GDE1_BOVIN
ID GDE1_BOVIN Reviewed; 331 AA.
AC Q3T0T0;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Glycerophosphodiester phosphodiesterase 1 {ECO:0000250|UniProtKB:Q9NZC3};
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:0000250|UniProtKB:Q9JL56};
DE AltName: Full=Membrane-interacting protein of RGS16 {ECO:0000250|UniProtKB:Q9JL56};
GN Name=GDE1 {ECO:0000250|UniProtKB:Q9JL56};
GN Synonyms=MIR16 {ECO:0000250|UniProtKB:Q9JL56};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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 (By
CC similarity). Hydrolyzes glycerophospho-N-acylethanolamines to N-
CC acylethanolamines in the brain and participates in bioactive N-
CC acylethanolamine biosynthesis such as anandamide (an endocannabinoid),
CC N-palmitoylethanolamine (an anti-inflammatory), and N-
CC oleoylethanolamine (an anorexic). In addition, has a lysophospholipase
CC D activity by hydrolyzing N-acyl-lysoplasmenylethanolamine (N-acyl-
CC lysoPlsEt) to N-acylethanolamine. However lysophospholipase D activity
CC is lower than glycerophosphodiester phosphodiesterase activity (By
CC similarity). Has little or no activity towards glycerophosphocholine
CC (By similarity). {ECO:0000250|UniProtKB:Q9JL55,
CC ECO:0000250|UniProtKB:Q9JL56}.
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:0000250|UniProtKB:Q9JL56};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53193;
CC Evidence={ECO:0000250|UniProtKB:Q9JL56};
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:Q9JL56};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53189;
CC Evidence={ECO:0000250|UniProtKB:Q9JL56};
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:Q9JL56};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53185;
CC Evidence={ECO:0000250|UniProtKB:Q9JL56};
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:0000250|UniProtKB:Q9JL56};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45445;
CC Evidence={ECO:0000250|UniProtKB:Q9JL56};
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:0000250|UniProtKB:Q9JL56};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45441;
CC Evidence={ECO:0000250|UniProtKB:Q9JL56};
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:Q9JL56};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45437;
CC Evidence={ECO:0000250|UniProtKB:Q9JL56};
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:0000250|UniProtKB:Q9JL56};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45433;
CC Evidence={ECO:0000250|UniProtKB:Q9JL56};
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:0000250|UniProtKB:Q9JL56};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45429;
CC Evidence={ECO:0000250|UniProtKB:Q9JL56};
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. Enhanced by magnesium chloride (By similarity).
CC Glycerophosphodiester phosphodiesterase activity can be modulated by G-
CC protein signaling pathways (By similarity).
CC {ECO:0000250|UniProtKB:Q9JL55, ECO:0000250|UniProtKB:Q9JL56}.
CC -!- SUBUNIT: Interacts with PRAF2 (By similarity). Interacts with RGS16 (By
CC similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q9JL55}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9JL55};
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 -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q9JL55}.
CC -!- SIMILARITY: Belongs to the glycerophosphoryl diester phosphodiesterase
CC family. {ECO:0000305}.
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DR EMBL; BC102273; AAI02274.1; -; mRNA.
DR RefSeq; NP_001029858.1; NM_001034686.2.
DR AlphaFoldDB; Q3T0T0; -.
DR SMR; Q3T0T0; -.
DR STRING; 9913.ENSBTAP00000002710; -.
DR PaxDb; Q3T0T0; -.
DR PRIDE; Q3T0T0; -.
DR Ensembl; ENSBTAT00000002710; ENSBTAP00000002710; ENSBTAG00000002101.
DR GeneID; 539978; -.
DR KEGG; bta:539978; -.
DR CTD; 51573; -.
DR VEuPathDB; HostDB:ENSBTAG00000002101; -.
DR VGNC; VGNC:29298; GDE1.
DR eggNOG; KOG2258; Eukaryota.
DR GeneTree; ENSGT00510000047820; -.
DR HOGENOM; CLU_030006_2_1_1; -.
DR InParanoid; Q3T0T0; -.
DR OMA; KHHWMTL; -.
DR OrthoDB; 1218115at2759; -.
DR TreeFam; TF313692; -.
DR Proteomes; UP000009136; Chromosome 25.
DR Bgee; ENSBTAG00000002101; Expressed in abomasum and 103 other tissues.
DR ExpressionAtlas; Q3T0T0; baseline and differential.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0008889; F:glycerophosphodiester phosphodiesterase activity; ISS:UniProtKB.
DR GO; GO:0047395; F:glycerophosphoinositol glycerophosphodiesterase activity; ISS:UniProtKB.
DR GO; GO:0004622; F:lysophospholipase activity; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006580; P:ethanolamine metabolic process; ISS:UniProtKB.
DR GO; GO:0070291; P:N-acylethanolamine metabolic process; ISS:UniProtKB.
DR GO; GO:0006644; P:phospholipid metabolic process; ISS: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 2: Evidence at transcript 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_0000251943"
FT TOPO_DOM 1..2
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 3..23
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 24..254
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 255..275
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 276..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 CARBOHYD 198
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 331 AA; 37653 MW; 852CAD36A3AF40D3 CRC64;
MWLWEEQGGL MGPFSFLLLV LLLLTRSPFN ACLFTGSLYL LLRLFSFEPV PSRRAMQVLK
PRDRVSAIAH RGGSHDAPEN TLAAIRQAAK NGAAGVELDL EFTADGIPVL MHDSTVDRTT
DGTGRLCDLT FEQIRKLNPA ANHRLRNDFP NEKIPTLREA VAECLNHNLT IFFDVKGHAY
KATDALKKVY MEFPKLYNNS IVCSFLPEVI YKMRQTDQNV VTALIHRPWS LSHTGDGKPR
FESFWKQSMF VALDILLDWS MHNILWYLCG VSAFLAQKDF ISPDYVKKWS AKGIQVVAWT
VNTFDEKSYY ESHLGSSYIT DSMLEDCTPE F
