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Q61847

- MEP1B_MOUSE

UniProt

Q61847 - MEP1B_MOUSE

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Protein

Meprin A subunit beta

Gene

Mep1b

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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
Complete GO annotation...

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-KW
Complete GO annotation...

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, 609-648.
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.
GeneTreeiENSGT00760000119227.
HOGENOMiHOG000043106.
HOVERGENiHBG052457.
InParanoidiQ61847.
KOiK08606.
OMAiFEEENIC.
OrthoDBiEOG73V6MT.
PhylomeDBiQ61847.
TreeFamiTF315280.

Family and domain databases

Gene3Di3.40.390.10. 1 hit.
InterProiIPR013320. ConA-like_dom.
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]
PANTHERiPTHR10127:SF312. PTHR10127:SF312. 1 hit.
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

        10         20         30         40         50
MDARHQPWFL VFATFLLVSG LPAPEKFVKD IDGGIDQDIF DINQGLGLDL
60 70 80 90 100
FEGDIKLEAN GKNSIIGDHK RWPHTIPYVL EDSLEMNAKG VILNAFERYR
110 120 130 140 150
LKTCIDFKPW SGEANYISVF KGSGCWSSVG NIHAGKQELS IGTNCDRIAT
160 170 180 190 200
VQHEFLHALG FWHEQSRADR DDYVIIVWDR IQPGKEHNFN IYNDSVSDSL
210 220 230 240 250
NVPYDYTSVM HYSKTAFQNG TESTIVTRIS EFEDVIGQRM DFSDYDLLKL
260 270 280 290 300
NQLYNCTSSL SFMDSCDFEL ENICGMIQSS GDSADWQRVS QVLSGPESDH
310 320 330 340 350
SKMGQCKDSG FFMHFNTSIL NEGATAMLES RLLYPKRGFQ CLEFYLYNSG
360 370 380 390 400
SGNDQLNIYT REYTTGQQGG VLTLQRQIKE VPIGSWQLHY VTLQVTKKFR
410 420 430 440 450
VVFEGLRGPG TSSGGLSIDD INLSETRCPH HIWHIQNFTQ ILGGQDTSVY
460 470 480 490 500
SPPFYSSKGY AFQIYMDLRS STNVGIYFHL ISGANDDQLQ WPCPWQQATM
510 520 530 540 550
TLLDQNPDIR QRMFNQRSIT TDPTMTSDNG SYFWDRPSKV GVTDVFPNGT
560 570 580 590 600
QFSRGIGYGT TVFITRERLK SREFIKGDDI YILLTVEDIS HLNSTSAVPD
610 620 630 640 650
PVPTLAVHNA CSEVVCQNGG ICVVQDGRAE CKCPAGEDWW YMGKRCEKRG
660 670 680 690 700
STRDTVIIAV SSTVTVFAVM LIITLVSVYC TRRKYRKKAR ANTAAMTLEN

QHAF
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, 609-648.
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 ENSGT00760000119227.
HOGENOMi HOG000043106.
HOVERGENi HBG052457.
InParanoidi Q61847.
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 IPR013320. ConA-like_dom.
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 ]
PANTHERi PTHR10127:SF312. PTHR10127:SF312. 1 hit.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 139 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