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Glycerophosphodiester phosphodiesterase 1 (EC 3.1.4.-) (EC 3.1.4.44) (Membrane-interacting protein of RGS16)

 GDE1_MOUSE              Reviewed;         331 AA.
Q9JL56; Q3UBU4;
03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
01-OCT-2000, sequence version 1.
25-OCT-2017, entry version 117.
RecName: Full=Glycerophosphodiester phosphodiesterase 1;
EC=3.1.4.- {ECO:0000269|PubMed:25596343};
EC=3.1.4.44 {ECO:0000250|UniProtKB:Q9JL55};
AltName: Full=Membrane-interacting protein of RGS16;
Name=Gde1; Synonyms=Mir16;
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], AND TISSUE SPECIFICITY.
PubMed=10760272; DOI=10.1073/pnas.97.8.3999;
Zheng B., Chen D., Farquhar M.G.;
"MIR16, a putative membrane glycerophosphodiester phosphodiesterase,
interacts with RGS16.";
Proc. Natl. Acad. Sci. U.S.A. 97:3999-4004(2000).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Bone marrow, and Cerebellum;
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).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=FVB/N; TISSUE=Mammary tumor;
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).
[4]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Kidney, and Lung;
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).
[5]
TISSUE SPECIFICITY, CATALYTIC ACTIVITY, AND FUNCTION.
PubMed=25596343; DOI=10.1016/j.bbalip.2015.01.002;
Tsuboi K., Okamoto Y., Rahman I.A., Uyama T., Inoue T., Tokumura A.,
Ueda N.;
"Glycerophosphodiesterase GDE4 as a novel lysophospholipase D: a
possible involvement in bioactive N-acylethanolamine biosynthesis.";
Biochim. Biophys. Acta 1851:537-548(2015).
-!- FUNCTION: Has glycerophosphoinositol phosphodiesterase activity.
Hydrolyzes lysoglycerophospholipids to produce lysophosphatidic
acid (LPA) and the corresponding amines (PubMed:25596343). Has
little or no activity towards glycerophosphocholine. GDE1 activity
can be modulated by G-protein signaling pathways (By similarity).
{ECO:0000250|UniProtKB:Q9JL55, ECO:0000269|PubMed:25596343}.
-!- CATALYTIC ACTIVITY: 1-(sn-glycero-3-phospho)-1D-myo-inositol +
H(2)O = myo-inositol + sn-glycerol 3-phosphate.
{ECO:0000250|UniProtKB:Q9JL55}.
-!- CATALYTIC ACTIVITY: N-acyl-sn-glycero-3-phosphoethanolamine +
H(2)O = N-acylethanolamine + sn-glycerol 3-phosphate.
{ECO:0000269|PubMed:25596343}.
-!- CATALYTIC ACTIVITY: 1-O-(alk-1Z-enyl)-sn-glycero-3-phospho-(N-
acyl)-ethanolamine + H(2)O = 1-O-(1Z-alkenyl)-sn-glycero-3-
phosphate + N-acylethanolamine. {ECO:0000269|PubMed:25596343}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000250|UniProtKB:Q9JL55};
-!- SUBUNIT: Interacts with PRAF2 (By similarity). Interacts with
RGS16 (By similarity). {ECO:0000250|UniProtKB:Q9JL55,
ECO:0000250|UniProtKB:Q9NZC3}.
-!- SUBCELLULAR LOCATION: Cell membrane
{ECO:0000250|UniProtKB:Q9JL55}; Multi-pass membrane protein
{ECO:0000255}. Cytoplasmic vesicle membrane
{ECO:0000250|UniProtKB:Q9JL55}; Multi-pass membrane protein
{ECO:0000255}. Note=Perinuclear vesicles and cell membrane.
{ECO:0000250|UniProtKB:Q9JL55}.
-!- TISSUE SPECIFICITY: Widely expressed.
{ECO:0000269|PubMed:10760272}.
-!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q9JL55}.
-!- SIMILARITY: Belongs to the glycerophosphoryl diester
phosphodiesterase family. {ECO:0000305}.
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EMBL; AF212860; AAF65232.1; -; mRNA.
EMBL; AK005361; BAB23975.1; -; mRNA.
EMBL; AK150807; BAE29870.1; -; mRNA.
EMBL; BC003902; AAH03902.1; -; mRNA.
CCDS; CCDS21774.1; -.
RefSeq; NP_062526.1; NM_019580.4.
UniGene; Mm.273142; -.
ProteinModelPortal; Q9JL56; -.
SMR; Q9JL56; -.
STRING; 10090.ENSMUSP00000046371; -.
SwissLipids; SLP:000001124; -.
iPTMnet; Q9JL56; -.
