Adam15
entrez
11490
canonical
uniprot
O88839
canonical
ensembl
ENSMUSG00000028041
resolver
ensp
ENSMUSP00000029676
resolver
ensp
ENSMUSP00000074167
resolver
ensp
ENSMUSP00000103072
resolver
ensp
ENSMUSP00000246819
resolver
ensp
ENSMUSP00000246820
resolver
ensp
ENSMUSP00000246827
resolver
ensp
ENSMUSP00000246830
resolver
ensp
ENSMUSP00000246837
resolver
ensp
ENSMUSP00000246861
resolver
genesymbol
Adam15
resolver
genesymbol_syn
Mdc15
resolver
uniprot
A4ZYV2
resolver
uniprot
Q3TDN7
resolver
uniprot
Q3U7C2
resolver
uniprot
Q3UE21
resolver
uniprot
Q8C7Z0
resolver
uniprot
Q91VS9
resolver
uniprot
Q9QYL2
resolver
uniprot_entry
ADA15_MOUSE
resolver
uniprot_sec
A4ZYV2
resolver
uniprot_sec
Q3TDN7
resolver
uniprot_sec
Q3U7C2
resolver
uniprot_sec
Q3UE21
resolver
uniprot_sec
Q8C7Z0
resolver
uniprot_sec
Q91VS9
resolver
uniprot_sec
Q9QYL2
resolver
amino_acid_sequence
MRLALLWALGLLGAGSPRPSPPLPNIGGTEEEQQASPERTLSGSMESRVVQDSPPMSLADVLQTGLPEALRISLELDSESHVLELLQNRDLIPGRPTLVWYQPDGTRMVSEGYSLENCCYRGRVQGHPSSWVSLCACSGIRGLIVLSPERGYTLELGPGDLQRPVISRIQDHLLLGHTCAPSWHASVPTRAGPDLLLEQHHAHRLKRDVVTETKIVELVIVADNSEVRKYPDFQQLLNRTLEAALLLDTFFQPLNVRVALVGLEAWTQHNLIEMSSNPAVLLDNFLRWRRTDLLPRLPHDSAQLVTVTSFSGPMVGMAIQNSICSPDFSGGVNMDHSTSILGVASSIAHELGHSLGLDHDSPGHSCPCPGPAPAKSCIMEASTDFLPGLNFSNCSRQALEKALLEGMGSCLFERQPSLAPMSSLCGNMFVDPGEQCDCGFPDECTDPCCDHFTCQLRPGAQCASDGPCCQNCKLHPAGWLCRPPTDDCDLPEFCPGDSSQCPSDIRLGDGEPCASGEAVCMHGRCASYARQCQSLWGPGAQPAAPLCLQTANTRGNAFGSCGRSPGGSYMPCAPRDVMCGQLQCQWGRSQPLLGSVQDRLSEVLEANGTQLNCSWVDLDLGNDVAQPLLALPGTACGPGLVCIGHRCQPVDLLGAQECRRKCHGHGVCDSSGHCRCEEGWAPPDCMTQLKATSSLTTGLLLSLLLLLVLVLLGASYWHRARLHQRLCQLKGSSCQYRAPQSCPPERPGPPQRAQQMTGTKQASVVSFPVPPSRPLPPNPVPKKLQAALADRSNPPTRPLPADPVVRRPKSQGPTKPPPPRKPLPANPQGQHPPGDLPGPGDGSLPLVVPSRPAPPPPAASSLYL
uniprot
proteins
ec_number
3.4.24.-
uniprot
proteins
function
FUNCTION: Active metalloproteinase with gelatinolytic and collagenolytic activity. Plays a role in the wound healing process. Mediates both heterotypic intraepithelial cell/T-cell interactions and homotypic T-cell aggregation. Inhibits beta-1 integrin-mediated cell adhesion and migration of airway smooth muscle cells. Suppresses cell motility on or towards fibronectin possibly by driving alpha-v/beta-1 integrin (ITAGV-ITGB1) cell surface expression via ERK1/2 inactivation. Cleaves E-cadherin in response to growth factor deprivation. Plays a role in glomerular cell migration (By similarity). Plays a role in pathological neovascularization. May play a role in cartilage remodeling. May be proteolytically processed, during sperm epididymal maturation and the acrosome reaction. May play a role in sperm-egg binding through its disintegrin domain. Interactions with egg membrane could be mediated via binding between the disintegrin-like domain to one or more integrin receptors on the egg. {ECO:0000250, ECO:0000269|PubMed:11882657, ECO:0000269|PubMed:12897135, ECO:0000269|PubMed:15818704, ECO:0000269|PubMed:18390692}.
uniprot
proteins
mass_dalton
92664
uniprot
proteins
mutagenesis
MUTAGEN 482; /note="R->A: Reduced binding to CHO cells expressing ITAG9-ITGB1."; /evidence="ECO:0000269|PubMed:11882657"; MUTAGEN 489; /note="D->A: Reduced binding to CHO cells expressing ITAG9-ITGB1."; /evidence="ECO:0000269|PubMed:11882657"; MUTAGEN 490; /note="L->A: Reduced binding to CHO cells expressing ITAG9-ITGB1."; /evidence="ECO:0000269|PubMed:11882657"; MUTAGEN 491; /note="P->A: Reduced binding to CHO cells expressing ITAG9-ITGB1."; /evidence="ECO:0000269|PubMed:11882657"; MUTAGEN 492; /note="E->A: Reduced binding to CHO cells expressing ITAG9-ITGB1."; /evidence="ECO:0000269|PubMed:11882657"; MUTAGEN 493; /note="F->A: Reduced binding to CHO cells expressing ITAG9-ITGB1."; /evidence="ECO:0000269|PubMed:11882657
uniprot
proteins
post_translational_modification
PTM: The precursor is cleaved by a furin endopeptidase. An additional membrane proximal site of cleavage affects a small percentage of the proteins and results in disulfide-linked fragments. The prodomain is apparently cleaved in several positions that are N-terminal of the furin cleavage site. {ECO:0000269|PubMed:9748307}.; PTM: May be partially sialylated.; PTM: Phosphorylation increases association with PTKs. {ECO:0000250}.
uniprot
proteins
pubmed
10531379
uniprot
proteins
pubmed
11882657
uniprot
proteins
pubmed
12897135
uniprot
proteins
pubmed
13679040
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15818704
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
18381816
uniprot
proteins
pubmed
18390692
uniprot
proteins
pubmed
9748307
uniprot
proteins
sequence_length
864
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Endomembrane system {ECO:0000269|PubMed:18390692}; Single-pass type I membrane protein {ECO:0000269|PubMed:18390692}. Cell junction, adherens junction {ECO:0000250}. Cell projection, cilium, flagellum {ECO:0000269|PubMed:18390692}. Cytoplasmic vesicle, secretory vesicle, acrosome {ECO:0000269|PubMed:18390692}. Note=The majority of the protein is localized in a perinuclear compartment which may correspond to the trans-Golgi network or the late endosome. The pro-protein is the major detectable form on the cell surface, whereas the majority of the protein in the cell is processed.
uniprot
proteins
transmembrane_region
TRANSMEM 697..717; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins