ID GDPD1_HUMAN Reviewed; 314 AA. AC Q8N9F7; A8W735; Q56VR1; Q8N4E3; DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot. DT 03-OCT-2006, sequence version 2. DT 10-FEB-2021, entry version 134. 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:18991142}; DE AltName: Full=Glycerophosphodiester phosphodiesterase domain-containing protein 1; GN Name=GDPD1 {ECO:0000312|HGNC:HGNC:20883}; GN Synonyms=GDE4 {ECO:0000303|PubMed:18991142}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), AND TISSUE SPECIFICITY. RC TISSUE=Fetal brain; RX PubMed=16147865; DOI=10.1080/10425170400020373; RA Wu M., Gu S., Xu J., Zou X., Zheng H., Jin Z., Xie Y., Ji C., Mao Y.; RT "A novel splice variant of human gene NPL, mainly expressed in human liver, RT kidney and peripheral blood leukocyte."; RL DNA Seq. 16:137-142(2005). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, AND RP 3D-STRUCTURE MODELING. RX PubMed=18991142; DOI=10.1080/09687680802537605; RA Chang P.A., Shao H.B., Long D.X., Sun Q., Wu Y.J.; RT "Isolation, characterization and molecular 3D model of human GDE4, a novel RT membrane protein containing glycerophosphodiester phosphodiesterase RT domain."; RL Mol. Membr. Biol. 25:557-566(2008). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Brain; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16625196; DOI=10.1038/nature04689; RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.; RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the RT human lineage."; RL Nature 440:1045-1049(2006). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Brain; 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 [7] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [8] RP FUNCTION, AND CATALYTIC ACTIVITY. 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 [9] RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, ACTIVITY REGULATION, RP AND TISSUE SPECIFICITY. 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:27637550, PubMed:25596343). Shows a preference for 1-O-alkyl- CC sn-glycero-3-phosphocholine (lyso-PAF), lysophosphatidylethanolamine CC (lyso-PE) and lysophosphatidylcholine (lyso-PC) (PubMed:27637550, CC PubMed:25596343). May be involved in bioactive N-acylethanolamine CC biosynthesis from both N-acyl-lysoplasmenylethanolamin (N-acyl- CC lysoPlsEt) and N-acyl-lysophosphatidylethanolamin (N-acyl-lysoPE) CC (PubMed:27637550, PubMed:25596343). In addition, hydrolyzes CC glycerophospho-N-acylethanolamine to N-acylethanolamine CC (PubMed:27637550). Does not display glycerophosphodiester CC phosphodiesterase activity, since it cannot hydrolyze either CC glycerophosphoinositol or glycerophosphocholine (By similarity). CC {ECO:0000250|UniProtKB:Q9CRY7, ECO:0000269|PubMed:25596343, CC 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:0000250|UniProtKB:Q9CRY7}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39928; CC Evidence={ECO:0000250|UniProtKB:Q9CRY7}; 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:0000250|UniProtKB:Q9CRY7}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38976; CC Evidence={ECO:0000250|UniProtKB:Q9CRY7}; 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:27637550}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45437; CC Evidence={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:27637550}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53169; CC Evidence={ECO:0000269|PubMed:27637550}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1-(1Z-octadecenyl)-sn-glycero-3-phospho-(N-hexadecanoyl)- CC ethanolamine + H2O = 1-(1Z-octadecenyl)-sn-glycero-3-phosphate + H(+) CC + 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:27637550}; 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:0000250|UniProtKB:Q9CRY7}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53173; CC Evidence={ECO:0000250|UniProtKB:Q9CRY7}; 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:0000250|UniProtKB:Q9CRY7}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41144; CC Evidence={ECO:0000250|UniProtKB:Q9CRY7}; CC -!