PLDA4_ARATH
ID PLDA4_ARATH Reviewed; 762 AA.
AC Q9C888;
DT 03-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Phospholipase D alpha 4 {ECO:0000303|PubMed:11891260};
DE Short=AtPLDalpha4 {ECO:0000303|PubMed:11891260};
DE Short=PLD alpha 4 {ECO:0000303|PubMed:11891260};
DE EC=3.1.4.4 {ECO:0000250|UniProtKB:Q38882};
DE AltName: Full=PLDalpha3;
DE AltName: Full=Phospholipase D epsilon {ECO:0000303|PubMed:19143999};
DE Short=AtPLDepsilon {ECO:0000303|PubMed:19143999};
DE Short=PLD epsilon {ECO:0000303|PubMed:19143999};
GN Name=PLDALPHA4 {ECO:0000303|PubMed:11891260};
GN Synonyms=PLDEPSILON {ECO:0000303|PubMed:19143999};
GN OrderedLocusNames=At1g55180 {ECO:0000312|Araport:AT1G55180};
GN ORFNames=F7A10.25 {ECO:0000312|EMBL:AAG51567.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=11891260; DOI=10.1104/pp.010928;
RA Qin C., Wang X.;
RT "The Arabidopsis phospholipase D family. Characterization of a calcium-
RT independent and phosphatidylcholine-selective PLD zeta 1 with distinct
RT regulatory domains.";
RL Plant Physiol. 128:1057-1068(2002).
RN [4]
RP FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=19143999; DOI=10.1111/j.1365-313x.2009.03788.x;
RA Hong Y., Devaiah S.P., Bahn S.C., Thamasandra B.N., Li M., Welti R.,
RA Wang X.;
RT "Phospholipase D epsilon and phosphatidic acid enhance Arabidopsis nitrogen
RT signaling and growth.";
RL Plant J. 58:376-387(2009).
CC -!- FUNCTION: Hydrolyzes glycerol-phospholipids at the terminal
CC phosphodiesteric bond to generate phosphatidic acids (PA). Promotes
CC growth and plays a role in nitrogen signaling.
CC {ECO:0000269|PubMed:19143999}.
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:Q38882};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000250|UniProtKB:Q38882};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:19143999}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, leaves, stems, siliques,flowers
CC and inflorescences. {ECO:0000269|PubMed:19143999}.
CC -!- DOMAIN: C2 domain is a calcium-binding fold, and the binding promotes
CC the protein association with membranes. {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: Reduced growth. {ECO:0000269|PubMed:19143999}.
CC -!- SIMILARITY: Belongs to the phospholipase D family. C2-PLD subfamily.
CC {ECO:0000305}.
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DR EMBL; AC027034; AAG51567.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE33199.1; -; Genomic_DNA.
DR PIR; E96593; E96593.
DR RefSeq; NP_175914.1; NM_104391.2.
DR AlphaFoldDB; Q9C888; -.
DR SMR; Q9C888; -.
DR BioGRID; 27186; 1.
DR IntAct; Q9C888; 1.
DR STRING; 3702.AT1G55180.1; -.
DR PaxDb; Q9C888; -.
DR PRIDE; Q9C888; -.
DR ProteomicsDB; 234967; -.
DR EnsemblPlants; AT1G55180.1; AT1G55180.1; AT1G55180.
DR GeneID; 841961; -.
DR Gramene; AT1G55180.1; AT1G55180.1; AT1G55180.
DR KEGG; ath:AT1G55180; -.
DR Araport; AT1G55180; -.
DR TAIR; locus:2035716; AT1G55180.
DR eggNOG; KOG1329; Eukaryota.
DR HOGENOM; CLU_004684_0_0_1; -.
DR InParanoid; Q9C888; -.
DR OrthoDB; 160458at2759; -.
DR PhylomeDB; Q9C888; -.
DR BRENDA; 3.1.4.4; 399.
DR PRO; PR:Q9C888; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9C888; baseline and differential.
DR Genevisible; Q9C888; AT.
DR GO; GO:0005886; C:plasma membrane; IDA:TAIR.
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; IDA:TAIR.
DR GO; GO:0051301; P:cell division; IMP:TAIR.
DR GO; GO:0006995; P:cellular response to nitrogen starvation; IMP:TAIR.
DR GO; GO:0016036; P:cellular response to phosphate starvation; IMP:TAIR.
DR GO; GO:0051365; P:cellular response to potassium ion starvation; IMP:TAIR.
DR GO; GO:0009825; P:multidimensional cell growth; IMP:TAIR.
DR GO; GO:0046470; P:phosphatidylcholine metabolic process; IEA:InterPro.
DR GO; GO:0009395; P:phospholipid catabolic process; IDA:TAIR.
DR GO; GO:0045848; P:positive regulation of nitrogen utilization; IMP:TAIR.
DR GO; GO:0009791; P:post-embryonic development; IMP:TAIR.
DR GO; GO:0006970; P:response to osmotic stress; IMP:TAIR.
DR GO; GO:0048364; P:root development; IMP:TAIR.
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; PF13091; PLDc_2; 1.
DR PIRSF; PIRSF036470; PLD_plant; 1.
DR SMART; SM00155; PLDc; 2.
DR SUPFAM; SSF49562; SSF49562; 1.
DR PROSITE; PS50004; C2; 1.
DR PROSITE; PS50035; PLD; 1.
PE 2: Evidence at transcript level;
KW Calcium; Cell membrane; Hydrolase; Lipid degradation; Lipid metabolism;
KW Membrane; Metal-binding; Reference proteome; Repeat.
FT CHAIN 1..762
FT /note="Phospholipase D alpha 4"
FT /id="PRO_0000218816"
FT DOMAIN 1..116
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 301..339
FT /note="PLD phosphodiesterase 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT DOMAIN 610..637
FT /note="PLD phosphodiesterase 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT ACT_SITE 306
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT ACT_SITE 308
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT ACT_SITE 313
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT ACT_SITE 615
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT ACT_SITE 617
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT ACT_SITE 622
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT BINDING 172
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q38882"
FT BINDING 306
FT /ligand="a 1,2-diacyl-sn-glycero-3-phosphate"
FT /ligand_id="ChEBI:CHEBI:58608"
FT /evidence="ECO:0000250|UniProtKB:Q38882"
FT BINDING 345
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q38882"
FT BINDING 377
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q38882"
FT BINDING 477
FT /ligand="a 1,2-diacyl-sn-glycero-3-phosphate"
FT /ligand_id="ChEBI:CHEBI:58608"
FT /evidence="ECO:0000250|UniProtKB:Q38882"
FT BINDING 615
FT /ligand="a 1,2-diacyl-sn-glycero-3-phosphate"
FT /ligand_id="ChEBI:CHEBI:58608"
FT /evidence="ECO:0000250|UniProtKB:Q38882"
FT BINDING 671
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:Q38882"
SQ SEQUENCE 762 AA; 86770 MW; 5E9DA51B463994CC CRC64;
MELEEQKKYF HGTLEITIFD ATPFSPPFPF NCICTKPKAA YVTIKINKKK VAKTSSEYDR
IWNQTFQILC AHPVTDTTIT ITLKTRCSVL GRFRISAEQI LTSNSAVING FFPLIADNGS
TKRNLKLKCL MWFRPAYLEP GWCRALEEAS FQGIRNASFP QRSNCRVVLY QDAHHKATFD
PRVDDVPFNA RNLWEDVYKA IESARHLVYI AGWALNPNLV LVRDNETEIP HAVGVTVGEL
LKRKSEEGVA VRVMLWNDET SLPMIKNKGV MRTNVERALA YFRNTNVVCR LCPRLHKKLP
TAFAHHQKTI TLDTRVTNSS TKEREIMSFL GGFDLCDGRY DTEEHSLFRT LGTEADFYQT
SVAGAKLSRG GPREPWHDCH VSVVGGAAWD VLKNFEQRWT KQCNPSVLVN TSGIRNLVNL
TGPTEENNRK WNVQVLRSID HISATEMPRG LPVEKSVHDG YVAAIRKAER FIYIENQYFM
GSCDHWESKN DKICSGCTNL IPVEIALKIA AKIRARERFA VYIVIPMWPE GPPESETVEE
ILHWTRETMS MMYQIIGEAI WEVGDKSHPR DYLNFFCLAN REEKRDGEFE AVSSPHQKTH
YWNAQRNRRF MVYVHSKLMI VDDTYILIGS ANINQRSMDG CRDTEIAIGC YQTNTNNTNE
IQAYRLSLWY EHTGGKITAD DLSSSEPESL ECVRGLRTIG EQMWEIYSGD KVVDMLGIHL
VAYPISVTGD GAVEEVGDGC FPDTKTLVKG KRSKMFPPVL TT
