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Monoacylglycerol lipase ABHD2 (EC 3.1.1.23) (2-arachidonoylglycerol hydrolase) (Abhydrolase domain-containing protein 2) (Lung alpha/beta hydrolase 2) (MmLABH2)

 ABHD2_MOUSE             Reviewed;         425 AA.
Q9QXM0; Q3U5E8; Q5FWC6; Q9D7Y8;
20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
05-DEC-2018, entry version 117.
RecName: Full=Monoacylglycerol lipase ABHD2 {ECO:0000305};
EC=3.1.1.23 {ECO:0000250|UniProtKB:P08910};
AltName: Full=2-arachidonoylglycerol hydrolase {ECO:0000305};
AltName: Full=Abhydrolase domain-containing protein 2 {ECO:0000305};
AltName: Full=Lung alpha/beta hydrolase 2 {ECO:0000303|PubMed:11922611};
Short=MmLABH2 {ECO:0000303|PubMed:11922611};
Name=Abhd2;
Synonyms=Labh-2 {ECO:0000303|PubMed:11922611},
Labh2 {ECO:0000303|PubMed:11922611};
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL
STAGE.
TISSUE=Lung;
PubMed=11922611; DOI=10.1006/bbrc.2002.6692;
Edgar A.J., Polak J.M.;
"Cloning and tissue distribution of three murine alpha/beta hydrolase
fold protein cDNAs.";
Biochem. Biophys. Res. Commun. 292:617-625(2002).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
Utleg A., White J., Lin B.;
"Cloning of an androgen-regulated a/b hydrolase.";
Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Egg, Stomach, and Thymus;
PubMed=16141072; DOI=10.1126/science.1112014;
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.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=FVB/N; TISSUE=Mammary tumor, and Testis;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND DISRUPTION
PHENOTYPE.
PubMed=15721306; DOI=10.1016/j.bbrc.2005.01.127;
Miyata K., Oike Y., Hoshii T., Maekawa H., Ogawa H., Suda T.,
Araki K., Yamamura K.;
"Increase of smooth muscle cell migration and of intimal hyperplasia
in mice lacking the alpha/beta hydrolase domain containing 2 gene.";
Biochem. Biophys. Res. Commun. 329:296-304(2005).
[6]
DISRUPTION PHENOTYPE.
PubMed=19250629; DOI=10.1016/j.bbrc.2009.01.098;
Jin S., Zhao G., Li Z., Nishimoto Y., Isohama Y., Shen J., Ito T.,
Takeya M., Araki K., He P., Yamamura K.;
"Age-related pulmonary emphysema in mice lacking alpha/beta hydrolase
domain containing 2 gene.";
Biochem. Biophys. Res. Commun. 380:419-424(2009).
[7]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver, and Pancreas;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[8]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=26989199; DOI=10.1126/science.aad6887;
Miller M.R., Mannowetz N., Iavarone A.T., Safavi R., Gracheva E.O.,
Smith J.F., Hill R.Z., Bautista D.M., Kirichok Y., Lishko P.V.;
"Unconventional endocannabinoid signaling governs sperm activation via
sex hormone progesterone.";
Science 352:555-559(2016).
-!- FUNCTION: Progesterone-dependent acylglycerol lipase that
catalyzes hydrolysis of endocannabinoid arachidonoylglycerol (AG)
from cell membrane. Acts as a progesterone receptor: progesterone-
binding activates the acylglycerol lipase activity, mediating
degradation of 1-arachidonoylglycerol (1AG) and 2-
arachidonoylglycerol (2AG) to glycerol and arachidonic acid (AA)
(By similarity). Involved in acrosomal reaction (PubMed:26989199).
May also play a role in smooth muscle cells migration
(PubMed:15721306). {ECO:0000250|UniProtKB:P08910,
ECO:0000269|PubMed:15721306, ECO:0000305|PubMed:26989199}.
-!- CATALYTIC ACTIVITY:
Reaction=Hydrolyzes glycerol monoesters of long-chain fatty
acids.; EC=3.1.1.23; Evidence={ECO:0000250|UniProtKB:P08910};
-!- ACTIVITY REGULATION: Acylglycerol lipase activity is activated
upon binding to progesterone. {ECO:0000250|UniProtKB:P08910}.
-!- SUBCELLULAR LOCATION: Cell membrane
{ECO:0000250|UniProtKB:P08910}; Single-pass type II membrane
protein {ECO:0000250|UniProtKB:P08910}. Cytoplasmic vesicle,
secretory vesicle, acrosome membrane
{ECO:0000269|PubMed:26989199}. Note=Absent from the sperm
flagellum. {ECO:0000269|PubMed:26989199}.
-!- TISSUE SPECIFICITY: Widely expressed with higher expression in
testis. Expressed by vascular smooth muscle cells, non vascular
smooth muscle cells and heart. {ECO:0000269|PubMed:11922611,
ECO:0000269|PubMed:15721306}.
-!- 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. {ECO:0000269|PubMed:11922611,
ECO:0000269|PubMed:15721306}.
-!- DISRUPTION PHENOTYPE: Neointimal hyperplasia (PubMed:15721306). In
lungs, decreased level of phosphatidylcholine in the
bronchoalveolar lavage is observed (PubMed:19250629). Mice develop
spontaneous gradual progression of emphysema (PubMed:19250629).
{ECO:0000269|PubMed:15721306, ECO:0000269|PubMed:19250629}.
-!- SIMILARITY: Belongs to the AB hydrolase superfamily. AB hydrolase
4 family. {ECO:0000305}.
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; AF201730; AAF17566.1; -; mRNA.
EMBL; AF546701; AAQ12022.1; -; mRNA.
EMBL; AK008690; BAB25836.1; -; mRNA.
EMBL; AK139526; BAE24049.1; -; mRNA.
EMBL; AK153642; BAE32131.1; -; mRNA.
EMBL; BC027098; AAH27098.1; -; mRNA.
EMBL; BC089477; AAH89477.1; -; mRNA.
CCDS; CCDS21380.1; -.
RefSeq; NP_061281.3; NM_018811.6.
UniGene; Mm.365490; -.
ProteinModelPortal; Q9QXM0; -.
STRING; 10090.ENSMUSP00000038361; -.
ESTHER; mouse-ABHD2; abh_upf0017.
MEROPS; S33.A56; -.
iPTMnet; Q9QXM0; -.
PhosphoSitePlus; Q9QXM0; -.
MaxQB; Q9QXM0; -.
PaxDb; Q9QXM0; -.
PeptideAtlas; Q9QXM0; -.
PRIDE; Q9QXM0; -.
Ensembl; ENSMUST00000037315; ENSMUSP00000038361; ENSMUSG00000039202.
GeneID; 54608; -.
KEGG; mmu:54608; -.
UCSC; uc009hyc.1; mouse.
CTD; 11057; -.
MGI; MGI:1914344; Abhd2.
eggNOG; KOG1838; Eukaryota.
eggNOG; COG0429; LUCA.
GeneTree; ENSGT00940000153712; -.
HOGENOM; HOG000230852; -.
HOVERGEN; HBG080812; -.
InParanoid; Q9QXM0; -.
KO; K13697; -.
OMA; CPWPIGE; -.
OrthoDB; EOG091G08XK; -.
PhylomeDB; Q9QXM0; -.
TreeFam; TF313195; -.
PRO; PR:Q9QXM0; -.
Proteomes; UP000000589; Chromosome 7.
Bgee; ENSMUSG00000039202; Expressed in 245 organ(s), highest expression level in pigmented layer of retina.
CleanEx; MM_ABHD2; -.
Genevisible; Q9QXM0; MM.
GO; GO:0002080; C:acrosomal membrane; IEA:UniProtKB-SubCell.
GO; GO:0001669; C:acrosomal vesicle; IDA:UniProtKB.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0036126; C:sperm flagellum; ISO:MGI.
GO; GO:0097524; C:sperm plasma membrane; ISO:MGI.
GO; GO:0047372; F:acylglycerol lipase activity; ISS:UniProtKB.
GO; GO:0042562; F:hormone binding; ISS:UniProtKB.
GO; GO:0016298; F:lipase activity; IBA:GO_Central.
GO; GO:0034338; F:short-chain carboxylesterase activity; IBA:GO_Central.
GO; GO:0003707; F:steroid hormone receptor activity; ISS:UniProtKB.
GO; GO:0007340; P:acrosome reaction; IMP:UniProtKB.
GO; GO:0046464; P:acylglycerol catabolic process; ISS:UniProtKB.
GO; GO:0044255; P:cellular lipid metabolic process; IBA:GO_Central.
GO; GO:0051792; P:medium-chain fatty acid biosynthetic process; IBA:GO_Central.
GO; GO:0051793; P:medium-chain fatty acid catabolic process; IBA:GO_Central.
GO; GO:0030336; P:negative regulation of cell migration; IMP:MGI.
GO; GO:0032570; P:response to progesterone; ISS:UniProtKB.
GO; GO:0009611; P:response to wounding; IMP:MGI.
GO; GO:0048240; P:sperm capacitation; ISO:MGI.
GO; GO:0043401; P:steroid hormone mediated signaling pathway; ISS:UniProtKB.
InterPro; IPR029058; AB_hydrolase.
InterPro; IPR000073; AB_hydrolase_1.
InterPro; IPR000952; AB_hydrolase_4_CS.
InterPro; IPR012020; ABHD4.
Pfam; PF00561; Abhydrolase_1; 1.
PIRSF; PIRSF005211; Ab_hydro_YheT; 1.
SUPFAM; SSF53474; SSF53474; 1.
PROSITE; PS01133; UPF0017; 1.
1: Evidence at protein level;
Cell membrane; Complete proteome; Cytoplasmic vesicle; Glycoprotein;
Hydrolase; Lipid degradation; Lipid metabolism; Membrane;
Reference proteome; Serine esterase; Signal-anchor; Transmembrane;
Transmembrane helix.
CHAIN 1 425 Monoacylglycerol lipase ABHD2.
/FTId=PRO_0000280782.
TOPO_DOM 1 9 Cytoplasmic. {ECO:0000305}.
TRANSMEM 10 30 Helical; Signal-anchor for type II
membrane protein. {ECO:0000255}.
TOPO_DOM 31 425 Extracellular. {ECO:0000305}.
DOMAIN 128 382 AB hydrolase-1. {ECO:0000255}.
ACT_SITE 207 207 Nucleophile.
{ECO:0000250|UniProtKB:Q86WA6}.
ACT_SITE 345 345 Charge relay system.
{ECO:0000250|UniProtKB:Q86WA6}.
ACT_SITE 376 376 Charge relay system.
{ECO:0000250|UniProtKB:Q86WA6}.
CARBOHYD 136 136 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CARBOHYD 410 410 N-linked (GlcNAc...) asparagine.
{ECO:0000255|PROSITE-ProRule:PRU00498}.
CONFLICT 21 21 A -> V (in Ref. 3; BAB25836).
{ECO:0000305}.
CONFLICT 63 63 T -> A (in Ref. 4; AAH89477).
{ECO:0000305}.
CONFLICT 338 338 M -> L (in Ref. 3; BAE32131).
{ECO:0000305}.
SEQUENCE 425 AA; 48378 MW; 82CC000D4A90004F CRC64;
MNAMLETPEL PAVFDGVKLA AVAAVLYVIV RCLNLKSPTA PPDLYFQDSG LSRFLLKSCP
LLTKEYIPPL IWGKSGHIQT ALYGKMGRVR SPHPYGHRKF ITMSDGATST FDLFEPLAEH
CVGDDITMVI CPGIANHSEK QYIRTFVDYA QKNGYRCAVL NHLGALPNIE LTSPRMFTYG
CTWEFGAMVN YIKRTYPQTQ LVVVGFSLGG NIVCKYLGET QANQEKVLCC VSVCQGYSAL
RAQETFMQWD QCRRFYNFLM ADNMKKIILS HRQALFGDHV KKPQSLEDTD LSRLYTATSL
MQIDDNVMRK FHGYNSLKEY YEEESCMRYL HRIYVPLMLV NAADDPLVHE SLLTIPKSLS
EKRENVMFVL PLHGGHLGFF EGSVLFPEPL TWMDKLVVEY ANAICQWERN KSQCSDTEQM
EAELE


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