- CATALYTIC ACTIVITY: CC Reaction=a 1-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + H2O = 1- CC (9Z-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:0000250|UniProtKB:Q9CRY7}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38916; CC Evidence={ECO:0000250|UniProtKB:Q9CRY7}; 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:0000250|UniProtKB:Q9CRY7}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45593; CC Evidence={ECO:0000250|UniProtKB:Q9CRY7}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1-(1Z-octadecenyl)-sn-glycero-3-phospho-(N-5Z,8Z,11Z,14Z- CC eicosatetraenoyl)-ethanolamine + H2O = 1-(1Z-octadecenyl)-sn-glycero- CC 3-phosphate + H(+) + N-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-ethanolamine; CC Xref=Rhea:RHEA:53192, ChEBI:CHEBI:2700, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:137016, ChEBI:CHEBI:137017; CC Evidence={ECO:0000250|UniProtKB:Q9CRY7}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53193; CC Evidence={ECO:0000250|UniProtKB:Q9CRY7}; CC -!- CATALYTIC ACTIVITY: CC Reaction=1-(1Z-octadecenyl)-sn-glycero-3-phospho-(N-9Z-octadecenoyl)- CC ethanolamine + H2O = 1-(1Z-octadecenyl)-sn-glycero-3-phosphate + H(+) CC + 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:0000250|UniProtKB:Q9CRY7}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53189; CC Evidence={ECO:0000250|UniProtKB:Q9CRY7}; CC -!- ACTIVITY REGULATION: Lysophospholipase D activity is increased by CC magnesium and manganese and inhibited by calcium in a concentration CC dependent manner (PubMed:27637550). Loss of lysophospholipase D CC activity by addition of EDTA (By similarity). CC {ECO:0000250|UniProtKB:Q9CRY7, ECO:0000269|PubMed:27637550}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18991142}. Membrane CC {ECO:0000305}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm, CC perinuclear region {ECO:0000269|PubMed:18991142}. Endoplasmic reticulum CC {ECO:0000269|PubMed:27637550}. Note=Concentrated at the perinuclear CC region and the cell periphery (PubMed:18991142). CC {ECO:0000269|PubMed:18991142}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=Q8N9F7-1; Sequence=Displayed; CC Name=2; CC IsoId=Q8N9F7-2; Sequence=VSP_020807, VSP_020808; CC Name=3; Synonyms=UGPQ; CC IsoId=Q8N9F7-3; Sequence=VSP_020806; CC -!- TISSUE SPECIFICITY: Widely expressed with high expression level in CC testis. {ECO:0000269|PubMed:16147865, ECO:0000269|PubMed:27637550}. CC -!- SIMILARITY: Belongs to the glycerophosphoryl diester phosphodiesterase CC family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AY271346; AAQ01751.1; -; mRNA. DR EMBL; EU192951; ABW73991.1; -; mRNA. DR EMBL; AK094770; BAC04419.1; -; mRNA. DR EMBL; AC091059; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC099850; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471109; EAW94412.1; -; Genomic_DNA. DR EMBL; BC034432; AAH34432.1; -; mRNA. DR CCDS; CCDS11616.1; -. [Q8N9F7-1] DR CCDS; CCDS58583.1; -. [Q8N9F7-3] DR CCDS; CCDS58584.1; -. [Q8N9F7-2] DR RefSeq; NP_001159465.1; NM_001165993.1. [Q8N9F7-3] DR RefSeq; NP_001159466.1; NM_001165994.1. [Q8N9F7-2] DR RefSeq; NP_872375.2; NM_182569.3. [Q8N9F7-1] DR SMR; Q8N9F7; -. DR BioGRID; 129776; 29. DR IntAct; Q8N9F7; 29. DR STRING; 9606.ENSP00000284116; -. DR SwissLipids; SLP:000001718; -. DR iPTMnet; Q8N9F7; -. DR PhosphoSitePlus; Q8N9F7; -. DR BioMuta; GDPD1; -. DR DMDM; 115502208; -. DR