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ADAMTS4 ADAM metallopeptidase with thrombospondin type 1 motif 4 [ Homo sapiens (human) ]

Gene ID: 9507, updated on 7-Dec-2018

Summary

Official Symbol
ADAMTS4provided by HGNC
Official Full Name
ADAM metallopeptidase with thrombospondin type 1 motif 4provided by HGNC
Primary source
HGNC:HGNC:220
See related
Ensembl:ENSG00000158859 MIM:603876
Gene type
protein coding
RefSeq status
REVIEWED
Organism
Homo sapiens
Lineage
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo
Also known as
ADMP-1; ADAMTS-2; ADAMTS-4
Summary
This gene encodes a member of the ADAMTS (a disintegrin and metalloproteinase with thrombospondin motifs) protein family. Members of this family share several distinct protein modules, including a propeptide region, a metalloproteinase domain, a disintegrin-like domain, and a thrombospondin type 1 (TS) motif. Individual members of this family differ in the number of C-terminal TS motifs, and some have unique C-terminal domains. The enzyme encoded by this gene lacks a C-terminal TS motif. The encoded preproprotein is proteolytically processed to generate the mature protease. This protease is responsible for the degradation of aggrecan, a major proteoglycan of cartilage, and brevican, a brain-specific extracellular matrix protein. The expression of this gene is upregulated in arthritic disease and this may contribute to disease progression through the degradation of aggrecan. Alternative splicing results in multiple transcript variants, at least one of which encodes an isoform that is proteolytically processed. [provided by RefSeq, Feb 2016]
Expression
Broad expression in gall bladder (RPKM 12.3), appendix (RPKM 11.7) and 19 other tissues See more
Orthologs

Genomic context

See ADAMTS4 in Genome Data Viewer
Location:
1q23.3
Exon count:
9
Annotation release Status Assembly Chr Location
109 current GRCh38.p12 (GCF_000001405.38) 1 NC_000001.11 (161189729..161202339, complement)
105 previous assembly GRCh37.p13 (GCF_000001405.25) 1 NC_000001.10 (161159538..161168845, complement)

Chromosome 1 - NC_000001.11Genomic Context describing neighboring genes Neighboring gene ubiquitin specific peptidase 21 Neighboring gene protoporphyrinogen oxidase Neighboring gene beta-1,4-galactosyltransferase 3 Neighboring gene NADH:ubiquinone oxidoreductase core subunit S2 Neighboring gene Fc fragment of IgE receptor Ig Neighboring gene apolipoprotein A2

Genomic regions, transcripts, and products

Expression

  • Project title: HPA RNA-seq normal tissues
  • Description: RNA-seq was performed of tissue samples from 95 human individuals representing 27 different tissues in order to determine tissue-specificity of all protein-coding genes
  • BioProject: PRJEB4337
  • Publication: PMID 24309898
  • Analysis date: Wed Apr 4 07:08:55 2018

Bibliography

GeneRIFs: Gene References Into FunctionsWhat's a GeneRIF?

Pathways from BioSystems

  • Defective B3GALTL causes Peters-plus syndrome (PpS), organism-specific biosystem (from REACTOME)
    Defective B3GALTL causes Peters-plus syndrome (PpS), organism-specific biosystemHuman beta-1,3-glucosyltransferase like protein (B3GALTL, HGNC Approved Gene Symbol: B3GLCT; MIM:610308; CAZy family GT31), localised on the ER membrane, glucosylates O-fucosylated proteins. The resu...
  • Degradation of the extracellular matrix, organism-specific biosystem (from REACTOME)
    Degradation of the extracellular matrix, organism-specific biosystemMatrix metalloproteinases (MMPs), previously referred to as matrixins because of their role in degradation of the extracellular matrix (ECM), are zinc and calcium dependent proteases belonging to the...
  • Disease, organism-specific biosystem (from REACTOME)
    Disease, organism-specific biosystemBiological processes are captured in Reactome by identifying the molecules (DNA, RNA, protein, small molecules) involved in them and describing the details of their interactions. From this molecular ...
  • Diseases associated with O-glycosylation of proteins, organism-specific biosystem (from REACTOME)
    Diseases associated with O-glycosylation of proteins, organism-specific biosystemGlycosylation is the most abundant modification of proteins, variations of which occur in all living cells. Glycosylation can be further categorized into N-linked (where the oligosaccharide is conjug...
  • Diseases of glycosylation, organism-specific biosystem (from REACTOME)
    Diseases of glycosylation, organism-specific biosystemDiseases of glycosylation, usually referred to as congenital disorders of glycosylation (CDG), are rare inherited disorders ascribing defects of nucleotide-sugar biosynthesis and transport, glycosylt...
  • Endochondral Ossification, organism-specific biosystem (from WikiPathways)
    Endochondral Ossification, organism-specific biosystemEndochondral ossification is the process by which the embryonic cartilaginous model of most bones contributes to longitudinal growth and is gradually replaced by bone. During endochondral ossificatio...
  • Extracellular matrix organization, organism-specific biosystem (from REACTOME)
    Extracellular matrix organization, organism-specific biosystemThe extracellular matrix is a component of all mammalian tissues, a network consisting largely of the fibrous proteins collagen, elastin and associated-microfibrils, fibronectin and laminins embedded...
  • Metabolism of proteins, organism-specific biosystem (from REACTOME)
    Metabolism of proteins, organism-specific biosystemProtein metabolism comprises the pathways of translation, post-translational modification and protein folding.
  • O-glycosylation of TSR domain-containing proteins, organism-specific biosystem (from REACTOME)
    O-glycosylation of TSR domain-containing proteins, organism-specific biosystemThe O-fucosylation of proteins containing thrombospondin type 1 repeat (TSR) domains is an important PTM, regulating many biological processes such as Notch signalling, inflammation, wound healing, a...
  • O-linked glycosylation, organism-specific biosystem (from REACTOME)
    O-linked glycosylation, organism-specific biosystemO-glycosylation is an important post-translational modification (PTM) required for correct functioning of many proteins (Van den Steen et al. 1998, Moremen et al. 2012). The O-glycosylation of protei...
  • Post-translational protein modification, organism-specific biosystem (from REACTOME)
    Post-translational protein modification, organism-specific biosystemAfter translation, many newly formed proteins undergo further covalent modifications that alter their functional properties and that are essentially irreversible under physiological conditions in the...

Interactions

Products Interactant Other Gene Complex Source Pubs Description

General gene information

Markers

Homology

Clone Names

  • KIAA0688

Gene Ontology Provided by GOA

Function Evidence Code Pubs
metal ion binding IEA
Inferred from Electronic Annotation
more info
 
metalloendopeptidase activity TAS
Traceable Author Statement
more info
 
metallopeptidase activity TAS
Traceable Author Statement
more info
PubMed 
peptidase activity TAS
Traceable Author Statement
more info
PubMed 
protease binding IPI
Inferred from Physical Interaction
more info
PubMed 
protein binding IPI
Inferred from Physical Interaction
more info
PubMed 
Process Evidence Code Pubs
extracellular matrix disassembly TAS
Traceable Author Statement
more info
 
proteolysis IEA
Inferred from Electronic Annotation
more info
 
skeletal system development TAS
Traceable Author Statement
more info
PubMed 
Component Evidence Code Pubs
collagen-containing extracellular matrix HDA PubMed 
extracellular region TAS
Traceable Author Statement
more info
 
extracellular space IDA
Inferred from Direct Assay
more info
PubMed 
nuclear speck IDA
Inferred from Direct Assay
more info
 

General protein information

Preferred Names
A disintegrin and metalloproteinase with thrombospondin motifs 4
Names
ADAM-TS 4
ADAM-TS4
a disintegrin-like and metalloprotease (reprolysin type) with thrombospondin type 1 motif, 4
aggrecanase-1
epididymis secretory sperm binding protein
NP_001307265.1
NP_005090.3

NCBI Reference Sequences (RefSeq)

RefSeqs maintained independently of Annotated Genomes

These reference sequences exist independently of genome builds. Explain

These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above.

mRNA and Protein(s)

  1. NM_001320336.1NP_001307265.1  A disintegrin and metalloproteinase with thrombospondin motifs 4 isoform 2 precursor

    Status: REVIEWED

    Description
    Transcript Variant: This variant (2, also known as ADAMTS4_v1) uses an alternate splice site in the 3' coding region resulting in a frameshift compared to variant 1. The encoded isoform (2) has a longer and distinct C-terminus compared to isoform 1, but may undergo proteolytic processing similar to isoform 1.
    Source sequence(s)
    AA603151, AB014588, AF148213, AY358886, BC063293, DA098917, DQ364570
    UniProtKB/Swiss-Prot
    O75173
    Conserved Domains (5) summary
    smart00209
    Location:531575
    TSP1; Thrombospondin type 1 repeats
    cd04273
    Location:218425
    ZnMc_ADAMTS_like; Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) are glycoproteins, which play roles in cell signaling, cell fusion, and cell-cell interactions. This particular subfamily represents domain architectures that ...
    pfam01421
    Location:218428
    Reprolysin; Reprolysin (M12B) family zinc metalloprotease
    pfam01562
    Location:70181
    Pep_M12B_propep; Reprolysin family propeptide
    cl15456
    Location:438509
    ADAM_CR; ADAM cysteine-rich
  2. NM_005099.6NP_005090.3  A disintegrin and metalloproteinase with thrombospondin motifs 4 isoform 1 preproprotein

    See identical proteins and their annotated locations for NP_005090.3

    Status: REVIEWED

    Description
    Transcript Variant: This variant (1) represents the longer transcript and encodes the shorter isoform (1).
    Source sequence(s)
    AA603151, AB014588, AF148213, AL590714, AY358886, BC063293, DA098917
    Consensus CDS
    CCDS1223.1
    UniProtKB/Swiss-Prot
    O75173
    Related
    ENSP00000356975.4, ENST00000367996.5
    Conserved Domains (6) summary
    smart00209
    Location:531575
    TSP1; Thrombospondin type 1 repeats
    cd04273
    Location:218425
    ZnMc_ADAMTS_like; Zinc-dependent metalloprotease, ADAMTS_like subgroup. ADAMs (A Disintegrin And Metalloprotease) are glycoproteins, which play roles in cell signaling, cell fusion, and cell-cell interactions. This particular subfamily represents domain architectures that ...
    pfam01421
    Location:218428
    Reprolysin; Reprolysin (M12B) family zinc metalloprotease
    pfam01562
    Location:70181
    Pep_M12B_propep; Reprolysin family propeptide
    pfam05986
    Location:687802
    ADAM_spacer1; ADAM-TS Spacer 1
    cl15456
    Location:438509
    ADAM_CR; ADAM cysteine-rich

RefSeqs of Annotated Genomes: Homo sapiens Annotation Release 109

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

Reference GRCh38.p12 Primary Assembly

Genomic

  1. NC_000001.11 Reference GRCh38.p12 Primary Assembly

    Range
    161189729..161202339 complement
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

RNA

  1. XR_001737549.2 RNA Sequence

  2. XR_001737548.2 RNA Sequence

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