Adam9
entrez
11502
canonical
uniprot
Q61072
canonical
ensembl
ENSMUSG00000031555
resolver
ensp
ENSMUSP00000146545
resolver
enst
ENSMUST00000208247
resolver
genesymbol
Adam9
resolver
genesymbol_syn
Kiaa0021
resolver
genesymbol_syn
Mdc9
resolver
genesymbol_syn
Mltng
resolver
uniprot
A0A140LHU0
resolver
uniprot
E9QPP2
resolver
uniprot
Q3U1W3
resolver
uniprot
Q3UG15
resolver
uniprot
Q60618
resolver
uniprot
Q61853
resolver
uniprot
Q80U94
resolver
uniprot_entry
A0A140LHU0_MOUSE
resolver
uniprot_entry
ADAM9_MOUSE
resolver
uniprot_entry
Q3U1W3_MOUSE
resolver
uniprot_entry
Q3UG15_MOUSE
resolver
uniprot_sec
E9QPP2
resolver
uniprot_sec
Q60618
resolver
uniprot_sec
Q61853
resolver
uniprot_sec
Q80U94
resolver
activity_regulation
ACTIVITY REGULATION: Synthesized as an inactive form which is proteolytically cleaved to generate an active enzyme. Processing at the upstream site is particularly important for activation of the proenzyme, whereas processing at the boundary between the pro-domain and the catalytic domain does not appear to be essential (PubMed:25795784). Inhibited by hydroxamic acid-based inhibitors (PubMed:9920899). {ECO:0000269|PubMed:25795784, ECO:0000269|PubMed:9920899}.
uniprot
proteins
amino_acid_sequence
MGPRALSPLASLRLRWLLACGLLGPVLEAGRPDLEQTVHLSSYEIITPWRLTRERREALGPSSQQISYVIQAQGKQHIIHLERNTDLLPNDFVVYTYDKEGSLLSDHPNVQSHCHYRGYVEGVQNSAVAVSACFGLRGLLHLENASFGIEPLHNSSHFEHIFYPMDGIHQEPLRCGVSNRDTEKEGTQGDEEEHPSVTQLLRRRRAVLPQTRYVELFIVVDKERYDMMGRNQTAVREEMIRLANYLDSMYIMLNIRIVLVGLEIWTDRNPINIIGGAGDVLGNFVQWREKFLITRWRHDSAQLVLKKGFGGTAGMAFVGTVCSRSHAGGINVFGQITVETFASIVAHELGHNLGMNHDDGRECFCGAKSCIMNSGASGSRNFSSCSAEDFEKLTLNKGGSCLLNIPKPDEAYSAPSCGNKLVDPGEECDCGTAKECEVDPCCEGSTCKLKSFAECAYGDCCKDCQFLPGGSMCRGKTSECDVPEYCNGSSQFCPPDVFIQNGYPCQNSKAYCYNGMCQYYDAQCQVIFGSKAKAAPRDCFIEVNSKGDRFGNCGFSGSEYKKCATGNALCGKLQCENVQDMPVFGIVPAIIQTPSRGTKCWGVDFQLGSDVPDPGMVNEGTKCDAGKICRNFQCVNASVLNYDCDIQGKCHGHGVCNSNKNCHCEDGWAPPHCDTKGYGGSVDSGPTYNAKSTALRDGLLVFFFLIVPLVAAAIFLFIKRDELRKTFRKKRSQMSDGRNQANVSRQPGDPSISRPPGGPNVSRPPGGPGVSRPPGGPGVSRPPGGPGVSRPPPGHGNRFPVPTYAAKQPAQFPSRPPPPQPKISSQGNLIPARPAPAPPLYSSLT
uniprot
proteins
ec_number
3.4.24.-
uniprot
proteins
function
FUNCTION: Metalloprotease that cleaves and releases a number of molecules with important roles in tumorigenesis and angiogenesis, such as TEK, KDR, EPHB4, CD40, VCAM1 and CDH5 (PubMed:19273593, PubMed:9920899). May mediate cell-cell, cell-matrix interactions and regulate the motility of cells via interactions with integrins (PubMed:10825303). {ECO:0000269|PubMed:10825303, ECO:0000269|PubMed:19273593, ECO:0000269|PubMed:9920899}.
uniprot
proteins
mass_dalton
92079
uniprot
proteins
mutagenesis
MUTAGEN 53; /note="R->A: Reduces the shedding activity; when associated with A-56. Does not prevent pro-domain processing between the pro- and metalloprotease domain; when associated with A-56."; /evidence="ECO:0000269|PubMed:25795784"; MUTAGEN 56; /note="R->A: Reduces the shedding activity; when associated with A-56. Does not prevent pro-domain processing between the pro- and metalloprotease domain; when associated with A-56."; /evidence="ECO:0000269|PubMed:25795784"; MUTAGEN 202; /note="R->A: Does not affect shedding activity; when associated with A-205."; /evidence="ECO:0000269|PubMed:25795784"; MUTAGEN 205; /note="R->A: Does not affect shedding activity; when associated with A-203."; /evidence="ECO:0000269|PubMed:25795784"; MUTAGEN 348; /note="E->A: Abolishes catalytic activity."; /evidence="ECO:0000269|PubMed:19273593
uniprot
proteins
post_translational_modification
PTM: Proteolytically cleaved in the trans-Golgi network before it reaches the plasma membrane to generate a mature protein. The removal of the pro-domain occurs via cleavage at two different sites. Processed most likely by a pro-protein convertase such as furin, at the boundary between the pro-domain and the catalytic domain. An additional upstream cleavage pro-protein convertase site (Arg-56/Glu-57) has an important role in the activation of ADAM9. {ECO:0000269|PubMed:25795784, ECO:0000269|PubMed:9920899}.; PTM: Phosphorylation is induced in vitro by phorbol-12-myristate-13-acetate (PMA) (PubMed:9920899). {ECO:0000269|PubMed:9920899}.
uniprot
proteins
pubmed
10531379
uniprot
proteins
pubmed
10825303
uniprot
proteins
pubmed
11839819
uniprot
proteins
pubmed
12693553
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
19273593
uniprot
proteins
pubmed
19409519
uniprot
proteins
pubmed
19468303
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
25795784
uniprot
proteins
pubmed
7566181
uniprot
proteins
pubmed
8146185
uniprot
proteins
pubmed
8647900
uniprot
proteins
pubmed
9920899
uniprot
proteins
sequence_length
845
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:25795784, ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
uniprot
proteins
transmembrane_region
TRANSMEM 698..718; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins