Reviewed, UniProtKB/Swiss-Prot Q54UK0 (PLDA_DICDI)

Names and origin

Protein names

Recommended name:
    Phospholipase D A
    EC=3.1.4.4
Alternative name(s):
    Phosphatase D1
      Short name=PLD 1

Gene names

Name:	pldA
Synonyms:	pld1
ORF Names:	DDB_G0281031

Organism

Dictyostelium discoideum (Slime mold) [Complete proteome]

Taxonomic identifier

44689 [NCBI]

Taxonomic lineage

Eukaryota › Amoebozoa › Mycetozoa › Dictyosteliida › Dictyostelium

Protein attributes

Sequence length	1269 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Function	Plays a role in cell growth. Hydrolyzes membrane phospholipids, such as PtdCho free headgroup and PtdOH (phosphatidic acid; signaling molecule on its own). Involved in the inhibition of actin-based motility and endocytosis. Its inhibition causes complete collapse of F-actin organization. Ref.2 Ref.3 Ref.5
Catalytic activity	A phosphatidylcholine + H2O = choline + a phosphatidate.
Enzyme regulation	Inhibited by butan-1-ol. Ref.5
Developmental stage	Expressed consistently in both vegetative and developing cells. Ref.6
Sequence similarities	Belongs to the phospholipase D family. Contains 2 PLD phosphodiesterase domains.

Ontologies

Keywords
Biological process	Lipid degradation
Domain	Coiled coil Repeat
Molecular function	Hydrolase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	lipid catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	NAPE-specific phospholipase D activity Inferred from electronic annotation. Source: EC phospholipase D activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1269	1269	Phospholipase D A		PRO_0000367470
Regions
	Domain	435 – 462	28	PLD phosphodiesterase 1
	Domain	704 – 731	28	PLD phosphodiesterase 2
	Coiled coil	131 – 192	62	Potential
	Coiled coil	803 – 835	33	Potential
	Coiled coil	1059 – 1096	38	Potential
	Compositional bias	90 – 93	4	Poly-Gly
	Compositional bias	101 – 114	14	Poly-Asn
	Compositional bias	239 – 242	4	Poly-Asn
	Compositional bias	256 – 268	13	Poly-Ser
	Compositional bias	801 – 819	19	Poly-Asn
	Compositional bias	822 – 834	13	Poly-Asn
	Compositional bias	837 – 840	4	Poly-Asn
	Compositional bias	878 – 881	4	Poly-Thr
	Compositional bias	882 – 886	5	Poly-Ala
	Compositional bias	887 – 899	13	Poly-Thr
	Compositional bias	988 – 991	4	Poly-Pro
	Compositional bias	996 – 1002	7	Poly-Pro
	Compositional bias	1054 – 1060	7	Poly-Thr
	Compositional bias	1062 – 1096	35	Poly-Gln
	Compositional bias	1099 – 1107	9	Poly-Gln
	Compositional bias	1110 – 1115	6	Poly-Gln
Sites
	Active site	440	1	Potential
	Active site	442	1	Potential
	Active site	447	1	Potential
	Active site	709	1	Potential
	Active site	711	1	Potential
	Active site	716	1	Potential

