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P40977 (PLC1_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 126. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase 1
EC=3.1.4.11
Alternative name(s):
Phospholipase C-1
Short name=PLC-1
Gene names
Name:plc1
ORF Names:SPAC22F8.11
OrganismSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) [Reference proteome]
Taxonomic identifier284812 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces ›

Protein attributes

Sequence length899 AA.
Sequence statusComplete.
Protein existenceEvidence at protein 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.

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 8998991-phosphatidylinositol 4,5-bisphosphate phosphodiesterase 1
PRO_0000088513

Regions

Domain330 – 36536EF-hand
Domain441 – 584144PI-PLC X-box
Domain638 – 753116PI-PLC Y-box
Domain769 – 86294C2
Calcium binding343 – 35412 Potential

Sites

Active site4561 By similarity
Active site5001 By similarity
Binding site5821Substrate By similarity
Binding site5841Substrate By similarity
Binding site6661Substrate By similarity
Binding site6931Substrate By similarity

Amino acid modifications

Modified residue831Phosphoserine Ref.4

Experimental info

Sequence conflict4801R → A in CAA58591. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P40977 [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: C7CC935DAB820245

FASTA899102,673
        10         20         30         40         50         60 
MNCEMVTSPE SVNLGDSNRA VSPFCLPDCS ENAVAQTRSK TLDNAALDLP YVGNRKKSEQ 

        70         80         90        100        110        120 
DFFKMLSSRD RDAHSTLRKR SNSLSSFLST KSTSASENKF HGGLNWLSLK LNLLLRLQGR 

       130        140        150        160        170        180 
MNSARTNTSM NPYSCDSNEN LSTLSSVNQN FNSRQLLATI VPESIQNGCS LLRITKKKVR 

       190        200        210        220        230        240 
QRKVSLDPIS GYLMLDKNTG KAYKKLCVDD IKEIRQGRDA RNYREQYKIS SENEKRWFTI 

       250        260        270        280        290        300 
IYCADNKLKA MHMISPTLDA HNQWIMALEG LKTYRLNEFI IGLNLVCHQG EKMIDYSENL 

       310        320        330        340        350        360 
NPWEKLEKEQ SAQLDLGDVH RMCQMLHLNA SMEFLEETFQ KADADHSGKL SFEEFQHFVS 

       370        380        390        400        410        420 
LLKTRSEIVD IFKEYTSGSD KMSLEQFRHF LSTSQKARLD SDSIRTLYVS FCSNDDSKMG 

       430        440        450        460        470        480 
LIEFTSFLLS PHNSPVVPVI QDMSRPLNEY LISSSHNTYL LGKQFGGESS IEGYIRSLQR 

       490        500        510        520        530        540 
GCKCIEIDCW DGPNGPVVCH GHTFTSMIKF NDVIDAIRKY AFVVSPYPLF ISLEIHCCPD 

       550        560        570        580        590        600 
QQRQMVSYMK QAFGDTLVMK PVTANESVLP SPEDLLNKIL LKVKCSATPL HQFSTDILKV 

       610        620        630        640        650        660 
GITDSSTDTT ESSELENSEL TGLRKGKRRM KNIIVQELQQ LAPYARSLKF RNFSLPESKT 

       670        680        690        700        710        720 
YSHIFSFSER TIKKHGKAMV PRLSKHNLRY LCRVYPGPLR VGSTNFNPQV YWRLGVQMVA 

       730        740        750        760        770        780 
LNWQTYDTGL QINDALFIAD PPTGYLLKPP CQRIIGTTVG EEGLPRKIKL TIDVISGQQL 

       790        800        810        820        830        840 
RRARELSNSE TLSPYVEIQV HSMEESPFRW CSKVVHENGF RPFWGETMVY ESIISDDFYS 

       850        860        870        880        890 
MIRFLVHHRG SNGNDSIFAN FTCPIDRLQQ GYRHIRLLDM QGENLLFSSL FLKIKKEDI

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning of the plc1+ gene of Schizosaccharomyces pombe, which encodes a putative phosphoinositide-specific phospholipase C."
Andoh T., Yoko-O T., Matsui Y., Toh-e A.
Yeast 11:179-185(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Growth of a mutant defective in a putative phosphoinositide-specific phospholipase C of Schizosaccharomyces pombe is restored by low concentrations of phosphate and inositol."
Fankhauser H., Schweingruber A.-M., Edenharter E., Schweingruber M.E.
Curr. Genet. 28:199-203(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 972 / ATCC 24843.
[3]"The genome sequence of Schizosaccharomyces pombe."
Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. expand/collapse author list , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 972 / ATCC 24843.
[4]"Phosphoproteome analysis of fission yeast."
Wilson-Grady J.T., Villen J., Gygi S.P.
J. Proteome Res. 7:1088-1097(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83, MASS SPECTROMETRY.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		D38309 Genomic DNA. Translation: BAA07426.1.
X83615 Genomic DNA. Translation: CAA58591.1.
CU329670 Genomic DNA. Translation: CAB52721.1.
PIRS55075.
S51092. S57259.
RefSeqNP_594734.1. NM_001020162.2.

3D structure databases

ProteinModelPortalP40977.
ModBaseSearch...

Protein-protein interaction databases

STRING4896.SPAC22F8.11-1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiSPAC22F8.11.1; SPAC22F8.11.1:pep; SPAC22F8.11.
GeneID2541439.
KEGGspo:SPAC22F8.11.

Organism-specific databases

PomBaseSPAC22F8.11.

Phylogenomic databases

eggNOGNOG149692.
KOK05857.
OMANGPVVCH.
OrthoDBEOG441TKH.

Family and domain databases

Gene3D1.10.238.10. 2 hits.
2.30.29.30. 1 hit.
3.20.20.190. 2 hits.
InterProIPR000008. C2_Ca-dep.
IPR008973. C2_Ca/lipid-bd_dom_CaLB.
IPR018029. C2_membr_targeting.
IPR011992. EF-hand-like_dom.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
IPR011993. PH_like_dom.
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]
PANTHERPTHR10336. PTHR10336. 1 hit.
PfamPF00168. C2. 1 hit.
PF00036. efhand. 1 hit.
PF09279. efhand_like. 1 hit.
PF00388. PI-PLC-X. 1 hit.
PF00387. PI-PLC-Y. 1 hit.
[Graphical view]
PRINTSPR00390. PHPHLIPASEC.
SMARTSM00239. C2. 1 hit.
SM00054. EFh. 2 hits.
SM00148. PLCXc. 1 hit.
SM00149. PLCYc. 1 hit.
[Graphical view]
SUPFAMSSF49562. C2_CaLB. 1 hit.
SSF51695. PLC-like_Pdiesterase_TIM-brl. 1 hit.
PROSITEPS50004. 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]
ProtoNetSearch...

Other

NextBio20802541.

Entry information

Entry namePLC1_SCHPO
AccessionPrimary (citable) accession number: P40977
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: May 1, 2013
This is version 126 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Schizosaccharomyces pombe

Schizosaccharomyces pombe: entries and gene names

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents