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    cpin-1 Amidohydrolase-related domain-containing protein [ Caenorhabditis elegans ]

    Gene ID: 185473, updated on 9-Dec-2024

    Summary

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    Official Symbol
    cpin-1
    Official Full Name
    Amidohydrolase-related domain-containing protein
    Primary source
    WormBase:WBGene00000775
    Locus tag
    CELE_F38E11.3
    See related
    AllianceGenome:WB:WBGene00000775
    Gene type
    protein coding
    RefSeq status
    REVIEWED
    Organism
    Caenorhabditis elegans (strain: Bristol N2)
    Lineage
    Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida; Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae; Caenorhabditis
    Summary
    Predicted to enable deaminase activity. Predicted to be active in cytosol. Orthologous to human GDA (guanine deaminase). [provided by Alliance of Genome Resources, Dec 2024]
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    Genomic context

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    See cpin-1 in Genome Data Viewer
    Location:
    chromosome: IV
    Exon count:
    7
    Sequence:
    Chromosome: IV; NC_003282.8 (9451334..9453372)

    Chromosome IV - NC_003282.8Genomic Context describing neighboring genes Neighboring gene SHSP domain-containing protein Neighboring gene SHSP domain-containing protein Neighboring gene ncRNA Neighboring gene PAN domain protein Neighboring gene ncRNA Neighboring gene putative coatomer subunit beta' Neighboring gene ncRNA

    Genomic regions, transcripts, and products

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    Genomic Sequence:
    NC_003282.8

    Go to nucleotide: Graphics FASTA GenBank

    Bibliography

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    Related articles in PubMed

    1. Developing a rapid throughput screen for detection of nematicidal activity of plant cysteine proteinases: the role of Caenorhabditis elegans cystatins. Phiri AM, et al. Parasitology, 2014 Feb. PMID 24001183
    2. Differentially expressed, abundant trans-spliced cDNAs from larval Brugia malayi. Gregory WF, et al. Mol Biochem Parasitol, 1997 Jul. PMID 9233676
    3. Cypin: a cytosolic regulator of PSD-95 postsynaptic targeting. Firestein BL, et al. Neuron, 1999 Nov. PMID 10595517
    4. Systems-level transcriptional regulation of Caenorhabditis elegans metabolism. Nanda S, et al. Mol Syst Biol, 2023 May 9. PMID 36942755, Free PMC Article
    5. Interactome analysis of Caenorhabditis elegans synapses by TurboID-based proximity labeling. Artan M, et al. J Biol Chem, 2021 Sep. PMID 34416233, Free PMC Article

    See all (9) citations in PubMed

    GeneRIFs: Gene References Into Functions

    Interactions

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    Products Interactant Other Gene Complex Source Pubs Description

    General gene information

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    Markers

    Homology

    Gene Ontology Provided by WormBase

    Function Evidence Code Pubs
    enables deaminase activity IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables hydrolase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds IEA
    Inferred from Electronic Annotation
    more info
    		  
    Component Evidence Code Pubs
    is_active_in cytosol IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  

    General protein information

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    Preferred Names
    Amidohydrolase-related domain-containing protein
    NP_501669.1
    • Confirmed by transcript evidence

    NCBI Reference Sequences (RefSeq)

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    Genome Annotation

    The following sections contain reference sequences that belong to a specific genome build. Explain

    Reference assembly

    Genomic

    1. NC_003282.8 Reference assembly

      Range
      9451334..9453372
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NM_069268.4 → NP_501669.1  Amidohydrolase-related domain-containing protein [Caenorhabditis elegans]

      See identical proteins and their annotated locations for NP_501669.1

      Status: REVIEWED

      UniProtKB/TrEMBL
      Q20166
      Conserved Domains (1) summary
      cd01313
      Location:13 → 420
      Met_dep_hydrolase_E; Metallo-dependent hydrolases, subgroup D is part of the superfamily of metallo-dependent hydrolases, a large group of proteins that show conservation in their 3-dimensional fold (TIM barrel) and in details of their active site. The vast majority of the ...
    Nucleotide Protein
    Heading Accession and Version

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