GDE1_MOUSE
ID GDE1_MOUSE Reviewed; 331 AA.
AC Q9JL56; Q3UBU4;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Glycerophosphodiester phosphodiesterase 1 {ECO:0000305};
DE AltName: Full=Glycerophosphoinositol glycerophosphodiesterase GDE1 {ECO:0000305};
DE EC=3.1.4.44 {ECO:0000250|UniProtKB:Q9JL55};
DE AltName: Full=Lysophospholipase D GDE1 {ECO:0000305};
DE EC=3.1.4.- {ECO:0000269|PubMed:21801852, ECO:0000269|PubMed:25596343};
DE AltName: Full=Membrane-interacting protein of RGS16 {ECO:0000303|PubMed:10760272};
GN Name=Gde1 {ECO:0000312|MGI:MGI:1891827};
GN Synonyms=Mir16 {ECO:0000303|PubMed:10760272};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=10760272; DOI=10.1073/pnas.97.8.3999;
RA Zheng B., Chen D., Farquhar M.G.;
RT "MIR16, a putative membrane glycerophosphodiester phosphodiesterase,
RT interacts with RGS16.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:3999-4004(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Bone marrow, and Cerebellum;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP CATALYTIC ACTIVITY, FUNCTION, ACTIVITY REGULATION, GLYCOSYLATION,
RP SUBCELLULAR LOCATION, BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE
RP SPECIFICITY.
RX PubMed=18227059; DOI=10.1074/jbc.m707807200;
RA Simon G.M., Cravatt B.F.;
RT "Anandamide biosynthesis catalyzed by the phosphodiesterase GDE1 and
RT detection of glycerophospho-N-acyl ethanolamine precursors in mouse
RT brain.";
RL J. Biol. Chem. 283:9341-9349(2008).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, and Lung;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP CATALYTIC ACTIVITY, AND FUNCTION.
RX PubMed=21801852; DOI=10.1016/j.bbalip.2011.07.009;
RA Tsuboi K., Okamoto Y., Ikematsu N., Inoue M., Shimizu Y., Uyama T.,
RA Wang J., Deutsch D.G., Burns M.P., Ulloa N.M., Tokumura A., Ueda N.;
RT "Enzymatic formation of N-acylethanolamines from N-acylethanolamine
RT plasmalogen through N-acylphosphatidylethanolamine-hydrolyzing
RT phospholipase D-dependent and -independent pathways.";
RL Biochim. Biophys. Acta 1811:565-577(2011).
RN [7]
RP TISSUE SPECIFICITY, CATALYTIC ACTIVITY, FUNCTION, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND ACTIVITY REGULATION.
RX PubMed=25596343; DOI=10.1016/j.bbalip.2015.01.002;
RA Tsuboi K., Okamoto Y., Rahman I.A., Uyama T., Inoue T., Tokumura A.,
RA Ueda N.;
RT "Glycerophosphodiesterase GDE4 as a novel lysophospholipase D: a possible
RT involvement in bioactive N-acylethanolamine biosynthesis.";
RL Biochim. Biophys. Acta 1851:537-548(2015).
CC -!- FUNCTION: Hydrolyzes the phosphodiester bond of glycerophosphodiesters
CC such as glycerophosphoinositol (GroPIns) and glycerophosphoethanolamine
CC (GroPEth), to yield a glycerol phosphate and an alcohol
CC (PubMed:18227059, PubMed:21801852, PubMed:25596343). Hydrolyzes
CC glycerophospho-N-acylethanolamines to N-acylethanolamines in the brain
CC and participates in bioactive N-acylethanolamine biosynthesis such as
CC anandamide (an endocannabinoid), N-palmitoylethanolamine (an anti-
CC inflammatory), and N-oleoylethanolamine (an anorexic)
CC (PubMed:18227059). In addition, has a lysophospholipase D activity by
CC hydrolyzing N-acyl-lysoplasmenylethanolamine (N-acyl-lysoPlsEt) to N-
CC acylethanolamine (PubMed:21801852, PubMed:25596343). However
CC lysophospholipase D activity is lower than glycerophosphodiester
CC phosphodiesterase activity (PubMed:21801852, PubMed:25596343). Has
CC little or no activity towards glycerophosphocholine (By similarity).
