Reviewed, UniProtKB/Swiss-Prot Q54WR4 (PLDB_DICDI)

Names and origin

Protein names

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

Gene names

Name:	pldB
Synonyms:	pld1
ORF Names:	DDB_G0279483

Organism

Dictyostelium discoideum (Slime mold) [Complete proteome]

Taxonomic identifier

44689 [NCBI]

Taxonomic lineage

Eukaryota › Amoebozoa › Mycetozoa › Dictyosteliida › Dictyostelium

Protein attributes

Sequence length	1216 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Function	Plays a role in cell growth. Hydrolyzes membrane phospholipids, such as PtdCho (phosphatidylcholine), producing the 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. Plays an important role in cell migration by localizing along the anterior cell membrane. Overexpression leads to the inability to aggregate even at higher cell density. Also known as a negative regulator of quorum sensing. Ref.2 Ref.3 Ref.5 Ref.6
Catalytic activity	A phosphatidylcholine + H2O = choline + a phosphatidate.
Enzyme regulation	Inhibited by butan-1-ol. Ref.5
Subcellular location	Cytoplasmic vesicle. Cytoplasm › cell cortex. Note: In migrating cells, localized at the protruding regions of pseudopodia. Ref.8
Developmental stage	Not expressed in vegetative cells. Expression is apparent by 8 hours and peaked by 16 hours. Becomes present during aggregation and throughout development. Ref.6
Disruption phenotype	Null cells show a motility defect; migration speed of vegetative cells is reduced to 73% of that of the wild-type, an aggregation ability at lower cell density and an ability to initiate and finish aggregation rapidly. Have altered cAR1 expression. Ref.6 Ref.8
Sequence similarities	Belongs to the phospholipase D family. Contains 2 EF-hand domains. Contains 1 PH domain. Contains 2 PLD phosphodiesterase domains.

Ontologies

Keywords
Biological process	Lipid degradation
Cellular component	Cytoplasm Cytoplasmic vesicle
Domain	Repeat
Ligand	Calcium
Molecular function	Hydrolase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	cellular component movement Ref.8 Inferred from genetic interaction. Source: dictyBase lipid catabolic process Inferred from electronic annotation. Source: UniProtKB-KW multicellular organismal development Ref.6 Inferred from mutant phenotype. Source: dictyBase
Cellular component	cell cortex Ref.8 Inferred from direct assay. Source: dictyBase cytoplasmic membrane-bounded vesicle Inferred from electronic annotation. Source: UniProtKB-SubCell pseudopodium Ref.8 Inferred from direct assay. Source: dictyBase vacuole Inferred from direct assay. Source: dictyBase
Molecular function	NAPE-specific phospholipase D activity Inferred from electronic annotation. Source: EC calcium ion binding Inferred from electronic annotation. Source: UniProtKB-KW 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 – 1216	1216	Phospholipase D B		PRO_0000367471
Regions
	Domain	196 – 231	36	EF-hand 1
	Domain	232 – 267	36	EF-hand 2
	Domain	347 – 462	116	PH
	Domain	585 – 612	28	PLD phosphodiesterase 1
	Domain	1036 – 1063	28	PLD phosphodiesterase 2
	Calcium binding	209 – 220	12	Potential
	Compositional bias	384 – 389	6	Poly-Lys
	Compositional bias	416 – 419	4	Poly-Lys
	Compositional bias	843 – 848	6	Poly-Asn
Sites
	Active site	590	1	Potential
	Active site	592	1	Potential
	Active site	597	1	Potential
	Active site	1041	1	Potential
	Active site	1043	1	Potential
	Active site	1048	1	Potential

Sequences

	Sequence		Length	Mass (Da)
	Q54WR4-1 [UniParc]. Last modified May 24, 2005. Version 1. Checksum: 895DB744505DE04D	FASTA	1,216	140,700
	10 20 30 40 50 60 MNLSQEHAIN QNLHKNQKNE EKIEKKTINK DGRGQMNYDG EEGQGEKSRF QKMVENEKIE 70 80 90 100 110 120 EPQQKDENIP NTDVIERKEV GVIERINSED VPILMTDNAT DYKVLQHNLK KGKVSKKSKE 130 140 150 160 170 180 QIEQISKQEE NDMLEYLKNY KSNEEFTIQL EDLLSFETYF SRDELHLLYR EFKTISKSGM 190 200 210 220 230 240 FMSKEDFISK LTPFSRNADL TISLMNAIDR NGDQKIAFPE FVQALSIMCR GTKKERLRFT 250 260 270 280 290 300 FEICDFNGDS LVSRDEVYST VKAISDIFSK FGYSKDKFGD PSEAVDSIFS SGLTTNGIYL 310 320 330 340 350 360 HNKKELTLNE FLERGELNPD LSKCFGMFDY FYLKFIGQID LLFKDKEINM NGQLTKIKPK 370 380 390 400 410 420 TIFNFNISHR RTLSLRDGFL IVYKKKKFKH DEDKPSKVIF LPGSTVKVVV GSQPSKKKKF 430 440 450 460 470 480 LSKKFHNYYG FRVTKGNYNR FFLMENRDEA LNWVNAIRFH SRQGFRFQSF SKVRSNISVE 490 500 510 520 530 540 WFINGSSYYN ELAETIRRAK HEIFITGWWV SPYVYLQRDN GIENMEKSRL DRILTEKAKE 550 560 570 580 590 600 GVKVYVLMWN ETNLGVQLGS RHAKNWLEGC HSNIHVIRHP KRYPLSWSHH QKNAIIDQQI 610 620 630 640 650 660 AFVGGIDICL MRYETSKFQL TDDQGKRFPG KDYGNLLGTV IRTGDPKKDQ FNRRECPRMP 670 680 690 700 710 720 WHDVHTKIVG PSAKDVASNF IQRWNHAIYV ERSNRFQPIL VPKNYTGLPS DDAKPDKWKN 730 740 750 760 770 780 LVSNIRKGFS HVSYGREKPT HYQRAGDNPK VRSHTRQGAF GLQSDQIDNK IDKQKNNSTN 790 800 810 820 830 840 SENSENSYSE FDEEDEEGNQ EEEDEDEFDE FEKDENQKQE NSKIPFNNKP SDAGGLKSKN 850 860 870 880 890 900 YKNNNNNNII ESLKDEESFE LPGTPKIDLN NDKLLKSIYH LSSNMSENSC VVQMVRSICP 910 920 930 940 950 960 WSAGTDVEDS CYKAYLGLIK NAQHFIYIQN LFFISSCGSK LPKNRIALAI LNRVRRAITL 970 980 990 1000 1010 1020 KEKFRVIIMV PISPSGDLAL ASSRMIIGWT NRTISQGGQS ILELLKNEFP DVDLDQYISF 1030 1040 1050 1060 1070 1080 NSIRQWEANG DRIFTEQIYV HSKVLIVDDR VAVIGSCNIN DRSMMGSRDS ELAVVVSDQS 1090 1100 1110 1120 1130 1140 KLLITMNGKP FKVGKFPHTL RVGLWKTHLN LTDSEISSII DPITDNAFIN IWRKTARNNS 1150 1160 1170 1180 1190 1200 IIYKEVFGDC ILENQRRLGI VQKKYIPKTN ELIVQLSQIQ GVLIEYPLDM FCESNLFNEQ 1210 VGIFTAESYV DVSIFT

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: FUNCTION, DISRUPTION PHENOTYPE, 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.
[8]	"Screening of genes involved in cell migration in Dictyostelium." Nagasaki A., Uyeda T.Q.P. Exp. Cell Res. 314:1136-1146(2008) [PubMed: 18164290] [Abstract] Cited for: DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AAFI02000031 Genomic DNA. Translation: EAL67680.1.
RefSeq	XP_641653.1.
3D structure databases
HSSP	HSSP built from PDB template 1S6C based on UniProtKB Q8R426.
SMR	Q54WR4. Positions 153-327, 478-1079.
ModBase	Search...
Genome annotation databases
GeneID	8622060.
KEGG	ddi:DDB_0231507.
Organism-specific databases
dictyBase	DDB_G0279483. pldB.
Phylogenomic databases
eggNOG	KOG1329.
InParanoid	Q54WR4.
OMA	NISHRRT.
PhylomeDB	Q54WR4.
Family and domain databases
InterPro	IPR011992. EF-hand-like_dom. IPR018247. EF_Hand_1_Ca_BS. IPR018249. EF_HAND_2. IPR002048. EF_hand_Ca_bd. IPR011993. PH_type. IPR015679. Phospholipase_D. IPR001849. Pleckstrin_homology. IPR001736. PLipase_D/transphosphatidylase. IPR001125. Recoverin. [Graphical view]
Gene3D	G3DSA:1.10.238.10. EF-Hand_type. 1 hit. G3DSA:2.30.29.30. PH_type. 1 hit.
PANTHER	PTHR18896. Phospholipase_D. 1 hit.
Pfam	PF00614. PLDc. 2 hits. [Graphical view]
PRINTS	PR00450. RECOVERIN.
SMART	SM00054. EFh. 2 hits. SM00233. PH. 1 hit. SM00155. PLDc. 2 hits. [Graphical view]
PROSITE	PS00018. EF_HAND_1. 1 hit. PS50222. EF_HAND_2. 2 hits. PS50003. PH_DOMAIN. 1 hit. PS50035. PLD. 2 hits. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PLDB_DICDI

Accession

Primary (citable) accession number: Q54WR4

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 24, 2009
Last sequence update:	May 24, 2005
Last modified:	February 9, 2010
This is version 44 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)