Mep1b
entrez
25727
canonical
uniprot
P28826
canonical
ensembl
ENSRNOG00000049345
resolver
ensembl
ENSRNOG00055018423
resolver
ensembl
ENSRNOG00060012398
resolver
ensp
ENSRNOP00000091050
resolver
ensp
ENSRNOP00055025268
resolver
ensp
ENSRNOP00060016643
resolver
enst
ENSRNOT00000118375
resolver
enst
ENSRNOT00055031310
resolver
enst
ENSRNOT00060021094
resolver
genesymbol
Mep1b
resolver
uniprot
Q642D0
resolver
uniprot_entry
MEP1B_RAT
resolver
uniprot_sec
Q642D0
resolver
activity_regulation
ACTIVITY REGULATION: Strongly inhibited by fetuin-A/AHSG. {ECO:0000250}.
uniprot
proteins
amino_acid_sequence
MDARHWPWFLVFATFLLVSGLPAPEKFVKDIDGGIDQDIFDINEDLGLDLFEGDIKLEASGRNSIIGDNYRWPHTIPYVLEDSLEMNAKGVILNAFERYRLKTCIDFKPWSGEENYISVFKGSGCWSSVGNIHAGKQELSIGTNCDRIATVQHEFLHALGFWHEQSRADRDDYITIVWDRILSGKEHNFNIYNDSVSDSLNVPYDYTSVMHYSKTAFQNGTESTIITKISDFEDVIGQRMDFSDYDLLKLNQLYSCTSSLSFMDSCDFELENICGMIQSSQDSADWQRLSQVLSGPENDHSNMGQCKDSGFFMHFNTSTGNGGVTAMLESRVLYPKRGFQCVEFYLYNSGSGNGQLNVYTREYTAGHQDGVLTLQREIRDIPTGSWQLYYVTLQVTEKFRVVFEGVGGPGASSGGLSIDDINLSETRCPHHIWHIQNFTQLLGGQTTVYSPPFYSSKGYAFQINLDLTSPTNVGLYFHLISGANDDQLQWPCPWQQATMTLLDQNPDIRQRMSNQRSITTDPKMTDDNGSYLWDRPSKVGVEAFFPNGTQFSRGRGYGTSVFITQERLKSREFLKGDDVYILLTVEDISHLNSTAAVPGPVPTTSTVHNACSEVECQNGGICTLQEGRAECKCPAGEDWWYMGKRCEKRGSTKDTIVIAVSSTVTVFAVMLIITLISVYCTRRKYRKKASAKTAAMNLENQHAF
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. {ECO:0000250|UniProtKB:Q61847}.
uniprot
proteins
mass_dalton
79236
uniprot
proteins
mutagenesis
MUTAGEN 274; /note="C->A: Predominantly occurs as a monomer, less than 10% occurs as dimer."; /evidence="ECO:0000269|PubMed:15695509"; MUTAGEN 306; /note="C->A: Only occurs as a monomer."; /evidence="ECO:0000269|PubMed:15695509"; MUTAGEN 492; /note="C->A: Only occurs as a monomer."; /evidence="ECO:0000269|PubMed:15695509
uniprot
proteins
post_translational_modification
PTM: N-glycosylated; contains high mannose and/or complex biantennary structures. {ECO:0000250}.; PTM: Proteolytically activated by trypsin in the intestinal lumen and kallikrein-related peptidases in other tissues. {ECO:0000250}.; 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
1377685
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15695509
uniprot
proteins
pubmed
8760356
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