ID A0A3B3TYU5_9TELE Unreviewed; 1059 AA.
AC A0A3B3TYU5;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Phospholipase {ECO:0000256|PIRNR:PIRNR009376};
DE EC=3.1.4.4 {ECO:0000256|PIRNR:PIRNR009376};
OS Poecilia latipinna (sailfin molly).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=48699 {ECO:0000313|Ensembl:ENSPLAP00000005798.1, ECO:0000313|Proteomes:UP000261500};
RN [1] {ECO:0000313|Ensembl:ENSPLAP00000005798.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1,2-diacyl-
CC sn-glycero-3-phosphate + choline + H(+); Xref=Rhea:RHEA:14445,
CC ChEBI:CHEBI:15354, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57643, ChEBI:CHEBI:58608; EC=3.1.4.4;
CC Evidence={ECO:0000256|PIRNR:PIRNR009376};
CC -!- SIMILARITY: Belongs to the phospholipase D family.
CC {ECO:0000256|ARBA:ARBA00008664, ECO:0000256|PIRNR:PIRNR009376}.
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DR RefSeq; XP_014893774.1; XM_015038288.1.
DR AlphaFoldDB; A0A3B3TYU5; -.
DR STRING; 48699.ENSPLAP00000005798; -.
DR Ensembl; ENSPLAT00000007308.1; ENSPLAP00000005798.1; ENSPLAG00000007870.1.
DR GeneID; 106951032; -.
DR KEGG; plai:106951032; -.
DR CTD; 556641; -.
DR GeneTree; ENSGT00940000155015; -.
DR OrthoDB; 335467at2759; -.
DR Proteomes; UP000261500; Unplaced.
DR GO; GO:0070290; F:N-acylphosphatidylethanolamine-specific phospholipase D activity; IEA:UniProtKB-UniRule.
DR GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR GO; GO:0004630; F:phospholipase D activity; IEA:UniProtKB-UniRule.
DR GO; GO:0001525; P:angiogenesis; IEA:Ensembl.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006654; P:phosphatidic acid biosynthetic process; IEA:InterPro.
DR CDD; cd01254; PH_PLD; 1.
DR Gene3D; 3.30.870.10; Endonuclease Chain A; 3.
DR Gene3D; 3.30.1520.10; Phox-like domain; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR025202; PLD-like_dom.
DR InterPro; IPR001736; PLipase_D/transphosphatidylase.
DR InterPro; IPR016555; PLipase_D_euk.
DR InterPro; IPR015679; PLipase_D_fam.
DR InterPro; IPR001683; PX_dom.
DR InterPro; IPR036871; PX_dom_sf.
DR PANTHER; PTHR18896; PHOSPHOLIPASE D; 1.
DR PANTHER; PTHR18896:SF57; PHOSPHOLIPASE D1; 1.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF00614; PLDc; 1.
DR Pfam; PF13091; PLDc_2; 1.
DR Pfam; PF00787; PX; 1.
DR PIRSF; PIRSF009376; Phospholipase_D_euk; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00155; PLDc; 2.
DR SMART; SM00312; PX; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF56024; Phospholipase D/nuclease; 3.
DR SUPFAM; SSF64268; PX domain; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50035; PLD; 2.
DR PROSITE; PS50195; PX; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR009376};
KW Lipid degradation {ECO:0000256|ARBA:ARBA00022963,
KW ECO:0000256|PIRNR:PIRNR009376};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00022963,
KW ECO:0000256|PIRNR:PIRNR009376};
KW Lipoprotein {ECO:0000256|ARBA:ARBA00023288}.
FT DOMAIN 102..235
FT /note="PX"
FT /evidence="ECO:0000259|PROSITE:PS50195"
FT DOMAIN 242..351
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 482..509
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 876..903
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT REGION 174..199
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 532..571
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1059 AA; 120894 MW; F46E54CA346F790E CRC64;
MLDKAQPTAS NLNLVNAEVS ETRAASDTLD GIDMADLVES LDARELDLEE GEELDYDGNY
LGDCRIPFSA VYATVGFKEA SAKVYLPTVP ITAKILEVER FTTAQDRFNL SQHRSVNKSL
PAVFKIEMKH GEFTWLVKRK EKHFLELHRE LRTYKTLIRI PLPSRSHTVR RKTVRKSEVR
EMPSLPRGGG DELARDEQVS SRRRQLEDYI NTLLKMAMYR KYHHTMEFID VSQLSFIHDL
GPKGLEGMIY KRSGGHRIPG MNCCGQGQAC YRWSKRWLVV KDSFLLYMKP DSGAISFVLL
VDKEFSIKMD SKETETQHGV RVDSLSRTLV FKCSSYRHAR WWGQSIESFV RSHGKAFLRE
HRFGSFAQEQ ENVPAKWYVN GKTYMEDVAD ALEEAKEEIF ITDWWLSPEI FLKRPVVEGN
RWRLDCILKR KAQQGVRIFV MLYKEVELAL GINSGYSKRT LMHLHPNIKV MRHPDHVSSS
VYLWAHHEKI VVIDQSVAFV GGIDLAYGRW DDKEHRLTDV GSVTRSVALE QASSASASAS
PPSSDKGVSA VHDVPQSNGL GTPTPDAAEL PKLKGVGRSR MVRFSLYRHL QKHTLQHVDS
VSSVDSAESG SVKSLKTGVG ELQGNTRFWH GKDYCNFVYK DWIQLEKPFD DFIDRYTTPR
MPWHDIASVV HGRGARDVAR HFIQRWNFTK IMKPKYRSLS YPFLLPKSHS SADELKYQVP
GCVNAKVQVL RSSADWSAGI KYHEESIHNA YIQVIAKSKH YVYIENQFFI SCADNRTVYN
KIGDAIIERI IRAHKEGKKY RVYVVTPLLP GFEGDITTGG GNAIQAVMHF NYRTMIRGEY
AIISQLKKEM DDQWMNYISF AGLRTHAELE GRLITELIYV HSKMLIADDN TVIIGSANIN
DRSMLGKRDS EVAVIVEDSE KVSSVMDGQE YQAGPYALEL RLECFRTILG GHTDTSIDLS
DPVSDRFYKE VWMTTAGRNA TIYEKVFRCL PSSLVRNMSE LEQFQSKPGL AQTEKARAQE
ELRKIRGFLV QFPLDFLSEH NLMPSVGSKE AMVPTEIWT
//
