ID A0A4W6DL66_LATCA Unreviewed; 904 AA.
AC A0A4W6DL66;
DT 18-SEP-2019, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2019, sequence version 1.
DT 18-JUN-2025, entry version 26.
DE RecName: Full=Phospholipase {ECO:0000256|PIRNR:PIRNR009376};
DE EC=3.1.4.4 {ECO:0000256|PIRNR:PIRNR009376};
GN Name=pld1a {ECO:0000313|Ensembl:ENSLCAP00010026064.1};
OS Lates calcarifer (Barramundi) (Holocentrus calcarifer).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Carangaria incertae sedis; Centropomidae; Lates.
OX NCBI_TaxID=8187 {ECO:0000313|Ensembl:ENSLCAP00010026064.1, ECO:0000313|Proteomes:UP000314980};
RN [1] {ECO:0000313|Proteomes:UP000314980}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Sai Rama Sridatta P.;
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLCAP00010026064.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (MAR-2025) 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 -!- SUBCELLULAR LOCATION: Endomembrane system
CC {ECO:0000256|ARBA:ARBA00037868}; Lipid-anchor
CC {ECO:0000256|ARBA:ARBA00037868}.
CC -!- SIMILARITY: Belongs to the phospholipase D family.
CC {ECO:0000256|ARBA:ARBA00008664, ECO:0000256|PIRNR:PIRNR009376}.
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DR AlphaFoldDB; A0A4W6DL66; -.
DR Ensembl; ENSLCAT00010026617.1; ENSLCAP00010026064.1; ENSLCAG00010011374.1.
DR GeneTree; ENSGT00940000155015; -.
DR Proteomes; UP000314980; Unassembled WGS sequence.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IEA:TreeGrafter.
DR GO; GO:0035091; F:phosphatidylinositol binding; IEA:InterPro.
DR GO; GO:0004630; F:phospholipase D activity; IEA:UniProtKB-UniRule.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0006654; P:phosphatidic acid biosynthetic process; IEA:InterPro.
DR GO; GO:0009395; P:phospholipid catabolic process; IEA:TreeGrafter.
DR GO; GO:0032534; P:regulation of microvillus assembly; IEA:TreeGrafter.
DR GO; GO:0060627; P:regulation of vesicle-mediated transport; IEA:TreeGrafter.
DR CDD; cd01254; PH_PLD; 1.
DR FunFam; 2.30.29.30:FF:000114; Phospholipase; 1.
DR FunFam; 3.30.870.10:FF:000005; Phospholipase; 1.
DR FunFam; 3.30.870.10:FF:000009; Phospholipase; 1.
DR FunFam; 3.30.870.10:FF:000018; Phospholipase; 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; 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 PIRSF; PIRSF009376; Phospholipase_D_euk; 2.
DR SMART; SM00233; PH; 1.
DR SMART; SM00155; PLDc; 2.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF56024; Phospholipase D/nuclease; 2.
DR SUPFAM; SSF64268; PX domain; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50035; PLD; 2.
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:ARBA00023098};
KW Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000314980};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 156..265
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 396..423
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 717..744
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
SQ SEQUENCE 904 AA; 104478 MW; 59CE5276B7B7CBEA CRC64;
TLNIRLSFSL PGDCRIPFSA VYATVGFKEA SARVYLPTVP ITARILEVER FTTSLPAVFK
IELKHGEFTW VVKRKEKHFM ELHRELRTYK TFMRIPLPSR RLAPTHLDLH SHMDMHMYKH
QQTQDLMCIL LLSLPVYSQM EFIDVSQLSF IHDLGPKGLE GMIYKRSGGH RIPGMNCCGH
SQACYRWSKR WLVVKDSCLL YMKPDSGAIS FVLLVDKEFS IKMDSKDTET KHGVRIDSLS
RTLVFKCSSY RHARWWGQSI ESFVRNHGKA FLRDHRFGSF AQEQENIPAK WYVNGKTYME
DVADALEEAK EEIFITDWWL SPEIFLKRPV VEGNRWRLDC ILKRKAQQGV HIFVMLYKEV
ELALGINSGY SKRTLMHLHP NIKVMRHPDH VSSSVYLWAH HEKIVVIDQS VAFVGGIDLA
YGRWDDREHR LTDSINQNIL ILFVCVCVGS GSVQSLKTGV GELQGNTRFW HGKDYCNFVY
KDWIQLEKPF DDFIDRYTTP RMPWHDIASV VHGRAARDVA RHFIQRWNFT KIMKPKYRSL
SYPFLLPKSH SSADDLRYQV PECVDAKVQV LRSSADWSAG IKYHEESIHN AYIQVIAKSK
HYIYIENQFF ISCADNRTVY NKIGDAIIER IIRAHKEGKK YRVYVVTPLL PGFEGDITTG
GGNAIQAVMH FNYRTMIRGE YSIISQLKRE MDDQWMNYIS FAGLRTHAEL EGRLVTELIY
VHSKMLIADD NTVIIGSANI NDRSMLGKRD SEVAVIVEDS QKVASVMDGQ EYEAGPYALQ
LRLECFRYVC LTILGGHTDT SIDLSDPISD RFYKEVWMTT AGRNATIYEK VFRCLPSSLV
RNMSELEQYQ SKPGLAQSDL TRAQEELRKI RGFLVQFPLD FLSEHNLMPS VGTKESMVPT
EIWT
//