PhosphoSitePlus; Q9JL56; -.
EPD; Q9JL56; -.
MaxQB; Q9JL56; -.
PaxDb; Q9JL56; -.
PeptideAtlas; Q9JL56; -.
PRIDE; Q9JL56; -.
Ensembl; ENSMUST00000038791; ENSMUSP00000046371; ENSMUSG00000033917.
GeneID; 56209; -.
KEGG; mmu:56209; -.
UCSC; uc009jki.1; mouse.
CTD; 51573; -.
MGI; MGI:1891827; Gde1.
eggNOG; KOG2258; Eukaryota.
eggNOG; COG0584; LUCA.
GeneTree; ENSGT00510000047820; -.
HOGENOM; HOG000006722; -.
HOVERGEN; HBG052946; -.
InParanoid; Q9JL56; -.
KO; K19179; -.
OMA; RSPFNAC; -.
OrthoDB; EOG091G0ALO; -.
PhylomeDB; Q9JL56; -.
TreeFam; TF313692; -.
Reactome; R-MMU-6814848; Glycerophospholipid catabolism.
PRO; PR:Q9JL56; -.
Proteomes; UP000000589; Chromosome 7.
Bgee; ENSMUSG00000033917; -.
CleanEx; MM_GDE1; -.
ExpressionAtlas; Q9JL56; baseline and differential.
Genevisible; Q9JL56; MM.
GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
GO; GO:0005887; C:integral component of plasma membrane; ISS:MGI.
GO; GO:0016020; C:membrane; IDA:MGI.
GO; GO:0008889; F:glycerophosphodiester phosphodiesterase activity; ISS:MGI.
GO; GO:0047395; F:glycerophosphoinositol glycerophosphodiesterase activity; IDA:MGI.
GO; GO:0004622; F:lysophospholipase activity; IDA:MGI.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0008081; F:phosphoric diester hydrolase activity; IDA:MGI.
GO; GO:0007186; P:G-protein coupled receptor signaling pathway; ISO:MGI.
GO; GO:0070291; P:N-acylethanolamine metabolic process; IDA:MGI.
GO; GO:0006644; P:phospholipid metabolic process; IDA:MGI.
Gene3D; 3.20.20.190; -; 1.
InterPro; IPR004129; GlyceroP-diester-Pdiesterase.
InterPro; IPR030395; GP_PDE_dom.
InterPro; IPR017946; PLC-like_Pdiesterase_TIM-brl.
PANTHER; PTHR23344; PTHR23344; 1.
Pfam; PF03009; GDPD; 1.
SUPFAM; SSF51695; SSF51695; 1.
PROSITE; PS51704; GP_PDE; 1.
1: Evidence at protein level;
Cell membrane; Complete proteome; Cytoplasmic vesicle; Glycoprotein;
Hydrolase; Magnesium; Membrane; Metal-binding; Reference proteome;
Transmembrane; Transmembrane helix.
CHAIN 1 331 Glycerophosphodiester phosphodiesterase
1.
/FTId=PRO_0000251945.
TOPO_DOM 1 3 Cytoplasmic. {ECO:0000255}.
TRANSMEM 4 24 Helical. {ECO:0000255}.
TOPO_DOM 25 248 Lumenal. {ECO:0000255}.
TRANSMEM 249 269 Helical. {ECO:0000255}.
TOPO_DOM 270 331 Cytoplasmic. {ECO:0000255}.
DOMAIN 65 331 GP-PDE.
METAL 97 97 Magnesium. {ECO:0000255}.
METAL 99 99 Magnesium. {ECO:0000255}.
METAL 174 174 Magnesium. {ECO:0000255}.
CARBOHYD 168 168 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CONFLICT 102 102 F -> L (in Ref. 2; BAE29870).
{ECO:0000305}.
SEQUENCE 331 AA; 37629 MW; C79A058AA884C10B CRC64;
MWLWEDQGGL LGPFSFVLVL LLVVTRSPFN ACVLTGSLYI LLRFFSFEPV PSRRALQVLK
PRDRVSAIAH RGGSHDAPEN TLAAIRQAAK NGATGVELDI EFTSDGVPVL MHDNTVDRTT
DGSGRLCDLT FEQVRKLNPA ANHRLRNEFP DERIPTLKEA VTECLRHNLT IFFDVKGHAD
MASAALKNIY TEFPQLYNNS MVCSFLPEVI YKMRQTDQKV ITALTHRPWS LSHTGDGKPR
YSVFWKQSVF VVLDILLDWS MHNVLWYLCG ISAFLMQKDF VSPDYLKKWS AKGIQVVSWT
VNTFDEKNYY ESHLGSSYIT DSMLEDCAPH F


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