Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Abhydrolase domain-containing protein 2

Gene

Abhd2

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

Functioni

May play a role in smooth muscle cells migration.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei207 – 2071Charge relay systemBy similarity
Active sitei345 – 3451Charge relay systemBy similarity
Active sitei376 – 3761Charge relay systemBy similarity

GO - Molecular functioni

  1. carboxylic ester hydrolase activity Source: UniProtKB-KW

GO - Biological processi

  1. negative regulation of cell migration Source: MGI
  2. response to wounding Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Serine esterase

Protein family/group databases

MEROPSiS33.A56.

Names & Taxonomyi

Protein namesi
Recommended name:
Abhydrolase domain-containing protein 2 (EC:3.1.1.-)
Alternative name(s):
Lung alpha/beta hydrolase 2
Short name:
MmLABH2
Gene namesi
Name:Abhd2
Synonyms:Labh-2, Labh2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 7

Organism-specific databases

MGIiMGI:1914344. Abhd2.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei10 – 3021Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Disruption phenotypei

Neointimal hyperplasia.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 425425Abhydrolase domain-containing protein 2PRO_0000280782Add
BLAST

Proteomic databases

MaxQBiQ9QXM0.
PaxDbiQ9QXM0.
PRIDEiQ9QXM0.

PTM databases

PhosphoSiteiQ9QXM0.

Expressioni

Tissue specificityi

Widely expressed with higher expression in testis. Expressed by vascular smooth muscle cells, non vascular smooth muscle cells and heart.2 Publications

Developmental stagei

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 E16.5.2 Publications

Gene expression databases

BgeeiQ9QXM0.
CleanExiMM_ABHD2.
GenevestigatoriQ9QXM0.

Structurei

3D structure databases

ProteinModelPortaliQ9QXM0.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0429.
GeneTreeiENSGT00530000062981.
HOGENOMiHOG000230852.
HOVERGENiHBG080812.
InParanoidiQ9QXM0.
KOiK13697.
OMAiLYIMTEN.
OrthoDBiEOG7RBZ87.
PhylomeDBiQ9QXM0.
TreeFamiTF313195.

Family and domain databases

Gene3Di3.40.50.1820. 2 hits.
InterProiIPR012020. AB-Hydro_YheT.
IPR029058. AB_hydrolase.
IPR000073. AB_hydrolase_1.
IPR000952. UPF0017_hydro-like_CS.
[Graphical view]
PfamiPF00561. Abhydrolase_1. 1 hit.
[Graphical view]
PIRSFiPIRSF005211. Ab_hydro_YheT. 1 hit.
SUPFAMiSSF53474. SSF53474. 1 hit.
PROSITEiPS01133. UPF0017. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9QXM0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNAMLETPEL PAVFDGVKLA AVAAVLYVIV RCLNLKSPTA PPDLYFQDSG
60 70 80 90 100
LSRFLLKSCP LLTKEYIPPL IWGKSGHIQT ALYGKMGRVR SPHPYGHRKF
110 120 130 140 150
ITMSDGATST FDLFEPLAEH CVGDDITMVI CPGIANHSEK QYIRTFVDYA
160 170 180 190 200
QKNGYRCAVL NHLGALPNIE LTSPRMFTYG CTWEFGAMVN YIKRTYPQTQ
210 220 230 240 250
LVVVGFSLGG NIVCKYLGET QANQEKVLCC VSVCQGYSAL RAQETFMQWD
260 270 280 290 300
QCRRFYNFLM ADNMKKIILS HRQALFGDHV KKPQSLEDTD LSRLYTATSL
310 320 330 340 350
MQIDDNVMRK FHGYNSLKEY YEEESCMRYL HRIYVPLMLV NAADDPLVHE
360 370 380 390 400
SLLTIPKSLS EKRENVMFVL PLHGGHLGFF EGSVLFPEPL TWMDKLVVEY
410 420
ANAICQWERN KSQCSDTEQM EAELE
Length:425
Mass (Da):48,378
Last modified:May 1, 2000 - v1
Checksum:i82CC000D4A90004F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti21 – 211A → V in BAB25836 (PubMed:16141072).Curated
Sequence conflicti63 – 631T → A in AAH89477 (PubMed:15489334).Curated
Sequence conflicti338 – 3381M → L in BAE32131 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS21380.1.
RefSeqiNP_061281.3. NM_018811.6.
UniGeneiMm.365490.

Genome annotation databases

EnsembliENSMUST00000037315; ENSMUSP00000038361; ENSMUSG00000039202.
GeneIDi54608.
KEGGimmu:54608.
UCSCiuc009hyc.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS21380.1.
RefSeqiNP_061281.3. NM_018811.6.
UniGeneiMm.365490.

3D structure databases

ProteinModelPortaliQ9QXM0.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

MEROPSiS33.A56.

PTM databases

PhosphoSiteiQ9QXM0.

Proteomic databases

MaxQBiQ9QXM0.
PaxDbiQ9QXM0.
PRIDEiQ9QXM0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000037315; ENSMUSP00000038361; ENSMUSG00000039202.
GeneIDi54608.
KEGGimmu:54608.
UCSCiuc009hyc.1. mouse.

Organism-specific databases

CTDi11057.
MGIiMGI:1914344. Abhd2.

Phylogenomic databases

eggNOGiCOG0429.
GeneTreeiENSGT00530000062981.
HOGENOMiHOG000230852.
HOVERGENiHBG080812.
InParanoidiQ9QXM0.
KOiK13697.
OMAiLYIMTEN.
OrthoDBiEOG7RBZ87.
PhylomeDBiQ9QXM0.
TreeFamiTF313195.

Miscellaneous databases

NextBioi311404.
PROiQ9QXM0.
SOURCEiSearch...

Gene expression databases

BgeeiQ9QXM0.
CleanExiMM_ABHD2.
GenevestigatoriQ9QXM0.

Family and domain databases

Gene3Di3.40.50.1820. 2 hits.
InterProiIPR012020. AB-Hydro_YheT.
IPR029058. AB_hydrolase.
IPR000073. AB_hydrolase_1.
IPR000952. UPF0017_hydro-like_CS.
[Graphical view]
PfamiPF00561. Abhydrolase_1. 1 hit.
[Graphical view]
PIRSFiPIRSF005211. Ab_hydro_YheT. 1 hit.
SUPFAMiSSF53474. SSF53474. 1 hit.
PROSITEiPS01133. UPF0017. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiABHD2_MOUSE
AccessioniPrimary (citable) accession number: Q9QXM0
Secondary accession number(s): Q3U5E8, Q5FWC6, Q9D7Y8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 20, 2007
Last sequence update: May 1, 2000
Last modified: January 7, 2015
This is version 96 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

External Data

Dasty 3

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 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.