1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase 1

Preferred order of sections

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 signal transduction Inferred from electronic annotation. Source: InterPro lipid catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	calcium ion binding Inferred from electronic annotation. Source: InterPro phosphatidylinositol 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)

Tools

O13433 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: D54D687D53A2829B
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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

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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.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	Y13975 Genomic DNA. Translation: CAA74308.1.
PIR	T18257.
3D structure databases
ProteinModelPortal	O13433.
ModBase	Search...
Protein-protein interaction databases
STRING	O13433.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
InterPro	IPR000008. C2_Ca-dep. IPR008973. C2_Ca/lipid-bd_dom_CaLB. IPR011992. EF-hand-like_dom. IPR011993. PH_type. IPR001192. Pinositol_PLipase_C. IPR017946. PLC-like_Pdiesterase_TIM-brl. 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.
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]
SUPFAM	SSF49562. C2_CaLB. 1 hit. SSF51695. PLC-like_Pdiesterase_TIM-brl. 1 hit.
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_CANAX

Accession

Primary (citable) accession number: O13433

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1999
Last sequence update:	January 1, 1998
Last modified:	October 19, 2011
This is version 70 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Family and domain databases

Entry information

Relevant documents