Reviewed, UniProtKB/Swiss-Prot O13433 (PLC1_CANAL)

Names and origin

Protein names

Recommended name:
    1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase 1
    EC=3.1.4.11
Alternative name(s):
    Phosphoinositide phospholipase C
    Phospholipase C-1
      Short name=PLC-1

Gene names

Name:

PLC1

Organism

Candida albicans (Yeast)

Taxonomic identifier

5476 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › mitosporic Saccharomycetales › Candida

Protein attributes

Sequence length	1099 AA.
Sequence status	Complete.
Protein existence	Predicted.

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.
Sequence similarities	Contains 1 C2 domain. Contains 1 PI-PLC X-box domain. Contains 1 PI-PLC Y-box domain.

Ontologies

Keywords
Biological process	Lipid degradation
Molecular function	Hydrolase Transducer
Gene Ontology (GO)
Biological process	intracellular signaling cascade Inferred from electronic annotation. Source: InterPro lipid catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	phosphoinositide phospholipase C activity Inferred from electronic annotation. Source: EC 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 – 1099	1099	1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase 1		PRO_0000088512
Regions
	Domain	566 – 726	161	PI-PLC X-box
	Domain	794 – 912	119	PI-PLC Y-box
	Domain	938 – 1066	129	C2
	Compositional bias	90 – 102	13	Poly-Ser
	Compositional bias	239 – 243	5	Poly-Thr
	Compositional bias	517 – 520	4	Poly-Asp
	Compositional bias	619 – 623	5	Poly-Thr
	Compositional bias	629 – 632	4	Poly-Asp
	Compositional bias	743 – 760	18	Poly-Thr
	Compositional bias	918 – 921	4	Poly-Ser
Sites
	Active site	579	1	By similarity
	Active site	642	1	By similarity
	Binding site	724	1	Substrate By similarity
	Binding site	726	1	Substrate By similarity
	Binding site	823	1	Substrate By similarity
	Binding site	852	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	O13433-1 [UniParc]. Last modified January 1, 1998. Version 1. Checksum: D54D687D53A2829B	FASTA	1,099	124,592
	10 20 30 40 50 60 MLESLNRRNS IDSNQADNDN DNDNHSNDEL SPSELYYSPS GSPPKSQLLL RKSSSPSSYS 70 80 90 100 110 120 PIKSDLPNIY SHLRSNDSES PPQPSPKQQS SLSSSSSSSS SSNTKSSTTK NIFKKLLRIN 130 140 150 160 170 180 KSSDNIDESR SIVSNNGGSP MSDSTTVTST LSTDTAPKRG KSIQRSQILH HTDSDSLYLE 190 200 210 220 230 240 NQIELRPEIS KSIGNIKIPS IFTNDGMPLL KISHKSKKRI LFWIDPSCFK FSWRMANSTT 250 260 270 280 290 300 TTTSATTSAT TSGLPQGITN TTALSNSAII STPAIATSAI HRLSITNRTT HEFVLDDIKS 310 320 330 340 350 360 IYIQNEGSGY REELNISQKL EKNWITIIYF NHKKNSLKSL HLITDNDHDF KKLISAIYNL 370 380 390 400 410 420 KQLRSQLAKE FLIDLNELDE NYVKMLLNKE LLAGDNGNVD GNEVDIRKSH KHVREFLSFN 430 440 450 460 470 480 DILKYSKRLN INVNTNHLQQ IFDQVLLLSS ATTEKPVSTP LFEKGLNFEQ FKQFVSILKD 490 500 510 520 530 540 RKDLQEIWDS LAQGKEVLQF DEIKNFIINI QKENFSDDDD NSTINLIFQK YCSNDNGWNK 550 560 570 580 590 600 ESLNEYLLSS YSTPYREITQ TQTNYYDYPL NEYFISSSHN TYLTGRQVAG DSSVEGYIRT 610 620 630 640 650 660 LQRGCRCVEI DIWNGDSNTT TTTVIGTKDD DDKNEYEPIV NHGRTFTKPI SFANVIRAIK 670 680 690 700 710 720 KFAFIVSPWP LILSLEIHCS PECQIKVVNI LKDILGENMI IAPIDIDSVI LPSPAELKHK 730 740 750 760 770 780 FIIKVKKTTS FQNLIETENG SFTTSTTTTT TTTTTTTTAT SLSEDNENNK SNSSSTSSFI 790 800 810 820 830 840 IRRRKNKSPK IINELSNLGI YTQGIKFRNF SLPESKTFNH CFSLGEKSIN RMIKDDDKKI 850 860 870 880 890 900 SLDKHNRRYL MRVYPSGTRL KSSNFNPLPY WSHGVQMVAT NWQTYDLGQQ LNEALFENKI 910 920 930 940 950 960 FQGYVLKPSV LRKPTLKSSS SNVDTRTSLT TTNSKTIRFN FEIISGHQLP KFPKDDYKDQ 970 980 990 1000 1010 1020 AINPYISFEI IGAQDVQWDN NDSSPIAPTT SSSPFIRTTK IIRENGFNPN FNTKFSGSII 1030 1040 1050 1060 1070 1080 TTTNDLIFIK FVVYASTSLN YPDYGENFPI AILVTKLNYL KQGYRYIYLN DLLGEQLVYS 1090 SIFIKIEYDE DLLNEFINK

References

[1]

"Genetic characterization of a phospholipase C gene from Candida albicans: presence of homologous sequences in Candida species other than Candida albicans." Bennett D.E., McCreary C.E., Coleman D.C. Microbiology 144:55-72(1998) [PubMed: 9467900] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 132A.

Cross-references

Sequence databases
EMBL GenBank DDBJ	Y13975 Genomic DNA. Translation: CAA74308.1.
PIR	T18257.
3D structure databases
SMR	O13433. Positions 470-1090.
ModBase	Search...
Enzyme and pathway databases
BRENDA	3.1.4.11. 1124.
Family and domain databases
InterPro	IPR000008. C2_Ca-dep. IPR008973. C2_Ca/lipid-bd_dom_CaLB. IPR001192. Phospholipase_C_Pinositol-sp_C. IPR001711. Phospholipase_C_Pinositol-sp_Y. IPR017946. PLC-like_Pdiesterase_TIM-brl. IPR000909. PLipase_C_PInositol-sp_X_dom. [Graphical view]
Gene3D	G3DSA:3.20.20.190. PLC-like_Pdiesterase_TIM-brl. 1 hit.
Pfam	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]
PROSITE	PS50004. C2. False negative. PS50007. PIPLC_X_DOMAIN. 1 hit. PS50008. PIPLC_Y_DOMAIN. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PLC1_CANAL

Accession

Primary (citable) accession number: O13433

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1999
Last sequence update:	January 1, 1998
Last modified:	January 19, 2010
This is version 58 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)