GenomeNet

Database: UniProt
Entry: M4A944_XIPMA
LinkDB: M4A944_XIPMA
Original site: M4A944_XIPMA 
ID   M4A944_XIPMA            Unreviewed;       317 AA.
AC   M4A944;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 52.
DE   SubName: Full=Glycerophosphodiester phosphodiesterase domain containing 1 {ECO:0000313|Ensembl:ENSXMAP00000010988.1};
OS   Xiphophorus maculatus (Southern platyfish) (Platypoecilus maculatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC   Xiphophorus.
OX   NCBI_TaxID=8083 {ECO:0000313|Ensembl:ENSXMAP00000010988.1, ECO:0000313|Proteomes:UP000002852};
RN   [1] {ECO:0000313|Proteomes:UP000002852}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RA   Walter R., Schartl M., Warren W.;
RL   Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000002852}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JP 163 A {ECO:0000313|Proteomes:UP000002852};
RX   PubMed=23542700; DOI=10.1038/ng.2604;
RA   Schartl M., Walter R.B., Shen Y., Garcia T., Catchen J., Amores A.,
RA   Braasch I., Chalopin D., Volff J.N., Lesch K.P., Bisazza A., Minx P.,
RA   Hillier L., Wilson R.K., Fuerstenberg S., Boore J., Searle S.,
RA   Postlethwait J.H., Warren W.C.;
RT   "The genome of the platyfish, Xiphophorus maculatus, provides insights into
RT   evolutionary adaptation and several complex traits.";
RL   Nat. Genet. 45:567-572(2013).
RN   [3] {ECO:0000313|Ensembl:ENSXMAP00000010988.1}
RP   IDENTIFICATION.
RC   STRAIN=JP 163 A {ECO:0000313|Ensembl:ENSXMAP00000010988.1};
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   RefSeq; XP_005803423.1; XM_005803366.1.
DR   AlphaFoldDB; M4A944; -.
DR   STRING; 8083.ENSXMAP00000010988; -.
DR   Ensembl; ENSXMAT00000011002.2; ENSXMAP00000010988.1; ENSXMAG00000010955.2.
DR   GeneID; 102219746; -.
DR   KEGG; xma:102219746; -.
DR   CTD; 284161; -.
DR   eggNOG; KOG2258; Eukaryota.
DR   GeneTree; ENSGT00940000156673; -.
DR   HOGENOM; CLU_030006_5_0_1; -.
DR   InParanoid; M4A944; -.
DR   OMA; VHVWTID; -.
DR   OrthoDB; 168061at2759; -.
DR   Proteomes; UP000002852; Unassembled WGS sequence.
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:UP000002852};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        6..28
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          38..308
FT                   /note="GP-PDE"
FT                   /evidence="ECO:0000259|PROSITE:PS51704"
SQ   SEQUENCE   317 AA;  36213 MW;  610856B4A24A4E61 CRC64;
     MCAAIYIVST VTGYVLTSAL LLKCPTLLHR RKRERFLSKH ISHRGGAGEN LENTMAAFKH
     AVDLGTDMLE LDCHLTKDEQ VVVSHDGNLK RVCGINANIS DLTYAELPPY LCKLGVTFQR
     ECFCEGGEDK RIPLLRDVFD AFPNTPINID IKVNNDTLIK KVSELVVKYD REDLTVWGNS
     RNHIVKKCYK ENPHIPVLFS FPRVLHLLGL FYTGLLPFVP LKEQFLEIPM PSLLTKLKDP
     SRLTRSQRLI AWLADTLLMR KALFQHLTAR GIQVYIWVLN DEEDFQRAFD LGATGVMTDF
     PTRLREFMDR NGISKPQ
//
DBGET integrated database retrieval system