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P47013 (DS1P1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 107. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Dihydrosphingosine 1-phosphate phosphatase LCB3

EC=3.1.3.-
Alternative name(s):
Long-chain base protein 3
Sphingolipid resistance protein 2
Gene names
Name:LCB3
Synonyms:LBP1, YSR2
Ordered Locus Names:YJL134W
ORF Names:J0671
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length409 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Dihydrosphingosine 1-phosphate phosphatase required for efficient ceramide synthesis from exogenous sphingoid bases. Involved in endocytosis and calcium-mediated signaling. Ref.4 Ref.5 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14

Subcellular location

Endoplasmic reticulum membrane; Multi-pass membrane protein Ref.5 Ref.7 Ref.9.

Post-translational modification

Glycosylated. Ref.13

Sequence similarities

Belongs to the type 2 lipid phosphate phosphatase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 409409Dihydrosphingosine 1-phosphate phosphatase LCB3
PRO_0000203037

Regions

Topological domain1 – 8686Lumenal Ref.13 Ref.15
Transmembrane87 – 10721Helical; Name=1
Topological domain108 – 1125Cytoplasmic Ref.13 Ref.15
Transmembrane113 – 13321Helical; Name=2
Topological domain134 – 18249Lumenal Ref.13 Ref.15
Transmembrane183 – 20321Helical; Name=3
Topological domain204 – 2074Cytoplasmic Ref.13 Ref.15
Transmembrane208 – 22821Helical; Name=4
Topological domain229 – 24517Lumenal Ref.13 Ref.15
Transmembrane246 – 26621Helical; Name=5
Topological domain267 – 27610Cytoplasmic Ref.13 Ref.15
Transmembrane277 – 29721Helical; Name=6
Topological domain298 – 31518Lumenal Ref.13 Ref.15
Transmembrane316 – 33621Helical; Name=7
Topological domain337 – 38448Cytoplasmic Ref.13 Ref.15
Transmembrane385 – 40521Helical; Name=8
Topological domain406 – 4094Lumenal Ref.13 Ref.15

Amino acid modifications

Modified residue161Phosphothreonine Ref.16 Ref.17
Modified residue181Phosphoserine Ref.16 Ref.17

Experimental info

Mutagenesis1281K → A: Impairs dihydrosphingosine 1-phosphate phosphatase activity. Ref.13
Mutagenesis1601H → A: Impairs dihydrosphingosine 1-phosphate phosphatase activity. Ref.13
Mutagenesis2101H → A: Impairs dihydrosphingosine 1-phosphate phosphatase activity. Ref.13

Sequences

Sequence LengthMass (Da)Tools
P47013 [UniParc].

Last modified February 1, 1996. Version 1.
Checksum: E0CD7D0F169447C3

FASTA40947,372
        10         20         30         40         50         60 
MVDGLNTSNI RKRARTLSNP NDFQEPNYLL DPGNHPSDHF RTRMSKFRFN IREKLLVFTN 

        70         80         90        100        110        120 
NQSFTLSRWQ KKYRSAFNDL YFTYTSLMGS HTFYVLCLPM PVWFGYFETT KDMVYILGYS 

       130        140        150        160        170        180 
IYLSGFFKDY WCLPRPRAPP LHRITLSEYT TKEYGAPSSH TANATGVSLL FLYNIWRMQE 

       190        200        210        220        230        240 
SSVMVQLLLS CVVLFYYMTL VFGRIYCGMH GILDLVSGGL IGIVCFIVRM YFKYRFPGLR 

       250        260        270        280        290        300 
IEEHWWFPLF SVGWGLLLLF KHVKPVDECP CFQDSVAFMG VVSGIECCDW LGKVFGVTLV 

       310        320        330        340        350        360 
YNLEPNCGWR LTLARLLVGL PCVVIWKYVI SKPMIYTLLI KVFHLKDDRN VAARKRLEAT 

