MEP1B
entrez
4225
canonical
uniprot
Q16820
canonical
ensembl
ENSG00000141434
resolver
ensp
ENSP00000269202
resolver
ensp
ENSP00000463280
resolver
ensp
ENSP00000665310
resolver
ensp
ENSP00000760534
resolver
enst
ENST00000269202
resolver
enst
ENST00000581447
resolver
genesymbol
MEP1B
resolver
hgnc
HGNC:7020
resolver
uniprot
B7ZM35
resolver
uniprot
B9EGL6
resolver
uniprot
J3QKX5
resolver
uniprot
Q670J1
resolver
uniprot_entry
J3QKX5_HUMAN
resolver
uniprot_entry
MEP1B_HUMAN
resolver
uniprot_sec
B7ZM35
resolver
uniprot_sec
B9EGL6
resolver
uniprot_sec
Q670J1
resolver
activity_regulation
ACTIVITY REGULATION: Strongly inhibited by fetuin-A/AHSG. {ECO:0000269|PubMed:20806899, ECO:0000269|PubMed:22940918}.
uniprot
proteins
amino_acid_sequence
MDLWNLSWFLFLDALLVISGLATPENFDVDGGMDQDIFDINEGLGLDLFEGDIRLDRAQIRNSIIGEKYRWPHTIPYVLEDSLEMNAKGVILNAFERYRLKTCIDFKPWAGETNYISVFKGSGCWSSVGNRRVGKQELSIGANCDRIATVQHEFLHALGFWHEQSRSDRDDYVRIMWDRILSGREHNFNTYSDDISDSLNVPYDYTSVMHYSKTAFQNGTEPTIVTRISDFEDVIGQRMDFSDSDLLKLNQLYNCSSSLSFMDSCSFELENVCGMIQSSGDNADWQRVSQVPRGPESDHSNMGQCQGSGFFMHFDSSSVNVGATAVLESRTLYPKRGFQCLQFYLYNSGSESDQLNIYIREYSADNVDGNLTLVEEIKEIPTGSWQLYHVTLKVTKKFRVVFEGRKGSGASLGGLSIDDINLSETRCPHHIWHIRNFTQFIGSPNGTLYSPPFYSSKGYAFQIYLNLAHVTNAGIYFHLISGANDDQLQWPCPWQQATMTLLDQNPDIRQRMSNQRSITTDPFMTTDNGNYFWDRPSKVGTVALFSNGTQFRRGGGYGTSAFITHERLKSRDFIKGDDVYILLTVEDISHLNSTQIQLTPAPSVQDLCSKTTCKNDGVCTVRDGKAECRCQSGEDWWYMGERCEKRGSTRDTIVIAVSSTVAVFALMLIITLVSVYCTRKKYRERMSSNRPNLTPQNQHAF
uniprot
proteins
ec_number
3.4.24.63
uniprot
proteins
function
FUNCTION: Membrane metallopeptidase that sheds many membrane-bound proteins. Exhibits a strong preference for acidic amino acids at the P1' position. Known substrates include: FGF19, VGFA, IL1B, IL18, procollagen I and III, E-cadherin, KLK7, gastrin, ADAM10, tenascin-C. The presence of several pro-inflammatory cytokine among substrates implicate MEP1B in inflammation. It is also involved in tissue remodeling due to its capability to degrade extracellular matrix components. Also cleaves the amyloid precursor protein/APP, thereby releasing neurotoxic amyloid beta peptides (PubMed:27180357). {ECO:0000269|PubMed:21693781, ECO:0000269|PubMed:27180357}.
uniprot
proteins
mass_dalton
79571
uniprot
proteins
mutagenesis
MUTAGEN 153; /note="E->A: Complete loss of activity."; /evidence="ECO:0000269|PubMed:34125978"; MUTAGEN 248; /note="K->Y: Decreased activity toward gastrin."; /evidence="ECO:0000269|PubMed:12888571"; MUTAGEN 595..607; /note="Missing: Abolishes secretion."; /evidence="ECO:0000269|PubMed:12387727"; MUTAGEN 694; /note="T->E: Almost complete loss of phosphorylation."; /evidence="ECO:0000269|PubMed:34125978
uniprot
proteins
post_translational_modification
PTM: Phosphorylated by PKC at multiple sites of its cytoplasmic part. Phosphorylation dcreases activity at the cell surface, leading to diminished substrate cleavage. {ECO:0000269|PubMed:34125978}.; PTM: N-glycosylated; contains high mannose and/or complex biantennary structures.; PTM: O-glycosylation protect the C-terminal region from proteolytic cleavage and diminish secretion, this seems to be specific to human. {ECO:0000269|PubMed:10215852, ECO:0000269|PubMed:12888571, ECO:0000269|PubMed:18478055, ECO:0000269|PubMed:18786924, ECO:0000269|PubMed:19748582, ECO:0000269|PubMed:21693781, ECO:0000269|PubMed:22940918}.; PTM: Proteolytically activated by trypsin in the intestinal lumen and kallikrein-related peptidases in other tissues.
uniprot
proteins
pubmed
10215852
uniprot
proteins
pubmed
12387727
uniprot
proteins
pubmed
12888571
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
18478055
uniprot
proteins
pubmed
18786924
uniprot
proteins
pubmed
19748582
uniprot
proteins
pubmed
20806899
uniprot
proteins
pubmed
21693781
uniprot
proteins
pubmed
22940918
uniprot
proteins
pubmed
22988105
uniprot
proteins
pubmed
23033978
uniprot
proteins
pubmed
27180357
uniprot
proteins
pubmed
34125978
uniprot
proteins
pubmed
8262185
uniprot
proteins
pubmed
9288916
uniprot
proteins
sequence_length
701
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:22988105, ECO:0000269|PubMed:27180357, ECO:0000269|PubMed:34125978}; Single-pass type I membrane protein. Secreted {ECO:0000269|PubMed:10215852}. Note=Homodimers are essentially membrane bound but may also be shed from the surface by ADAM-10 and ADAM-17. {ECO:0000269|PubMed:22988105}.
uniprot
proteins
transmembrane_region
TRANSMEM 653..673; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins