PLDA1_CYNCA
ID PLDA1_CYNCA Reviewed; 808 AA.
AC Q70EW5;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 2.
DT 03-AUG-2022, entry version 53.
DE RecName: Full=Phospholipase D alpha 1 {ECO:0000250|UniProtKB:Q43007, ECO:0000312|EMBL:CAE47482.2};
DE Short=PLD 1 {ECO:0000250|UniProtKB:Q43007};
DE EC=3.1.4.4;
DE AltName: Full=Choline phosphatase 1 {ECO:0000250|UniProtKB:Q43007};
DE AltName: Full=Phosphatidylcholine-hydrolyzing phospholipase D 1 {ECO:0000250|UniProtKB:Q43007};
GN Name=PLD1 {ECO:0000250|UniProtKB:Q43007}; Synonyms=PLDALPHA;
OS Cynara cardunculus (Cardoon).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Asterales; Asteraceae; Carduoideae; Cardueae;
OC Carduinae; Cynara.
OX NCBI_TaxID=4265;
RN [1] {ECO:0000305, ECO:0000312|EMBL:CAE47482.2}
RP NUCLEOTIDE SEQUENCE [MRNA], AND INTERACTION WITH CARDA.
RX PubMed=16279943; DOI=10.1111/j.1742-4658.2005.04967.x;
RA Simoes I., Mueller E.C., Otto A., Bur D., Cheung A.Y., Faro C., Pires E.;
RT "Molecular analysis of the interaction between cardosin A and phospholipase
RT D(alpha). Identification of RGD/KGE sequences as binding motifs for C2
RT domains.";
RL FEBS J. 272:5786-5798(2005).
CC -!- FUNCTION: Hydrolyzes glycerol-phospholipids at the terminal
CC phosphodiesteric bond. Plays an important role in various cellular
CC processes. {ECO:0000305}.
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:0000250|UniProtKB:Q43007};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000250|UniProtKB:Q43007};
CC -!- SUBUNIT: Interacts (via C2 domain) with CARDA (via RGD or KGE motifs).
CC {ECO:0000269|PubMed:16279943}.
CC -!- DOMAIN: C2 domain is a calcium-binding fold, and the binding promotes
CC the protein association with membranes. A lower affinity toward calcium
CC can be anticipated for PLD alpha due to the absence of two potential
CC calcium ligands. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the phospholipase D family. C2-PLD subfamily.
CC {ECO:0000255}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAE47482.2; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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; AJ583515; CAE47482.2; ALT_INIT; mRNA.
DR AlphaFoldDB; Q70EW5; -.
DR SMR; Q70EW5; -.
DR PRIDE; Q70EW5; -.
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 Gene3D; 2.60.40.150; -; 1.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR025202; PLD-like_dom.
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; PTHR18896; 1.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF12357; PLD_C; 1.
DR Pfam; PF00614; PLDc; 1.
DR Pfam; PF13091; PLDc_2; 1.
DR PIRSF; PIRSF036470; PLD_plant; 1.
DR SMART; SM00239; C2; 1.
DR SMART; SM00155; PLDc; 2.
DR SUPFAM; SSF49562; SSF49562; 1.
DR PROSITE; PS50004; C2; 1.
DR PROSITE; PS50035; PLD; 2.
PE 1: Evidence at protein level;
KW Calcium; Hydrolase; Lipid degradation; Lipid metabolism; Metal-binding;
KW Repeat.
FT CHAIN 1..808
FT /note="Phospholipase D alpha 1"
FT /id="PRO_0000394449"
FT DOMAIN 1..125
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 326..364
FT /note="PLD phosphodiesterase 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT DOMAIN 654..681
FT /note="PLD phosphodiesterase 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT ACT_SITE 331
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT ACT_SITE 333
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT ACT_SITE 338
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT ACT_SITE 659
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT ACT_SITE 661
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT ACT_SITE 666
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT BINDING 186
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q38882"
FT BINDING 331
FT /ligand="a 1,2-diacyl-sn-glycero-3-phosphate"
FT /ligand_id="ChEBI:CHEBI:58608"
FT /evidence="ECO:0000250|UniProtKB:Q38882"
FT BINDING 370
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q38882"
FT BINDING 404
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q38882"
FT BINDING 520
FT /ligand="a 1,2-diacyl-sn-glycero-3-phosphate"
FT /ligand_id="ChEBI:CHEBI:58608"
FT /evidence="ECO:0000250|UniProtKB:Q38882"
FT BINDING 659
FT /ligand="a 1,2-diacyl-sn-glycero-3-phosphate"
FT /ligand_id="ChEBI:CHEBI:58608"
FT /evidence="ECO:0000250|UniProtKB:Q38882"
FT BINDING 720
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q38882"
SQ SEQUENCE 808 AA; 91784 MW; ED991515608E2C51 CRC64;
MSKVLLHGTL HVTVYEVDKL REGGGPNVFG KLMANIQETV GFGEGTPKIY ATIDLEKSRV
GRTRMIENEP QNPRWYESFH IYCAHHASNI IFTVKDDNPI GATLLGRAYM PVRELLDGDE
VDKWIEIMDE DNNPTPAGSK IHVKLQYFDV TQDRNWDRGI KTGKYPGVPY TFFAQRQGCR
VSLYQDAHVP DNFIPKISLA GGKYYEPHRC WEDIFDAISD AKHFIYITGW SVYTQIPLIR
DPNRQKPGGD VLLGQLLKKK ADEGVRVAML VWDDRTSVNV FKEDGLMATH DEETENFFKD
TDVHCILCPR DPDDGGSIIQ DLKVSTMFTH HQKIVVVDHE LPRGGSQKRR VMSFVGGIDL
CDGRYDSAFH PLFSTLDSAH HDDFHQPNYA GASIAKGGPR EPWHDIHSRV EGPIAWDVLF
NFEQRWRKQG GKNVLVDLKQ LDDILIPPSP VTFPNDQETW NVQLFRSIDG GAAFGFPDTP
EEASKSGLVS GKDNIIDRSI QDAYINAIRR AKHFIYIENQ YFLGSSFAWK SDDIDVDEVG
ALHLIPKELS LKIVTKIQEG EKFIVYIVVP MWPEGIPENG SVQAILDWQR RTMEMMYKDI
VDALQDKGLD DDPREYLTFF CLGNREAKKS GEYEPTEAPE PDSGYLHAQE NRRFMIYVHS
KMMIVDDEYI IVGSANINQR SMDGARDSEI AMGAYQPYHL ATQTPARGHV HGFRMALWYE
HLGMLDDSFE RPENKDCVNK ANEMADKCWD LYASEDLDRD LPGHLLRYPV GVTRKGDITE
LPGTECFPDT SARILGAKSD YLPPILTT
