Reviewed, UniProtKB/Swiss-Prot P40977 (PLC1_SCHPO)

Names and origin

Protein names

Recommended 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

Organism

Schizosaccharomyces pombe (Fission yeast) [Complete proteome]

Taxonomic identifier

4896 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces

Protein attributes

Sequence length	899 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	Lipid degradation
Ligand	Calcium
Molecular function	Hydrolase Transducer
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	cellular response to UV Inferred from mutant phenotype. Source: GeneDB_SPombe inositol lipid-mediated signaling Inferred by curator. Source: GeneDB_SPombe lipid catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytosol Inferred from direct assay. Source: GeneDB_SPombe nucleus Inferred from direct assay. Source: GeneDB_SPombe
Molecular function	calcium ion binding Inferred from electronic annotation. Source: UniProtKB-KW phosphoinositide phospholipase C activity Ref.1 Traceable author statement. Source: GeneDB_SPombe protein binding Inferred from physical interaction. Source: GeneDB_SPombe 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 – 899	899	1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase 1		PRO_0000088513
Regions
	Domain	330 – 365	36	EF-hand
	Domain	441 – 584	144	PI-PLC X-box
	Domain	638 – 753	116	PI-PLC Y-box
	Domain	769 – 862	94	C2
	Calcium binding	343 – 354	12	Potential
Sites
	Active site	456	1	By similarity
	Active site	500	1	By similarity
	Binding site	582	1	Substrate By similarity
	Binding site	584	1	Substrate By similarity
	Binding site	666	1	Substrate By similarity
	Binding site	693	1	Substrate By similarity
Amino acid modifications
	Modified residue	83	1	Phosphoserine Ref.4
Experimental info
	Sequence conflict	480	1	R → A in CAA58591. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P40977-1 [UniParc]. Last modified February 1, 1995. Version 1. Checksum: C7CC935DAB820245	FASTA	899	102,673
	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

References

	« Hide 'large scale' referencesShow '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: 7732727] [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: 8590474] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 38366 / 972.
[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. , 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: 11859360] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 38366 / 972.
[4]	"Phosphoproteome analysis of fission yeast." Wilson-Grady J.T., Villen J., Gygi S.P. J. Proteome Res. 7:1088-1097(2008) [PubMed: 18257517] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83, MASS SPECTROMETRY.

Cross-references

Sequence databases
EMBLGenBankDDBJ	D38309 Genomic DNA. Translation: BAA07426.1. X83615 Genomic DNA. Translation: CAA58591.1. CU329670 Genomic DNA. Translation: CAB52721.1.
PIR	S55075. S51092. S57259.
RefSeq	NP_594734.1.
3D structure databases
HSSP	HSSP built from PDB template 1DJX based on UniProtKB P10688.
ModBase	Search...
Protein-protein interaction databases
STRING	P40977.
Genome annotation databases
GeneID	2541439.
GenomeReviews	Gene locus plc1 in contig CU329670_GR.
KEGG	spo:SPAC22F8.11.
NMPDR	fig|4896.1.peg.4704.
Organism-specific databases
GeneDB_Spombe	SPAC22F8.11.
Phylogenomic databases
OMA	PKVNIKE.
Enzyme and pathway databases
BioCyc	SPOM-XXX-01:SPOM-XXX-01-002813-MON.
BRENDA	3.1.4.11. 653.
Gene expression databases
ArrayExpress	P40977.
Family and domain databases
InterPro	IPR000008. C2_Ca-dep. IPR018029. C2_membr_targeting. IPR011992. EF-Hand_type. IPR018248. EF_hand. IPR018247. EF_HAND_1_Ca_BS. IPR018249. EF_HAND_2. IPR002048. EF_hand_Ca_bd. IPR011993. PH_type. IPR015359. Phospholipase_C_EF-hand-like. IPR001192. Phospholipase_C_Pinositol-sp_C. IPR000909. Phospholipase_C_Pinositol-sp_X. IPR001711. Phospholipase_C_Pinositol-sp_Y. IPR017946. PLC-like_Pdiesterase_TIM-brl. [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. 1 hit.
Pfam	PF00168. 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]
PRINTS	PR00390. PHPHLIPASEC.
ProDom	PD001202. PI_PLC_Y. 1 hit. [Graphical view] [Entries sharing at least one domain]
SMART	SM00239. C2. 1 hit. SM00054. EFh. 2 hits. SM00148. PLCXc. 1 hit. SM00149. PLCYc. 1 hit. [Graphical view]
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

PLC1_SCHPO

Accession

Primary (citable) accession number: P40977

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	February 1, 1995
Last modified:	November 3, 2009
This is version 90 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)