Q02158 (PLC_DICDI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase
EC=3.1.4.11

Alternative name(s):
Phosphoinositide phospholipase C
Short name=PLC

Gene names

Name:	plc
Synonyms:	pipA
ORF Names:	DDB_G0292736

Organism

Dictyostelium discoideum (Slime mold)

Taxonomic identifier

44689 [NCBI]

Taxonomic lineage

Eukaryota › Amoebozoa › Mycetozoa › Dictyosteliida › Dictyostelium

Protein attributes

Sequence length	801 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes.
Catalytic activity	1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O = 1D-myo-inositol 1,4,5-trisphosphate + diacylglycerol.
Developmental stage	Expressed at all stages; increase in expression in the culminating fruiting body and during starvation.
Sequence similarities	Contains 1 C2 domain. Contains 1 EF-hand domain. Contains 1 PI-PLC X-box domain. Contains 1 PI-PLC Y-box domain.
Caution	It is uncertain whether Met-1 is the initiator.

Ontologies

Keywords
Biological process	Lipid degradation
Ligand	Calcium
Molecular function	Hydrolase Transducer
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	inositol trisphosphate biosynthetic process Inferred from mutant phenotype. Source: dictyBase intracellular signal transduction Inferred from electronic annotation. Source: InterPro lipid catabolic process Inferred from electronic annotation. Source: UniProtKB-KW negative regulation of chemotaxis Inferred from mutant phenotype. Source: dictyBase sporulation resulting in formation of a cellular spore Traceable author statement Ref.2. Source: dictyBase
Molecular function	calcium ion binding Inferred from electronic annotation. Source: InterPro phosphatidylinositol phospholipase C activity Inferred from mutant phenotype Ref.1. Source: dictyBase signal transducer activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 801	801	1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase		PRO_0000088509
Regions
	Domain	206 – 241	36	EF-hand
	Domain	322 – 464	143	PI-PLC X-box
	Domain	542 – 652	111	PI-PLC Y-box
	Domain	661 – 765	105	C2
	Calcium binding	490 – 501	12	Potential
Sites
	Active site	337	1	By similarity
	Active site	382	1	By similarity
	Binding site	463	1	Substrate By similarity
	Binding site	566	1	Substrate By similarity
	Binding site	593	1	Substrate By similarity
Amino acid modifications
	Modified residue	524	1	Phosphoserine Potential
	Modified residue	531	1	Phosphothreonine; by PKA and PKG Potential

Sequences

	Sequence		Length	Mass (Da)
	Q02158 [UniParc]. Last modified October 1, 1993. Version 1. Checksum: DB4FA8C829812DD9	FASTA	801	91,280
	10 20 30 40 50 60 MDTLTNSQDY SNVDLSLESL AEELYNIQSF NKDVILDSFD IDDYDHTQLD TTIDFNKFKI 70 80 90 100 110 120 GLTILKISSK GKPQKKKLIF DLARNQIVCG KKKKVNFSEI DEIRVGHKTN IFNQFKSSKN 130 140 150 160 170 180 LKEDIESIQQ SFSILFSGNL RKTMDFVCSD IPERRQIVSA LYHVVQESKS VNNEYNFVKR 190 200 210 220 230 240 EWDRVGKDSI DFSTLKKILA RLNFTTSDAV LHNLMKFSDS NSDYHLDFSE FSNLLKLLRS 250 260 270 280 290 300 HPEMKPVFYK YNGGNGEWVP IQGMIDFFRI EQSEVWTVEQ CRDLIKKYHH ERLDCISFEN 310 320 330 340 350 360 FEEFICGEAN LAQYPHTSTV YQDTSKPLSY YFINSSHNTY LSGHQLKGLS TSEMYTNTLR 370 380 390 400 410 420 QGCKCVELDV WDGNDGDPII FHGNTLTSQI KFSHVCETIK ARGFETSPYP VILSLEVHCS 430 440 450 460 470 480 VPQQIMMANH MKEIFGEMLP TPLPEGTKEL PTLDSLKYKI LLKGHTSHTH VSAVGNSSAS 490 500 510 520 530 540 SSQSNIQTDD NDDDGAVDLT EYDEVDDRSA SSSSSSFSLS FGSSGKKKKI TKIKIAPEFE 550 560 570 580 590 600 ELIYLVSHGF KSGNTTKEIP SYKIHSLVEE KVKQLVQSEP REVVEASQNH LLRVYPRGTR 610 620 630 640 650 660 FDSSNFDPMP GWSIGCQLAA LNQQTSSEPM WINDGMFSDN GGCGYVLKPP CLLPGECETY 670 680 690 700 710 720 DPTSPERIKS SKYSRLIVNV ISARQLPKYT KSTKGEVIDP YVTLSIVGTH FDQKVEKTKV 730 740 750 760 770 780 IDNNGFNPHW GEEFEFPLYN SQLSMLLIRV DDKDKVGHNR IGHHCIRVEN IRPGYRILKL 790 800 KNNFNRTIPL ANLLCKFTFV E

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning and expression of a phosphoinositide-specific phospholipase C of Dictyostelium discoideum." Drayer A.L., van Haastert P.J. J. Biol. Chem. 267:18387-18392(1992) [PubMed: 1326523] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: NC-4.
[2]	"Identification of genes dependent on the MADS box transcription factor SrfA in Dictyostelium discoideum development." Escalante R., Iranfar N., Sastre L., Loomis W.F. Eukaryot. Cell 3:564-566(2004) [PubMed: 15075287] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"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.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M95783 mRNA. Translation: AAA33235.1. AY392433 Genomic DNA. Translation: AAQ98875.1. AAFI02000196 Genomic DNA. Translation: EAL61042.1.
PIR	A44165.
RefSeq	XP_629476.1. XM_629474.1.
3D structure databases
ProteinModelPortal	Q02158.
ModBase	Search...
Protein-protein interaction databases
STRING	Q02158.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblProtists	DDB0201656; DDB0201656; DDB_G0292736.
GeneID	8628866.
GenomeReviews	Gene locus plc in contig CM000155_GR.
KEGG	ddi:DDB_G0292736.
Organism-specific databases
dictyBase	DDB_G0292736. plc.
Phylogenomic databases
eggNOG	KOG0169.
GeneTree	EPrGT00050000000740.
OMA	DICEESS.
PhylomeDB	Q02158.
Family and domain databases
InterPro	IPR000008. C2_Ca-dep. IPR008973. C2_Ca/lipid-bd_dom_CaLB. IPR018029. C2_membr_targeting. IPR011992. EF-hand-like_dom. IPR018249. EF_HAND_2. IPR011993. PH_type. IPR001192. Pinositol_PLipase_C. IPR017946. PLC-like_Pdiesterase_TIM-brl. IPR015359. PLipase_C_EF-hand-like. IPR000909. PLipase_C_PInositol-sp_X_dom. IPR001711. PLipase_C_Pinositol-sp_Y. [Graphical view]
Gene3D	G3DSA:1.10.238.10. EF-Hand_type. 1 hit. G3DSA:2.30.29.30. PH_type. 1 hit. G3DSA:3.20.20.190. PLC-like_Pdiesterase_TIM-brl. 2 hits.
KO	K05857.
Pfam	PF00168. C2. 1 hit. PF09279. efhand_like. 1 hit. PF00388. PI-PLC-X. 1 hit. PF00387. PI-PLC-Y. 1 hit. [Graphical view]
PRINTS	PR00390. PHPHLIPASEC.
SMART	SM00239. C2. 1 hit. SM00148. PLCXc. 1 hit. SM00149. PLCYc. 1 hit. [Graphical view]
SUPFAM	SSF49562. C2_CaLB. 1 hit. SSF51695. PLC-like_Pdiesterase_TIM-brl. 1 hit.
PROSITE	PS50004. C2. 1 hit. PS00018. EF_HAND_1. 1 hit. PS50222. EF_HAND_2. 1 hit. PS50007. PIPLC_X_DOMAIN. 1 hit. PS50008. PIPLC_Y_DOMAIN. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PLC_DICDI

Accession

Primary (citable) accession number: Q02158
Secondary accession number(s): Q54CR5

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1993
Last sequence update:	October 1, 1993
Last modified:	November 16, 2011
This is version 101 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)