ID A0A6P6X0A5_COFAR Unreviewed; 987 AA.
AC A0A6P6X0A5;
DT 02-DEC-2020, integrated into UniProtKB/TrEMBL.
DT 02-DEC-2020, sequence version 1.
DT 18-JUN-2025, entry version 22.
DE RecName: Full=Phospholipase {ECO:0000256|PIRNR:PIRNR009376};
DE EC=3.1.4.4 {ECO:0000256|PIRNR:PIRNR009376};
GN Name=LOC113738076 {ECO:0000313|RefSeq:XP_027121040.1};
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_027121040.1};
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_027121040.1}
RP IDENTIFICATION.
RC TISSUE=Leaves {ECO:0000313|RefSeq:XP_027121040.1};
RG RefSeq;
RL Submitted (MAR-2025) 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 ECO:0000256|PIRNR:PIRNR009376};
CC -!- SIMILARITY: Belongs to the phospholipase D family.
CC {ECO:0000256|PIRNR:PIRNR009376}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR RefSeq; XP_027121040.1; XM_027265239.1.
DR AlphaFoldDB; A0A6P6X0A5; -.
DR GeneID; 113738076; -.
DR Proteomes; UP000515148; Chromosome 3e.
DR GO; GO:0005886; C:plasma membrane; IEA:TreeGrafter.
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 CDD; cd01254; PH_PLD; 1.
DR CDD; cd09138; PLDc_vPLD1_2_yPLD_like_1; 1.
DR CDD; cd09141; PLDc_vPLD1_2_yPLD_like_2; 1.
DR FunFam; 3.30.870.10:FF:000011; Phospholipase; 1.
DR Gene3D; 3.30.870.10; Endonuclease Chain A; 2.
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; IPR025202; PLD-like_dom.
DR InterPro; IPR001736; PLipase_D/transphosphatidylase.
DR InterPro; IPR016555; PLipase_D_euk.
DR InterPro; IPR015679; PLipase_D_fam.
DR PANTHER; PTHR18896:SF76; PHOSPHOLIPASE; 1.
DR PANTHER; PTHR18896; PHOSPHOLIPASE D; 1.
DR Pfam; PF00614; PLDc; 1.
DR Pfam; PF13091; PLDc_2; 1.
DR PIRSF; PIRSF009376; Phospholipase_D_euk; 2.
DR SMART; SM00155; PLDc; 2.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF56024; Phospholipase D/nuclease; 2.
DR PROSITE; PS50035; PLD; 2.
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 Reference proteome {ECO:0000313|Proteomes:UP000515148};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 353..380
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 783..810
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT REGION 547..572
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 551..560
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 987 AA; 112605 MW; B4E85B13D026136E CRC64;
MMKKLKMRPF LCVMMKVSKT GSFLFRDVPS SAALPIIRPA LGRQNSMSDR SKVAMQGYLN
HFLGNMDIVN SREVCRFLEV SRLSFLPEYG PKLKEDYVMV KHLPKIPSDD EHQGCCSCQW
FSCCKDNWQK VWAVLKPGFL AFLKDPFDAQ PLDIIVFDVL PASDGNGDGR VSLAKEVKDH
NPLRHYFRVS CGIRCIKVRT KANAKVKDWV AAINDAGLRP PEGWCHPHRF GSFAPPRGLT
EDGSQAQWFV DGRVAFEAIA LAIEDAKSEI FICGWWLCPE LYLRRPFDAH ASSRLDALLE
MKAKQGVQIY ILLYKEVALA LKINSVYSKK KLLGIHENVR VLRYPDHFST GVYLWSHHEK
IVIVDHHICF LGGLDLCFGR YDSFEHKVGD YPPCNWPGKD YYNPRESEPN SWEDTMKDEL
DRQKYPRMPW HDVHCAFWGP PCRDVARHFV QRWNYAKRNK APYEEAIPLL MPQHHMVIPH
YMGINRDIDD EIKNDGNIRK RTKKQESFSS RSSCQDIPLL MPQEADGLDA SEGQLKLNGL
SREYGFHDQA SRPSKSPFSF RKSKVEPINP DMPMKGFVDD LDASHMLQEL SSMQPGFKPS
GNEWWETQDR SGQVDLADES GQVGPRVSCR CQVIRSVSQW SAGTSQIEES IHSAYCSLIE
KAEHFIYIEN QFFISGLSGD EIIRNRVLEA LYQRIMRAYK EKKCFRVIIV IPLLPGFQGG
VDDGGAASVR AIMHWQYRTI CRGRNSILDN LYDHIGPRVH DYISFYGLRA HGRLFEGGPV
ASSQVYVHSK IMIVDDCITL VGSANINDRS LLGSRDSEIG VLVEDKELFD SLMGGKPWKA
GKFASSLRLS LWSEHLGLRA GEVHQIRDPV IDSTYKGIWM ATAKTNTMIY QDVFSCIPND
LIHSRASLRQ CMVYWKEKLG QATIDLGIAP NKLESYQDGD IKCTDPLERL ESVRGHLVSF
PLDFMSKEDL RPVFNESEYY ASSQVFH
//
