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    cri-2 Putative metalloproteinase inhibitor tag-225 [ Caenorhabditis elegans ]

    Gene ID: 179197, updated on 9-Dec-2024

    Summary

    Official Symbol
    cri-2
    Official Full Name
    Putative metalloproteinase inhibitor tag-225
    Primary source
    WormBase:WBGene00019478
    Locus tag
    CELE_K07C11.5
    See related
    AllianceGenome:WB:WBGene00019478
    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 metalloendopeptidase inhibitor activity. Predicted to be involved in negative regulation of membrane protein ectodomain proteolysis. Predicted to be located in extracellular region. Predicted to be active in extracellular matrix and extracellular space. Is expressed in several structures, including enteric muscle; gonad; hyp12; nerve ring; and tail hypodermis. Human ortholog(s) of this gene implicated in Moyamoya disease; Sorsby's fundus dystrophy; breast carcinoma; nephroblastoma; and urinary bladder cancer. Orthologous to several human genes including TIMP2 (TIMP metallopeptidase inhibitor 2). [provided by Alliance of Genome Resources, Dec 2024]
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    Genomic context

    See cri-2 in Genome Data Viewer
    Location:
    chromosome: V
    Exon count:
    3
    Sequence:
    Chromosome: V; NC_003283.11 (8201808..8202523)

    Chromosome V - NC_003283.11Genomic Context describing neighboring genes Neighboring gene Uncharacterized protein Neighboring gene ncRNA Neighboring gene Rieske domain-containing protein Neighboring gene Carboxylic ester hydrolase Neighboring gene ncRNA Neighboring gene NTR domain-containing protein Neighboring gene Calcineurin-like phosphoesterase domain-containing protein;UPF0046 protein K07C11.7

    Interactions

    Products Interactant Other Gene Complex Source Pubs Description

    General gene information

    Markers

    Gene Ontology Provided by WormBase

    Function Evidence Code Pubs
    enables metal ion binding IEA
    Inferred from Electronic Annotation
    more info
     
    enables metalloendopeptidase inhibitor activity IBA
    Inferred from Biological aspect of Ancestor
    more info
     
    enables metalloendopeptidase inhibitor activity IEA
    Inferred from Electronic Annotation
    more info
     
    enables peptidase inhibitor activity IEA
    Inferred from Electronic Annotation
    more info
     
    Process Evidence Code Pubs
    involved_in negative regulation of membrane protein ectodomain proteolysis IBA
    Inferred from Biological aspect of Ancestor
    more info
     
    Component Evidence Code Pubs
    is_active_in extracellular matrix IBA
    Inferred from Biological aspect of Ancestor
    more info
     
    located_in extracellular region IEA
    Inferred from Electronic Annotation
    more info
     
    is_active_in extracellular space IBA
    Inferred from Biological aspect of Ancestor
    more info
     

    General protein information

    Preferred Names
    Putative metalloproteinase inhibitor tag-225
    NP_505113.1
    • 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_003283.11 Reference assembly

      Range
      8201808..8202523
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NM_072712.8NP_505113.1  Putative metalloproteinase inhibitor tag-225 [Caenorhabditis elegans]

      See identical proteins and their annotated locations for NP_505113.1

      Status: REVIEWED

      UniProtKB/Swiss-Prot
      Q21265
      Conserved Domains (1) summary
      cd03577
      Location:21149
      NTR_TIMP_like; NTR domain, TIMP-like subfamily; TIMPs, or tissue inibitors of metalloproteases, are essential regulators of extracellular matrix turnover and remodeling. They form complexes with matrix metalloproteases (MMPs) and inactivate them irreversibly by ...