ADAM9
entrez
8754
canonical
uniprot
Q13443
canonical
ensembl
ENSG00000168615
resolver
ensp
ENSP00000419446
resolver
ensp
ENSP00000693465
resolver
genesymbol
ADAM9
resolver
genesymbol_syn
KIAA0021
resolver
genesymbol_syn
MCMP
resolver
genesymbol_syn
MDC9
resolver
genesymbol_syn
MLTNG
resolver
hgnc
HGNC:216
resolver
uniprot
B7ZLN7
resolver
uniprot
Q10718
resolver
uniprot
Q8NFM6
resolver
uniprot_entry
ADAM9_HUMAN
resolver
uniprot_sec
B7ZLN7
resolver
uniprot_sec
Q10718
resolver
uniprot_sec
Q8NFM6
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. Inhibited by hydroxamic acid-based inhibitors. {ECO:0000250|UniProtKB:Q61072}.
uniprot
proteins
amino_acid_sequence
MGSGARFPSGTLRVRWLLLLGLVGPVLGAARPGFQQTSHLSSYEIITPWRLTRERREAPRPYSKQVSYVIQAEGKEHIIHLERNKDLLPEDFVVYTYNKEGTLITDHPNIQNHCHYRGYVEGVHNSSIALSDCFGLRGLLHLENASYGIEPLQNSSHFEHIIYRMDDVYKEPLKCGVSNKDIEKETAKDEEEEPPSMTQLLRRRRAVLPQTRYVELFIVVDKERYDMMGRNQTAVREEMILLANYLDSMYIMLNIRIVLVGLEIWTNGNLINIVGGAGDVLGNFVQWREKFLITRRRHDSAQLVLKKGFGGTAGMAFVGTVCSRSHAGGINVFGQITVETFASIVAHELGHNLGMNHDDGRDCSCGAKSCIMNSGASGSRNFSSCSAEDFEKLTLNKGGNCLLNIPKPDEAYSAPSCGNKLVDAGEECDCGTPKECELDPCCEGSTCKLKSFAECAYGDCCKDCRFLPGGTLCRGKTSECDVPEYCNGSSQFCQPDVFIQNGYPCQNNKAYCYNGMCQYYDAQCQVIFGSKAKAAPKDCFIEVNSKGDRFGNCGFSGNEYKKCATGNALCGKLQCENVQEIPVFGIVPAIIQTPSRGTKCWGVDFQLGSDVPDPGMVNEGTKCGAGKICRNFQCVDASVLNYDCDVQKKCHGHGVCNSNKNCHCENGWAPPNCETKGYGGSVDSGPTYNEMNTALRDGLLVFFFLIVPLIVCAIFIFIKRDQLWRSYFRKKRSQTYESDGKNQANPSRQPGSVPRHVSPVTPPREVPIYANRFAVPTYAAKQPQQFPSRPPPPQPKVSSQGNLIPARPAPAPPLYSSLT
uniprot
proteins
disease_involvement
DISEASE: Cone-rod dystrophy 9 (CORD9) [MIM:612775]: An inherited retinal dystrophy characterized by retinal pigment deposits visible on fundus examination, predominantly in the macular region, and initial loss of cone photoreceptors followed by rod degeneration. This leads to decreased visual acuity and sensitivity in the central visual field, followed by loss of peripheral vision. Severe loss of vision occurs earlier than in retinitis pigmentosa, due to cone photoreceptors degenerating at a higher rate than rod photoreceptors. {ECO:0000269|PubMed:19409519}. Note=The disease is caused by variants affecting the gene represented in this entry.
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. May mediate cell-cell, cell-matrix interactions and regulate the motility of cells via interactions with integrins. {ECO:0000250|UniProtKB:Q61072}.; FUNCTION: [Isoform 2]: May act as alpha-secretase for amyloid precursor protein (APP). {ECO:0000269|PubMed:12054541}.
uniprot
proteins
mass_dalton
90556
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:0000250|UniProtKB:Q61072}.; PTM: Phosphorylation is induced in vitro by phorbol-12-myristate-13-acetate (PMA). {ECO:0000250|UniProtKB:Q61072}.
uniprot
proteins
pubmed
10531379
uniprot
proteins
pubmed
12054541
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
19409519
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
7584026
uniprot
proteins
pubmed
8647900
uniprot
proteins
pubmed
8809033
uniprot
proteins
pubmed
9016778
uniprot
proteins
sequence_length
819
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane {ECO:0000269|PubMed:8647900}; Single-pass type I membrane protein {ECO:0000255}.; SUBCELLULAR LOCATION: [Isoform 2]: Secreted {ECO:0000269|PubMed:12054541}.
uniprot
proteins
transmembrane_region
TRANSMEM 698..718; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins