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Protein

Dihydrosphingosine 1-phosphate phosphatase LCB3

Gene

LCB3

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei160Proton donorBy similarity1
Active sitei210NucleophileBy similarity1
Sitei214Stabilizes the active site histidine for nucleophilic attackBy similarity1

GO - Molecular functioni

  • sphingosine-1-phosphate phosphatase activity Source: SGD

GO - Biological processi

  • calcium-mediated signaling Source: SGD
  • sphingolipid biosynthetic process Source: SGD

Keywordsi

Molecular functionHydrolase
Biological processLipid metabolism, Sphingolipid metabolism

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER3O-419.
YEAST:MONOMER3O-419.
ReactomeiR-SCE-1660661. Sphingolipid de novo biosynthesis.

Chemistry databases

SwissLipidsiSLP:000000932.

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
Proteomesi
  • UP000002311 Componenti: Chromosome X

Organism-specific databases

EuPathDBiFungiDB:YJL134W.
SGDiS000003670. LCB3.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 86Lumenal1 PublicationAdd BLAST86
Transmembranei87 – 107Helical; Name=1Sequence analysisAdd BLAST21
Topological domaini108 – 112Cytoplasmic1 Publication5
Transmembranei113 – 133Helical; Name=2Sequence analysisAdd BLAST21
Topological domaini134 – 182Lumenal1 PublicationAdd BLAST49
Transmembranei183 – 203Helical; Name=3Sequence analysisAdd BLAST21
Topological domaini204 – 207Cytoplasmic1 Publication4
Transmembranei208 – 228Helical; Name=4Sequence analysisAdd BLAST21
Topological domaini229 – 245Lumenal1 PublicationAdd BLAST17
Transmembranei246 – 266Helical; Name=5Sequence analysisAdd BLAST21
Topological domaini267 – 276Cytoplasmic1 Publication10
Transmembranei277 – 297Helical; Name=6Sequence analysisAdd BLAST21
Topological domaini298 – 315Lumenal1 PublicationAdd BLAST18
Transmembranei316 – 336Helical; Name=7Sequence analysisAdd BLAST21
Topological domaini337 – 384Cytoplasmic1 PublicationAdd BLAST48
Transmembranei385 – 405Helical; Name=8Sequence analysisAdd BLAST21
Topological domaini406 – 409Lumenal1 Publication4

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi128K → A: Impairs dihydrosphingosine 1-phosphate phosphatase activity. 1 Publication1
Mutagenesisi160H → A: Impairs dihydrosphingosine 1-phosphate phosphatase activity. 1 Publication1
Mutagenesisi210H → A: Impairs dihydrosphingosine 1-phosphate phosphatase activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002030371 – 409Dihydrosphingosine 1-phosphate phosphatase LCB3Add BLAST409

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei16PhosphothreonineCombined sources1
Modified residuei18PhosphoserineCombined sources1

Post-translational modificationi

Glycosylated.1 Publication

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiP47013.
PRIDEiP47013.

PTM databases

iPTMnetiP47013.

Interactioni

Protein-protein interaction databases

BioGridi33622. 117 interactors.
DIPiDIP-5685N.
IntActiP47013. 4 interactors.
MINTiMINT-572017.
STRINGi4932.YJL134W.

Structurei

3D structure databases

ProteinModelPortaliP47013.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni128 – 136Phosphatase sequence motif ICurated9
Regioni157 – 160Phosphatase sequence motif IICurated4
Regioni203 – 214Phosphatase sequence motif IIICuratedAdd BLAST12

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

GeneTreeiENSGT00390000017322.
HOGENOMiHOG000066080.
InParanoidiP47013.
KOiK04716.
OMAiYKFVTYS.
OrthoDBiEOG092C3MDD.

Family and domain databases

InterProiView protein in InterPro
IPR036938. P_Acid_Pase_2/haloperoxi_sf.
IPR000326. P_Acid_Pase_2/haloperoxidase.
PfamiView protein in Pfam
PF01569. PAP2. 1 hit.
SMARTiView protein in SMART
SM00014. acidPPc. 1 hit.
SUPFAMiSSF48317. SSF48317. 1 hit.

Sequencei

Sequence statusi: Complete.

P47013-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVDGLNTSNI RKRARTLSNP NDFQEPNYLL DPGNHPSDHF RTRMSKFRFN
60 70 80 90 100
IREKLLVFTN NQSFTLSRWQ KKYRSAFNDL YFTYTSLMGS HTFYVLCLPM
110 120 130 140 150
PVWFGYFETT KDMVYILGYS IYLSGFFKDY WCLPRPRAPP LHRITLSEYT
160 170 180 190 200
TKEYGAPSSH TANATGVSLL FLYNIWRMQE SSVMVQLLLS CVVLFYYMTL
210 220 230 240 250
VFGRIYCGMH GILDLVSGGL IGIVCFIVRM YFKYRFPGLR IEEHWWFPLF
260 270 280 290 300
SVGWGLLLLF KHVKPVDECP CFQDSVAFMG VVSGIECCDW LGKVFGVTLV
310 320 330 340 350
YNLEPNCGWR LTLARLLVGL PCVVIWKYVI SKPMIYTLLI KVFHLKDDRN
360 370 380 390 400
VAARKRLEAT HKEGASKYEC PLYIGEPKID ILGRFIIYAG VPFTVVMCSP

VLFSLLNIA
Length:409
Mass (Da):47,372
Last modified:February 1, 1996 - v1
Checksum:iE0CD7D0F169447C3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

Similar proteinsi

Entry informationi

Entry nameiDS1P1_YEAST
AccessioniPrimary (citable) accession number: P47013
Secondary accession number(s): D6VW50
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: November 22, 2017
This is version 138 of the entry and version 1 of the sequence. See 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