ID A0A3B4X6F9_SERLL Unreviewed; 1041 AA.
AC A0A3B4X6F9;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Phospholipase {ECO:0000256|PIRNR:PIRNR009376};
DE EC=3.1.4.4 {ECO:0000256|PIRNR:PIRNR009376};
GN Name=PLD1 {ECO:0000313|Ensembl:ENSSLDP00000011711.1};
OS Seriola lalandi dorsalis.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Carangiformes; Carangidae; Seriola.
OX NCBI_TaxID=1841481 {ECO:0000313|Ensembl:ENSSLDP00000011711.1, ECO:0000313|Proteomes:UP000261360};
RN [1] {ECO:0000313|Ensembl:ENSSLDP00000011711.1}
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 AlphaFoldDB; A0A3B4X6F9; -.
DR STRING; 1841481.ENSSLDP00000011711; -.
DR Ensembl; ENSSLDT00000012134.1; ENSSLDP00000011711.1; ENSSLDG00000009257.1.
DR GeneTree; ENSGT00940000155015; -.
DR Proteomes; UP000261360; 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: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; 2.
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 71..204
FT /note="PX"
FT /evidence="ECO:0000259|PROSITE:PS50195"
FT DOMAIN 211..320
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 451..478
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 858..885
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT REGION 139..167
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 548..587
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1041 AA; 119427 MW; 9596B3F0374B772B CRC64;
LTMLRQSEPT SSTLQLVAND MTGIMETLDT RELDLGDGEY DTTDTSTPEA RLPFTAIYHT
VGFKEPEAKV FLSSPITAKI LEVERFTSAQ DRFNIELKHG EFTWVVKRKE KHFMDLHREL
RTYKTFMRLP LPTRSHTIKR HTAARSEERQ MPNLPRGGGD ELGREEQVSS RRKQLEDYLN
NLLKMPMYRN YHATMEFIDA SQLSFIHDLG PKGLEGMVLK RSGGHRIPGL NCCGHSKMCY
RWSKRWLVVK DSFLLYMKPD SGAISFVMLV DKEFSILMDS KDTETRHGVR IDSLSRSLVL
KCSSYRHARW WGQAIEGFVQ KHGSAFLTDH RFGSFARQEE NIPAKWYVNG RTYMEDVADA
LEEAKEEIFI TDWWLSPEIF LKRPVVEGNR WRLDCILKRK AQQGVRVFVM LYKEVELALG
INSGYSKRTL LHLHPNIKVM RHPDHVSSAV YLWAHHEKII VIDQSVAFVG GIDLAYGRWD
DKEHRLTDVG SVTLSNLDKA AASNGSGAVS QTNGKNIFTV TDSVDQPKLK GQGRPKRTRF
SIRRHLQKHG LAQADSDSDL EAEESEWHTH THTHTHTHTH THTHTGLYHN DGSVRSLHTG
VGELFGNTRF WHGKDYCNFV HKDWIQLDKP FDDFIDRHTT PRMPWHDISS VVHGKAARDV
ARHFIQRWNF TKQVKPKYRS LSYPYLLPKS HTTAGEQRYQ VPNCIPTKVQ ILRSASDWSA
GIKYHEESIH NAYIHAIKNS QHFVYIENQF FISCADNRHV FNKIGDTIAE RIIRAYREGK
KYRVYVVTPL LPGFEGDINT GGGSAIQAVM HFNYRTMNRG EHSIISQLRR EMGEHWINYI
SIAGLRTHAE LGGKLVTELI YVHSKMLIAD DNTVIIGSAN INDRSMLGKR DSEVAVIVED
SETVTAVMDG EKYQAGKYAL QLRLECFKMI LGANTDPSID LSDPVSDQFY KEVWMATCAR
NATIYQKVFR CLPSSDVRNI LELDGYLAKT GLEKEDPARA HEELKKIRGF LVQFPLQFLC
EQNLLPPIGS KEAMVPMEVW T
//
