GDPD1_RAT
ID GDPD1_RAT Reviewed; 314 AA.
AC Q0VGK4;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Lysophospholipase D GDPD1 {ECO:0000305};
DE EC=3.1.4.- {ECO:0000250|UniProtKB:Q9CRY7};
DE AltName: Full=Glycerophosphodiester phosphodiesterase 4 {ECO:0000250|UniProtKB:Q8N9F7};
DE AltName: Full=Glycerophosphodiester phosphodiesterase domain-containing protein 1;
GN Name=Gdpd1 {ECO:0000312|RGD:1311813};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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).
CC -!- FUNCTION: Hydrolyzes lysoglycerophospholipids to produce
CC lysophosphatidic acid (LPA) and the corresponding amines. Shows a
CC preference for 1-O-alkyl-sn-glycero-3-phosphocholine (lyso-PAF),
CC lysophosphatidylethanolamine (lyso-PE) and lysophosphatidylcholine
CC (lyso-PC). May be involved in bioactive N-acylethanolamine biosynthesis
CC from both N-acyl-lysoplasmenylethanolamin (N-acyl-lysoPlsEt) and N-
CC acyl-lysophosphatidylethanolamin (N-acyl-lysoPE). In addition,
CC hydrolyzes glycerophospho-N-acylethanolamine to N-acylethanolamine.
CC Does not display glycerophosphodiester phosphodiesterase activity,
CC since it cannot hydrolyze either glycerophosphoinositol or
CC glycerophosphocholine. {ECO:0000250|UniProtKB:Q9CRY7}.
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=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=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:0000250|UniProtKB:Q9CRY7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45437;
CC Evidence={ECO:0000250|UniProtKB:Q9CRY7};
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:0000250|UniProtKB:Q9CRY7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45545;
CC Evidence={ECO:0000250|UniProtKB:Q9CRY7};
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:0000250|UniProtKB:Q9CRY7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56461;
CC Evidence={ECO:0000250|UniProtKB:Q9CRY7};
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:0000250|UniProtKB:Q9CRY7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53169;
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 -!- 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:0000250|UniProtKB:Q9CRY7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53185;
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 (By similarity). Loss of lysophospholipase D activity
CC by addition of EDTA (By similarity). {ECO:0000250|UniProtKB:Q8N9F7,
CC ECO:0000250|UniProtKB:Q9CRY7}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8N9F7}.
CC Membrane {ECO:0000250|UniProtKB:Q8N9F7}; Multi-pass membrane protein
CC {ECO:0000255}. Cytoplasm, perinuclear region
CC {ECO:0000250|UniProtKB:Q8N9F7}. Endoplasmic reticulum
CC {ECO:0000250|UniProtKB:Q8N9F7}. Note=Concentrated at the perinuclear
CC region and the cell periphery. {ECO:0000250|UniProtKB:Q8N9F7}.
CC -!- SIMILARITY: Belongs to the glycerophosphoryl diester phosphodiesterase
CC family. {ECO:0000305}.
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DR EMBL; BC105620; AAI05621.1; -; mRNA.
DR RefSeq; NP_001037703.1; NM_001044238.1.
DR AlphaFoldDB; Q0VGK4; -.
DR SMR; Q0VGK4; -.
DR STRING; 10116.ENSRNOP00000048572; -.
DR iPTMnet; Q0VGK4; -.
DR PhosphoSitePlus; Q0VGK4; -.
DR jPOST; Q0VGK4; -.
DR PaxDb; Q0VGK4; -.
DR PRIDE; Q0VGK4; -.
DR Ensembl; ENSRNOT00000079311; ENSRNOP00000074578; ENSRNOG00000060561.
DR GeneID; 303407; -.
DR KEGG; rno:303407; -.
DR CTD; 284161; -.
DR RGD; 1311813; Gdpd1.
DR eggNOG; KOG2258; Eukaryota.
DR GeneTree; ENSGT00940000156673; -.
DR InParanoid; Q0VGK4; -.
DR OrthoDB; 1143305at2759; -.
DR PhylomeDB; Q0VGK4; -.
DR TreeFam; TF328545; -.
DR PRO; PR:Q0VGK4; -.
DR Proteomes; UP000002494; Chromosome 10.
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; ISO:RGD.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
DR GO; GO:0004622; F:lysophospholipase activity; ISO:RGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008081; F:phosphoric diester hydrolase activity; ISS:UniProtKB.
DR GO; GO:0046475; P:glycerophospholipid catabolic process; IBA:GO_Central.
DR GO; GO:0070291; P:N-acylethanolamine metabolic process; ISS:UniProtKB.
DR GO; GO:0006644; P:phospholipid metabolic process; ISO:RGD.
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 2: Evidence at transcript 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_0000251933"
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"
SQ SEQUENCE 314 AA; 35811 MW; E79B6AA1599F96DD CRC64;
MSSTAAFCLL STLGGYLVTS FLLLKYPALL HQRKKQRFLS RHISHRGGAG ENLENTMAAF
QHAVTIGTDM LELDCHITKD EQVVVSHDAN LKRSTGVNVN VSDLKYCELP PYLCKLDVPF
QRACKCEGTD TRIPLLKEVF EAFPETPINI DIKVNNNVLI QKVSELVKQY KREHLTVWGN
ASSEIVDKCY KENSDIPILF SLQRVLLILG LFFTGLLPFV PIREQFFEIP MPSIILKLKE
PHIISKGHKF LIWLSDTLLM RKALFDHLTA RGIQVYIWVL NEEHEYKRAF DLGATGVMTD
YPTKLKEFLN NMSA
