PLDA1_CARPA
ID PLDA1_CARPA Reviewed; 808 AA.
AC P86387;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2012, sequence version 1.
DT 03-AUG-2022, entry version 27.
DE RecName: Full=Phospholipase D alpha 1 {ECO:0000250|UniProtKB:Q41142};
DE Short=CpPLD1 {ECO:0000303|PubMed:22450361};
DE EC=3.1.4.4 {ECO:0000269|PubMed:22450361};
DE AltName: Full=Choline phosphatase 1 {ECO:0000250|UniProtKB:Q41142};
DE AltName: Full=Phosphatidylcholine-hydrolyzing phospholipase D 1 {ECO:0000250|UniProtKB:Q41142};
GN Name=PLD1 {ECO:0000250|UniProtKB:Q41142};
OS Carica papaya (Papaya).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Caricaceae; Carica.
OX NCBI_TaxID=3649;
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. SunUp {ECO:0000305};
RX PubMed=18432245; DOI=10.1038/nature06856;
RA Ming R., Hou S., Feng Y., Yu Q., Dionne-Laporte A., Saw J.H., Senin P.,
RA Wang W., Ly B.V., Lewis K.L., Salzberg S.L., Feng L., Jones M.R.,
RA Skelton R.L., Murray J.E., Chen C., Qian W., Shen J., Du P., Eustice M.,
RA Tong E., Tang H., Lyons E., Paull R.E., Michael T.P., Wall K., Rice D.W.,
RA Albert H., Wang M.L., Zhu Y.J., Schatz M., Nagarajan N., Acob R.A.,
RA Guan P., Blas A., Wai C.M., Ackerman C.M., Ren Y., Liu C., Wang J.,
RA Wang J., Na J.K., Shakirov E.V., Haas B., Thimmapuram J., Nelson D.,
RA Wang X., Bowers J.E., Gschwend A.R., Delcher A.L., Singh R., Suzuki J.Y.,
RA Tripathi S., Neupane K., Wei H., Irikura B., Paidi M., Jiang N., Zhang W.,
RA Presting G., Windsor A., Navajas-Perez R., Torres M.J., Feltus F.A.,
RA Porter B., Li Y., Burroughs A.M., Luo M.C., Liu L., Christopher D.A.,
RA Mount S.M., Moore P.H., Sugimura T., Jiang J., Schuler M.A., Friedman V.,
RA Mitchell-Olds T., Shippen D.E., dePamphilis C.W., Palmer J.D., Freeling M.,
RA Paterson A.H., Gonsalves D., Wang L., Alam M.;
RT "The draft genome of the transgenic tropical fruit tree papaya (Carica
RT papaya Linnaeus).";
RL Nature 452:991-996(2008).
RN [2] {ECO:0000305}
RP PROTEIN SEQUENCE OF 401-425; 467-509 AND 537-547, AND CATALYTIC ACTIVITY.
RC TISSUE=Latex {ECO:0000269|PubMed:22450361};
RX PubMed=22450361; DOI=10.1016/j.gene.2012.03.033;
RA Abdelkafi S., Abousalham A., Fendri I., Ogata H., Barouh N., Fouquet B.,
RA Scheirlinckx F., Villeneuve P., Carriere F.;
RT "Identification of a new phospholipase D in Carica papaya latex.";
RL Gene 499:243-249(2012).
CC -!- FUNCTION: Hydrolyzes glycerol-phospholipids at the terminal
CC phosphodiesteric bond. Plays an important role in various cellular
CC processes (By similarity). {ECO:0000250|UniProtKB:P55939}.
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:0000269|PubMed:22450361};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000250|UniProtKB:P55939};
CC Note=Ca(2+) requirement for activity depends on pH. Active either under
CC acidic conditions with micromolar levels of calcium (PIP2-dependent) or
CC at neutral pH with millimolar levels of calcium (PIP2-independent).
CC {ECO:0000250|UniProtKB:P55939};
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 (By similarity). {ECO:0000250|UniProtKB:P55939}.
CC -!- SIMILARITY: Belongs to the phospholipase D family. C2-PLD subfamily.
CC {ECO:0000255}.
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; ABIM01003647; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; P86387; -.
DR SMR; P86387; -.
DR OrthoDB; 128697at2759; -.
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:0034638; P:phosphatidylcholine catabolic process; IDA:UniProtKB.
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 1: Evidence at protein level;
KW Calcium; Direct protein sequencing; Hydrolase; Lipid degradation;
KW Lipid metabolism; Metal-binding; Repeat.
FT CHAIN 1..808
FT /note="Phospholipase D alpha 1"
FT /id="PRO_0000419018"
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; 92037 MW; 0FACFC2511AE3B94 CRC64;
MAHYLMHGTL HATVYEVDKL HSGGISGFFG KILANVEGTI GIGKGVTQLY ATIDLERARV
GRTRIIKDEP NNPKWYESFH IYCAHMASNV VFTVKDDNPI GATLIGRAYV PVEELIRGDQ
VDRWVEILDE DKNPIEGDSK IHVKLQFFDV KKDSNWNMGI KGARYLGVPY TFYSQRRGCR
VSLYQDAHVP DGFIPKIPLA GGKYYEPHRC WEDVFDAITN ARHLIYITGW SVYTEITLIR
DSRRPKPGGD VTLGELLKQK ASEGVKVLML VWDDRTSVGL LKKDGLMATH DEETANYFQN
TDVHCVLCPR NPDDGGSFVQ GLQISTMFTH HQKIVVVDGE MPSGESQMRR IVSFVGGIDL
CDGRYDTPFH SLFRTLDTAH HDDFHQPNFA GSSITKGGPR EPWHDIHSRL EGPVAWDVLF
NFEQRWRQQG GKDVLVNLRE LDNIIIPPSP VMFPDDHETW NVQLFRSIDG GAAFGFPETP
EEAARAGLVS GKDNIIDRSI QDAYINAIRR AKNFIYIENQ YFLGSSFDWS SDDIKREDIN
ALHLIPKELS LKIVSKIERG ERFTVYVVVP MWPEGVPESA SVQAILDWQR RTMEMMYKDI
IQALRAKDRE EDPRNYLTFF CLGNREVKKS GEYEPSERPE DDSDYIRAQE ARRFMIYVHT
KMMIVDDEYI IVGSANINQR SMDGARDSEI AMGAYQPYHL TINQPARGQI HGFRMALWYE
HLGMLDDTFL EPENIECVQK VNRVAGKYWD LYASELLEHD LPGHLLRYPI GVSSEGDVTE
LPGTEFFPDT KARVLGAKSD YLPPILTT
