UniProt ID | MEP1B_RAT | |
---|---|---|
UniProt AC | P28826 | |
Protein Name | Meprin A subunit beta | |
Gene Name | Mep1b | |
Organism | Rattus norvegicus (Rat). | |
Sequence Length | 704 | |
Subcellular Localization |
Cell membrane Single-pass type I membrane protein . Secreted . Homodimers are essentially membrane bound but may also be shed from the surface by ADAM-10 and ADAM-17. |
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Protein Description | 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.. | |
Protein Sequence | MDARHWPWFLVFATFLLVSGLPAPEKFVKDIDGGIDQDIFDINEDLGLDLFEGDIKLEASGRNSIIGDNYRWPHTIPYVLEDSLEMNAKGVILNAFERYRLKTCIDFKPWSGEENYISVFKGSGCWSSVGNIHAGKQELSIGTNCDRIATVQHEFLHALGFWHEQSRADRDDYITIVWDRILSGKEHNFNIYNDSVSDSLNVPYDYTSVMHYSKTAFQNGTESTIITKISDFEDVIGQRMDFSDYDLLKLNQLYSCTSSLSFMDSCDFELENICGMIQSSQDSADWQRLSQVLSGPENDHSNMGQCKDSGFFMHFNTSTGNGGVTAMLESRVLYPKRGFQCVEFYLYNSGSGNGQLNVYTREYTAGHQDGVLTLQREIRDIPTGSWQLYYVTLQVTEKFRVVFEGVGGPGASSGGLSIDDINLSETRCPHHIWHIQNFTQLLGGQTTVYSPPFYSSKGYAFQINLDLTSPTNVGLYFHLISGANDDQLQWPCPWQQATMTLLDQNPDIRQRMSNQRSITTDPKMTDDNGSYLWDRPSKVGVEAFFPNGTQFSRGRGYGTSVFITQERLKSREFLKGDDVYILLTVEDISHLNSTAAVPGPVPTTSTVHNACSEVECQNGGICTLQEGRAECKCPAGEDWWYMGKRCEKRGSTKDTIVIAVSSTVTVFAVMLIITLISVYCTRRKYRKKASAKTAAMNLENQHAF | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
193 | N-linked_Glycosylation | EHNFNIYNDSVSDSL CCCCCCCCCCCCCCC | 31.14 | - | |
219 | N-linked_Glycosylation | YSKTAFQNGTESTII EEEEHHCCCCEEEEE | 53.56 | - | |
316 | N-linked_Glycosylation | SGFFMHFNTSTGNGG CCEEEEEEECCCCCC | 20.59 | - | |
422 | N-linked_Glycosylation | GLSIDDINLSETRCP CCCCCCCCCCCCCCC | 44.50 | - | |
437 | N-linked_Glycosylation | HHIWHIQNFTQLLGG CHHEEECCHHHHHCC | 41.13 | - | |
528 | N-linked_Glycosylation | DPKMTDDNGSYLWDR CCCCCCCCCCCCCCC | 44.09 | - | |
547 | N-linked_Glycosylation | GVEAFFPNGTQFSRG CCEEECCCCCCCCCC | 62.07 | - | |
592 | N-linked_Glycosylation | VEDISHLNSTAAVPG EHHHHCCCCCCCCCC | 31.71 | - |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
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Oops, there are no upstream regulatory protein records of MEP1B_RAT !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of MEP1B_RAT !! |
* Distance = the distance between SAP position and PTM sites.
Modified Location | Modification | Variant Position (Distance <= 10) |
Residue Change | SAP | Related Disease | Reference |
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Oops, there are no SNP-PTM records of MEP1B_RAT !! |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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