ID A0A164XCZ3_DAUCS Unreviewed; 808 AA.
AC A0A164XCZ3;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
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=DCAR_016258 {ECO:0000313|EMBL:KZM93013.1};
OS Daucus carota subsp. sativus (Carrot).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Apiales; Apiaceae; Apioideae; Scandiceae; Daucinae;
OC Daucus; Daucus sect. Daucus.
OX NCBI_TaxID=79200 {ECO:0000313|EMBL:KZM93013.1, ECO:0000313|Proteomes:UP000077755};
RN [1] {ECO:0000313|EMBL:KZM93013.1, ECO:0000313|Proteomes:UP000077755}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. DH1 {ECO:0000313|Proteomes:UP000077755};
RC TISSUE=Leaf {ECO:0000313|EMBL:KZM93013.1};
RX PubMed=27158781; DOI=10.1038/ng.3565;
RA Iorizzo M., Ellison S., Senalik D., Zeng P., Satapoomin P., Huang J.,
RA Bowman M., Iovene M., Sanseverino W., Cavagnaro P., Yildiz M.,
RA Macko-Podgorni A., Moranska E., Grzebelus E., Grzebelus D., Ashrafi H.,
RA Zheng Z., Cheng S., Spooner D., Van Deynze A., Simon P.;
RT "A high-quality carrot genome assembly provides new insights into
RT carotenoid accumulation and asterid genome evolution.";
RL Nat. Genet. 48:657-666(2016).
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:KZM93013.1}.
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DR EMBL; LNRQ01000005; KZM93013.1; -; Genomic_DNA.
DR RefSeq; XP_017252291.1; XM_017396802.1.
DR AlphaFoldDB; A0A164XCZ3; -.
DR STRING; 79200.A0A164XCZ3; -.
DR EnsemblPlants; KZM93013; KZM93013; DCAR_016258.
DR GeneID; 108222858; -.
DR Gramene; KZM93013; KZM93013; DCAR_016258.
DR KEGG; dcr:108222858; -.
DR OMA; PNWGRGI; -.
DR OrthoDB; 3014064at2759; -.
DR Proteomes; UP000077755; Chromosome 5.
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 CDD; cd09199; PLDc_pPLDalpha_2; 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 2; 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|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:UP000077755}.
FT DOMAIN 1..125
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 326..364
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 654..681
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
SQ SEQUENCE 808 AA; 91693 MW; C44A6F7EA95B7224 CRC64;
MAQILLHGTL HVTIFEVDHL KAGSGGGFLG KLKANLEEAV GFGEGTPKIY ASIDLDKARV
GRTRMIENEP NNPKWNESFH IYCGHSTTNV IFTVKDDNPI GATLIGRAYL PVEEILDGEE
VDRWVEILDE DKNPISEGSK IHVQLQFFDI SQDRNWARGV KSSKFPGVPY TFFSQRPGCR
ISLYQDAHVP DNFVPKIPLS GGKFYEPHRC WEDIFDAITN AKHFIYITGW SVYTEFALIR
DTRRPKPGGD IMLGELLKKK ADEGVRVLML VWDDRTSVGQ LKKDGLMATH DQETEEYFRD
SNVHCVLCLR NPDDSGGIIQ GLTISTIFTH HQKIVVVDSE MPTPGSENRR VVSFVGGIDL
CDGRYDTPFH SLFRTLDTAH HDDFHQPNFE GAAITKGGPR EPWHDIHSRL EGPVAWDVLF
NFEQRWRKQG GKDILLNLRE LQDIIIPPSP VTFPDDDETW NVQLFRSIDE GAAFGFPQTP
EEAAKAGLVS GKENIIDRSI QDAYIHAIRR AKNFIYIENQ YFLGSSFGWN SEDIKDEDIG
ALHLIPKELS LKIVSKIEAG ERFTVYVVLP MWPEGIPESG SVQAILDWQR RTMEMMYKDI
IQALQAKGIE EDPRNYLTFF CLGNREVKRD GEYEPSEQPD PDTDYSRAQE SRRFMIYVHA
KMMIVDDEYI IIGSANINQR SMDGAKDSEI AMGAYQPHHL ATREPARGQI HGFRMSLWYE
HLGMLDDLFA QPHNVDCVHK VNTVADKYWD LYSSETLEKD LPGHLLRYPI GVSSEGTVTE
LPGMEFFPDT KARVLGAKSD YLPPILTT
//
