ID A0A2D0S6X6_ICTPU Unreviewed; 316 AA.
AC A0A2D0S6X6;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Lysophospholipase D GDPD1 {ECO:0000313|RefSeq:XP_017338499.1};
GN Name=gdpd3b {ECO:0000313|RefSeq:XP_017338499.1};
OS Ictalurus punctatus (Channel catfish) (Silurus punctatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Siluriformes;
OC Ictaluridae; Ictalurus.
OX NCBI_TaxID=7998 {ECO:0000313|RefSeq:XP_017338499.1};
RN [1] {ECO:0000313|RefSeq:XP_017338499.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_017338499.1};
RG RefSeq;
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_017338499.1; XM_017483010.3.
DR AlphaFoldDB; A0A2D0S6X6; -.
DR STRING; 7998.ENSIPUP00000025208; -.
DR Ensembl; ENSIPUT00000026253; ENSIPUP00000025208; ENSIPUG00000017046.
DR GeneID; 108273646; -.
DR KEGG; ipu:108273646; -.
DR CTD; 567286; -.
DR OMA; DSHIMAK; -.
DR OrthoDB; 168061at2759; -.
DR Proteomes; UP000221080; Chromosome 13.
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:SF3; LYSOPHOSPHOLIPASE D GDPD3; 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 Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..25
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 207..232
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 41..310
FT /note="GP-PDE"
FT /evidence="ECO:0000259|PROSITE:PS51704"
SQ SEQUENCE 316 AA; 36290 MW; 5275CB120CDD4AB1 CRC64;
MDAELGVGLL VVAVGCYILC SLYLLRNPLI LHKKKRLAFY SRHISHRGGG GERIENTIEA
FTHAVDVGTE MFELDCHLTR DGYVVVCHDK YLERQTGSDV DISLVKFQDL PLYREKLEVT
FSVGHFGTGQ DRRIALLEDV FKKFPHMPIN IEVKQNNDLL IQKVSALVKK YDRDNITVWA
SDDSHIMAKC RKQNPYMPYS FTMRRGILLL ALYYTGLLPF CPLGESLLQF YLPRVINRGY
IPEESYLKKR FMVSLIEKLT MRKSLFEHLV KRGMQVQLFV CNTEKDMAAA FAFGATGVMS
DYPTMLSDYL KKHPAI
//
