Adam10
entrez
11487
canonical
uniprot
O35598
canonical
ensembl
ENSMUSG00000054693
resolver
ensp
ENSMUSP00000063839
resolver
enst
ENSMUST00000067880
resolver
genesymbol
Adam10
resolver
genesymbol_syn
Kuz
resolver
genesymbol_syn
Madm
resolver
uniprot
B8JJJ0
resolver
uniprot
Q6NZC0
resolver
uniprot_entry
ADA10_MOUSE
resolver
uniprot_entry
Q6NZC0_MOUSE
resolver
uniprot_sec
B8JJJ0
resolver
activity_regulation
ACTIVITY REGULATION: Catalytically inactive when the propeptide is intact and associated with the mature enzyme (By similarity). The disintegrin and cysteine-rich regions modulate access of substrates to exerts an inhibitory effect on the cleavage of ADAM10 substrates (By similarity). {ECO:0000250|UniProtKB:O14672, ECO:0000250|UniProtKB:Q10741}.
uniprot
proteins
amino_acid_sequence
MVLPTVLILLLSWAAGLGGQYGNPLNKYIRHYEGLSYNVDSLHQKHQRAKRAVSHEDQFLLLDFHAHGRQFNLRMKRDTSLFSDEFKVETSNKVLDYDTSHIYTGHIYGEEGSFSHGSVIDGRFEGFIKTRGGTFYIEPAERYIKDRILPFHSVIYHEDDINYPHKYGPQGGCADHSVFERMRKYQMTGVEEGARAHPEKHAASSGPELLRKKRTTLAERNTCQLYIQTDHLFFKYYGTREAVIAQISSHVKAIDTIYQTTDFSGIRNISFMVKRIRINTTSDEKDPTNPFRFPNIGVEKFLELNSEQNHDDYCLAYVFTDRDFDDGVLGLAWVGAPSGSSGGICEKSKLYSDGKKKSLNTGIITVQNYGSHVPPKVSHITFAHEVGHNFGSPHDSGTECTPGESKNLGQKENGNYIMYARATSGDKLNNNKFSLCSIRNISQVLEKKRNNCFVESGQPICGNGMVEQGEECDCGYSDQCKDDCCFDANQPEGKKCKLKPGKQCSPSQGPCCTAQCAFKSKSEKCRDDSDCAKEGICNGFTALCPASDPKPNFTDCNRHTQVCINGQCAGSICEKYDLEECTCASSDGKDDKELCHVCCMKKMAPSTCASTGSLQWSKQFSGRTITLQPGSPCNDFRGYCDVFMRCRLVDADGPLARLKKAIFSPQLYENIAEWIVAHWWAVLLMGIALIMLMAGFIKICSVHTPSSNPKLPPPKPLPGTLKRRRPPQPIQQPPRQRPRESYQMGHMRR
uniprot
proteins
ec_number
3.4.24.81
uniprot
proteins
function
FUNCTION: Transmembrane metalloprotease which mediates the ectodomain shedding of a myriad of transmembrane proteins, including adhesion proteins, growth factor precursors and cytokines being essential for development and tissue homeostasis (PubMed:17245433, PubMed:29325091, PubMed:29430990, PubMed:30639848). Associates with six members of the tetraspanin superfamily TspanC8 which regulate its exit from the endoplasmic reticulum and its substrate selectivity (PubMed:26668317, PubMed:30463011, PubMed:9244301). Cleaves the membrane-bound precursor of TNF to its mature soluble form. Responsible for the proteolytical release of soluble JAM3 from endothelial cells surface (By similarity). Responsible for the proteolytic release of several other cell-surface proteins, including heparin-binding epidermal growth-like factor, ephrin-A2, CD44, CDH2 and for constitutive and regulated alpha-secretase cleavage of amyloid precursor protein (APP) at '687-Lys-|-Leu-688' (By similarity). Contributes to the normal cleavage of the cellular prion protein (By similarity). Involved in the cleavage of the adhesion molecule L1 at the cell surface and in released membrane vesicles, suggesting a vesicle-based protease activity (By similarity). Also controls the proteolytic processing of Notch and mediates lateral inhibition during neurogenesis (PubMed:9244301). Required for the development of type 1 transitional B cells into marginal zone B cells, probably by cleaving Notch (PubMed:28068307). Responsible for the FasL ectodomain shedding and for the generation of the remnant ADAM10-processed FasL (FasL APL) transmembrane form (By similarity). Also cleaves the ectodomain of the integral membrane proteins CORIN and ITM2B (By similarity). Mediates the proteolytic cleavage of LAG3, leading to release the secreted form of LAG3 (PubMed:17245433). Mediates the proteolytic cleavage of IL6R and IL11RA, leading to the release of secreted forms of IL6R and IL11RA (PubMed:26876177). Enhances the cleavage of CHL1 by BACE1 (PubMed:29325091). Cleaves NRCAM (PubMed:29430990). Cleaves TREM2, resulting in shedding of the TREM2 ectodomain (By similarity). Involved in the development and maturation of glomerular and coronary vasculature (PubMed:29397483, PubMed:30446855). During development of the cochlear organ of Corti, promotes pillar cell separation by forming a ternary complex with CADH1 and EPHA4 and cleaving CADH1 at adherens junctions (PubMed:30639848). May regulate the EFNA5-EPHA3 signaling (By similarity). {ECO:0000250|UniProtKB:O14672, ECO:0000269|PubMed:17245433, ECO:0000269|PubMed:26668317, ECO:0000269|PubMed:28068307, ECO:0000269|PubMed:29325091, ECO:0000269|PubMed:29397483, ECO:0000269|PubMed:29430990, ECO:0000269|PubMed:30446855, ECO:0000269|PubMed:30463011, ECO:0000269|PubMed:30639848, ECO:0000269|PubMed:9244301}.
uniprot
proteins
mass_dalton
83968
uniprot
proteins
mutagenesis
MUTAGEN 385; /note="E->A: Loss of catalytic activity."; /evidence="ECO:0000269|PubMed:29325091"; MUTAGEN 735..737; /note="RQR->AQA: Loss of binding to AP2A1 and AP2A2. Decreased localization to the plasma membrane."; /evidence="ECO:0000269|PubMed:23676497"; MUTAGEN 736; /note="Q->A: No loss of binding to AP2A1 and AP2A2."; /evidence="ECO:0000269|PubMed:23676497
uniprot
proteins
post_translational_modification
PTM: The precursor is cleaved by furin and PCSK7. {ECO:0000250|UniProtKB:Q10741}.
uniprot
proteins
pubmed
10958785
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
17245433
uniprot
proteins
pubmed
19349973
uniprot
proteins
pubmed
19468303
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
23035126
uniprot
proteins
pubmed
23676497
uniprot
proteins
pubmed
26668317
uniprot
proteins
pubmed
26876177
uniprot
proteins
pubmed
28068307
uniprot
proteins
pubmed
29325091
uniprot
proteins
pubmed
29397483
uniprot
proteins
pubmed
29430990
uniprot
proteins
pubmed
30446855
uniprot
proteins
pubmed
30463011
uniprot
proteins
pubmed
30639848
uniprot
proteins
pubmed
9244301
uniprot
proteins
sequence_length
749
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23676497, ECO:0000269|PubMed:26668317, ECO:0000269|PubMed:28068307, ECO:0000269|PubMed:30463011}; Single-pass type I membrane protein {ECO:0000305}. Golgi apparatus membrane {ECO:0000250|UniProtKB:O14672}; Single-pass type I membrane protein {ECO:0000305}. Cytoplasmic vesicle, clathrin-coated vesicle {ECO:0000250|UniProtKB:O14672}. Cell projection, axon {ECO:0000269|PubMed:29325091}. Cell projection, dendrite {ECO:0000269|PubMed:29325091}. Cell junction, adherens junction {ECO:0000269|PubMed:30463011, ECO:0000269|PubMed:30639848}. Cytoplasm {ECO:0000269|PubMed:30463011}. Note=Is localized in the plasma membrane but is also expressed in the Golgi apparatus and in clathrin-coated vesicles derived likely from the Golgi (By similarity). During long term depression, it is recruited to the cell membrane by DLG1 (PubMed:23676497). The immature form is mainly located near cytoplasmic fibrillar structures, while the mature form is predominantly located at zonula adherens and the cell membrane (PubMed:30463011). The localization and clustering of mature ADAM10 to zonula adherens is regulated by AFDN, TSPAN33, PLEKHA7 and PDZD11 (PubMed:30463011). {ECO:0000250|UniProtKB:O14672, ECO:0000269|PubMed:23676497, ECO:0000269|PubMed:30463011}.
uniprot
proteins
transmembrane_region
TRANSMEM 674..694; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins