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P40015 (ISC1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 112. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Inositol phosphosphingolipids phospholipase C

Short name=IPS phospholipase C
Short name=IPS-PLC
EC=3.1.4.-
Alternative name(s):
Neutral sphingomyelinase
Short name=N-SMase
Short name=nSMase
Gene names
Name:ISC1
Ordered Locus Names:YER019W
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length477 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Responsible for the hydrolysis of the phosphosphingolipids (IPS), inositol phosphorylceramide (IPC), mannosylinositol phosphorylceramide (MIPC), and mannosyldiinositol phosphorylceramide (M(IP)2C). Also active on sphingomyelin, but this activity is probably not physiologically relevant.

Cofactor

Magnesium.

Pathway

Lipid metabolism; sphingolipid metabolism.

Subcellular location

Membrane; Multi-pass membrane protein.

Miscellaneous

Present with 2170 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the neutral sphingomyelinase family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

AGP1P253761EBI-9371,EBI-2357
PMP2P409751EBI-9371,EBI-2043041

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 477477Inositol phosphosphingolipids phospholipase C
PRO_0000075695

Regions

Topological domain1 – 398398Cytoplasmic Potential
Transmembrane399 – 41719Helical; Potential
Topological domain418 – 4247Extracellular Potential
Transmembrane425 – 44925Helical; Potential
Topological domain450 – 47728Cytoplasmic Potential

Sites

Active site3341Proton acceptor By similarity
Metal binding1001Magnesium By similarity
Site2331Important for substrate recognition By similarity

Sequences

Sequence LengthMass (Da)Tools
P40015 [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: 0670FD303FEB8EFF

FASTA47753,940
        10         20         30         40         50         60 
MYNRKDRDVH ERKEDGQSEF EALNGTNAIM SDNSKAYSIK FLTFNTWGLK YVSKHRKERL 

        70         80         90        100        110        120 
RAIADKLAGH SMLTPISDEL LPNGGDSNEN EDYDVIALQE IWCVEDWKYL ASACASKYPY 

       130        140        150        160        170        180 
QRLFHSGILT GPGLAILSKV PIESTFLYRF PINGRPSAVF RGDWYVGKSI AITVLNTGTR 

       190        200        210        220        230        240 
PIAIMNSHMH APYAKQGDAA YLCHRSCQAW DFSRLIKLYR QAGYAVIVVG DLNSRPGSLP 

       250        260        270        280        290        300 
HKFLTQEAGL VDSWEQLHGK QDLAVIARLS PLQQLLKGCT TCDSLLNTWR AQRQPDEACR 

       310        320        330        340        350        360 
LDYALIDPDF LQTVDAGVRF TERIPHLDCS VSDHFAYSCT LNIVPQGTES RPSTSVKRAK 

       370        380        390        400        410        420 
THDRELILQR YSNYETMIEC IHTYLKTAQR QKFFRGLHFW ASILLLIASL VVTTFTANKA 

       430        440        450        460        470 
GWSSIFWVLF AIAVSISGTI DGAISFLFGR SEIRALIEVE QEVLDAEHHL QTFLSEK 

« Hide

References

« Hide 'large scale' references
[1]"The nucleotide sequence of Saccharomyces cerevisiae chromosome V."
Dietrich F.S., Mulligan J.T., Hennessy K.M., Yelton M.A., Allen E., Araujo R., Aviles E., Berno A., Brennan T., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Guzman E., Hartzell G., Hunicke-Smith S., Hyman R.W. expand/collapse author list , Kayser A., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Norgren R., Oefner P., Oh C., Petel F.X., Roberts D., Sehl P., Schramm S., Shogren T., Smith V., Taylor P., Wei Y., Botstein D., Davis R.W.
Nature 387:78-81(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[2]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[3]"Identification of ISC1 (YER019w) as inositol phosphosphingolipid phospholipase C in Saccharomyces cerevisiae."
Sawai H., Okamoto Y., Luberto C., Mao C., Bielawska A., Domae N., Hannun Y.A.
J. Biol. Chem. 275:39793-39798(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
[4]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[5]"A global topology map of the Saccharomyces cerevisiae membrane proteome."
Kim H., Melen K., Oesterberg M., von Heijne G.
Proc. Natl. Acad. Sci. U.S.A. 103:11142-11147(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: TOPOLOGY [LARGE SCALE ANALYSIS].
Strain: ATCC 208353 / W303-1A.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U18778 Genomic DNA. Translation: AAB64552.1.
BK006939 Genomic DNA. Translation: DAA07671.1.
PIRS50477.
RefSeqNP_010935.1. NM_001178910.1.

3D structure databases

ProteinModelPortalP40015.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid36752. 172 interactions.
DIPDIP-5002N.
IntActP40015. 3 interactions.
MINTMINT-486977.
STRING4932.YER019W.

Proteomic databases

MaxQBP40015.
PaxDbP40015.
PeptideAtlasP40015.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYER019W; YER019W; YER019W.
GeneID856739.
KEGGsce:YER019W.

Organism-specific databases

CYGDYER019w.
SGDS000000821. ISC1.

Phylogenomic databases

eggNOGNOG269293.
GeneTreeENSGT00390000009166.
HOGENOMHOG000215232.
KOK01128.
OMANSHMHAP.
OrthoDBEOG7J70QP.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-17704.
YEAST:YER019W-MONOMER.
UniPathwayUPA00222.

Gene expression databases

GenevestigatorP40015.

Family and domain databases

Gene3D3.60.10.10. 1 hit.
InterProIPR005135. Endo/exonuclease/phosphatase.
[Graphical view]
PfamPF03372. Exo_endo_phos. 1 hit.
[Graphical view]
SUPFAMSSF56219. SSF56219. 1 hit.
ProtoNetSearch...

Other

NextBio982867.
PROP40015.

Entry information

Entry nameISC1_YEAST
AccessionPrimary (citable) accession number: P40015
Secondary accession number(s): D3DLR7
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: May 14, 2014
This is version 112 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome V

Yeast (Saccharomyces cerevisiae) chromosome V: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways