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Q61847

- MEP1B_MOUSE

UniProt

Q61847 - MEP1B_MOUSE

Protein

Meprin A subunit beta

Gene

Mep1b

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 138 (01 Oct 2014)
      Sequence version 2 (13 Jul 2010)
      Previous versions | rss
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    Functioni

    Membrane metallopeptidase that sheds many membrane-bound proteins. 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.By similarity

    Catalytic activityi

    Hydrolysis of proteins, including azocasein, and peptides. Hydrolysis of 5-His-|-Leu-6, 6-Leu-|-Cys-7, 14-Ala-|-Leu-15 and 19-Cys-|-Gly-20 bonds in insulin B chain. Exhibits a strong preference for acidic amino acids at the P1' position.2 Publications

    Cofactori

    Binds 1 zinc ion per subunit.By similarity

    Enzyme regulationi

    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.By similarity1 Publication

    Temperature dependencei

    The half-life at 58 degrees Celsius is less than 3 minutes.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi54 – 541Zinc; catalyticPROSITE-ProRule annotation
    Metal bindingi153 – 1531Zinc; via tele nitrogen; catalyticBy similarity
    Active sitei154 – 1541PROSITE-ProRule annotation
    Metal bindingi157 – 1571Zinc; via tele nitrogen; catalyticBy similarity
    Metal bindingi163 – 1631Zinc; via tele nitrogen; catalyticBy similarity
    Sitei239 – 2391Mediates preference for acidic residues at subsite P1'By similarity

    GO - Molecular functioni

    1. metalloendopeptidase activity Source: Ensembl
    2. zinc ion binding Source: InterPro

    GO - Biological processi

    1. inflammatory response Source: UniProtKB-KW

    Keywords - Molecular functioni

    Hydrolase, Metalloprotease, Protease

    Keywords - Biological processi

    Inflammatory response

    Keywords - Ligandi

    Metal-binding, Zinc

    Protein family/group databases

    MEROPSiM12.004.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Meprin A subunit beta (EC:3.4.24.63)
    Alternative name(s):
    Endopeptidase-2
    Meprin B
    Gene namesi
    Name:Mep1b
    Synonyms:Mep-1b
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 18

    Organism-specific databases

    MGIiMGI:96964. Mep1b.

    Subcellular locationi

    GO - Cellular componenti

    1. integral component of membrane Source: UniProtKB-KW
    2. membrane Source: MGI
    3. plasma membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell membrane, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2020Sequence AnalysisAdd
    BLAST
    Propeptidei21 – 6444By similarityPRO_0000028885Add
    BLAST
    Chaini65 – 704640Meprin A subunit betaPRO_0000028886Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi104 ↔ 256PROSITE-ProRule annotation
    Disulfide bondi125 ↔ 145PROSITE-ProRule annotation
    Glycosylationi193 – 1931N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi219 – 2191N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi255 – 2551N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi266 ↔ 428PROSITE-ProRule annotation
    Disulfide bondi274 – 274InterchainPROSITE-ProRule annotation
    Disulfide bondi306 – 306InterchainPROSITE-ProRule annotation
    Glycosylationi316 – 3161N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi422 – 4221N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi437 – 4371N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi493 – 493InterchainPROSITE-ProRule annotation
    Glycosylationi529 – 5291N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi548 – 5481N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi593 – 5931N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi611 ↔ 622PROSITE-ProRule annotation
    Disulfide bondi616 ↔ 631PROSITE-ProRule annotation
    Disulfide bondi633 ↔ 646PROSITE-ProRule annotation

    Post-translational modificationi

    Proteolytically activated by trypsin in the intestinal lumen and kallikrein-related peptidases in other tissues.By similarity
    N-glycosylated; contains high mannose and/or complex biantennary structures.1 Publication

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Zymogen

    Proteomic databases

    MaxQBiQ61847.
    PaxDbiQ61847.
    PRIDEiQ61847.

    PTM databases

    PhosphoSiteiQ61847.

    Expressioni

    Tissue specificityi

    Isoform 1 is expressed in kidney, intestinal brush borders, and salivary ducts. Isoform 2 has been found in carcinoma cells.

    Inductioni

    By retinoic acid.

    Gene expression databases

    BgeeiQ61847.
    CleanExiMM_MEP1B.
    GenevestigatoriQ61847.

    Interactioni

    Subunit structurei

    Homotetramer consisting of disulfide-linked beta subunits, or heterotetramer of two alpha and two beta subunits formed by non-covalent association of two disulfide-linked heterodimers. Interacts with MBL2 through its carbohydrate moiety. This interaction may inhibit its catalytic activity.2 Publications

    Protein-protein interaction databases

    IntActiQ61847. 4 interactions.
    MINTiMINT-4101747.
    STRINGi10090.ENSMUSP00000111506.

    Structurei

    3D structure databases

    ProteinModelPortaliQ61847.
    SMRiQ61847. Positions 30-595.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini21 – 654634ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini679 – 70426CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei655 – 67824HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini261 – 430170MAMPROSITE-ProRule annotationAdd
    BLAST
    Domaini431 – 586156MATHPROSITE-ProRule annotationAdd
    BLAST
    Domaini607 – 64741EGF-likePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni63 – 260198MetalloproteaseAdd
    BLAST

    Sequence similaritiesi

    Belongs to the peptidase M12A family.Curated
    Contains 1 EGF-like domain.PROSITE-ProRule annotation
    Contains 1 MAM domain.PROSITE-ProRule annotation
    Contains 1 MATH domain.PROSITE-ProRule annotation

    Keywords - Domaini

    EGF-like domain, Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG322115.
    GeneTreeiENSGT00740000115357.
    HOGENOMiHOG000043106.
    HOVERGENiHBG052457.
    KOiK08606.
    OMAiFEEENIC.
    OrthoDBiEOG73V6MT.
    PhylomeDBiQ61847.
    TreeFamiTF315280.

    Family and domain databases

    Gene3Di3.40.390.10. 1 hit.
    InterProiIPR008985. ConA-like_lec_gl_sf.
    IPR000742. EG-like_dom.
    IPR000998. MAM_dom.
    IPR002083. MATH.
    IPR008294. Meprin.
    IPR024079. MetalloPept_cat_dom.
    IPR001506. Peptidase_M12A.
    IPR006026. Peptidase_Metallo.
    IPR008974. TRAF-like.
    [Graphical view]
    PfamiPF01400. Astacin. 1 hit.
    PF00008. EGF. 1 hit.
    PF00629. MAM. 1 hit.
    PF00917. MATH. 1 hit.
    [Graphical view]
    PIRSFiPIRSF001196. Meprin. 1 hit.
    PRINTSiPR00480. ASTACIN.
    PR00020. MAMDOMAIN.
    SMARTiSM00181. EGF. 1 hit.
    SM00137. MAM. 1 hit.
    SM00061. MATH. 1 hit.
    SM00235. ZnMc. 1 hit.
    [Graphical view]
    SUPFAMiSSF49599. SSF49599. 1 hit.
    SSF49899. SSF49899. 1 hit.
    PROSITEiPS50026. EGF_3. 1 hit.
    PS00740. MAM_1. 1 hit.
    PS50060. MAM_2. 1 hit.
    PS50144. MATH. 1 hit.
    PS00142. ZINC_PROTEASE. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative promoter usage and alternative splicing. Align

    Isoform 1 (identifier: Q61847-1) [UniParc]FASTAAdd to Basket

    Also known as: Beta

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MDARHQPWFL VFATFLLVSG LPAPEKFVKD IDGGIDQDIF DINQGLGLDL    50
    FEGDIKLEAN GKNSIIGDHK RWPHTIPYVL EDSLEMNAKG VILNAFERYR 100
    LKTCIDFKPW SGEANYISVF KGSGCWSSVG NIHAGKQELS IGTNCDRIAT 150
    VQHEFLHALG FWHEQSRADR DDYVIIVWDR IQPGKEHNFN IYNDSVSDSL 200
    NVPYDYTSVM HYSKTAFQNG TESTIVTRIS EFEDVIGQRM DFSDYDLLKL 250
    NQLYNCTSSL SFMDSCDFEL ENICGMIQSS GDSADWQRVS QVLSGPESDH 300
    SKMGQCKDSG FFMHFNTSIL NEGATAMLES RLLYPKRGFQ CLEFYLYNSG 350
    SGNDQLNIYT REYTTGQQGG VLTLQRQIKE VPIGSWQLHY VTLQVTKKFR 400
    VVFEGLRGPG TSSGGLSIDD INLSETRCPH HIWHIQNFTQ ILGGQDTSVY 450
    SPPFYSSKGY AFQIYMDLRS STNVGIYFHL ISGANDDQLQ WPCPWQQATM 500
    TLLDQNPDIR QRMFNQRSIT TDPTMTSDNG SYFWDRPSKV GVTDVFPNGT 550
    QFSRGIGYGT TVFITRERLK SREFIKGDDI YILLTVEDIS HLNSTSAVPD 600
    PVPTLAVHNA CSEVVCQNGG ICVVQDGRAE CKCPAGEDWW YMGKRCEKRG 650
    STRDTVIIAV SSTVTVFAVM LIITLVSVYC TRRKYRKKAR ANTAAMTLEN 700
    QHAF 704
    Length:704
    Mass (Da):79,501
    Last modified:July 13, 2010 - v2
    Checksum:i04F92C493F701525
    GO
    Isoform 2 (identifier: Q61847-2) [UniParc]FASTAAdd to Basket

    Also known as: Beta'

    The sequence of this isoform differs from the canonical sequence as follows:
         1-27: MDARHQPWFLVFATFLLVSGLPAPEKF → MNSTAGPASRSRHSFKCRMKLLKAPRDGMYMMTFG

    Show »
    Length:712
    Mass (Da):80,348
    Checksum:i6A876F36D70B70EC
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti18 – 181V → A in AAA75234. (PubMed:8407940)Curated
    Sequence conflicti26 – 261K → G AA sequence (PubMed:1894622)Curated
    Sequence conflicti29 – 291K → S AA sequence (PubMed:1894622)Curated
    Sequence conflicti470 – 4701S → Y in AAA75234. (PubMed:8407940)Curated
    Sequence conflicti470 – 4701S → Y no nucleotide entry (PubMed:8567689)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 2727MDARH…APEKF → MNSTAGPASRSRHSFKCRMK LLKAPRDGMYMMTFG in isoform 2. 1 PublicationVSP_005460Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L15193 mRNA. Translation: AAA75234.1.
    CH466557 Genomic DNA. Translation: EDK96962.1.
    BC125627 mRNA. Translation: AAI25628.1.
    BC145979 mRNA. Translation: AAI45980.1.
    CCDSiCCDS37747.1. [Q61847-1]
    PIRiA48040.
    RefSeqiNP_032612.2. NM_008586.2. [Q61847-1]
    UniGeneiMm.2682.

    Genome annotation databases

    EnsembliENSMUST00000082235; ENSMUSP00000080866; ENSMUSG00000024313. [Q61847-1]
    GeneIDi17288.
    KEGGimmu:17288.
    UCSCiuc008eff.1. mouse. [Q61847-1]

    Keywords - Coding sequence diversityi

    Alternative promoter usage, Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L15193 mRNA. Translation: AAA75234.1 .
    CH466557 Genomic DNA. Translation: EDK96962.1 .
    BC125627 mRNA. Translation: AAI25628.1 .
    BC145979 mRNA. Translation: AAI45980.1 .
    CCDSi CCDS37747.1. [Q61847-1 ]
    PIRi A48040.
    RefSeqi NP_032612.2. NM_008586.2. [Q61847-1 ]
    UniGenei Mm.2682.

    3D structure databases

    ProteinModelPortali Q61847.
    SMRi Q61847. Positions 30-595.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q61847. 4 interactions.
    MINTi MINT-4101747.
    STRINGi 10090.ENSMUSP00000111506.

    Protein family/group databases

    MEROPSi M12.004.

    PTM databases

    PhosphoSitei Q61847.

    Proteomic databases

    MaxQBi Q61847.
    PaxDbi Q61847.
    PRIDEi Q61847.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000082235 ; ENSMUSP00000080866 ; ENSMUSG00000024313 . [Q61847-1 ]
    GeneIDi 17288.
    KEGGi mmu:17288.
    UCSCi uc008eff.1. mouse. [Q61847-1 ]

    Organism-specific databases

    CTDi 4225.
    MGIi MGI:96964. Mep1b.

    Phylogenomic databases

    eggNOGi NOG322115.
    GeneTreei ENSGT00740000115357.
    HOGENOMi HOG000043106.
    HOVERGENi HBG052457.
    KOi K08606.
    OMAi FEEENIC.
    OrthoDBi EOG73V6MT.
    PhylomeDBi Q61847.
    TreeFami TF315280.

    Miscellaneous databases

    NextBioi 291804.
    PROi Q61847.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q61847.
    CleanExi MM_MEP1B.
    Genevestigatori Q61847.

    Family and domain databases

    Gene3Di 3.40.390.10. 1 hit.
    InterProi IPR008985. ConA-like_lec_gl_sf.
    IPR000742. EG-like_dom.
    IPR000998. MAM_dom.
    IPR002083. MATH.
    IPR008294. Meprin.
    IPR024079. MetalloPept_cat_dom.
    IPR001506. Peptidase_M12A.
    IPR006026. Peptidase_Metallo.
    IPR008974. TRAF-like.
    [Graphical view ]
    Pfami PF01400. Astacin. 1 hit.
    PF00008. EGF. 1 hit.
    PF00629. MAM. 1 hit.
    PF00917. MATH. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF001196. Meprin. 1 hit.
    PRINTSi PR00480. ASTACIN.
    PR00020. MAMDOMAIN.
    SMARTi SM00181. EGF. 1 hit.
    SM00137. MAM. 1 hit.
    SM00061. MATH. 1 hit.
    SM00235. ZnMc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49599. SSF49599. 1 hit.
    SSF49899. SSF49899. 1 hit.
    PROSITEi PS50026. EGF_3. 1 hit.
    PS00740. MAM_1. 1 hit.
    PS50060. MAM_2. 1 hit.
    PS50144. MATH. 1 hit.
    PS00142. ZINC_PROTEASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning, expression, and chromosomal localization of the mouse meprin beta subunit."
      Gorbea C.M., Marchand P., Jiang W., Copeland N.G., Gilbert D.J., Jenkins N.A., Bond J.S.
      J. Biol. Chem. 268:21035-21043(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 65-88; 96-109; 329-345 AND 541-549.
      Tissue: Kidney.
    2. "A novel meprin beta' mRNA in mouse embryonal and human colon carcinoma cells."
      Dietrich J.M., Bond J.S., Jiang W.
      J. Biol. Chem. 271:2271-2278(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
      Tissue: Kidney.
    3. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
      Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (ISOFORM 1).
    4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    5. "Meprin-A and -B. Cell surface endopeptidases of the mouse kidney."
      Kounnas M.Z., Wolz R.L., Gorbea C.M., Bond J.S.
      J. Biol. Chem. 266:17350-17357(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 21-30 (ISOFORM 1), CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, GLYCOSYLATION.
      Strain: C3H/He.
      Tissue: Kidney.
    6. "Homo- and heterotetrameric forms of the membrane-bound metalloendopeptidases meprin A and B."
      Gorbea C.M., Flannery A.V., Bond J.S.
      Arch. Biochem. Biophys. 290:549-553(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBUNIT.
    7. "Marked differences between metalloproteases meprin A and B in substrate and peptide bond specificity."
      Bertenshaw G.P., Turk B.E., Hubbard S.J., Matters G.L., Bylander J.E., Crisman J.M., Cantley L.C., Bond J.S.
      J. Biol. Chem. 276:13248-13255(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: CATALYTIC ACTIVITY.
    8. "Mannan-binding protein blocks the activation of metalloproteases meprin alpha and beta."
      Hirano M., Ma B.Y., Kawasaki N., Okimura K., Baba M., Nakagawa T., Miwa K., Kawasaki N., Oka S., Kawasaki T.
      J. Immunol. 175:3177-3185(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MBL2.

    Entry informationi

    Entry nameiMEP1B_MOUSE
    AccessioniPrimary (citable) accession number: Q61847
    Secondary accession number(s): Q059K0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: July 13, 2010
    Last modified: October 1, 2014
    This is version 138 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. Peptidase families
      Classification of peptidase families and list of entries
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3