GDPD1_HUMAN
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 03-AUG-2022, entry version 140.
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-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: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=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: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-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:0000250|UniProtKB:Q9CRY7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53193;
CC Evidence={ECO:0000250|UniProtKB:Q9CRY7};
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: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}.
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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 AlphaFoldDB; Q8N9F7; -.
DR SMR; Q8N9F7; -.
DR BioGRID; 129776; 34.
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; 115 antibodies from 15 providers.
DR DNASU; 284161; -.
DR Ensembl; ENST00000284116.9; ENSP00000284116.4; ENSG00000153982.11. [Q8N9F7-1]
DR Ensembl; ENST00000581140.5; ENSP00000463273.1; ENSG00000153982.11. [Q8N9F7-3]
DR Ensembl; ENST00000581276.5; ENSP00000464690.1; ENSG00000153982.11. [Q8N9F7-2]
DR GeneID; 284161; -.
DR KEGG; hsa:284161; -.
DR MANE-Select; ENST00000284116.9; ENSP00000284116.4; NM_182569.4; NP_872375.2.
DR UCSC; uc002ixj.4; human. [Q8N9F7-1]
DR CTD; 284161; -.
DR GeneCards; GDPD1; -.
DR HGNC; HGNC:20883; GDPD1.
DR HPA; ENSG00000153982; Low tissue specificity.
DR MIM; 616317; gene.
DR neXtProt; NX_Q8N9F7; -.
DR OpenTargets; ENSG00000153982; -.
DR PharmGKB; PA134879258; -.
DR VEuPathDB; HostDB:ENSG00000153982; -.
DR eggNOG; KOG2258; Eukaryota.
DR GeneTree; ENSGT00940000156673; -.
DR HOGENOM; CLU_030006_5_0_1; -.
DR InParanoid; Q8N9F7; -.
DR OMA; AFHHAVN; -.
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 SignaLink; Q8N9F7; -.
DR BioGRID-ORCS; 284161; 7 hits in 1078 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 Brodmann (1909) area 23 and 149 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 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 Alternative splicing; Cytoplasm; Endoplasmic reticulum; Hydrolase;
KW Lipid metabolism; Membrane; Metal-binding; Reference proteome;
KW Transmembrane; 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 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 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
