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Protein

Dihydrosphingosine 1-phosphate phosphatase YSR3

Gene

YSR3

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Protein inferred from homologyi

Functioni

Dihydrosphingosine 1-phosphate phosphatase required for efficient ceramide synthesis from exogenous sphingoid bases. Involved in endocytosis and calcium-mediated signaling.5 Publications

GO - Molecular functioni

  • sphingosine-1-phosphate phosphatase activity Source: SGD

GO - Biological processi

  • phospholipid dephosphorylation Source: SGD
  • sphingolipid biosynthetic process Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Lipid metabolism, Sphingolipid metabolism

Enzyme and pathway databases

BioCyciMetaCyc:YKR053C-MONOMER.
YEAST:YKR053C-MONOMER.
ReactomeiR-SCE-1660661. Sphingolipid de novo biosynthesis.

Chemistry

SwissLipidsiSLP:000000933.

Names & Taxonomyi

Protein namesi
Recommended name:
Dihydrosphingosine 1-phosphate phosphatase YSR3 (EC:3.1.3.-)
Alternative name(s):
Long-chain base protein 2
Sphingolipid resistance protein 3
Gene namesi
Name:YSR3
Synonyms:LBP2
Ordered Locus Names:YKR053C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XI

Organism-specific databases

EuPathDBiFungiDB:YKR053C.
SGDiS000001761. YSR3.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 8686LumenalBy similarityAdd
BLAST
Transmembranei87 – 10721Helical; Name=1Sequence analysisAdd
BLAST
Topological domaini108 – 1136CytoplasmicBy similarity
Transmembranei114 – 13421Helical; Name=2Sequence analysisAdd
BLAST
Topological domaini135 – 15420LumenalBy similarityAdd
BLAST
Transmembranei155 – 17622Helical; Name=3Sequence analysisAdd
BLAST
Topological domaini177 – 1826CytoplasmicBy similarity
Transmembranei183 – 20321Helical; Name=4Sequence analysisAdd
BLAST
Topological domaini204 – 21512LumenalBy similarityAdd
BLAST
Transmembranei216 – 23621Helical; Name=5Sequence analysisAdd
BLAST
Topological domaini237 – 2415CytoplasmicBy similarity
Transmembranei242 – 26221Helical; Name=6Sequence analysisAdd
BLAST
Topological domaini263 – 31957LumenalBy similarityAdd
BLAST
Transmembranei320 – 34021Helical; Name=7Sequence analysisAdd
BLAST
Topological domaini341 – 37939CytoplasmicBy similarityAdd
BLAST
Transmembranei380 – 40021Helical; Name=8Sequence analysisAdd
BLAST
Topological domaini401 – 4044LumenalBy similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 404404Dihydrosphingosine 1-phosphate phosphatase YSR3PRO_0000203216Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi62 – 621N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Glycoprotein

Interactioni

Protein-protein interaction databases

BioGridi34184. 89 interactions.
DIPiDIP-5258N.
MINTiMINT-516588.

Structurei

3D structure databases

ProteinModelPortaliP23501.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

GeneTreeiENSGT00390000017322.
HOGENOMiHOG000066080.
InParanoidiP23501.
KOiK04717.
OMAiGNHPAEH.
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.

P23501-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTIIQTVTEL GVTEDTIKVQ MAPSGGKHLL ADPGNHPAEH FESQMSWLRF
60 70 80 90 100
QTRQYLTRFT DNQSDFVHSL QKKHRTPFRD VYFKYTSLMG SHMFYVIVLP
110 120 130 140 150
MPVWLGYRDL TRDMIYVLGY SIYLSGYLKD YWCLPRPKSP PVDRITLSEY
160 170 180 190 200
TTKEYGAPSS HSANATAVSL LFFWRICLSD TLVWPTKLLL LSLVIFYYLT
210 220 230 240 250
LVFGRVYCGM HGMLDLFSGA AVGAICFFIR IWVVHALRNF QIGEHLWFPL
260 270 280 290 300
LSVAWGLFIL FNHVRPIDEC PCFEDSVAFI GVVSGLDCSD WLTERYGWNL
310 320 330 340 350
VCSRYASCGS KVFLRPLVGV ASVIVWKDVI SKTAVYTLLI KLLRFHDDRS
360 370 380 390 400
EKVHFHNETS EEEECLLYSG VSKVEIVGRF LIYAGIPTTV FLLCPVFFTW

TNLR
Length:404
Mass (Da):46,488
Last modified:June 1, 1994 - v2
Checksum:i0CDB272FBF868BF8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z28278 Genomic DNA. Translation: CAA82131.1.
X56444 Genomic DNA. Translation: CAA39827.1.
BK006944 Genomic DNA. Translation: DAA09204.1.
PIRiS38127.
RefSeqiNP_012979.3. NM_001179843.3.

Genome annotation databases

EnsemblFungiiYKR053C; YKR053C; YKR053C.
GeneIDi853927.
KEGGisce:YKR053C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z28278 Genomic DNA. Translation: CAA82131.1.
X56444 Genomic DNA. Translation: CAA39827.1.
BK006944 Genomic DNA. Translation: DAA09204.1.
PIRiS38127.
RefSeqiNP_012979.3. NM_001179843.3.

3D structure databases

ProteinModelPortaliP23501.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi34184. 89 interactions.
DIPiDIP-5258N.
MINTiMINT-516588.

Chemistry

SwissLipidsiSLP:000000933.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYKR053C; YKR053C; YKR053C.
GeneIDi853927.
KEGGisce:YKR053C.

Organism-specific databases

EuPathDBiFungiDB:YKR053C.
SGDiS000001761. YSR3.

Phylogenomic databases

GeneTreeiENSGT00390000017322.
HOGENOMiHOG000066080.
InParanoidiP23501.
KOiK04717.
OMAiGNHPAEH.
OrthoDBiEOG7F519P.

Enzyme and pathway databases

BioCyciMetaCyc:YKR053C-MONOMER.
YEAST:YKR053C-MONOMER.
ReactomeiR-SCE-1660661. Sphingolipid de novo biosynthesis.

Miscellaneous databases

NextBioi975288.
PROiP23501.

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.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Complete DNA sequence of yeast chromosome XI."
    Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V., Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P., Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L., Daignan-Fornier B., del Rey F., Dion C.
    , Domdey H., Duesterhoeft A., Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H., Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L., Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M., Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H., Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J., Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H., Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J., Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S., Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F., Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R., Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W., Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M., Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C., Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H., Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L., van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S., von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M., Becker I., Mewes H.-W.
    Nature 369:371-378(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  3. "MRS3 and MRS4, two suppressors of mtRNA splicing defects in yeast, are new members of the mitochondrial carrier family."
    Wiesenberger G., Link T.A., von Ahsen U., Waldherr M., Schweyen R.J.
    J. Mol. Biol. 217:23-37(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 197-404.
    Strain: M1301.
  4. "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.
  5. "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.
  6. "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.
  7. "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.
  8. "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.

Entry informationi

Entry nameiDS1P2_YEAST
AccessioniPrimary (citable) accession number: P23501
Secondary accession number(s): D6VXB4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: June 1, 1994
Last modified: May 11, 2016
This is version 119 of the entry and version 2 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 XI
    Yeast (Saccharomyces cerevisiae) chromosome XI: entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.