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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
 
 
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