CC {ECO:0000250|UniProtKB:Q9JL55, ECO:0000269|PubMed:18227059,
CC ECO:0000269|PubMed:21801852, ECO:0000269|PubMed:25596343}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + sn-glycero-3-phospho-1D-myo-inositol = H(+) + myo-
CC inositol + sn-glycerol 3-phosphate; Xref=Rhea:RHEA:16501,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17268,
CC ChEBI:CHEBI:57597, ChEBI:CHEBI:58444; EC=3.1.4.44;
CC Evidence={ECO:0000250|UniProtKB:Q9JL55};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16502;
CC Evidence={ECO:0000250|UniProtKB:Q9JL55};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-O-(1Z-octadecenyl)-sn-glycero-3-phospho-(N-5Z,8Z,11Z,14Z-
CC eicosatetraenoyl)-ethanolamine + H2O = 1-O-(1Z-octadecenyl)-sn-
CC glycero-3-phosphate + H(+) + N-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-
CC ethanolamine; Xref=Rhea:RHEA:53192, ChEBI:CHEBI:2700,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:137016,
CC ChEBI:CHEBI:137017; Evidence={ECO:0000269|PubMed:25596343};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53193;
CC Evidence={ECO:0000269|PubMed:25596343};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-O-(1Z-octadecenyl)-sn-glycero-3-phospho-(N-9Z-octadecenoyl)-
CC ethanolamine + H2O = 1-O-(1Z-octadecenyl)-sn-glycero-3-phosphate +
CC H(+) + N-(9Z-octadecenoyl) ethanolamine; Xref=Rhea:RHEA:53188,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:71466,
CC ChEBI:CHEBI:137010, ChEBI:CHEBI:137017;
CC Evidence={ECO:0000269|PubMed:25596343};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53189;
CC Evidence={ECO:0000269|PubMed:25596343};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-O-(1Z-octadecenyl)-sn-glycero-3-phospho-N-hexadecanoyl-
CC ethanolamine + H2O = 1-O-(1Z-octadecenyl)-sn-glycero-3-phosphate +
CC H(+) + N-hexadecanoylethanolamine; Xref=Rhea:RHEA:53184,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:71464,
CC ChEBI:CHEBI:137009, ChEBI:CHEBI:137017;
CC Evidence={ECO:0000269|PubMed:21801852, ECO:0000269|PubMed:25596343};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53185;
CC Evidence={ECO:0000269|PubMed:25596343};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-(4Z,7Z,10Z,13Z,16Z,19Z)-docosahexaenoyl-sn-glycero-3-
CC phosphoethanolamine = H(+) + N-(4Z,7Z,10Z,13Z,16Z,19Z)-
CC docosahexaenoyl ethanolamine + sn-glycerol 3-phosphate;
CC Xref=Rhea:RHEA:45444, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57597, ChEBI:CHEBI:85250, ChEBI:CHEBI:85252;
CC Evidence={ECO:0000269|PubMed:18227059};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45445;
CC Evidence={ECO:0000269|PubMed:18227059};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-eicosanoyl-sn-glycero-3-phosphoethanolamine = H(+) +
CC N-eicosanoyl ethanolamine + sn-glycerol 3-phosphate;
CC Xref=Rhea:RHEA:45440, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57597, ChEBI:CHEBI:85228, ChEBI:CHEBI:85253;
CC Evidence={ECO:0000269|PubMed:18227059};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45441;
CC Evidence={ECO:0000269|PubMed:18227059};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-hexadecanoyl-sn-glycero-3-phosphoethanolamine = H(+) +
CC N-hexadecanoylethanolamine + sn-glycerol 3-phosphate;
CC Xref=Rhea:RHEA:45436, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57597, ChEBI:CHEBI:71464, ChEBI:CHEBI:85226;
CC Evidence={ECO:0000269|PubMed:18227059, ECO:0000269|PubMed:21801852,
CC ECO:0000269|PubMed:25596343};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45437;
CC Evidence={ECO:0000269|PubMed:18227059};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-(9Z-octadecenoyl)-sn-glycero-3-phosphoethanolamine =
CC H(+) + N-(9Z-octadecenoyl) ethanolamine + sn-glycerol 3-phosphate;
CC Xref=Rhea:RHEA:45432, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57597, ChEBI:CHEBI:71466, ChEBI:CHEBI:85229;
CC Evidence={ECO:0000269|PubMed:18227059};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45433;
CC Evidence={ECO:0000269|PubMed:18227059};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-
CC phosphoethanolamine = H(+) + N-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-
CC ethanolamine + sn-glycerol 3-phosphate; Xref=Rhea:RHEA:45428,
CC ChEBI:CHEBI:2700, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57597, ChEBI:CHEBI:85230;
CC Evidence={ECO:0000269|PubMed:18227059};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45429;
CC Evidence={ECO:0000269|PubMed:18227059};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q9JL55};
CC -!- ACTIVITY REGULATION: Inhibited by EDTA, calcium chloride, and zinc
CC chloride (PubMed:18227059, PubMed:25596343). Enhanced by magnesium
CC chloride (PubMed:18227059, PubMed:25596343). Glycerophosphodiester
CC phosphodiesterase activity can be modulated by G-protein signaling
CC pathways (By similarity). {ECO:0000250|UniProtKB:Q9JL55,
CC ECO:0000269|PubMed:18227059, ECO:0000269|PubMed:25596343}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7.4. {ECO:0000269|PubMed:18227059,
CC ECO:0000269|PubMed:25596343};
CC -!- SUBUNIT: Interacts with PRAF2 (By similarity). Interacts with RGS16 (By
CC similarity). {ECO:0000250|UniProtKB:Q9JL55,
CC ECO:0000250|UniProtKB:Q9NZC3}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18227059};
CC Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle membrane
CC {ECO:0000250|UniProtKB:Q9JL55}; Multi-pass membrane protein
CC {ECO:0000255}. Note=Perinuclear vesicles and cell membrane.
CC {ECO:0000250|UniProtKB:Q9JL55}.
CC -!- TISSUE SPECIFICITY: Widely expressed (PubMed:10760272). Highly
CC expressed in the brain and spinal cord, followed by kidney, liver, and
CC testis. In contrast, little or no expression is detected in the heart
CC or spleen (PubMed:18227059). {ECO:0000269|PubMed:10760272,
CC ECO:0000269|PubMed:18227059}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:18227059}.
CC -!- SIMILARITY: Belongs to the glycerophosphoryl diester phosphodiesterase
CC family. {ECO:0000305}.
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DR EMBL; AF212860; AAF65232.1; -; mRNA.
DR EMBL; AK005361; BAB23975.1; -; mRNA.
DR EMBL; AK150807; BAE29870.1; -; mRNA.
DR EMBL; BC003902; AAH03902.1; -; mRNA.
DR CCDS; CCDS21774.1; -.
DR RefSeq; NP_062526.1; NM_019580.4.
DR AlphaFoldDB; Q9JL56; -.
DR SMR; Q9JL56; -.
DR STRING; 10090.ENSMUSP00000046371; -.
DR SwissLipids; SLP:000001124; -.
DR GlyConnect; 2355; 6 N-Linked glycans (2 sites).
DR GlyGen; Q9JL56; 2 sites, 6 N-linked glycans (2 sites).
DR iPTMnet; Q9JL56; -.
DR PhosphoSitePlus; Q9JL56; -.
DR SwissPalm; Q9JL56; -.
DR EPD; Q9JL56; -.
DR jPOST; Q9JL56; -.
DR MaxQB; Q9JL56; -.
DR PaxDb; Q9JL56; -.
DR PeptideAtlas; Q9JL56; -.
DR PRIDE; Q9JL56; -.
DR ProteomicsDB; 267427; -.
DR Antibodypedia; 25375; 170 antibodies from 24 providers.
DR DNASU; 56209; -.
DR Ensembl; ENSMUST00000038791; ENSMUSP00000046371; ENSMUSG00000033917.
DR GeneID; 56209; -.
DR KEGG; mmu:56209; -.
DR UCSC; uc009jki.1; mouse.
DR CTD; 51573; -.
DR MGI; MGI:1891827; Gde1.
DR VEuPathDB; HostDB:ENSMUSG00000033917; -.
DR eggNOG; KOG2258; Eukaryota.
DR GeneTree; ENSGT00510000047820; -.
DR HOGENOM; CLU_030006_2_1_1; -.
DR InParanoid; Q9JL56; -.
DR OMA; KHHWMTL; -.
DR OrthoDB; 1218115at2759; -.
DR PhylomeDB; Q9JL56; -.
DR TreeFam; TF313692; -.
DR Reactome; R-MMU-6814848; Glycerophospholipid catabolism.
DR BioGRID-ORCS; 56209; 2 hits in 75 CRISPR screens.
DR ChiTaRS; Gde1; mouse.
DR PRO; PR:Q9JL56; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q9JL56; protein.
DR Bgee; ENSMUSG00000033917; Expressed in epithelium of stomach and 263 other tissues.
DR ExpressionAtlas; Q9JL56; baseline and differential.
DR Genevisible; Q9JL56; MM.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; ISO:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:MGI.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; IMP:UniProtKB.
DR GO; GO:0008889; F:glycerophosphodiester phosphodiesterase activity; IMP:UniProtKB.
DR GO; GO:0047395; F:glycerophosphoinositol glycerophosphodiesterase activity; IDA:MGI.
DR GO; GO:0004622; F:lysophospholipase activity; IDA:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008081; F:phosphoric diester hydrolase activity; IDA:MGI.
DR GO; GO:0006580; P:ethanolamine metabolic process; IMP:UniProtKB.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISO:MGI.
DR GO; GO:0070291; P:N-acylethanolamine metabolic process; IDA:MGI.
DR GO; GO:0006644; P:phospholipid metabolic process; IDA:MGI.
DR Gene3D; 3.20.20.190; -; 1.
DR InterPro; IPR030395; GP_PDE_dom.
DR InterPro; IPR017946; PLC-like_Pdiesterase_TIM-brl.
DR Pfam; PF03009; GDPD; 1.
DR SUPFAM; SSF51695; SSF51695; 1.
DR PROSITE; PS51704; GP_PDE; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cytoplasmic vesicle; Glycoprotein; Hydrolase;
KW Lipid metabolism; Magnesium; Membrane; Metal-binding; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..331
FT /note="Glycerophosphodiester phosphodiesterase 1"
FT /id="PRO_0000251945"
FT TOPO_DOM 1..3
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 4..24
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 25..248
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 249..269
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 270..331
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 65..331
FT /note="GP-PDE"
FT BINDING 97
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255"
FT BINDING 99
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255"
FT BINDING 174
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255"
FT CARBOHYD 168
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 102
FT /note="F -> L (in Ref. 2; BAE29870)"
FT /evidence="ECO:0000305"
SQ 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
