PLDA_DICDI
ID PLDA_DICDI Reviewed; 1269 AA.
AC Q54UK0;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Phospholipase D A;
DE EC=3.1.4.4;
DE AltName: Full=Phosphatase D1;
DE Short=PLD 1;
GN Name=pldA; Synonyms=pld1; ORFNames=DDB_G0281031;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
RN [2]
RP FUNCTION.
RX PubMed=6498208; DOI=10.1016/0005-2760(84)90343-6;
RA Ellingson J.S., Dischinger H.C.;
RT "Comparison of the hydrolysis of phosphatidylethanolamine and
RT phosphatidyl(N-acyl)ethanolamine in Dictyostelium discoideum amoebae.";
RL Biochim. Biophys. Acta 796:155-162(1984).
RN [3]
RP FUNCTION.
RX PubMed=8394342; DOI=10.1016/s0021-9258(19)85353-x;
RA Cubitt A.B., Dharmawardhane S., Firtel R.A.;
RT "Developmentally regulated changes in 1,2-diacylglycerol in Dictyostelium.
RT Regulation by light and G proteins.";
RL J. Biol. Chem. 268:17431-17439(1993).
RN [4]
RP NOMENCLATURE.
RX PubMed=15225639; DOI=10.1016/j.febslet.2004.05.071;
RA Rigden D.J.;
RT "A distant evolutionary relationship between GPI-specific phospholipase D
RT and bacterial phosphatidylcholine-preferring phospholipase C.";
RL FEBS Lett. 569:229-234(2004).
RN [5]
RP ACTIVITY REGULATION, AND FUNCTION.
RX PubMed=15769249; DOI=10.1042/bj20050085;
RA Zouwail S., Pettitt T.R., Dove S.K., Chibalina M.V., Powner D.J.,
RA Haynes L., Wakelam M.J.O., Insall R.H.;
RT "Phospholipase D activity is essential for actin localization and actin-
RT based motility in Dictyostelium.";
RL Biochem. J. 389:207-214(2005).
RN [6]
RP DEVELOPMENTAL STAGE.
RX PubMed=15821129; DOI=10.1128/ec.4.4.694-702.2005;
RA Chen Y., Rodrick V., Yan Y., Brazill D.;
RT "PldB, a putative phospholipase D homologue in Dictyostelium discoideum
RT mediates quorum sensing during development.";
RL Eukaryot. Cell 4:694-702(2005).
RN [7]
RP NOMENCLATURE.
RX PubMed=16762450; DOI=10.1016/j.ejcb.2006.04.011;
RA Vlahou G., Rivero F.;
RT "Rho GTPase signaling in Dictyostelium discoideum: insights from the
RT genome.";
RL Eur. J. Cell Biol. 85:947-959(2006).
CC -!- FUNCTION: Plays a role in cell growth. Hydrolyzes membrane
CC phospholipids, such as PtdCho free headgroup and PtdOH (phosphatidic
CC acid; signaling molecule on its own). Involved in the inhibition of
CC actin-based motility and endocytosis. Its inhibition causes complete
CC collapse of F-actin organization. {ECO:0000269|PubMed:15769249,
CC ECO:0000269|PubMed:6498208, ECO:0000269|PubMed:8394342}.
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 -!- ACTIVITY REGULATION: Inhibited by butan-1-ol.
CC {ECO:0000269|PubMed:15769249}.
CC -!- DEVELOPMENTAL STAGE: Expressed consistently in both vegetative and
CC developing cells. {ECO:0000269|PubMed:15821129}.
CC -!- SIMILARITY: Belongs to the phospholipase D family. {ECO:0000305}.
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DR EMBL; AAFI02000040; EAL66812.1; -; Genomic_DNA.
DR RefSeq; XP_640776.1; XM_635684.1.
DR AlphaFoldDB; Q54UK0; -.
DR SMR; Q54UK0; -.
DR STRING; 44689.DDB0231506; -.
DR PaxDb; Q54UK0; -.
DR EnsemblProtists; EAL66812; EAL66812; DDB_G0281031.
DR GeneID; 8622829; -.
DR KEGG; ddi:DDB_G0281031; -.
DR dictyBase; DDB_G0281031; pldA.
DR eggNOG; KOG1329; Eukaryota.
DR HOGENOM; CLU_264129_0_0_1; -.
DR InParanoid; Q54UK0; -.
DR OMA; LRSMDEW; -.
DR BRENDA; 3.1.4.4; 1939.
DR Reactome; R-DDI-1483166; Synthesis of PA.
DR Reactome; R-DDI-2029485; Role of phospholipids in phagocytosis.
DR Reactome; R-DDI-9013149; RAC1 GTPase cycle.
DR Reactome; R-DDI-9013404; RAC2 GTPase cycle.
DR PRO; PR:Q54UK0; -.
DR Proteomes; UP000002195; Chromosome 3.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0070290; F:N-acylphosphatidylethanolamine-specific phospholipase D activity; IEA:UniProtKB-EC.
DR GO; GO:0004630; F:phospholipase D activity; ISS:dictyBase.
DR GO; GO:0009395; P:phospholipid catabolic process; IBA:GO_Central.
DR GO; GO:0006644; P:phospholipid metabolic process; ISS:dictyBase.
DR InterPro; IPR025202; PLD-like_dom.
DR InterPro; IPR001736; PLipase_D/transphosphatidylase.
DR InterPro; IPR015679; PLipase_D_fam.
DR PANTHER; PTHR18896; PTHR18896; 2.
DR Pfam; PF00614; PLDc; 1.
DR Pfam; PF13091; PLDc_2; 1.
DR SMART; SM00155; PLDc; 2.
DR PROSITE; PS50035; PLD; 2.
PE 2: Evidence at transcript level;
KW Coiled coil; Hydrolase; Lipid degradation; Lipid metabolism;
KW Reference proteome; Repeat.
FT CHAIN 1..1269
FT /note="Phospholipase D A"
FT /id="PRO_0000367470"
FT DOMAIN 435..462
FT /note="PLD phosphodiesterase 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT DOMAIN 704..731
FT /note="PLD phosphodiesterase 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT REGION 55..121
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 222..269
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 300..320
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 810..966
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 983..1007
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1116..1167
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 131..192
FT /evidence="ECO:0000255"
FT COILED 803..835
FT /evidence="ECO:0000255"
FT COILED 1059..1096
FT /evidence="ECO:0000255"
FT COMPBIAS 810..944
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 989..1005
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 440
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT ACT_SITE 442
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT ACT_SITE 447
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT ACT_SITE 709
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT ACT_SITE 711
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT ACT_SITE 716
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
SQ SEQUENCE 1269 AA; 142142 MW; F719CC299648C287 CRC64;
MSNNSKSPPN EQHQQQPHPP DVLVQLTESF QHFFQSLSPQ YQSMTSLPSI NKDSYTSVGS
APTTNNNSNS NSNSNSSNRS LNNSGSSNSG GGGSNSNKKV NNNNNNNNNN NNNNLQSPTQ
SQFPYHYQYS SKALHDFEEK RKLLIEQLKS VKINLDTQCD DDPISFIKIR MELTKVKTSL
ETELKSLDEL LHTTSEVEEP NPTPIDSITS LLTMIMPSSI SNSVTNNTPS SATPLTLSNN
NNYTSSSLAT SPTTNSSSSS SSSSSSSSTH YYNSSISSNS LSSNLPPSSI PILNTSNNKN
SYPNSIIPQG TPLDNPDPNL PRFPQRDHIS VKLYVDCDDY FAASAQAIEN ATREVFITAW
FLSPEVYLIR FPSLDERYRL DNLLKRKAMQ GVKIFIILWD ETKIATFKGS KRAKDKLEEL
HTNIKVIKHP PIIPIYWSHH QKTLIIDQEI AFVGGVDFCF GRFDTWCHHL IDVNSTLWKG
KDYYNPILGD MGDILVPFED SVDRKKIPRM PWHDVMAGVN GLAARDVALN FILRWNHHKD
DYYPQLYFDT TPLSPVGTSQ CQLLRSMDEW SGGGRIERSI HTAYVQAIED ANHYIYIENQ
NFVSTHAPNV WNQISFEIVK RIKRAIRKKE VFRVFIVIPC QQDGKVEETQ IKGLMHWQYS
TIIRGENTIM KLLRRDCPDV DLTEYICFLS LRTHAFLEGT FVTEQIYVHS KLMIVDDRTI
IVGSANINDR SLIGERDSEL AFIIRDEIDT IQTKMNGQDY IASRLVFNFR LRLWKEHLGL
LPQINYPPHD QINNDINNIV NLNNNNNSNI NNNINNNNNE INNNNNNNNN NNSNEINNNN
SDGILNNSNS FHHGSVSDNL PPLNPSSNLN SSNKKLPTTT TAAAAATTTT TTTTTTTTTN
GTGTTNKQKT SHHRSNSFQG LVLQSPGSNR SNLSSPQDSP QDSPRLKNLA EEISPPPTEQ
HQHQSPITDI NLILENVDTI IHSNEQLPPP PSSTTPPPPP PPLTTTDSVI IEDYKSDGGN
LNIENNNSNN TILTNAATSM NNSTSSLSST SLPTTTTTTT AQQQQQQQQQ QQQQQQQQQQ
QQQQQQQQQQ QQQQQQPSQQ QQQQQQQLSQ QQQLQIKKKR SSISPSTSSN KLLLSGNGSG
DSIRVVTDSG SSPRGQPRSM SSLHDHADSS YCQKSNIDLI DPTCSDFYFG VWIATAASNT
RIYDTVFPAI PKNSIKTCEQ FAQLQKIPVS LADSKLLSEV RGNLVFHPLD FLEGEDLQPS
FLFTDDLFQ