       370        380        390        400 
HKEGASKYEC PLYIGEPKID ILGRFIIYAG VPFTVVMCSP VLFSLLNIA 

« Hide

References

« Hide 'large scale' references
[1]"Sequence analysis of a 40.7 kb segment from the left arm of yeast chromosome X reveals 14 known genes and 13 new open reading frames including homologues of genes clustered on the right arm of chromosome XI."
Katsoulou C., Tzermia M., Tavernarakis N., Alexandraki D.
Yeast 12:787-797(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 96604 / S288c / FY1679.
[2]"Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X."
Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C., Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D., Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J., Heumann K. expand/collapse author list , Hilger F., Hollenberg C.P., Huang M.-E., Jacq C., Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E., Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T., Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R., Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N., To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H., von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.
EMBO J. 15:2031-2049(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[3]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[4]"Identification of a Saccharomyces gene, LCB3, necessary for incorporation of exogenous long chain bases into sphingolipids."
Qie L., Nagiec M.M., Baltisberger J.A., Lester R.L., Dickson R.C.
J. Biol. Chem. 272:16110-16117(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[5]"Identification and characterization of Saccharomyces cerevisiae dihydrosphingosine-1-phosphate phosphatase."
Mao C., Wadleigh M., Jenkins G.M., Hannun Y.A., Obeid L.M.
J. Biol. Chem. 272:28690-28694(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[6]"Sphingoid base 1-phosphate phosphatase: a key regulator of sphingolipid metabolism and stress response."
Mandala S.M., Thornton R., Tu Z., Kurtz M.B., Nickels J., Broach J., Menzeleev R., Spiegel S.
Proc. Natl. Acad. Sci. U.S.A. 95:150-155(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[7]"The dihydrosphingosine-1-phosphate phosphatases of Saccharomyces cerevisiae are important regulators of cell proliferation and heat stress responses."
Mao C., Saba J.D., Obeid L.M.
Biochem. J. 342:667-675(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[8]"Sphingoid base synthesis requirement for endocytosis in Saccharomyces cerevisiae."
Zanolari B., Friant S., Funato K., Suetterlin C., Stevenson B.J., Riezman H.
EMBO J. 19:2824-2833(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[9]"Yeast sphingosine-1-phosphate phosphatases: assay, expression, deletion, purification, and cellular localization by GFP tagging."
Mao C., Obeid L.M.
Methods Enzymol. 311:223-232(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[10]"Calcium influx and signaling in yeast stimulated by intracellular sphingosine 1-phosphate accumulation."
Birchwood C.J., Saba J.D., Dickson R.C., Cunningham K.W.
J. Biol. Chem. 276:11712-11718(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[11]"Mutant analysis reveals complex regulation of sphingolipid long chain base phosphates and long chain bases during heat stress in yeast."
Ferguson-Yankey S.R., Skrzypek M.S., Lester R.L., Dickson R.C.
Yeast 19:573-586(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[12]"Ceramide/long-chain base phosphate rheostat in Saccharomyces cerevisiae: regulation of ceramide synthesis by Elo3p and Cka2p."
Kobayashi S.D., Nagiec M.M.
Eukaryot. Cell 2:284-294(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[13]"Transmembrane topology of sphingoid long-chain base-1-phosphate phosphatase, Lcb3p."
Kihara A., Sano T., Iwaki S., Igarashi Y.
Genes Cells 8:525-535(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF LYS-128; HIS-160 AND HIS-210, GLYCOSYLATION, TOPOLOGY.
[14]"Lcb4p is a key regulator of ceramide synthesis from exogenous long chain sphingoid base in Saccharomyces cerevisiae."
Funato K., Lombardi R., Vallee B., Riezman H.
J. Biol. Chem. 278:7325-7334(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[15]"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.
[16]"Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-16 AND SER-18, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Strain: ADR376.
[17]"Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-16 AND SER-18, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[18]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X87371 Genomic DNA. Translation: CAA60821.1.
Z49410 Genomic DNA. Translation: CAA89430.1.
BK006943 Genomic DNA. Translation: DAA08666.1.
PIRS55178.
RefSeqNP_012401.1. NM_001181567.1.

3D structure databases

ProteinModelPortalP47013.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid33622. 76 interactions.
DIPDIP-5685N.
IntActP47013. 4 interactions.
MINTMINT-572017.
STRING4932.YJL134W.

Proteomic databases

PaxDbP47013.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYJL134W; YJL134W; YJL134W.
GeneID853307.
KEGGsce:YJL134W.

Organism-specific databases

CYGDYJL134w.
SGDS000003670. LCB3.

Phylogenomic databases

eggNOGCOG0671.
GeneTreeENSGT00390000017322.
HOGENOMHOG000066080.
KOK04716.
OMAQYAGLAW.
OrthoDBEOG7F519P.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER3O-419.
YEAST:MONOMER3O-419.

Gene expression databases

GenevestigatorP47013.

Family and domain databases

Gene3D1.20.144.10. 1 hit.
InterProIPR000326. P_Acid_Pase_2/haloperoxidase.
[Graphical view]
PfamPF01569. PAP2. 1 hit.
[Graphical view]
SMARTSM00014. acidPPc. 1 hit.
[Graphical view]
SUPFAMSSF48317. SSF48317. 1 hit.
ProtoNetSearch...

Other

NextBio973636.

Entry information

Entry nameDS1P1_YEAST
AccessionPrimary (citable) accession number: P47013
Secondary accession number(s): D6VW50
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: April 16, 2014
This is version 107 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 X

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

Yeast

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

SIMILARITY comments

Index of protein domains and families