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TIMP3 TIMP metallopeptidase inhibitor 3 [ Cercocebus atys (sooty mangabey) ]

Gene ID: 105575771, updated on 19-Jun-2024

Summary

Gene symbol
TIMP3
Gene description
TIMP metallopeptidase inhibitor 3
See related
Ensembl:ENSCATG00000042645
Gene type
protein coding
RefSeq status
MODEL
Organism
Cercocebus atys
Lineage
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Cercopithecidae; Cercopithecinae; Cercocebus
Orthologs
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Genomic context

Location:
chromosome: Un
Exon count:
5
Annotation release Status Assembly Chr Location
100 current Caty_1.0 (GCF_000955945.1) Unplaced Scaffold NW_012004276.1 (8205558..8268557)

NW_012004276.1Genomic Context describing neighboring genes Neighboring gene uncharacterized LOC105575773 Neighboring gene uncharacterized LOC105575772 Neighboring gene synapsin III Neighboring gene LARGE xylosyl- and glucuronyltransferase 1 Neighboring gene aconitate hydratase, mitochondrial pseudogene

Genomic regions, transcripts, and products

Genomic Sequence:
NW_012004276.1 Unplaced Scaffold Reference Caty_1.0

General protein information

Preferred Names
metalloproteinase inhibitor 3

NCBI Reference Sequences (RefSeq)

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RefSeqs of Annotated Genomes: Cercocebus atys Annotation Release 100 details...Open this link in a new tab

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

Reference Caty_1.0

Genomic

  1. NW_012004276.1 Reference Caty_1.0

    Range
    8205558..8268557
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. XM_012038003.1XP_011893393.1  metalloproteinase inhibitor 3

    See identical proteins and their annotated locations for XP_011893393.1

    UniProtKB/TrEMBL
    A0A2K5NRJ2
    Related
    ENSCATP00000040148.1, ENSCATT00000064465.1
    Conserved Domains (1) summary
    cd03585
    Location:24200
    NTR_TIMP; NTR domain, TIMP 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 ...