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Protein Overview: Vha100-1-PC, Vha...

General Information:
Name(s) found: Vha100-1-PE / FBpp0084750 [FlyBase]
Vha100-1-PC / FBpp0084743 [FlyBase]
Description(s) found:
Found 35 descriptions.
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  • The gene Vha100-1 is referred to in FlyBase by the symbol Dmel\Vha100-1 (CG1709, FBgn0028671). It is a protein_coding_gene from Drosophila melanogaster. Its sequence location is 3R:24956772..24963702. It has the cytological map location 98F12. There is experimental evidence that it has the molecular function</span>: calmodulin binding. An electronic pipeline based on InterPro domains suggests that it is involved in the biological process</span>: ATP synthesis coupled proton transport. 10 alleles are reported. No phenotypic data is available. It has 10 annotated transcripts and 10 annotated polypeptides. [FlyBase]
  • The gene Vha100-1 is referred to in FlyBase by the symbol Dmel\Vha100-1 (CG1709, FBgn0028671). It is a protein_coding_gene from Drosophila melanogaster. Its sequence location is 3R:24956772..24963702. It has the cytological map location 98F12. There is experimental evidence that it has the molecular function</span>: calmodulin binding. An electronic pipeline based on InterPro domains suggests that it is involved in the biological process</span>: ATP synthesis coupled proton transport. 10 alleles are reported. No phenotypic data is available. It has 10 annotated transcripts and 10 annotated polypeptides. [FlyBase]
    • Organism: Drosophila melanogaster
    Length: 855 amino acids

    Gene Ontology:
    Cellular Component: vacuolar proton-transporting V-type ATPase, V0 domain [ISS]
    synapse [IDA]
    Biological Process: ATP synthesis coupled proton transport [IEA]
    Molecular Function: calmodulin binding [IDA]
    hydrogen-exporting ATPase activity, phosphorylative mechanism [ISS]


    Sequence:
    Sequence:
    [PDR BLAST]
    [ProtParam] 
          1          11         21         31         41         51         
      |          |          |          |          |          |          
    1 MGSLFRSEEM ALCQLFLQSE AAYACVSELG ELGLVQFRDL NPDVNAFQRK FVNEVRRCDE  60
   61 MERKLRYLEK EIKKDGIPML DTGESPEAPQ PREMIDLEAT FEKLENELRE VNQNAEALKR 120
  121 NFLELTELKH ILRKTQVFFD ESVPTVYKSS GAYSSSKYRR YPQMADNQNE DEQAQLLGEE 180
  181 GVRASQPGQN LKLGFVAGVI LRERLPAFER MLWRACRGNV FLRQAMIETP LEDPTNGDQV 240
  241 HKSVFIIFFQ GDQLKTRVKK ICEGFRATLY PCPEAPADRR EMAMGVMTRI EDLNTVLGQT 300
  301 QDHRHRVLVA AAKNLKNWFV KVRKIKAIYH TLNLFNLDVT QKCLIAECWV PLLDIETIQL 360
  361 ALRRGTERSG SSVPPILNRM QTFENPPTYN RTNKFTKAFQ ALIDAYGVAS YREMNPAPYT 420
  421 IITFPFLFAV MFGDLGHGAI MALFGLWMIR KEKGLAAQKT DNEIWNIFFG GRYIIFLMGV 480
  481 FSMYTGLIYN DIFSKSLNIF GSHWHLSYNK STVMENKFLQ LSPKGDYEGA PYPFGMDPIW 540
  541 QVAGANKIIF HNAYKMKISI IFGVIHMIFG VVMSWHNHTY FRNRISLLYE FIPQLVFLLL 600
  601 LFFYMVLLMF IKWIKFAATN DKPYSEACAP SILITFIDMV LFNTPKPPPE NCETYMFMGQ 660
  661 HFIQVLFVLV AVGCIPVMLL AKPLLIMQAR KQANVQPIAG ATSDAEAGGV SNSGSHGGGG 720
  721 GHEEEEELSE IFIHQSIHTI EYVLGSVSHT ASYLRLWALS LAHAQLAEVL WTMVLSIGLK 780
  781 QEGPVGGIVL TCVFAFWAIL TVGILVLMEG LSAFLHTLRL HWVEFQSKFY KGQGYAFQPF 840
  841 SFDAIIENGA AAAEE

    Protein Complex Data

    No complex found for this protein.

    Mass Spectrometry Data

    No mass spectrometry results found for this protein.

    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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    No microscopy data found in the PDR for this protein.

    Protein Structure Data


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    [View Top Sequence Alignments] [Show Ginzu Version Information]

    Domains predicted:

    #   Region(s) Method Confidence Match Description
    1 View Details [1..497] PSI-BLAST 6.69897 COLICIN IA
    2 View Details [498..724] deduced N/A No confident structure predictions are available.
    3 View Details [725..855] MSA 3.123969 View MSA. No confident structure predictions are available.


    Reference: Drew K, et al. (2011) The proteome folding project: Proteome-scale prediction of structure and function. Genome Res. 2011 Sep 16


    Philius Transmembrane Prediction:

    [View Details]
    Source: Reynolds et al. 2008. Manuscript submitted Philius confidence legend
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