ID H2SZF7_TAKRU Unreviewed; 332 AA.
AC H2SZF7;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 3.
DT 27-MAR-2024, entry version 64.
DE SubName: Full=Glycerophosphodiester phosphodiesterase domain containing 1 {ECO:0000313|Ensembl:ENSTRUP00000017795.3};
GN Name=gdpd1 {ECO:0000313|Ensembl:ENSTRUP00000017795.3};
OS Takifugu rubripes (Japanese pufferfish) (Fugu rubripes).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Takifugu.
OX NCBI_TaxID=31033 {ECO:0000313|Ensembl:ENSTRUP00000017795.3, ECO:0000313|Proteomes:UP000005226};
RN [1] {ECO:0000313|Ensembl:ENSTRUP00000017795.3, ECO:0000313|Proteomes:UP000005226}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21551351;
RA Kai W., Kikuchi K., Tohari S., Chew A.K., Tay A., Fujiwara A., Hosoya S.,
RA Suetake H., Naruse K., Brenner S., Suzuki Y., Venkatesh B.;
RT "Integration of the genetic map and genome assembly of fugu facilitates
RT insights into distinct features of genome evolution in teleosts and
RT mammals.";
RL Genome Biol. Evol. 3:424-442(2011).
RN [2] {ECO:0000313|Ensembl:ENSTRUP00000017795.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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:0000256|ARBA:ARBA00036725};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53185;
CC Evidence={ECO:0000256|ARBA:ARBA00036725};
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:0000256|ARBA:ARBA00036083};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41144;
CC Evidence={ECO:0000256|ARBA:ARBA00036083};
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:0000256|ARBA:ARBA00035902};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:56461;
CC Evidence={ECO:0000256|ARBA:ARBA00035902};
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:0000256|ARBA:ARBA00023561};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45545;
CC Evidence={ECO:0000256|ARBA:ARBA00023561};
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:0000256|ARBA:ARBA00036780};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53169;
CC Evidence={ECO:0000256|ARBA:ARBA00036780};
CC -!- SIMILARITY: Belongs to the glycerophosphoryl diester phosphodiesterase
CC family. {ECO:0000256|ARBA:ARBA00007277}.
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DR RefSeq; XP_003968287.2; XM_003968238.2.
DR AlphaFoldDB; H2SZF7; -.
DR STRING; 31033.ENSTRUP00000017795; -.
DR Ensembl; ENSTRUT00000017869.3; ENSTRUP00000017795.3; ENSTRUG00000007222.3.
DR GeneID; 101062546; -.
DR KEGG; tru:101062546; -.
DR CTD; 284161; -.
DR eggNOG; KOG2258; Eukaryota.
DR GeneTree; ENSGT00940000156673; -.
DR HOGENOM; CLU_030006_5_0_1; -.
DR InParanoid; H2SZF7; -.
DR OMA; VHVWTID; -.
DR OrthoDB; 168061at2759; -.
DR TreeFam; TF328545; -.
DR Proteomes; UP000005226; Chromosome 11.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0008081; F:phosphoric diester hydrolase activity; IEA:InterPro.
DR GO; GO:0006629; P:lipid metabolic process; IEA:InterPro.
DR CDD; cd08612; GDPD_GDE4; 1.
DR Gene3D; 3.20.20.190; Phosphatidylinositol (PI) phosphodiesterase; 1.
DR InterPro; IPR030395; GP_PDE_dom.
DR InterPro; IPR017946; PLC-like_Pdiesterase_TIM-brl.
DR PANTHER; PTHR42758:SF1; LYSOPHOSPHOLIPASE D GDPD1; 1.
DR PANTHER; PTHR42758; PHOSPHATIDYLGLYCEROL PHOSPHOLIPASE C; 1.
DR Pfam; PF03009; GDPD; 1.
DR SUPFAM; SSF51695; PLC-like phosphodiesterases; 1.
DR PROSITE; PS51704; GP_PDE; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000005226};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 18..37
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 53..323
FT /note="GP-PDE"
FT /evidence="ECO:0000259|PROSITE:PS51704"
SQ SEQUENCE 332 AA; 38049 MW; 5DF2568A879EE4C3 CRC64;
MLTLNTTILR NKQTEMSVAV YILSTVTGYM LTSALLLKCP GLLHRRRKET FISRHISHRG
GAGENLENTM AAFKHAVDLG TDMLELDCHL TKDEQVVVSH DANLERCTGT DTRVSELAYS
ELPSYLCKLG VTFQRECFCE GGEDTRIPLL REVFEAFPYT PVNIDIKVNN DTLIKKVSEL
VVKYDREHLT VWGNSNNQIV KKCYKENPSI PVLFSLPRVL QLLGLFYTGL LPFVPLKEQF
LEIPMPSIIS KLRGPNRLNR RQRLLIWLAD ILLMRKSLFK HLTDRGIQVY IWVLNDEEDF
QRAFDLGATG VMTDFPTRLK DFMDRNGISK PQ
//
