ID A0A2P6PZF3_ROSCH Unreviewed; 854 AA.
AC A0A2P6PZF3;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 24-JAN-2024, entry version 22.
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_Chr6g0303711 {ECO:0000313|EMBL:PRQ27286.1};
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:PRQ27286.1, ECO:0000313|Proteomes:UP000238479};
RN [1] {ECO:0000313|EMBL:PRQ27286.1, 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:PRQ27286.1}.
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 EMBL; PDCK01000044; PRQ27286.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2P6PZF3; -.
DR STRING; 74649.A0A2P6PZF3; -.
DR EnsemblPlants; PRQ27286; PRQ27286; RchiOBHm_Chr6g0303711.
DR Gramene; PRQ27286; PRQ27286; RchiOBHm_Chr6g0303711.
DR OMA; RKVSHWK; -.
DR Proteomes; UP000238479; Chromosome 6.
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:SF60; PHOSPHOLIPASE D; 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..140
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 354..389
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 700..727
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
SQ SEQUENCE 854 AA; 96936 MW; C73FDE7A456A3176 CRC64;
MAEDNSEPLV VYLHGNLDLK IIEARYLPNM DMLSERFRRL FSACRKPFSS PKQHRSHHKI
ITSDPYVTVC LAGATVARTR VISNSQNPEW KEHFKIPLAH PVSQVEFYVK DNDMFGADLI
GVASVSAQRI LSGETISDWF PIIGPLGKPP KPDSAVRLEM RFTKCEDDPL YQYGISHERF
GGVENCYFPA RRGGHVTLYQ DAHVPDSVME DIELDDGVQF EHGKCWEDIC HAILEAHHLV
YIVGWSIYHK VKVVREPSKP LPSGGNLNLG ELLKYKSQEG LRVLLLVWDD KTSHSKFFIN
TTGVMQTHDE ETRKFFKHSS VSCVLSPRYA SSKLSIFKQQ ACFIYHGSVT VVGTLFTHHQ
KCVIVDTQAS GNNRKITAFI GGLDLCDGRY DTPEHRLFRD VDTVFQGDFH NPTLAGTKGP
RQPWHDLHCK IEGPAAYDVL TNFEQRWKRA TKWSELGQRF KRVSRWHDDA LIKLERISWI
LSPAPKSSND DPALRVSDED DPQNWRVQIF RSIDSGSVKG FPKDVYEAEN QNLFCAKNLV
IDKSIQTAYI EAIRSAQHFI YIENQYFLGS SYAWPTYKEA GADNLIPMEL ALKIASKIRA
KERFAVYVVI PMWPEGVPSS APVQQILFWQ GQTMQMMYEI IAKELKSMNI ANAHPQDYLN
FYCLGNRETL PATVSCTNNQ APRTGSPSHT VSASQKFQRF MIYVHAKGMV VDDEYVIIGS
ANINQRSMAG SRDTEIAMGA YQPHHTWGKK KRHPHGQVYG YRMSLWAEHM GMVENCFKEP
QTVECVKRVN DIGQDNWSRF VADDFIELQG HLIKYPVEVY ANGKVGALPG RESFPDVGGK
ILGARTNLPD ALTT
//
