Mep1b
entrez
17288
canonical
uniprot
Q61847
canonical
ensembl
ENSMUSG00000024313
resolver
ensp
ENSMUSP00000080866
resolver
genesymbol
Mep1b
resolver
genesymbol_syn
Mep-1b
resolver
uniprot
Q059K0
resolver
uniprot_entry
MEP1B_MOUSE
resolver
uniprot_sec
Q059K0
resolver
activity_regulation
ACTIVITY REGULATION: Strongly inhibited by fetuin-A/AHSG (By similarity). Inhibited by cysteine and by the metal ion chelators EDTA and 1,10-phenanthroline. Not inhibited by 3,4-dichloroisocourmarin, soybean trypsin inhibitor, or the cysteine proteinase inhibitors iodoacetic acid and E-64. {ECO:0000250, ECO:0000269|PubMed:1894622}.
uniprot
proteins
amino_acid_sequence
MDARHQPWFLVFATFLLVSGLPAPEKFVKDIDGGIDQDIFDINQGLGLDLFEGDIKLEANGKNSIIGDHKRWPHTIPYVLEDSLEMNAKGVILNAFERYRLKTCIDFKPWSGEANYISVFKGSGCWSSVGNIHAGKQELSIGTNCDRIATVQHEFLHALGFWHEQSRADRDDYVIIVWDRIQPGKEHNFNIYNDSVSDSLNVPYDYTSVMHYSKTAFQNGTESTIVTRISEFEDVIGQRMDFSDYDLLKLNQLYNCTSSLSFMDSCDFELENICGMIQSSGDSADWQRVSQVLSGPESDHSKMGQCKDSGFFMHFNTSILNEGATAMLESRLLYPKRGFQCLEFYLYNSGSGNDQLNIYTREYTTGQQGGVLTLQRQIKEVPIGSWQLHYVTLQVTKKFRVVFEGLRGPGTSSGGLSIDDINLSETRCPHHIWHIQNFTQILGGQDTSVYSPPFYSSKGYAFQIYMDLRSSTNVGIYFHLISGANDDQLQWPCPWQQATMTLLDQNPDIRQRMFNQRSITTDPTMTSDNGSYFWDRPSKVGVTDVFPNGTQFSRGIGYGTTVFITRERLKSREFIKGDDIYILLTVEDISHLNSTSAVPDPVPTLAVHNACSEVVCQNGGICVVQDGRAECKCPAGEDWWYMGKRCEKRGSTRDTVIIAVSSTVTVFAVMLIITLVSVYCTRRKYRKKARANTAAMTLENQHAF
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 (PubMed:11278902). 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 (By similarity). {ECO:0000250|UniProtKB:Q16820, ECO:0000269|PubMed:11278902}.
uniprot
proteins
mass_dalton
79501
uniprot
proteins
post_translational_modification
PTM: Proteolytically activated by trypsin in the intestinal lumen and kallikrein-related peptidases in other tissues. {ECO:0000250}.; PTM: N-glycosylated; contains high mannose and/or complex biantennary structures. {ECO:0000269|PubMed:1894622}.; PTM: Phosphorylated by PKC at multiple sites of its cytoplasmic part. Phosphorylation dcreases activity at the cell surface, leading to diminished substrate cleavage. {ECO:0000250|UniProtKB:Q16820}.
uniprot
proteins
pubmed
11278902
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16116208
uniprot
proteins
pubmed
1894622
uniprot
proteins
pubmed
1929422
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
8407940
uniprot
proteins
pubmed
8567689
uniprot
proteins
sequence_length
704
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q16820}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q16820}. Secreted {ECO:0000250|UniProtKB:Q16820}. Note=Homodimers are essentially membrane bound but may also be shed from the surface by ADAM-10 and ADAM-17. {ECO:0000250|UniProtKB:Q16820}.
uniprot
proteins
transmembrane_region
TRANSMEM 655..678; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins