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Protein Overview: DAP2

General Information:
Name(s) found: DAP2 / YHR028C [SGD]
Description(s) found:
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  • pir||A30107 dipeptidyl aminopeptidase B (EC 3.4.14.-) - yeast (Saccharomyces cerevisiae) [NCBI NR]
  • gi|729295|sp|P18962.2|DAP2_YEAST RecName: Full=Dipeptidyl aminopeptidase B; Short=DPAP B; AltName: Full=YSCV [NCBI NR]
  • gi|6321817|ref|NP_011893.1| Dipeptidyl aminopeptidase, synthesized as a glycosylated precursor; localizes to the vacuolar membrane; similar to Ste13p; Dap2p [Saccharomyces cerevisiae] [NCBI NR]
  • gi|500698|gb|AAB68879.1| Dap2p: Dipeptidyl aminopeptidase B (DAP2_YEAST) [Saccharomyces cerevisiae] [NCBI NR]
  • Dipeptidyl aminopeptidase B OS=Saccharomyces cerevisiae GN=DAP2 PE=2 SV=2 [Swiss-Prot]
  • DAP2 Serine hydrolase/alpha/beta hydrolase subset, dipeptidyl aminopeptidase B [mips]
  • Dipeptidyl aminopeptidase, synthesized as a glycosylated precursor; localizes to the vacuolar membrane; similar to Ste13p [SGD]
  • DAP2, Chr VIII from 164969-167425, reverse complement [yeast_orfs2]
  • Chr VIII from 164969-167425, reverse complement [yeastorf3.fasta]
  • Chr VIII from 167425-164969, reverse complement [yeastorf5.fasta]
  • (P18962) Dipeptidyl aminopeptidase B (EC 3.4.14.-) (DPAP B) (YSCV) [4932.FASTACCERV.txt]
  • DAP2 SGDID:S0001070, Chr VIII from 167426-164970, reverse complement, Verified ORF [yeastflysequest.fasta]
  • Dap2p [Saccharomyces cerevisiae]gi|7428199|pir||A30107 dipeptidyl aminopeptidase B (EC 3.4.14.-) - yeast (Saccharomyces cerevisiae)gi|500698|gb|AAB68879.1| Dap2p: Dipeptidyl aminopeptidase B (DAP2_YEAST) [Saccharomyces cerevisiae]gi|729295|sp|P18962|D [nrdb_11152004_Chlamydomonas]
  • DAP2 SGDID:S000001070, Chr VIII from 167427-164971, reverse complement, Verified ORF, "Dipeptidyl aminopeptidase, synthesized as a glycosylated precursor; localizes to the vacuolar membrane; similar to Ste13p" [SGD_S-cerevisiae_na_12-16-2005_con_reversed.fasta]
  • Dipeptidyl aminopeptidase B (DPAP B) (YSCV) [nr-271106-contam.fasta]
  • Dap2p: Dipeptidyl aminopeptidase B (DAP2_YEAST) [Saccharomyces cerevisiae] [nr-271106-contam.fasta]
  • Dipeptidyl aminopeptidase, synthesized as a glycosylated precursor; localizes to the vacuolar membrane; similar to Ste13p; Dap2p [Saccharomyces cerevisiae] [nr-271106-contam.fasta]
  • [chemostatdb.fasta]
  • Dipeptidyl aminopeptidase B OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) GN=DAP2 PE=1 SV=2 [UniProt_S_cerevisiae_20120516_05-16-2012_reversed.fasta]
  • DAP2 SGDID:S000001070, Chr VIII from 167434-164978, Genome Release 64-1-1, reverse complement, Verified ORF, "Dipeptidyl aminopeptidase, synthesized as a glycosylated precursor; localizes to the vacuolar membrane; similar to Ste13p" [yeast-030211-contam.fasta]
  • DAP2 SGDID:S000001070, Chr VIII from 167434-164978, Genome Release 64-2-1, reverse complement, Verified ORF, "Dipeptidyl aminopeptidase; synthesized as a glycosylated precursor; localizes to the vacuolar membrane; similar to Ste13p" [20141208_orf_trans.fasta]
  • YHR028C SGDID:S000001070, Chr VIII from 167434-164978, Genome Release 64-1-1, reverse complement, Verified ORF, "Dipeptidyl aminopeptidase, synthesized as a glycosylated precursor; localizes to the vacuolar membrane; similar to Ste13p" [2016-01-SGD_Yeast_Contam_Riffle_20140507-Ska-Hec-110-tubulin.fasta]
    • Organism: Saccharomyces cerevisiae
    Length: 818 amino acids

    Gene Ontology:
    Cellular Component: fungal-type vacuole membrane [IDALink to PubMed article]
    Biological Process: protein processing [ISSLink to PubMed article]
    Molecular Function: dipeptidyl-peptidase and tripeptidyl-peptidase activity [IDALink to PubMed article]


    Sequence:
    Sequence:
    [PDR BLAST]
    [ProtParam] 
          1          11         21         31         41         51         
      |          |          |          |          |          |          
    1 MEGGEEEVER IPDELFDTKK KHLLDKLIRV GIILVLLIWG TVLLLKSIPH HSNTPDYQEP  60
   61 NSNYTNDGKL KVSFSVVRNN TFQPKYHELQ WISDNKIESN DLGLYVTFMN DSYVVKSVYD 120
  121 DSYNSVLLEG KTFIHNGQNL TVESITASPD LKRLLIRTNS VQNWRHSTFG SYFVYDKSSS 180
  181 SFEEIGNEVA LAIWSPNSND IAYVQDNNIY IYSAISKKTI RAVTNDGSSF LFNGKPDWVY 240
  241 EEEVFEDDKA AWWSPTGDYL AFLKIDESEV GEFIIPYYVQ DEKDIYPEMR SIKYPKSGTP 300
  301 NPHAELWVYS MKDGTSFHPR ISGNKKDGSL LITEVTWVGN GNVLVKTTDR SSDILTVFLI 360
  361 DTIAKTSNVV RNESSNGGWW EITHNTLFIP ANETFDRPHN GYVDILPIGG YNHLAYFENS 420
  421 NSSHYKTLTE GKWEVVNGPL AFDSMENRLY FISTRKSSTE RHVYYIDLRS PNEIIEVTDT 480
  481 SEDGVYDVSF SSGRRFGLLT YKGPKVPYQK IVDFHSRKAE KCDKGNVLGK SLYHLEKNEV 540
  541 LTKILEDYAV PRKSFRELNL GKDEFGKDIL VNSYEILPND FDETLSDHYP VFFFAYGGPN 600
  601 SQQVVKTFSV GFNEVVASQL NAIVVVVDGR GTGFKGQDFR SLVRDRLGDY EARDQISAAS 660
  661 LYGSLTFVDP QKISLFGWSY GGYLTLKTLE KDGGRHFKYG MSVAPVTDWR FYDSVYTERY 720
  721 MHTPQENFDG YVESSVHNVT ALAQANRFLL MHGTGDDNVH FQNSLKFLDL LDLNGVENYD 780
  781 VHVFPDSDHS IRYHNANVIV FDKLLDWAKR AFDGQFVK

    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 VAM3 sample: hx3 Hao Xu, et al. (2010)
    View Run VAM3 Sample: HX11 - both fusion and trans-SNARE complex formation take place. Hao Xu, et al. (2010)
    View Run VAM3 Sample: HX12 - trans-SNARE complex formation and fusion are inhibited (control). Hao Xu, et al. (2010)
    View Run VAM3 Sample: HX13 - trans-SNARE complex forms but fusion is blocked. Hao Xu, et al. (2010)
    View Run VAM3 Sample: HX14 - mixture in detergent (control). Hao Xu, et al. (2010)

    Yeast Two-Hybrid Data

    The following interactions contain this protein:

    SHOWING SINGLE HITS. [ Hide 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


    [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..257] PSI-BLAST 35.09691 Tup1, C-terminal domain
    2 View Details [258..353]
    [365..555]    		 PSI-BLAST 83.0 Prolyl oligopeptidase, N-terminal domain; Prolyl oligopeptidase, C-terminal domain
    3 View Details [354..364]
    [556..818]    		 PSI-BLAST 83.0 Prolyl oligopeptidase, N-terminal domain; Prolyl oligopeptidase, C-terminal domain

    Functions predicted (by domain):

    # Gene Ontology predictions
    1
    Term Confidence Notes
  • hydrolase activity
    		•  4.09944423676394 bayes_pls_golite062009
  • peptidase activity
    		•  2.49064988313037 bayes_pls_golite062009
  • peptidase activity, acting on L-amino acid peptides
    		•  2.10044305272656 bayes_pls_golite062009
  • catalytic activity
    		•  1.39629727416851 bayes_pls_golite062009
  • palmitoyl-(protein) hydrolase activity
    		•  1.01438408843885 bayes_pls_golite062009
  • binding
    		•  0.549512873906854 bayes_pls_golite062009
  • heparin binding
    		•  0.437236652275566 bayes_pls_golite062009
  • endopeptidase activity
    		•  0.43631945855397 bayes_pls_golite062009
  • hydrolase activity, acting on ester bonds
    		•  0.282381128231187 bayes_pls_golite062009
    2 No functions predicted.
    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:

    [View Details]
    Source: Reynolds et al. 2008. Manuscript submitted Philius confidence legend
    YRC Informatics Platform - Version 3.0
    Created and Maintained by: Michael Riffle