ID A0A6I9RYE0_ELAGV Unreviewed; 1064 AA.
AC A0A6I9RYE0;
DT 07-OCT-2020, integrated into UniProtKB/TrEMBL.
DT 07-OCT-2020, sequence version 1.
DT 18-JUN-2025, entry version 25.
DE RecName: Full=phospholipase D {ECO:0000256|ARBA:ARBA00012027};
DE EC=3.1.4.4 {ECO:0000256|ARBA:ARBA00012027};
GN Name=LOC105054164 {ECO:0000313|RefSeq:XP_010933911.1};
OS Elaeis guineensis var. tenera (Oil palm).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Arecaceae; Arecoideae; Cocoseae;
OC Elaeidinae; Elaeis.
OX NCBI_TaxID=51953 {ECO:0000313|Proteomes:UP000504607, ECO:0000313|RefSeq:XP_010933911.1};
RN [1] {ECO:0000313|RefSeq:XP_010933911.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (MAR-2025) to UniProtKB.
CC -!- FUNCTION: Hydrolyzes glycerol-phospholipids at the terminal
CC phosphodiesteric bond. Plays an important role in various cellular
CC processes. {ECO:0000256|ARBA:ARBA00056354}.
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 -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|ARBA:ARBA00001913};
CC -!- SIMILARITY: Belongs to the phospholipase D family. C2-PLD subfamily.
CC {ECO:0000256|ARBA:ARBA00010683}.
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DR RefSeq; XP_010933911.1; XM_010935609.3.
DR AlphaFoldDB; A0A6I9RYE0; -.
DR FunCoup; A0A6I9RYE0; 1241.
DR GeneID; 105054164; -.
DR KEGG; egu:105054164; -.
DR InParanoid; A0A6I9RYE0; -.
DR OrthoDB; 14911at2759; -.
DR Proteomes; UP000504607; Chromosome 11.
DR GO; GO:0005886; C:plasma membrane; IEA:TreeGrafter.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004630; F:phospholipase D activity; IEA:UniProtKB-EC.
DR GO; GO:0009395; P:phospholipid catabolic process; IEA:TreeGrafter.
DR CDD; cd04015; C2_plant_PLD; 1.
DR FunFam; 3.30.870.10:FF:000027; Phospholipase D; 1.
DR FunFam; 3.30.870.10:FF:000025; Phospholipase D delta; 1.
DR Gene3D; 2.60.40.150; C2 domain; 1.
DR Gene3D; 3.30.870.10; Endonuclease Chain A; 2.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR001736; PLipase_D/transphosphatidylase.
DR InterPro; IPR024632; PLipase_D_C.
DR InterPro; IPR015679; PLipase_D_fam.
DR PANTHER; PTHR18896; PHOSPHOLIPASE D; 1.
DR PANTHER; PTHR18896:SF65; PHOSPHOLIPASE D BETA 1; 1.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF12357; PLD_C; 1.
DR Pfam; PF00614; PLDc; 2.
DR SMART; SM00239; C2; 1.
DR SMART; SM00155; PLDc; 2.
DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR SUPFAM; SSF56024; Phospholipase D/nuclease; 2.
DR PROSITE; PS50004; C2; 1.
DR PROSITE; PS50035; PLD; 2.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Lipid degradation {ECO:0000256|ARBA:ARBA00022963};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000504607};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 238..376
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 577..612
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 910..937
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT REGION 23..163
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 177..226
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 63..77
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 78..94
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 131..163
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1064 AA; 118889 MW; 6D06264AEC9E2EA5 CRC64;
MDNYGNPYPY PYGYLPPPNP DPYHYRPPHY LHPSNSFPSP PMNPDPQFNH SGHLDYPPPA
FPPASVSSSS PSYDPYYNPE PNPYPYPLPR PYPGPYVSMP YDSDPNSPSL HHAGSSRYEP
TAPIAPPSSY PPSRSDSFST HSLPPDHPSL STPPSLSHSS STSSMYPLND LLASIRLSDQ
PPDLPSISGS HHRPSMSFSS SFPQAPPSFS PQTSFSGPLD PHGGSHHGQN LQLVPYENTG
GLKASLKVLL LHGSLDVWVC EARNLPNMDM FSKTLGDMIG KRLTSSLSGK MEHLSSMTSD
PYVSITVCGA VVGRTYVVSN SENPDWMQHF NVPVAHHAAE VEFVVKDSDI VGAQLIGTVS
IPVESIYSGQ RVEGIYPILG PNGKPCKPGA VLRLAIQYIP IERLSMFHNG VGAGPDYRGV
PGTYFPLRKG NKVTLYQDAH VPDGCLPDLR LDHGMHYVHG KCWRDIFDAI SQARHLVYIT
GWSVFHTVHL VRDAGYGSDC TLGDLLKTKS QEGVRVLLLV WDDPTSRSIL GYQTDGLMGT
HDEETRRFFK HSSVQVLLCP RSAGKRHSWV KQQETGTIYT HHQKTVIVDA DAANNKRKII
AFIGGLDLCG GRYDTPRHPL FRTLQTLHKD DYHQPNFAGP DASGPREPWH DLHSRIDGPA
AYDIVTNFEE RWLKASKRHG IKKLKRSSDD ALLRIERIPY IIGIQDLPYL DDNDPETWHV
QVFRSIDSNS VKGFPKDPRN ATAKNLVCGK NVLIDMSIHT AYVNAIRAAQ HFIYIENQYF
LGSSFNWDSN KDLGANNLIP IEIALKIANK IKAKERFSAY IVVPMWPEGN PTGAATQRIL
HWQNKTMQMM YETIYGALKE VGLEDTYEPQ DYLNFFCLGN HEVSDPNHFS DGGLKSANTP
QVLAKKNRRF MIYVHSKGMI VDDEYVILGS ANINQRSMEG TRDTEIAMGA YQPQHTWARK
LSGPHGQIYG YRMSLWAEHT GTLEECFTRP ESLECMKRVR DMGEQNWKQY VADEITEMRG
HLLKYPVSVD RKGKVKPLPG CETFPDMGGN ICGSFIAIQE NLTI
//
