PLDA1_SPUBR
ID PLDA1_SPUBR Reviewed; 808 AA.
AC O04883;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Phospholipase D alpha 1;
DE Short=PLD alpha 1;
DE EC=3.1.4.4;
DE AltName: Full=Choline phosphatase 1;
DE AltName: Full=Phosphatidylcholine-hydrolyzing phospholipase D 1;
GN Name=PLD1; Synonyms=PLD;
OS Spuriopimpinella brachycarpa (Chamnamul) (Pimpinella brachycarpa).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Apiales; Apiaceae; Apioideae; Acronema clade;
OC Spuriopimpinella.
OX NCBI_TaxID=45043;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Cha Y.Y., Lee K.-W., Kim J.C., Han T.J., Lee W.S., Cho S.H.;
RT "Nucleotide sequence of a cDNA encoding phospholipase D from Pimpinella
RT brachycarpa.";
RL (er) Plant Gene Register PGR97-092(1997).
CC -!- FUNCTION: Hydrolyzes glycerol-phospholipids at the terminal
CC phosphodiesteric bond. Plays an important role in various cellular
CC processes.
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 -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
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.
CC -!- SIMILARITY: Belongs to the phospholipase D family. C2-PLD subfamily.
CC {ECO:0000305}.
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DR EMBL; U96438; AAB70463.1; -; mRNA.
DR AlphaFoldDB; O04883; -.
DR SMR; O04883; -.
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; 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; 2.
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 2: Evidence at transcript 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_0000218822"
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 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; 91673 MW; E83DA015B06F2164 CRC64;
MAKTLLHGTL HVTIFEVDHL KAGSVVVFSE SLRRTLRKPL VLAKGTPKIY ASIDLDKARV
GRTRMIENEP NNPKWNESFH IYCGHPSTNV IFTVKDDNPI GATLIGRAYL PVHELLEGEE
VDKWVEILDE DKNPISEGSK IHVKLQYFDI TQDRNWAHGI RSSKFPGVPY TFFSQRPGCR
ISLYQDAHVP DNFVPKIPLS GGKFYEPHRC WEDVFDAITN AKHFIYITGW SVYTEFALIR
DTRRPKPGGD IMLGELLKKK ADEGVRVLML VWDDRTSVGL LKKDGLMATH DQETEEYFRD
SNVHCVLCLR NPDDGGGIIQ GLTISTIFTH HQKIVVVDSE MPTSGSENRR VVSFVGGIDL
CDGRYDTPFH SLFRTLDTAH HDDFHQPNFE GAAITKGGPR EPWHDIHSRL EGPVAWDVLF
NFEQRWRKQG GKDILLNLRE LQDVIIPPSP VTFPDDDETW NVQLFRSIDE GAAFFFPQTP
EEAAKAGLVS GKENIIVRSI QDAYIHAIRG PKISFILKIS IFLEALLAGI QRILKMRTSV
LCILIPKELS LKIVSKIEAG KRFTVYVVLP MWPEGIPESG SVQAILDWQR RTMEMMYKDI
IQALQANGIE EDPRNYLTFF CLGNREVKRD GEYEPSEKPD PDTDYSRAQE SRRFMIYVHA
KMMIVDDEYI IIGSANINQR SMDGAKDSEI AMGAYQPHHL ATREPARGQI HGFRMSLWYE
HLGMLDDTLA LPESVDCVQK VNTVADKYWD LYSSETLEND LPGHLLRYPI AVASEGNVTE
LPGTEFFPDT KARVLGAKSD FLPPILTT
