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P47013

- DS1P1_YEAST

UniProt

P47013 - DS1P1_YEAST

Protein

Dihydrosphingosine 1-phosphate phosphatase LCB3

Gene

LCB3

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 110 (01 Oct 2014)
      Sequence version 1 (01 Feb 1996)
      Previous versions | rss
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    Functioni

    Dihydrosphingosine 1-phosphate phosphatase required for efficient ceramide synthesis from exogenous sphingoid bases. Involved in endocytosis and calcium-mediated signaling.11 Publications

    GO - Molecular functioni

    1. sphingosine-1-phosphate phosphatase activity Source: SGD

    GO - Biological processi

    1. calcium-mediated signaling Source: SGD
    2. dephosphorylation Source: GOC
    3. sphingolipid biosynthetic process Source: SGD

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Lipid metabolism, Sphingolipid metabolism

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER3O-419.
    YEAST:MONOMER3O-419.
    ReactomeiREACT_189220. Sphingolipid de novo biosynthesis.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Dihydrosphingosine 1-phosphate phosphatase LCB3 (EC:3.1.3.-)
    Alternative name(s):
    Long-chain base protein 3
    Sphingolipid resistance protein 2
    Gene namesi
    Name:LCB3
    Synonyms:LBP1, YSR2
    Ordered Locus Names:YJL134W
    ORF Names:J0671
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome X

    Organism-specific databases

    CYGDiYJL134w.
    SGDiS000003670. LCB3.

    Subcellular locationi

    Endoplasmic reticulum membrane 3 Publications; Multi-pass membrane protein 3 Publications

    GO - Cellular componenti

    1. endoplasmic reticulum Source: SGD
    2. endoplasmic reticulum membrane Source: UniProtKB-SubCell
    3. integral component of membrane Source: UniProtKB-KW

    Keywords - Cellular componenti

    Endoplasmic reticulum, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi128 – 1281K → A: Impairs dihydrosphingosine 1-phosphate phosphatase activity. 1 Publication
    Mutagenesisi160 – 1601H → A: Impairs dihydrosphingosine 1-phosphate phosphatase activity. 1 Publication
    Mutagenesisi210 – 2101H → A: Impairs dihydrosphingosine 1-phosphate phosphatase activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 409409Dihydrosphingosine 1-phosphate phosphatase LCB3PRO_0000203037Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei16 – 161Phosphothreonine2 Publications
    Modified residuei18 – 181Phosphoserine2 Publications

    Post-translational modificationi

    Glycosylated.1 Publication

    Keywords - PTMi

    Glycoprotein, Phosphoprotein

    Proteomic databases

    MaxQBiP47013.
    PaxDbiP47013.

    Expressioni

    Gene expression databases

    GenevestigatoriP47013.

    Interactioni

    Protein-protein interaction databases

    BioGridi33622. 76 interactions.
    DIPiDIP-5685N.
    IntActiP47013. 4 interactions.
    MINTiMINT-572017.
    STRINGi4932.YJL134W.

    Structurei

    3D structure databases

    ProteinModelPortaliP47013.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 8686LumenalAdd
    BLAST
    Topological domaini108 – 1125Cytoplasmic
    Topological domaini134 – 18249LumenalAdd
    BLAST
    Topological domaini204 – 2074Cytoplasmic
    Topological domaini229 – 24517LumenalAdd
    BLAST
    Topological domaini267 – 27610Cytoplasmic
    Topological domaini298 – 31518LumenalAdd
    BLAST
    Topological domaini337 – 38448CytoplasmicAdd
    BLAST
    Topological domaini406 – 4094Lumenal

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei87 – 10721Helical; Name=1Add
    BLAST
    Transmembranei113 – 13321Helical; Name=2Add
    BLAST
    Transmembranei183 – 20321Helical; Name=3Add
    BLAST
    Transmembranei208 – 22821Helical; Name=4Add
    BLAST
    Transmembranei246 – 26621Helical; Name=5Add
    BLAST
    Transmembranei277 – 29721Helical; Name=6Add
    BLAST
    Transmembranei316 – 33621Helical; Name=7Add
    BLAST
    Transmembranei385 – 40521Helical; Name=8Add
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG0671.
    GeneTreeiENSGT00390000017322.
    HOGENOMiHOG000066080.
    KOiK04716.
    OMAiNTVCLMG.
    OrthoDBiEOG7F519P.

