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Protein Overview: DPL1

General Information:
Name(s) found: DPL1 / YDR294C [SGD]
Description(s) found:
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  • gi|6320500|ref|NP_010580.1| Dihydrosphingosine phosphate lyase, regulates intracellular levels of sphingolipid long-chain base phosphates (LCBPs), degrades phosphorylated long chain bases, prefers C16 dihydrosphingosine-l-phosphate as a substrate; Dpl1p [ [NCBI NR]
  • gi|37999490|sp|Q05567.1|SGPL_YEAST RecName: Full=Sphingosine-1-phosphate lyase; Short=SP-lyase; Short=ySPL; AltName: Full=Sphingosine-1-phosphate aldolase; AltName: Full=Bestowed of sphingosine tolerance 1 [NCBI NR]
  • pir||S70123 sphingosine-1-phosphate lyase (EC 4.-.-.-) [similarity] - yeast (Saccharomyces cerevisiae) [NCBI NR]
  • gi|1230658|gb|AAB64470.1| Ydr294cp [Saccharomyces cerevisiae] [NCBI NR]
  • Sphingosine-1-phosphate lyase OS=Saccharomyces cerevisiae GN=DPL1 PE=1 SV=1 [Swiss-Prot]
  • DPL1 Dihydrosphingosine phosphate lyase [mips]
  • Dihydrosphingosine phosphate lyase, regulates intracellular levels of sphingolipid long-chain base phosphates (LCBPs), degrades phosphorylated long chain bases, prefers C16 dihydrosphingosine-l-phosphate as a substrate [SGD]
  • DPL1, Chr IV from 1050450-1052219, reverse complement [yeast_orfs2]
  • Chr IV from 1050450-1052219, reverse complement [yeastorf3.fasta]
  • Chr IV from 1052219-1050450, reverse complement [yeastorf5.fasta]
  • (Q05567) Sphingosine-1-phosphate lyase (EC 4.1.2.27) (SP-lyase) (ySPL) (Sphingosine-1-phosphate aldolase) (Bestowed of sphingosine tolerance 1) [4932.FASTACCERV.txt]
  • DPL1 SGDID:S0002702, Chr IV from 1052220-1050451, reverse complement, Verified ORF [yeastflysequest.fasta]
  • DPL1 SGDID:S0002702, Chr IV from 1052222-1050453, reverse complement, Verified ORF [10112005cervSGD.fasta]
  • Dihydrosphingosine phosphate lyase, regulates intracellular levels of sphingolipid long-chain base phosphates (LCBPs), degrades phosphorylated long chain bases, prefers C16 dihydrosphingosine-l-phosphate as a substrate [Saccharomyces cerevisiae]gi|379994 [nrdb_11152004_Chlamydomonas]
  • DPL1 SGDID:S000002702, Chr IV from 1052222-1050453, reverse complement, Verified ORF, "Dihydrosphingosine phosphate lyase, regulates intracellular levels of sphingolipid long-chain base phosphates (LCBPs), degrades phosphorylated long chain bases, prefers [SGD_S-cerevisiae_na_12-16-2005_con_reversed.fasta]
  • DPL1 SGDID:S000002702, Chr IV from 1052224-1050455, reverse complement, Verified ORF, "Dihydrosphingosine phosphate lyase, regulates intracellular levels of sphingolipid long-chain base phosphates (LCBPs), degrades phosphorylated long chain bases, prefers [yeast-contam.fasta]
  • DPL1 SGDID:S000002702, Chr IV from 1052225-1050456, reverse complement, Verified ORF, "Dihydrosphingosine phosphate lyase, regulates intracellular levels of sphingolipid long-chain base phosphates (LCBPs), degrades phosphorylated long chain bases, prefers [SGD_S-cerevisiae_na_08-19-2008_con_reversed.fasta]
  • Sphingosine-1-phosphate lyase (SP-lyase) (ySPL) (Sphingosine-1-phosphate aldolase) (Bestowed of sphingosine tolerance 1) [nr-271106-contam.fasta]
  • Ydr294cp [Saccharomyces cerevisiae] [nr-271106-contam.fasta]
  • Dihydrosphingosine phosphate lyase, regulates intracellular levels of sphingolipid long-chain base phosphates (LCBPs), degrades phosphorylated long chain bases, prefers C16 dihydrosphingosine-l-phosphate as a substrate; Dpl1p [Saccharomyces cerevisiae] [nr-271106-contam.fasta]
  • DPL1 SGDID:S000002702, Chr IV from 1052225-1050456, reverse complement, Verified ORF, "Dihydrosphingosine phosphate lyase, regulates intracellular levels of sphingolipid long-chain base phosphates (LCBPs), degrades phosphorylated long chain bases, prefers C16 dihydrosphingosine-l-phosphate as a substrate" [yeast-bovrabprots.fasta]
  • DPL1 SGDID:S000002702, Chr IV from 1052224-1050455, reverse complement, Verified ORF, "Dihydrosphingosine phosphate lyase, regulates intracellular levels of sphingolipid long-chain base phosphates (LCBPs), degrades phosphorylated long chain bases, prefers C16 dihydrosphingosine-l-phosphate as a substrate" [yeast-contam_custom.fasta]
  • [chemostatdb.fasta]
  • Sphingosine-1-phosphate lyase OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) GN=DPL1 PE=1 SV=1 [UniProt_S_cerevisiae_20120516_05-16-2012_reversed.fasta]
  • DPL1 SGDID:S000002702, Chr IV from 1052228-1050459, Genome Release 64-1-1, reverse complement, Verified ORF, "Dihydrosphingosine phosphate lyase, regulates intracellular levels of sphingolipid long-chain base phosphates (LCBPs), degrades phosphorylated long chain bases, prefers C16 dihydrosphingosine-l-phosphate as a substrate" [yeast-030211-contam.fasta]
  • DPL1 SGDID:S000002702, Chr IV from 1052228-1050459, Genome Release 64-2-1, reverse complement, Verified ORF, "Dihydrosphingosine phosphate lyase; regulates intracellular levels of sphingolipid long-chain base phosphates (LCBPs), degrades phosphorylated long chain bases, prefers C16 dihydrosphingosine-l-phosphate as a substrate" [20141208_orf_trans.fasta]
  • YDR294C SGDID:S000002702, Chr IV from 1052228-1050459, Genome Release 64-1-1, reverse complement, Verified ORF, "Dihydrosphingosine phosphate lyase, regulates intracellular levels of sphingolipid long-chain base phosphates (LCBPs), degrades phosphorylated long chain bases, prefers C16 dihydrosphingosine-l-phosphate as a substrate" [2016-01-SGD_Yeast_Contam_Riffle_20140507-Ska-Hec-110-tubulin.fasta]
    • Organism: Saccharomyces cerevisiae
    Length: 589 amino acids

    Gene Ontology:
    Cellular Component: endoplasmic reticulum [IDALink to PubMed article]
    Biological Process: cellular response to starvation [IMPLink to PubMed article]
    calcium-mediated signaling [IMPLink to PubMed article]
    sphingolipid metabolic process [IGILink to PubMed article][IMPLink to PubMed article]
    Molecular Function: sphinganine-1-phosphate aldolase activity [IDALink to PubMed article]


    Sequence:
    Sequence:
    [PDR BLAST]
    [ProtParam] 
          1          11         21         31         41         51         
      |          |          |          |          |          |          
    1 MSGVSNKTVS INGWYGMPIH LLREEGDFAQ FMILTINELK IAIHGYLRNT PWYNMLKDYL  60
   61 FVIFCYKLIS NFFYLLKVYG PVRLAVRTYE HSSRRLFRWL LDSPFLRGTV EKEVTKVKQS 120
  121 IEDELIRSDS QLMNFPQLPS NGIPQDDVIE ELNKLNDLIP HTQWKEGKVS GAVYHGGDDL 180
  181 IHLQTIAYEK YCVANQLHPD VFPAVRKMES EVVSMVLRMF NAPSDTGCGT TTSGGTESLL 240
  241 LACLSAKMYA LHHRGITEPE IIAPVTAHAG FDKAAYYFGM KLRHVELDPT TYQVDLGKVK 300
  301 KFINKNTILL VGSAPNFPHG IADDIEGLGK IAQKYKLPLH VDSCLGSFIV SFMEKAGYKN 360
  361 LPLLDFRVPG VTSISCDTHK YGFAPKGSSV IMYRNSDLRM HQYYVNPAWT GGLYGSPTLA 420
  421 GSRPGAIVVG CWATMVNMGE NGYIESCQEI VGAAMKFKKY IQENIPDLNI MGNPRYSVIS 480
  481 FSSKTLNIHE LSDRLSKKGW HFNALQKPVA LHMAFTRLSA HVVDEICDIL RTTVQELKSE 540
  541 SNSKPSPDGT SALYGVAGSV KTAGVADKLI VGFLDALYKL GPGEDTATK

