ID A0A2P6RLK9_ROSCH Unreviewed; 858 AA.
AC A0A2P6RLK9;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=Phospholipase D {ECO:0000256|ARBA:ARBA00012027, ECO:0000256|PIRNR:PIRNR036470};
DE EC=3.1.4.4 {ECO:0000256|ARBA:ARBA00012027, ECO:0000256|PIRNR:PIRNR036470};
GN ORFNames=RchiOBHm_Chr2g0098271 {ECO:0000313|EMBL:PRQ47307.1};
OS Rosa chinensis (China rose).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Rosaceae; Rosoideae; Rosoideae incertae sedis;
OC Rosa.
OX NCBI_TaxID=74649 {ECO:0000313|EMBL:PRQ47307.1, ECO:0000313|Proteomes:UP000238479};
RN [1] {ECO:0000313|EMBL:PRQ47307.1, ECO:0000313|Proteomes:UP000238479}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Old Blush {ECO:0000313|Proteomes:UP000238479};
RA Bendahmane M.;
RT "The Rosa genome provides new insights in the design of modern roses.";
RL Nat. Genet. 0:0-0(2018).
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}.
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:PRQ47307.1}.
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DR EMBL; PDCK01000040; PRQ47307.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2P6RLK9; -.
DR STRING; 74649.A0A2P6RLK9; -.
DR EnsemblPlants; PRQ47307; PRQ47307; RchiOBHm_Chr2g0098271.
DR Gramene; PRQ47307; PRQ47307; RchiOBHm_Chr2g0098271.
DR OMA; KHGIAGD; -.
DR OrthoDB; 3014064at2759; -.
DR Proteomes; UP000238479; Chromosome 2.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
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 GO; GO:0046470; P:phosphatidylcholine metabolic process; IEA:InterPro.
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; 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:SF86; PHOSPHOLIPASE D DELTA; 1.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF12357; PLD_C; 1.
DR Pfam; PF00614; PLDc; 1.
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|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:ARBA00022963,
KW ECO:0000256|PIRNR:PIRNR036470};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000238479}.
FT DOMAIN 1..154
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 359..394
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 703..730
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
SQ SEQUENCE 858 AA; 97869 MW; C84E4EF5A02D342A CRC64;
MAEPTSSEQI VYLHGDLDLQ IIEARYLPNM DIVSERLRRC FTACDTVNCT GSRSDNPDAG
HGAEDRKKLH HRKIITSDSY VSVVVPQATV ARTRVIKNSQ NPLWKESFSI PLAHPAAKLE
FQVKDNDLFG AELIGTASIP AVEIAAGNEI SGWYEIIGPT GKPPKPDCAI KVKLKFTPFE
INPVYRHGIA GDPERKGVPK TYFPMRKGSH VRLYQDAHVP EGMLPQIELD GRKVYKPENC
WEDICYAISE AHHMIYVVGW SVFHKVRLVR EPSRKLPRGG ELTLGELLKY KSEEGVRVLL
LVWDDKTSHD KFFFKSAGMM QTHDEETRKF FKHSSVTCVL APRYGSSKLS IMKQQVVGTL
FTHHQKCVIV DTQASGNNRK ITTFLGGLDL CDGRYDTPEH RLFRDLDTVF KEDFHQPTFP
AGTKAPRQPW HDLHCRIDGP AAYDVLINFE QRWRRATQWR EFGLRKKVSH WHDDALIKID
RISWILSPKM SHSKDVTIVP EDDPALWVQR EDDPEDWHVQ IFRSIDSGSL KGFPKDVIQA
QSKNLICSKD LVIDKSIQKA YINAIRSAQH FIYIENQYFL GSSYAWPDYK NAGADNLIPM
ELALKIASKI RANERFAVYI VLPMWPEGDP KTGAMQEILY WQSQTMQMMY GVVARELRAL
QLQDLHPQDF LNFYCLGNRE KLSEETSNNN GATISDAYKY QRFMIYVHAK GMIVDDEYVI
VGSANINQRS MAGTKDTEIA MGAYQPHHSW SEKKRHPCGQ IYGYRMSLWA EHLGKSDPCF
KEAESLECVR NVNGIAEENW RRYTSPDFTE LQGHLLRYPL QVDGDGNVRP RPGYENFPDV
GGKVIGAHSA TLPDQLTT
//