EPD; Q8N9F7; -. DR jPOST; Q8N9F7; -. DR MassIVE; Q8N9F7; -. DR MaxQB; Q8N9F7; -. DR PaxDb; Q8N9F7; -. DR PeptideAtlas; Q8N9F7; -. DR PRIDE; Q8N9F7; -. DR ProteomicsDB; 72526; -. [Q8N9F7-1] DR ProteomicsDB; 72527; -. [Q8N9F7-2] DR ProteomicsDB; 72528; -. [Q8N9F7-3] DR TopDownProteomics; Q8N9F7-2; -. [Q8N9F7-2] DR Antibodypedia; 66215; 113 antibodies. DR Ensembl; ENST00000284116; ENSP00000284116; ENSG00000153982. [Q8N9F7-1] DR Ensembl; ENST00000581140; ENSP00000463273; ENSG00000153982. [Q8N9F7-3] DR Ensembl; ENST00000581276; ENSP00000464690; ENSG00000153982. [Q8N9F7-2] DR GeneID; 284161; -. DR KEGG; hsa:284161; -. DR UCSC; uc002ixj.4; human. [Q8N9F7-1] DR CTD; 284161; -. DR GeneCards; GDPD1; -. DR HGNC; HGNC:20883; GDPD1. DR HPA; ENSG00000153982; Tissue enhanced (brain). DR MIM; 616317; gene. DR neXtProt; NX_Q8N9F7; -. DR OpenTargets; ENSG00000153982; -. DR PharmGKB; PA134879258; -. DR VEuPathDB; HostDB:ENSG00000153982.10; -. DR eggNOG; KOG2258; Eukaryota. DR GeneTree; ENSGT00940000156673; -. DR HOGENOM; CLU_030006_5_0_1; -. DR InParanoid; Q8N9F7; -. DR OMA; RVCVGSF; -. DR OrthoDB; 1143305at2759; -. DR PhylomeDB; Q8N9F7; -. DR TreeFam; TF328545; -. DR BRENDA; 3.1.4.46; 2681. DR PathwayCommons; Q8N9F7; -. DR Reactome; R-HSA-6814848; Glycerophospholipid catabolism. DR BioGRID-ORCS; 284161; 2 hits in 874 CRISPR screens. DR ChiTaRS; GDPD1; human. DR GenomeRNAi; 284161; -. DR Pharos; Q8N9F7; Tbio. DR PRO; PR:Q8N9F7; -. DR Proteomes; UP000005640; Chromosome 17. DR RNAct; Q8N9F7; protein. DR Bgee; ENSG00000153982; Expressed in primary visual cortex and 181 other tissues. DR ExpressionAtlas; Q8N9F7; baseline and differential. DR Genevisible; Q8N9F7; HS. DR GO; GO:0005783; C:endoplasmic reticulum; IMP: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; HDA:UniProtKB. DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB. DR GO; GO:0004622; F:lysophospholipase activity; IMP:MGI. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008081; F:phosphoric diester hydrolase activity; IMP:UniProtKB. DR GO; GO:0046475; P:glycerophospholipid catabolic process; IBA:GO_Central. DR GO; GO:0070291; P:N-acylethanolamine metabolic process; IMP:UniProtKB. DR GO; GO:0006644; P:phospholipid metabolic process; IBA:GO_Central. DR Gene3D; 3.20.20.190; -; 2. 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 Alternative splicing; Cytoplasm; Endoplasmic reticulum; Hydrolase; KW Membrane; Metal-binding; Reference proteome; Transmembrane; KW Transmembrane helix. FT CHAIN 1..314 FT /note="Lysophospholipase D GDPD1" FT /id="PRO_0000251931" 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 METAL 72 FT /note="Divalent metal cation" FT /evidence="ECO:0000255" FT METAL 74 FT /note="Divalent metal cation" FT /evidence="ECO:0000255" FT METAL 87 FT /note="Divalent metal cation" FT /evidence="ECO:0000255" FT VAR_SEQ 266..314 FT /note="DHLTARGIQVYIWVLNEEQEYKRAFDLGATGVMTDYPTKLRDFLHNFSA -> FT EPLHPASKRNFEGHCSYLVVSCYF (in isoform 3)" FT /evidence="ECO:0000303|PubMed:16147865" FT /id="VSP_020806" FT VAR_SEQ 276..290 FT /note="YIWVLNEEQEYKRAF -> SFWNDAFWKQHSSPV (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_020807" FT VAR_SEQ 291..314 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_020808" FT CONFLICT 70 FT /note="M -> T (in Ref. 3; BAC04419)" FT /evidence="ECO:0000305" SQ SEQUENCE 314 AA; 36167 MW; 8666D98E3A8084A9 CRC64; MSSTAAFYLL STLGGYLVTS FLLLKYPTLL HQRKKQRFLS KHISHRGGAG ENLENTMAAF QHAVKIGTDM LELDCHITKD EQVVVSHDEN LKRATGVNVN ISDLKYCELP PYLGKLDVSF QRACQCEGKD NRIPLLKEVF EAFPNTPINI DIKVNNNVLI KKVSELVKRY NREHLTVWGN ANYEIVEKCY KENSDIPILF SLQRVLLILG LFFTGLLPFV PIREQFFEIP MPSIILKLKE PHTMSRSQKF LIWLSDLLLM RKALFDHLTA RGIQVYIWVL NEEQEYKRAF DLGATGVMTD YPTKLRDFLH NFSA //