    Protein Complex Data

    No complex found for this protein.

    Mass Spectrometry Data

    The following runs contain data for this protein:

      BAIT COMMENTS PUBLICATION
    View Run MIH1 experimental2 - mih1-2 McCusker D, et al (2007)
    View Run MLP2 #32 Asynchronous Prep-No Phosphopeptide enrichment Keck JM, et al. (2011)
    View Run MLP2 #29 Asynchronous Prep5-TiO2 Flowthrough Keck JM, et al. (2011)
    View Run MLP2 #10 Mitotic Prep1-TiO2 Phosphopeptide enrichment Keck JM, et al. (2011)

    Yeast Two-Hybrid Data

    The following interactions contain this protein:

    NOT SHOWING SINGLE HITS. [ Show Single Hits ]

    [View our yeast two-hybrid interpretation guidelines.]

    No yeast two-hybrid interactions found for this protein.

    Microscopy / Localization Data

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      PROTEIN(S) PUBLICATION
    View Data DPL1 Huh WK, et al. (2003)

    Protein Structure Data


    [What does the above image mean?]
    [View Top Sequence Alignments] [Show Ginzu Version Information]

    Domains predicted:

    #   Region(s) Method Confidence Match Description
    1 View Details [1..79] deduced N/A No confident structure predictions are available.
    2 View Details [80..162] PSI-BLAST 107.0 DOPA decarboxylase
    3 View Details [163..589] PSI-BLAST 107.0 DOPA decarboxylase

    Functions predicted (by domain):

    # Gene Ontology predictions
    1 No functions predicted.
    2
    Term Confidence Notes
  • serine C-palmitoyltransferase activity
    		•  4.27273846204139 bayes_pls_golite062009
  • C-palmitoyltransferase activity
    		•  4.27273846204139 bayes_pls_golite062009
  • catalytic activity
    		•  2.29878871754893 bayes_pls_golite062009
  • transferase activity, transferring nitrogenous groups
    		•  1.18577404365776 bayes_pls_golite062009
  • transaminase activity
    		•  1.15255422926249 bayes_pls_golite062009
  • transferase activity
    		•  0.737426388870721 bayes_pls_golite062009
  • transcription regulator activity
    		•  0.691073358419788 bayes_pls_golite062009
  • binding
    		•  0.661198018681765 bayes_pls_golite062009
  • DNA binding
    		•  0.579562080072574 bayes_pls_golite062009
  • nucleic acid binding
    		•  0.547593348248892 bayes_pls_golite062009
  • C-acyltransferase activity
    		•  0.46392133442786 bayes_pls_golite062009
  • transcription factor activity
    		•  0.352624414131738 bayes_pls_golite062009
  • 4-aminobutyrate transaminase activity
    		•  0.122706514261728 bayes_pls_golite062009
    3 No functions predicted.


    Reference: Malmström L, et al. (2007) Superfamily assignments for the yeast proteome through integration of structure prediction with the gene ontology. PLoS Biol 5(4): e76. doi:10.1371/journal.pbio.0050076


    Philius Transmembrane Prediction:

    Protein predicted to be: GLOBULAR (No transmembrane regions or signal peptide)
    Confidence of classification: 0.94

    Source: Reynolds et al. (2008)

    YRC Informatics Platform - Version 3.0
    Created and Maintained by: Michael Riffle