ID A0A9D3QEJ9_MEGAT Unreviewed; 963 AA.
AC A0A9D3QEJ9;
DT 03-MAY-2023, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2023, sequence version 1.
DT 18-JUN-2025, entry version 11.
DE RecName: Full=Phospholipase {ECO:0000256|PIRNR:PIRNR009376};
DE EC=3.1.4.4 {ECO:0000256|PIRNR:PIRNR009376};
GN ORFNames=MATL_G00053770 {ECO:0000313|EMBL:KAG7484857.1};
OS Megalops atlanticus (Tarpon) (Clupea gigantea).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Elopiformes; Megalopidae; Megalops.
OX NCBI_TaxID=7932 {ECO:0000313|EMBL:KAG7484857.1, ECO:0000313|Proteomes:UP001046870};
RN [1] {ECO:0000313|EMBL:KAG7484857.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=YG-15Mar2019-1 {ECO:0000313|EMBL:KAG7484857.1};
RC TISSUE=Brain {ECO:0000313|EMBL:KAG7484857.1};
RA Zahm M., Roques C., Cabau C., Klopp C., Donnadieu C., Jouanno E.,
RA Lampietro C., Louis A., Herpin A., Echchiki A., Berthelot C., Parey E.,
RA Roest-Crollius H., Braasch I., Postlethwait J., Bobe J., Montfort J.,
RA Bouchez O., Begum T., Mejri S., Adams A., Chen W.-J., Guiguen Y.;
RL Submitted (JAN-2021) to the EMBL/GenBank/DDBJ databases.
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|ARBA:ARBA00000798,
CC 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KAG7484857.1}.
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DR EMBL; JAFDVH010000003; KAG7484857.1; -; Genomic_DNA.
DR OrthoDB; 14911at2759; -.
DR Proteomes; UP001046870; Chromosome 3.
DR GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
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:0060627; P:regulation of vesicle-mediated transport; IEA:TreeGrafter.
DR CDD; cd01254; PH_PLD; 1.
DR CDD; cd09843; PLDc_vPLD2_1; 1.
DR FunFam; 3.30.1520.10:FF:000027; Phospholipase; 1.
DR FunFam; 3.30.870.10:FF:000005; Phospholipase; 1.
DR FunFam; 3.30.870.10:FF:000011; Phospholipase; 1.
DR Gene3D; 3.30.870.10; Endonuclease Chain A; 2.
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:SF121; PHOSPHOLIPASE D2; 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 SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF56024; Phospholipase D/nuclease; 2.
DR SUPFAM; SSF64268; PX 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:ARBA00023098};
KW Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW Reference proteome {ECO:0000313|Proteomes:UP001046870};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 83..210
FT /note="PX"
FT /evidence="ECO:0000259|PROSITE:PS50195"
FT DOMAIN 453..480
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 780..807
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT REGION 501..528
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 963 AA; 110484 MW; F6164F89B7E1BE7B CRC64;
MYSPKESLAQ SANTMAGAEE GVVEATRVRG LMRRFYSHDD SPLSQDELDS LKQNSEERPF
LVVHHLQAAK DGGVPLLLQG TPVTCRVEST ERYTTRSKVR VCTLYTVRLT HGQFSWTVKR
KYKHFQELHR DLYKHKMLLH FLPLGRFAIQ RQQLNAMTEE MPSLHSGDRA RRTSSKPKYL
EDYLNGLLEN TFCKNYHGML EFLDVSPLSF IKDLGPKGLE GFILKRSGGH RIQGLNCIGH
DRFCYRWSRR WLVVKDSFLL YMNREAGVIS FVLLFDPELK VQVGRCHTDT KHGVCIQNFS
RTLIIKCSSY KQAQWWSHEI RRLAERCDFL QTHRFQGFAP PREDTLTKWY VNGSGYFADL
ADALEQAKEE IFITDWWLSP EVFLKRPATD TYWRLDQILK RKAEQGVKVC VLLYKEVELA
LGINSGYSKR MLMNMHPNIK VMRHPDHVSS IVFLWAHHEK MVAIDQSVAF IGGIDLAFGR
WDDSHYRLTD LASVEMANHN AGAGDTVDRG SDGSPSQPVT AEPGPEDLTG NSQLWLGKDY
SNFINKDWVQ LDRPFEDNID RSQVPRMPWR DLAVALHGKA ARDVSRHFIQ RWNFTKVFKN
KYKDNFFPCL LPKSHTTADS LPFIVPGSRK ASVQVLRSVD RWSAGTCESS IHNAYVNVIK
NSQHYIYIEN QFFISCADGR SVHNGIGDAI VQRILQAHSE QKKYRVYVVV PLLPGFEGDI
STGGGNAIQA ILHFTYRTIC RGEFSILARL KEHMQDQWTQ YISLCGLRTH SELSQSLVTE
LIYVHSKTII ADDRCYIIGS ANINDRSMLG SRDSELAVLV EDQERVPSRM GGEEYQAGPL
TLALRMECFR VLLGVESASG IDIQDPISDE FFREVWNRTA QSNPNIYDTV FRCLPSNTIR
NLRALRELTS AERLCEADPE RARKELEAVR GLLVHFPLHF LCEEYLLPPI SSKERMVPME
VWT
//
