526 mRNA. Translation: BAE24049.1.
AK153642 mRNA. Translation: BAE32131.1.
BC027098 mRNA. Translation: AAH27098.1.
BC089477 mRNA. Translation: AAH89477.1.
CCDSCCDS21380.1.
RefSeqNP_061281.3. NM_018811.6.
UniGeneMm.365490.

3D structure databases

ProteinModelPortalQ9QXM0.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

MEROPSS33.A56.

PTM databases

PhosphoSiteQ9QXM0.

Proteomic databases

PaxDbQ9QXM0.
PRIDEQ9QXM0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000037315; ENSMUSP00000038361; ENSMUSG00000039202.
GeneID54608.
KEGGmmu:54608.
UCSCuc009hyc.1. mouse.

Organism-specific databases

CTD11057.
MGIMGI:1914344. Abhd2.

Phylogenomic databases

eggNOGCOG0429.
GeneTreeENSGT00530000062981.
HOGENOMHOG000230852.
HOVERGENHBG080812.
InParanoidQ9QXM0.
KOK13697.
OMAFSGHVQT.
OrthoDBEOG7RBZ87.
PhylomeDBQ9QXM0.
TreeFamTF313195.

Gene expression databases

BgeeQ9QXM0.
CleanExMM_ABHD2.
GenevestigatorQ9QXM0.

Family and domain databases

Gene3D3.40.50.1820. 2 hits.
InterProIPR012020. AB-Hydro_YheT.
IPR029058. AB_hydrolase.
IPR000073. AB_hydrolase_1.
IPR000952. UPF0017_hydro-like_CS.
[Graphical view]
PfamPF00561. Abhydrolase_1. 1 hit.
[Graphical view]
PIRSFPIRSF005211. Ab_hydro_YheT. 1 hit.
SUPFAMSSF53474. SSF53474. 1 hit.
PROSITEPS01133. UPF0017. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio311404.
PROQ9QXM0.
SOURCESearch...

Entry information

Entry nameABHD2_MOUSE
AccessionPrimary (citable) accession number: Q9QXM0
Secondary accession number(s): Q3U5E8, Q5FWC6, Q9D7Y8
Entry history
Integrated into UniProtKB/Swiss-Prot: March 20, 2007
Last sequence update: May 1, 2000
Last modified: July 9, 2014
This is version 93 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