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Database: UniProt
Entry: A0A3B6RIN3_WHEAT
LinkDB: A0A3B6RIN3_WHEAT
Original site: A0A3B6RIN3_WHEAT 
ID   A0A3B6RIN3_WHEAT        Unreviewed;       681 AA.
AC   A0A3B6RIN3;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   RecName: Full=phospholipase D {ECO:0000256|ARBA:ARBA00012027};
DE            EC=3.1.4.4 {ECO:0000256|ARBA:ARBA00012027};
OS   Triticum aestivum (Wheat).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX   NCBI_TaxID=4565 {ECO:0000313|EnsemblPlants:TraesCS7A02G376500.2};
RN   [1] {ECO:0000313|EnsemblPlants:TraesCS7A02G376500.2}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Chinese Spring
RC   {ECO:0000313|EnsemblPlants:TraesCS7A02G376500.2};
RX   PubMed=30115783; DOI=10.1126/science.aar7191;
RG   International wheat genome sequencing consortium (IWGSC);
RT   "Shifting the limits in wheat research and breeding using a fully annotated
RT   reference genome.";
RL   Science 361:EAAR7191-EAAR7191(2018).
RN   [2] {ECO:0000313|EnsemblPlants:TraesCS7A02G376500.2}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (OCT-2018) 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|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   AlphaFoldDB; A0A3B6RIN3; -.
DR   EnsemblPlants; TraesCS7A02G376500.2; TraesCS7A02G376500.2; TraesCS7A02G376500.
DR   Gramene; TraesCS7A02G376500.2; TraesCS7A02G376500.2; TraesCS7A02G376500.
DR   Gramene; TraesCS7A03G0916400.1; TraesCS7A03G0916400.1.CDS; TraesCS7A03G0916400.
DR   Proteomes; UP000019116; Chromosome 7A.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0070290; F:N-acylphosphatidylethanolamine-specific phospholipase D activity; IEA:UniProtKB-EC.
DR   GO; GO:0004630; F:phospholipase D activity; IEA:UniProtKB-EC.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR   CDD; cd04015; C2_plant_PLD; 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; IPR015679; PLipase_D_fam.
DR   PANTHER; PTHR18896; PHOSPHOLIPASE D; 1.
DR   PANTHER; PTHR18896:SF59; PHOSPHOLIPASE D ALPHA 2; 1.
DR   Pfam; PF00168; C2; 1.
DR   Pfam; PF00614; PLDc; 1.
DR   SMART; SM00239; C2; 1.
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; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Lipid degradation {ECO:0000256|ARBA:ARBA00022963};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00022963};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000019116}.
FT   DOMAIN          1..132
FT                   /note="C2"
FT                   /evidence="ECO:0000259|PROSITE:PS50004"
FT   DOMAIN          335..374
FT                   /note="PLD phosphodiesterase"
FT                   /evidence="ECO:0000259|PROSITE:PS50035"
SQ   SEQUENCE   681 AA;  76441 MW;  B1C8DA2F06556BD8 CRC64;
     MAHRLLHGTL HATILEADNL TNPDRATGGA PQIFRRFVEG FEETIGRGKG STQLYATVDL
     GKARVGRTRV IAGDPVNPRW YEEFHIYCAH FAADVVFTVK AAQPIGATLI GRAYLPVREL
     LDAGGREIER RLDVLDPSKK KIHHGPTIHV RLRFCDVAAN PREWGAGLGG ARHPGVPYTF
     FSQRPGCRVT LYQDAHTPDA FAPRIPLSGG RTYQQGRCWE DVFDAISDAR HLIYVTGWSV
     YTEITLIRDG SRPRPGGDAT LGELLKRKAS EGVRVLMLVW DDRTSVESLG MTWGYMGTHD
     AETAEYFRGT DVQCVLCPRN PDIGRSAVMG LQTAYMISHH QKIIAVDHDM PVRGSLSRRR
     IVSFVGGLDL CDGRYDTQFH SLFRTMDTAH HKDFHQPNFV DTSITKGGPR EPWHDIHAKI
     EGPAAWDILY NFEQRWRKQG GDNDLLVDLR ALANLIIPPS TVTFPDDQEA WNVQVFRSID
     GGASFGFPNT PEQAARSGLV SGKNNTLDRS IQDAYIHAIR RAQHFIYIEN QYFLGSSFAW
     KADDIRPEEI EALHLIPREL SLKIVSKIEA GEHFVVYVVV PMWPEGAPEG GSVQAILDWQ
     RRTMDMMYYD ISIALKAKGI DASPKDYLTF FCLGNREAKR SGEYEPADHP LPGSGYEKAQ
     NARRFMIYVH SKMMIVCLIS S
//
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