Version 5.4
Mus musculus Gene: Adamts7
Summary
InnateDB Gene IDBG-190774.6
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol Adamts7
Gene Name a disintegrin-like and metallopeptidase (reprolysin type) with thrombospondin type 1 motif, 7
Synonyms ADAM-TS7; ADAMTS7B
Species Mus musculus
Ensembl Gene ENSMUSG00000032363
Encoded Proteins
IDBP-254662
a disintegrin-like and metallopeptidase (reprolysin type) with thrombospondin type 1 motif, 7
IDBP-254664
a disintegrin-like and metallopeptidase (reprolysin type) with thrombospondin type 1 motif, 7
IDBP-539183
a disintegrin-like and metallopeptidase (reprolysin type) with thrombospondin type 1 motif, 7
IDBP-534219
a disintegrin-like and metallopeptidase (reprolysin type) with thrombospondin type 1 motif, 7
IDBP-622706
a disintegrin-like and metallopeptidase (reprolysin type) with thrombospondin type 1 motif, 7
Protein Structure
Useful resources Stemformatics EHFPI ImmGen
Entrez Gene
Summary This gene does not have any Entrez summary - the following is the summary from its human ortholog ENSG00000136378:
The protein encoded by this gene is a member of the ADAMTS (a disintegrin and metalloproteinase with thrombospondin motifs) 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 protein encoded by this gene contains two C-terminal TS motifs. [provided by RefSeq, Jul 2008]
Gene Information
Type Protein coding
Genomic Location Chromosome 9:90163069-90208071
Strand Forward strand
Band E3.1
Transcripts
ENSMUST00000113060 ENSMUSP00000108683
ENSMUST00000113059 ENSMUSP00000108682
ENSMUST00000134996 ENSMUSP00000119744
ENSMUST00000147250 ENSMUSP00000115972
ENSMUST00000144943
ENSMUST00000138227
ENSMUST00000124441
ENSMUST00000167122 ENSMUSP00000129292
Interactions
Number of Interactions This gene and/or its encoded proteins are associated with 0 experimentally validated interaction(s) in this database.
Gene Ontology

Molecular Function
Accession GO Term
GO:0004222 metalloendopeptidase activity
GO:0005515 protein binding
GO:0008233 peptidase activity
GO:0008237 metallopeptidase activity
GO:0008270 zinc ion binding
Biological Process
GO:0006508 proteolysis
GO:0032331 negative regulation of chondrocyte differentiation
GO:0051603 proteolysis involved in cellular protein catabolic process
GO:0071347 cellular response to interleukin-1
GO:0071356 cellular response to tumor necrosis factor
GO:0071773 cellular response to BMP stimulus
Cellular Component
GO:0005576 extracellular region
GO:0005578 proteinaceous extracellular matrix
GO:0009986 cell surface
GO:0031012 extracellular matrix
Orthologs
Species
Homo sapiens
Bos taurus
Gene ID
Gene Order
ENSG00000136378
View Gene Order
ENSBTAG00000001396
Not yet available
Pathways
NETPATH
REACTOME
REACT_211817
O-glycosylation of TSR domain-containing proteins pathway
REACT_247926
Metabolism of proteins pathway
REACT_236283
Post-translational protein modification pathway
REACT_204003
O-linked glycosylation pathway
KEGG
INOH
PID NCI
Pathway Predictions based on Human Orthology Data
NETPATH
REACTOME
REACT_22161
Post-translational protein modification pathway
REACT_200727
O-linked glycosylation pathway
REACT_17015
Metabolism of proteins pathway
REACT_200626
O-glycosylation of TSR domain-containing proteins pathway
KEGG
INOH
PID NCI
Cross-References
SwissProt
TrEMBL
UniProt Splice Variant
Entrez Gene 108153
UniGene Mm.102141
RefSeq XM_006510761 NM_001003911 XM_006510758 XM_006510759 XM_006510763
OMIM
CCDS CCDS40724
HPRD
IMGT
MGI ID MGI:1347346
MGI Symbol Adamts7
EMBL
GenPept
RNA Seq Atlas 108153

If you use InnateDB for your research, please cite the following publication:

Breuer et al., InnateDB: systems biology of innate immunity and beyond - recent updates and continuing curation. Nucl. Acids Res. (2013) 41 (D1) 

InnateDB is being developed jointly by the Brinkman Laboratory (Simon Fraser University, British Columbia, Canada), the Hancock Laboratory (University of British Columbia, Vancouver, British Columbia) and the Lynn EMBL Australia Group (South Australian Health & Medical Research Institute and Flinders University, Adelaide, Australia).

Funding is currently provided by Allergen and EMBL Australia. Previous funding has been provided by Genome Canada, the Foundation for the National Institutes of Health through the Grand Challenges in Global Health initiative and by Teagasc. InnateDB curated interactions are licensed under the Design Science License. All other data is licensed under the terms of the originating database. Contact: innatedb-mail@sfu.ca