GDPD1_MOUSE
ID GDPD1_MOUSE Reviewed; 314 AA.
AC Q9CRY7; Q9CT14; Q9D4X7;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Lysophospholipase D GDPD1 {ECO:0000305};
DE EC=3.1.4.- {ECO:0000269|PubMed:25596343, ECO:0000269|PubMed:27637550};
DE AltName: Full=Glycerophosphodiester phosphodiesterase 4 {ECO:0000303|PubMed:25528375};
DE AltName: Full=Glycerophosphodiester phosphodiesterase domain-containing protein 1;
GN Name=Gdpd1 {ECO:0000312|MGI:MGI:1913819};
GN Synonyms=Gde4 {ECO:0000303|PubMed:25528375};
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 [LARGE SCALE MRNA].
RC STRAIN=BALB/cJ, and C57BL/6J; TISSUE=Embryo, Embryonic head, and Testis;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Lung, Pancreas, Spleen, and Testis;
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 [5]
RP TISSUE SPECIFICITY, CATALYTIC ACTIVITY, FUNCTION, SUBCELLULAR LOCATION, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
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).
RN [6]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, INDUCTION, AND FUNCTION.
RX PubMed=25528375; DOI=10.1074/jbc.m114.614537;
RA Ohshima N., Kudo T., Yamashita Y., Mariggio S., Araki M., Honda A.,
RA Nagano T., Isaji C., Kato N., Corda D., Izumi T., Yanaka N.;
RT "New members of the mammalian glycerophosphodiester phosphodiesterase
RT family: GDE4 and GDE7 produce lysophosphatidic acid by lysophospholipase D
RT activity.";
RL J. Biol. Chem. 290:4260-4271(2015).
RN [7]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=27637550; DOI=10.1016/j.bbalip.2016.09.008;
RA Rahman I.A., Tsuboi K., Hussain Z., Yamashita R., Okamoto Y., Uyama T.,
RA Yamazaki N., Tanaka T., Tokumura A., Ueda N.;
RT "Calcium-dependent generation of N-acylethanolamines and lysophosphatidic
RT acids by glycerophosphodiesterase GDE7.";
RL Biochim. Biophys. Acta 1861:1881-1892(2016).
CC -!- FUNCTION: Hydrolyzes lysoglycerophospholipids to produce
CC lysophosphatidic acid (LPA) and the corresponding amines
CC (PubMed:25528375, PubMed:25596343, PubMed:27637550). Shows a preference
CC for 1-O-alkyl-sn-glycero-3-phosphocholine (lyso-PAF),
CC lysophosphatidylethanolamine (lyso-PE) and lysophosphatidylcholine
CC (lyso-PC) (PubMed:25528375, PubMed:25596343, PubMed:27637550). May be
CC involved in bioactive N-acylethanolamine biosynthesis from both N-acyl-
CC lysoplasmenylethanolamin (N-acyl-lysoPlsEt) and N-acyl-
CC lysophosphatidylethanolamin (N-acyl-lysoPE) (PubMed:25596343,
CC PubMed:27637550). In addition, hydrolyzes glycerophospho-N-
CC acylethanolamine to N-acylethanolamine (PubMed:25596343,
CC PubMed:27637550). Does not display glycerophosphodiester
CC phosphodiesterase activity, since it cannot hydrolyze either
CC glycerophosphoinositol or glycerophosphocholine (PubMed:25528375).
CC {ECO:0000269|PubMed:25528375, ECO:0000269|PubMed:25596343,
CC ECO:0000269|PubMed:27637550}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-sn-glycero-3-phosphocholine + H2O = 1-
CC hexadecanoyl-sn-glycero-3-phosphate + choline + H(+);
CC Xref=Rhea:RHEA:38975, ChEBI:CHEBI:15354, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57518, ChEBI:CHEBI:72998;
CC Evidence={ECO:0000269|PubMed:25528375, ECO:0000269|PubMed:25596343};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38976;
CC Evidence={ECO:0000269|PubMed:25528375};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-sn-glycero-3-phosphoethanolamine + H2O = 1-
CC hexadecanoyl-sn-glycero-3-phosphate + ethanolamine + H(+);
CC Xref=Rhea:RHEA:53172, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57518, ChEBI:CHEBI:57603, ChEBI:CHEBI:73004;
CC Evidence={ECO:0000269|PubMed:25596343};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53173;
CC Evidence={ECO:0000305|PubMed:25596343};
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:25596343, ECO:0000269|PubMed:27637550};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45437;
CC Evidence={ECO:0000305|PubMed:25596343, ECO:0000305|PubMed:27637550};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-1-(9Z-octadecenoyl)-
CC sn-glycero-3-phosphoethanolamine = 1-(9Z-octadecenoyl)-sn-glycero-3-
CC phosphate + H(+) + N-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-ethanolamine;
CC Xref=Rhea:RHEA:45544, ChEBI:CHEBI:2700, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:74544, ChEBI:CHEBI:85223;
CC Evidence={ECO:0000269|PubMed:27637550};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45545;
CC Evidence={ECO:0000305|PubMed:27637550};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N,1-di-(9Z-octadecenoyl)-sn-glycero-3-
CC phosphoethanolamine = 1-(9Z-octadecenoyl)-sn-glycero-3-phosphate +
CC H(+) + N-(9Z-octadecenoyl) ethanolamine; Xref=Rhea:RHEA:56460,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:71466,
CC ChEBI:CHEBI:74544, ChEBI:CHEBI:85222;
CC Evidence={ECO:0000269|PubMed:27637550};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56461;
CC Evidence={ECO:0000305|PubMed:27637550};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N-hexadecanoyl-1-(9Z-octadecenoyl)-sn-glycero-3-
CC phosphoethanolamine = 1-(9Z-octadecenoyl)-sn-glycero-3-phosphate +
CC H(+) + N-hexadecanoylethanolamine; Xref=Rhea:RHEA:53168,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:71464,
CC ChEBI:CHEBI:74544, ChEBI:CHEBI:85217;
CC Evidence={ECO:0000269|PubMed:25596343, ECO:0000269|PubMed:27637550};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53169;
CC Evidence={ECO:0000269|PubMed:25596343, ECO:0000269|PubMed:27637550};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-O-alkyl-sn-glycero-3-phosphocholine + H2O = 1-O-alkyl-sn-
CC glycero-3-phosphate + choline + H(+); Xref=Rhea:RHEA:39927,
CC ChEBI:CHEBI:15354, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30909, ChEBI:CHEBI:58014;
CC Evidence={ECO:0000269|PubMed:25528375};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39928;
CC Evidence={ECO:0000305|PubMed:25528375};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-O-hexadecyl-sn-glycero-3-phosphocholine + H2O = 1-O-
CC hexadecyl-sn-glycero-3-phosphate + choline + H(+);
CC Xref=Rhea:RHEA:41143, ChEBI:CHEBI:15354, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:64496, ChEBI:CHEBI:77580;
CC Evidence={ECO:0000269|PubMed:25596343};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41144;
CC Evidence={ECO:0000305|PubMed:25596343};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + H2O = 1-(9Z-
CC octadecenoyl)-sn-glycero-3-phosphate + choline + H(+);
CC Xref=Rhea:RHEA:38915, ChEBI:CHEBI:15354, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:28610, ChEBI:CHEBI:74544;
CC Evidence={ECO:0000269|PubMed:25596343};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38916;
CC Evidence={ECO:0000305|PubMed:25596343};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N,1-dihexadecanoyl-sn-glycero-3-phosphoethanolamine = 1-
CC hexadecanoyl-sn-glycero-3-phosphate + H(+) + N-
CC hexadecanoylethanolamine; Xref=Rhea:RHEA:45592, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57518, ChEBI:CHEBI:71464,
CC ChEBI:CHEBI:85335; Evidence={ECO:0000269|PubMed:25596343};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45593;
CC Evidence={ECO:0000305|PubMed:25596343};
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:25596343, ECO:0000269|PubMed:27637550};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53185;
CC Evidence={ECO:0000305|PubMed:25596343, ECO:0000305|PubMed:27637550};
CC -!- ACTIVITY REGULATION: Lysophospholipase D activity is increased by
CC magnesium and manganese and inhibited by calcium in a concentration
CC dependent manner (By similarity). Loss of lysophospholipase D activity
CC by addition of EDTA (PubMed:25596343). {ECO:0000250|UniProtKB:Q8N9F7,
CC ECO:0000269|PubMed:25596343}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.0 mM for lysophosphatidylcholine (lyso-PC)
CC {ECO:0000269|PubMed:25528375};
CC KM=0.32 mM for 1-O-alkyl-sn-glycero-3-phosphocholine (lyso-PAF)
CC {ECO:0000269|PubMed:25528375};
CC Note=kcat is 0.032 sec(-1) with lysophosphatidylcholine as substrate.
CC kcat is 0.077 sec(-1) with 1-O-alkyl-sn-glycero-3-phosphocholine as
CC substrate. {ECO:0000269|PubMed:25528375};
CC pH dependence:
CC Optimum pH is 7.4. {ECO:0000269|PubMed:25596343};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8N9F7}.
CC Membrane {ECO:0000269|PubMed:25596343}; Multi-pass membrane protein
CC {ECO:0000255}. Cytoplasm, perinuclear region
CC {ECO:0000269|PubMed:25596343}. Endoplasmic reticulum
CC {ECO:0000250|UniProtKB:Q8N9F7}. Note=Concentrated at the perinuclear
CC region and the cell periphery. {ECO:0000250|UniProtKB:Q8N9F7}.
CC -!- TISSUE SPECIFICITY: Widely expressed (PubMed:25528375,
CC PubMed:25596343). {ECO:0000269|PubMed:25528375,
CC ECO:0000269|PubMed:25596343}.
CC -!- INDUCTION: Up-regulated in white adipose tissue of obese mice.
CC {ECO:0000269|PubMed:25528375}.
CC -!- SIMILARITY: Belongs to the glycerophosphoryl diester phosphodiesterase
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB27650.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK011487; BAB27650.1; ALT_FRAME; mRNA.
DR EMBL; AK013864; BAB29022.1; -; mRNA.
DR EMBL; AK016023; BAB30083.1; -; mRNA.
DR EMBL; AK167812; BAE39839.1; -; mRNA.
DR EMBL; AL713917; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC016541; AAH16541.1; -; mRNA.
DR CCDS; CCDS25206.1; -.
DR RefSeq; NP_079914.1; NM_025638.2.
DR AlphaFoldDB; Q9CRY7; -.
DR SMR; Q9CRY7; -.
DR BioGRID; 211560; 2.
DR STRING; 10090.ENSMUSP00000020804; -.
DR SwissLipids; SLP:000001717; -.
DR PhosphoSitePlus; Q9CRY7; -.
DR EPD; Q9CRY7; -.
DR MaxQB; Q9CRY7; -.
DR PaxDb; Q9CRY7; -.
DR PeptideAtlas; Q9CRY7; -.
DR PRIDE; Q9CRY7; -.
DR ProteomicsDB; 271208; -.
DR Antibodypedia; 66215; 115 antibodies from 15 providers.
DR DNASU; 66569; -.
DR Ensembl; ENSMUST00000020804; ENSMUSP00000020804; ENSMUSG00000061666.
DR GeneID; 66569; -.
DR KEGG; mmu:66569; -.
DR UCSC; uc007kte.2; mouse.
DR CTD; 284161; -.
DR MGI; MGI:1913819; Gdpd1.
DR VEuPathDB; HostDB:ENSMUSG00000061666; -.
DR eggNOG; KOG2258; Eukaryota.
DR GeneTree; ENSGT00940000156673; -.
DR HOGENOM; CLU_030006_5_0_1; -.
DR InParanoid; Q9CRY7; -.
DR OMA; AFHHAVN; -.
DR OrthoDB; 1143305at2759; -.
DR PhylomeDB; Q9CRY7; -.
DR TreeFam; TF328545; -.
DR BRENDA; 3.1.4.39; 3474.
DR BioGRID-ORCS; 66569; 1 hit in 74 CRISPR screens.
DR ChiTaRS; Gdpd1; mouse.
DR PRO; PR:Q9CRY7; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q9CRY7; protein.
DR Bgee; ENSMUSG00000061666; Expressed in primary oocyte and 264 other tissues.
DR Genevisible; Q9CRY7; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
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:0046475; P:glycerophospholipid catabolic process; IBA:GO_Central.
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 Cytoplasm; Endoplasmic reticulum; Hydrolase; Lipid metabolism; Membrane;
KW Metal-binding; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..314
FT /note="Lysophospholipase D GDPD1"
FT /id="PRO_0000251932"
FT TOPO_DOM 1..3
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 4..24
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 25..195
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 196..216
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 217..314
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 40..309
FT /note="GP-PDE"
FT BINDING 72
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255"
FT BINDING 74
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255"
FT BINDING 87
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000255"
FT CONFLICT 109
FT /note="L -> I (in Ref. 1; BAB27650)"
FT /evidence="ECO:0000305"
FT CONFLICT 296
FT /note="G -> R (in Ref. 1; BAB30083)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 314 AA; 35867 MW; AEDB140CB872A00C CRC64;
MSSTAAFCLL STLGGYLVTS FLLLKYPALL HQRKKQRFLS RHISHRGGAG ENLENTMAAF
QHAVTIGTDM LELDCHITKD EQVVVSHDAN LKRSTGVNVN VSDLKYCELP PYLCKLDVPF
QRACKCEGKD TRIPLLKEVF EAFPETPINI DIKVNNNVLI KKVSELVKQY KREHLTVWGN
ANSEIVDKCY KENSDIPILF SLQRVLLILG LFFTGLLPFV PIREQFFEIP MPSIILKLKE
PHTISKGHKF LIWLSDTLLM RKALFDHLTA RGIQVYVWVL NEEYEYKRAF DLGATGVMTD
YPTKLKDFLN NFSA