Sequences

	Sequence		Length	Mass (Da)
	Q54UK0-1 [UniParc]. Last modified May 24, 2005. Version 1. Checksum: F719CC299648C287	FASTA	1,269	142,142
	10 20 30 40 50 60 MSNNSKSPPN EQHQQQPHPP DVLVQLTESF QHFFQSLSPQ YQSMTSLPSI NKDSYTSVGS 70 80 90 100 110 120 APTTNNNSNS NSNSNSSNRS LNNSGSSNSG GGGSNSNKKV NNNNNNNNNN NNNNLQSPTQ 130 140 150 160 170 180 SQFPYHYQYS SKALHDFEEK RKLLIEQLKS VKINLDTQCD DDPISFIKIR MELTKVKTSL 190 200 210 220 230 240 ETELKSLDEL LHTTSEVEEP NPTPIDSITS LLTMIMPSSI SNSVTNNTPS SATPLTLSNN 250 260 270 280 290 300 NNYTSSSLAT SPTTNSSSSS SSSSSSSSTH YYNSSISSNS LSSNLPPSSI PILNTSNNKN 310 320 330 340 350 360 SYPNSIIPQG TPLDNPDPNL PRFPQRDHIS VKLYVDCDDY FAASAQAIEN ATREVFITAW 370 380 390 400 410 420 FLSPEVYLIR FPSLDERYRL DNLLKRKAMQ GVKIFIILWD ETKIATFKGS KRAKDKLEEL 430 440 450 460 470 480 HTNIKVIKHP PIIPIYWSHH QKTLIIDQEI AFVGGVDFCF GRFDTWCHHL IDVNSTLWKG 490 500 510 520 530 540 KDYYNPILGD MGDILVPFED SVDRKKIPRM PWHDVMAGVN GLAARDVALN FILRWNHHKD 550 560 570 580 590 600 DYYPQLYFDT TPLSPVGTSQ CQLLRSMDEW SGGGRIERSI HTAYVQAIED ANHYIYIENQ 610 620 630 640 650 660 NFVSTHAPNV WNQISFEIVK RIKRAIRKKE VFRVFIVIPC QQDGKVEETQ IKGLMHWQYS 670 680 690 700 710 720 TIIRGENTIM KLLRRDCPDV DLTEYICFLS LRTHAFLEGT FVTEQIYVHS KLMIVDDRTI 730 740 750 760 770 780 IVGSANINDR SLIGERDSEL AFIIRDEIDT IQTKMNGQDY IASRLVFNFR LRLWKEHLGL 790 800 810 820 830 840 LPQINYPPHD QINNDINNIV NLNNNNNSNI NNNINNNNNE INNNNNNNNN NNSNEINNNN 850 860 870 880 890 900 SDGILNNSNS FHHGSVSDNL PPLNPSSNLN SSNKKLPTTT TAAAAATTTT TTTTTTTTTN 910 920 930 940 950 960 GTGTTNKQKT SHHRSNSFQG LVLQSPGSNR SNLSSPQDSP QDSPRLKNLA EEISPPPTEQ 970 980 990 1000 1010 1020 HQHQSPITDI NLILENVDTI IHSNEQLPPP PSSTTPPPPP PPLTTTDSVI IEDYKSDGGN 1030 1040 1050 1060 1070 1080 LNIENNNSNN TILTNAATSM NNSTSSLSST SLPTTTTTTT AQQQQQQQQQ QQQQQQQQQQ 1090 1100 1110 1120 1130 1140 QQQQQQQQQQ QQQQQQPSQQ QQQQQQQLSQ QQQLQIKKKR SSISPSTSSN KLLLSGNGSG 1150 1160 1170 1180 1190 1200 DSIRVVTDSG SSPRGQPRSM SSLHDHADSS YCQKSNIDLI DPTCSDFYFG VWIATAASNT 1210 1220 1230 1240 1250 1260 RIYDTVFPAI PKNSIKTCEQ FAQLQKIPVS LADSKLLSEV RGNLVFHPLD FLEGEDLQPS FLFTDDLFQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The genome of the social amoeba Dictyostelium discoideum." Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T., Lehmann R., Hamlin N. , Davies R., Gaudet P., Fey P., Pilcher K., Chen G., Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N., Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E., Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N., Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D., Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T., Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D., Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A., Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M., Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A., Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y., Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C., Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R., Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A. Nature 435:43-57(2005) [PubMed: 15875012] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: AX4.
[2]	"Comparison of the hydrolysis of phosphatidylethanolamine and phosphatidyl(N-acyl)ethanolamine in Dictyostelium discoideum amoebae." Ellingson J.S., Dischinger H.C. Biochim. Biophys. Acta 796:155-162(1984) [PubMed: 6498208] [Abstract] Cited for: FUNCTION.
[3]	"Developmentally regulated changes in 1,2-diacylglycerol in Dictyostelium. Regulation by light and G proteins." Cubitt A.B., Dharmawardhane S., Firtel R.A. J. Biol. Chem. 268:17431-17439(1993) [PubMed: 8394342] [Abstract] Cited for: FUNCTION.
[4]	"A distant evolutionary relationship between GPI-specific phospholipase D and bacterial phosphatidylcholine-preferring phospholipase C." Rigden D.J. FEBS Lett. 569:229-234(2004) [PubMed: 15225639] [Abstract] Cited for: NOMENCLATURE.
[5]	"Phospholipase D activity is essential for actin localization and actin-based motility in Dictyostelium." Zouwail S., Pettitt T.R., Dove S.K., Chibalina M.V., Powner D.J., Haynes L., Wakelam M.J.O., Insall R.H. Biochem. J. 389:207-214(2005) [PubMed: 15769249] [Abstract] Cited for: ENZYME REGULATION, FUNCTION.
[6]	"PldB, a putative phospholipase D homologue in Dictyostelium discoideum mediates quorum sensing during development." Chen Y., Rodrick V., Yan Y., Brazill D. Eukaryot. Cell 4:694-702(2005) [PubMed: 15821129] [Abstract] Cited for: DEVELOPMENTAL STAGE.
[7]	"Rho GTPase signaling in Dictyostelium discoideum: insights from the genome." Vlahou G., Rivero F. Eur. J. Cell Biol. 85:947-959(2006) [PubMed: 16762450] [Abstract] Cited for: NOMENCLATURE.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AAFI02000040 Genomic DNA. Translation: EAL66812.1.
RefSeq	XP_640776.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q54UK0.
Genome annotation databases
GeneID	3391857.
GenomeReviews	Gene locus pldA in contig CM000152_GR.
KEGG	ddi:DDB_0231506.
Organism-specific databases
dictyBase	DDB_G0281031. pldA.
Family and domain databases
InterPro	IPR015679. Phospholipase_D. IPR001736. PLipase_D/transphosphatidylase. [Graphical view]
PANTHER	PTHR18896. Phospholipase_D. 1 hit.
Pfam	PF00614. PLDc. 2 hits. [Graphical view]
SMART	SM00155. PLDc. 2 hits. [Graphical view]
PROSITE	PS50035. PLD. 2 hits. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PLDA_DICDI

Accession

Primary (citable) accession number: Q54UK0

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 24, 2009
Last sequence update:	May 24, 2005
Last modified:	September 22, 2009
This is version 34 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)