ID A0A6P6XI88_COFAR Unreviewed; 809 AA.
AC A0A6P6XI88;
DT 02-DEC-2020, integrated into UniProtKB/TrEMBL.
DT 02-DEC-2020, sequence version 1.
DT 18-JUN-2025, entry version 24.
DE RecName: Full=Phospholipase D {ECO:0000256|PIRNR:PIRNR036470};
DE EC=3.1.4.4 {ECO:0000256|PIRNR:PIRNR036470};
GN Name=LOC113742843 {ECO:0000313|RefSeq:XP_027126646.1,
GN ECO:0000313|RefSeq:XP_027126647.1};
OS Coffea arabica (Arabian coffee).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Gentianales; Rubiaceae; Ixoroideae; Gardenieae complex;
OC Bertiereae - Coffeeae clade; Coffeeae; Coffea.
OX NCBI_TaxID=13443 {ECO:0000313|Proteomes:UP000515148, ECO:0000313|RefSeq:XP_027126646.1};
RN [1] {ECO:0000313|Proteomes:UP000515148}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Caturra red {ECO:0000313|Proteomes:UP000515148};
RA Zimin A.V., Yepes M., Maldonado C.E., Navarro L., Kovaka S., Pertea M.,
RA Gaitan A. and Aldwinckle H.;
RT "The Coffea arabica cultivar Caturra genome provides a strong foundation
RT for breeding and functional genomics studies in coffee.";
RL Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|RefSeq:XP_027126646.1, ECO:0000313|RefSeq:XP_027126647.1}
RP IDENTIFICATION.
RC TISSUE=Leaves {ECO:0000313|RefSeq:XP_027126646.1,
RC ECO:0000313|RefSeq:XP_027126647.1};
RG RefSeq;
RL Submitted (MAR-2025) to UniProtKB.
CC -!- FUNCTION: Hydrolyzes glycerol-phospholipids at the terminal
CC phosphodiesteric bond. {ECO:0000256|PIRNR:PIRNR036470}.
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:PIRNR036470};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|ARBA:ARBA00001913,
CC ECO:0000256|PIRNR:PIRNR036470};
CC -!- SIMILARITY: Belongs to the phospholipase D family. C2-PLD subfamily.
CC {ECO:0000256|ARBA:ARBA00010683, ECO:0000256|PIRNR:PIRNR036470}.
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DR RefSeq; XP_027126646.1; XM_027270845.1.
DR RefSeq; XP_027126647.1; XM_027270846.1.
DR GeneID; 113742843; -.
DR OrthoDB; 14911at2759; -.
DR Proteomes; UP000515148; Chromosome 4e.
DR GO; GO:0005886; C:plasma membrane; IEA:TreeGrafter.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0004630; F:phospholipase D activity; IEA:UniProtKB-EC.
DR GO; GO:0046470; P:phosphatidylcholine metabolic process; IEA:InterPro.
DR GO; GO:0009395; P:phospholipid catabolic process; IEA:TreeGrafter.
DR CDD; cd04015; C2_plant_PLD; 1.
DR CDD; cd09199; PLDc_pPLDalpha_2; 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 InterPro; IPR011402; PLipase_D_pln.
DR PANTHER; PTHR18896; PHOSPHOLIPASE D; 1.
DR PANTHER; PTHR18896:SF115; PHOSPHOLIPASE D ALPHA 1; 1.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF12357; PLD_C; 1.
DR Pfam; PF00614; PLDc; 2.
DR PIRSF; PIRSF036470; PLD_plant; 1.
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, ECO:0000256|PIRNR:PIRNR036470};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR036470};
KW Lipid degradation {ECO:0000256|ARBA:ARBA00022963,
KW ECO:0000256|PIRNR:PIRNR036470};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000515148};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 1..126
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 327..365
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 655..682
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
SQ SEQUENCE 809 AA; 92263 MW; 03D23D29D5952A03 CRC64;
MDPVLLHGTL HVTILEVDKL HGEGGGPNVF RKLMANIEET VGFGKGTPKI YATIDLEKAR
VGRTRMIENE PNNPRWYESF HIYCAHEASN VIFTVKDDNP IGATLIGRAY VPVHELLEGE
EIDRWVEILD EDKNPIKEES KIQVKLQYFD VTRDRNWARG IRSSKFPGVP YTFYSQRTGC
RVSLYQDAHI PDNFVPRIPL AGGKLYEPHR CWEDIFDAIS NAKHMIYITG WSVYTEITLI
RDSRRQKPGG DVTIGELLKK KASEGVRVLM LVWDDRTSVG LLKKDGLMAT HDEETEQFFQ
GTDVHCVLCP RNPDDGGSFV QDLQISTMFT HHQKIVVVDS DMPGGEPQKR RIVSFVGGID
LCDGRYDTPF HSLFRTLDTA HHDDFHQPNF TGASITKGGP REPWHDIHSR LEGPIAWDVL
FNFEQRWRKQ GGKDILVNLR ELDDIIIPPS PVMFPDDHES WHVQLFRSID GGAAFGFPET
PEDAARAGLV SGKDNIIDRS IQDAYIHAIR RAKNFIYIEN QYFLGSCFGW KADDIKVEDV
GALHLIPKEL SLKIASKIEA GERFTVYVVV PMWPEGIPES GSVQAILDWQ RRTMEMMYKD
IIKALRDKGL EEDPRNYLTF FCLGNREVKR SGEYEPSEQP EPDSDYIRAQ EARRFMIYVH
TKMMIVDDEY IIIGSANINQ RSMDGSRDSE IAMGAYQPYH LATRQPARGQ IHGFRMSLWY
EHLGMLDDTF LHPESEECIA KVNQAAEKYW DLYASESVER DLPGHLLRYP IGVAGEGDVT
ELPGMEFFPD TKARILGTKS DYLPPILTT
//
