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TIMP4 TIMP metallopeptidase inhibitor 4 [ Callorhinus ursinus (northern fur seal) ]

Gene ID: 112834000, updated on 15-Mar-2024

Summary

Gene symbol
TIMP4
Gene description
TIMP metallopeptidase inhibitor 4
See related
EnsemblRapid:ENSCURG00000013743
Gene type
protein coding
RefSeq status
MODEL
Organism
Callorhinus ursinus
Lineage
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Laurasiatheria; Carnivora; Caniformia; Pinnipedia; Otariidae; Callorhinus
Orthologs
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Genomic context

Location:
chromosome: Un
Exon count:
5
Annotation release Status Assembly Chr Location
100 current ASM326570v1 (GCF_003265705.1) Unplaced Scaffold NW_020312913.1 (5019734..5030464)

NW_020312913.1Genomic Context describing neighboring genes Neighboring gene uncharacterized LOC112834041 Neighboring gene peroxisome proliferator activated receptor gamma Neighboring gene synapsin II Neighboring gene 40S ribosomal protein S20 pseudogene Neighboring gene TAM41 mitochondrial translocator assembly and maintenance homolog

Genomic regions, transcripts, and products

Genomic Sequence:
NW_020312913 Unplaced Scaffold Reference ASM326570v1 Primary Assembly

General protein information

Preferred Names
metalloproteinase inhibitor 4

NCBI Reference Sequences (RefSeq)

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RefSeqs of Annotated Genomes: Callorhinus ursinus 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 ASM326570v1 Primary Assembly

Genomic

  1. NW_020312913.1 Reference ASM326570v1 Primary Assembly

    Range
    5019734..5030464
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. XM_025885441.1XP_025741226.1  metalloproteinase inhibitor 4

    UniProtKB/TrEMBL
    A0A3Q7RL49
    Related
    ENSCURP00000022239.1, ENSCURT00000025564.1
    Conserved Domains (1) summary
    cd03585
    Location:30213
    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 ...