    Family and domain databases

    Gene3Di1.20.144.10. 1 hit.
    InterProiIPR000326. P_Acid_Pase_2/haloperoxidase.
    [Graphical view]
    PfamiPF01569. PAP2. 1 hit.
    [Graphical view]
    SMARTiSM00014. acidPPc. 1 hit.
    [Graphical view]
    SUPFAMiSSF48317. SSF48317. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    P47013-1 [UniParc]FASTAAdd to Basket

    « Hide

    MVDGLNTSNI RKRARTLSNP NDFQEPNYLL DPGNHPSDHF RTRMSKFRFN    50
    IREKLLVFTN NQSFTLSRWQ KKYRSAFNDL YFTYTSLMGS HTFYVLCLPM 100
    PVWFGYFETT KDMVYILGYS IYLSGFFKDY WCLPRPRAPP LHRITLSEYT 150
    TKEYGAPSSH TANATGVSLL FLYNIWRMQE SSVMVQLLLS CVVLFYYMTL 200
    VFGRIYCGMH GILDLVSGGL IGIVCFIVRM YFKYRFPGLR IEEHWWFPLF 250
    SVGWGLLLLF KHVKPVDECP CFQDSVAFMG VVSGIECCDW LGKVFGVTLV 300
    YNLEPNCGWR LTLARLLVGL PCVVIWKYVI SKPMIYTLLI KVFHLKDDRN 350
    VAARKRLEAT HKEGASKYEC PLYIGEPKID ILGRFIIYAG VPFTVVMCSP 400
    VLFSLLNIA 409
    Length:409
    Mass (Da):47,372
    Last modified:February 1, 1996 - v1
    Checksum:iE0CD7D0F169447C3
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X87371 Genomic DNA. Translation: CAA60821.1.
    Z49410 Genomic DNA. Translation: CAA89430.1.
    BK006943 Genomic DNA. Translation: DAA08666.1.
    PIRiS55178.
    RefSeqiNP_012401.1. NM_001181567.1.

    Genome annotation databases

    EnsemblFungiiYJL134W; YJL134W; YJL134W.
    GeneIDi853307.
    KEGGisce:YJL134W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X87371 Genomic DNA. Translation: CAA60821.1 .
    Z49410 Genomic DNA. Translation: CAA89430.1 .
    BK006943 Genomic DNA. Translation: DAA08666.1 .
    PIRi S55178.
    RefSeqi NP_012401.1. NM_001181567.1.

    3D structure databases

    ProteinModelPortali P47013.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 33622. 76 interactions.
    DIPi DIP-5685N.
    IntActi P47013. 4 interactions.
    MINTi MINT-572017.
    STRINGi 4932.YJL134W.

    Proteomic databases

    MaxQBi P47013.
    PaxDbi P47013.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YJL134W ; YJL134W ; YJL134W .
    GeneIDi 853307.
    KEGGi sce:YJL134W.

    Organism-specific databases

    CYGDi YJL134w.
    SGDi S000003670. LCB3.

    Phylogenomic databases

    eggNOGi COG0671.
    GeneTreei ENSGT00390000017322.
    HOGENOMi HOG000066080.
    KOi K04716.
    OMAi NTVCLMG.
    OrthoDBi EOG7F519P.

    Enzyme and pathway databases

    BioCyci MetaCyc:MONOMER3O-419.
    YEAST:MONOMER3O-419.
    Reactomei REACT_189220. Sphingolipid de novo biosynthesis.

    Miscellaneous databases

    NextBioi 973636.

    Gene expression databases

    Genevestigatori P47013.

    Family and domain databases

    Gene3Di 1.20.144.10. 1 hit.
    InterProi IPR000326. P_Acid_Pase_2/haloperoxidase.
    [Graphical view ]
    Pfami PF01569. PAP2. 1 hit.
    [Graphical view ]
    SMARTi SM00014. acidPPc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48317. SSF48317. 1 hit.
    ProtoNeti Search...

    Publicationsi

    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.
      , 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. 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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiDS1P1_YEAST
    AccessioniPrimary (citable) accession number: P47013
    Secondary accession number(s): D6VW50
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1996
    Last sequence update: February 1, 1996
    Last modified: October 1, 2014
    This is version 110 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families
    2. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    3. Yeast chromosome X
      Yeast (Saccharomyces cerevisiae) chromosome X: entries and gene names

    External Data

    Dasty 3