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UniProtKB/Swiss-Prot entry P28825


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name MEP1A_MOUSE
Primary accession number P28825
Secondary accession numbers None
Integrated into Swiss-Prot on December 1, 1992
Sequence was last modified on November 1, 1997 (Sequence version 3)
Annotations were last modified on    November 25, 2008 (Entry version 91)
Name and origin of the protein
Protein name Meprin A subunit alpha [Precursor]
Synonyms EC 3.4.24.18
Endopeptidase-2
MEP-1
Gene name
Name: Mep1a
From
Mus musculus (Mouse) [TaxID: 10090] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae; Murinae; Mus.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
STRAIN=C3H/He, and C57BL/6;
TISSUE=Kidney;
PubMed=1374387 [NCBI, ExPASy, EBI, Israel, Japan]
Jiang W., Gorbea C.M., Flannery A.V., Beynon R.J., Grant G.A., Bond J.S.;
"The alpha subunit of meprin A. Molecular cloning and sequencing, differential expression in inbred mouse strains, and evidence for divergent evolution of the alpha and beta subunits.";
J. Biol. Chem. 267:9185-9193(1992).
[2]
PROTEIN SEQUENCE OF 21-25 AND 65-69.
PubMed=8615815 [NCBI, ExPASy, EBI, Israel, Japan]
Beynon R.J., Oliver S., Robertson D.H.L.;
"Characterization of the soluble, secreted form of urinary meprin.";
Biochem. J. 315:461-465(1996).
[3]
NUCLEOTIDE SEQUENCE OF 64-262.
PubMed=1939172 [NCBI, ExPASy, EBI, Israel, Japan]
Dumermuth E., Sterchi E.E., Jiang W., Wolz R.L., Bond J.S., Flannery A.V., Beynon R.J.;
"The astacin family of metalloendopeptidases.";
J. Biol. Chem. 266:21381-21385(1991).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 62-258.
STRAIN=129;
DOI=10.1016/S0378-1119(96)00834-7; PubMed=9161413 [NCBI, ExPASy, EBI, Israel, Japan]
Jiang W., Flannery A.V.;
"Correlation of the exon/intron organization to the secondary structures of the protease domain of mouse meprin alpha subunit.";
Gene 189:65-71(1997).
[5]
CHARACTERIZATION.
DOI=10.1021/bi00098a029; PubMed=1883833 [NCBI, ExPASy, EBI, Israel, Japan]
Wolz R.L., Harris R.B., Bond J.S.;
"Mapping the active site of meprin-A with peptide substrates and inhibitors.";
Biochemistry 30:8488-8493(1991).
[6]
3D-STRUCTURE MODELING.
PubMed=8508794 [NCBI, ExPASy, EBI, Israel, Japan]
Stoecker W., Gomis-Rueth F.-X., Bode W., Zwilling R.;
"Implications of the three-dimensional structure of astacin for the structure and function of the astacin family of zinc-endopeptidases.";
Eur. J. Biochem. 214:215-231(1993).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
M74897; AAA75354.1; ALT_INIT; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U62765; AAC53194.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A40195; A40195.
UniGene Mm.5346
3D structure databases
PDB
1IAF; Model; -; A=65-261.[ExPASy / RCSB / EBI]
PDBsum 1IAF; -.
ModBase P28825.
Protein family/group databases
MEROPS M12.002; -.
Organism-specific databases
MGI MGI:96963; Mep1a.
Gene expression databases
ArrayExpress P28825; -.
CleanEx MM_MEP1A; -.
GermOnline ENSMUSG00000023914; Mus musculus.
Ontologies
GO
GO:0005624; Cellular component: membrane fraction (inferred from direct assay from MGI).
GO:0004222; Molecular function: metalloendopeptidase activity (inferred from electronic annotation from InterPro).
GO:0008270; Molecular function: zinc ion binding (inferred from electronic annotation from InterPro).
GO:0006508; Biological process: proteolysis (inferred from electronic annotation from InterPro).
QuickGo view.
Family and domain databases
InterPro IPR006210; EGF.
IPR000742; EGF_3.
IPR006209; EGF_like.
IPR013032; EGF_like_reg_CS.
IPR000998; MAM.
IPR002083; MATH.
IPR008294; Pept_M12A_Meprin.
IPR006025; Pept_M_Zn_BS.
IPR006026; Peptidase_M.
IPR001506; Peptidase_M12A.
IPR013322; TRAF-type.
Graphical view of domain structure.
Gene3D G3DSA:2.60.210.10; TRAF-type; 1.
Pfam PF01400; Astacin; 1.
PF00008; EGF; 1.
PF00629; MAM; 1.
PF00917; MATH; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF001196; Meprin; 1.
PRINTS PR00480; ASTACIN.
PR00020; MAMDOMAIN.
SMART SM00181; EGF; 1.
SM00137; MAM; 1.
SM00061; MATH; 1.
SM00235; ZnMc; 1.
SMART graphical view of domain structure.
PROSITE PS00022; EGF_1; FALSE_NEG.
PS01186; EGF_2; FALSE_NEG.
PS50026; EGF_3; 1.
PS00740; MAM_1; 1.
PS50060; MAM_2; 1.
PS50144; MATH; 1.
PS00142; ZINC_PROTEASE; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS P28825.
ProtoNet P28825.
Genome annotation databases
Ensembl ENSMUSG00000023914; Mus musculus. [Contig view]
Phylogenomic databases
HOVERGEN P28825; -.
Other
SOURCE Mep1a; Mus musculus.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Direct protein sequencing; EGF-like domain; Glycoprotein; Hydrolase; Membrane; Metal-binding; Metalloprotease; Protease; Signal; Transmembrane; Zinc; Zymogen.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
SIGNAL   1    20  20      
PROPEP   21    64  44      PRO_0000028879
CHAIN   65   747  683     Meprin A subunit alpha. PRO_0000028880
TOPO_DOM   65   713  649     Extracellular (Potential). 
TRANSMEM   714   741  28     Potential. 
TOPO_DOM   742   747  6     Cytoplasmic (Potential). 
DOMAIN   263   432  170     MAM. 
DOMAIN   433   594  162     MATH. 
DOMAIN   671   711  41     EGF-like. 
REGION   65   262  198     Metalloprotease. 
ACT_SITE   155   155        By similarity. 
METAL   154   154        Zinc; catalytic (By similarity). 
METAL   158   158        Zinc; catalytic (By similarity). 
METAL   164   164        Zinc; catalytic (By similarity). 
CARBOHYD   28    28        N-linked (GlcNAc...) (Potential). 
CARBOHYD   139   139        N-linked (GlcNAc...) (Potential). 
CARBOHYD   221   221        N-linked (GlcNAc...) (Potential). 
CARBOHYD   257   257        N-linked (GlcNAc...) (Potential). 
CARBOHYD   317   317        N-linked (GlcNAc...) (Potential). 
CARBOHYD   413   413        N-linked (GlcNAc...) (Potential). 
CARBOHYD   439   439        N-linked (GlcNAc...) (Potential). 
CARBOHYD   533   533        N-linked (GlcNAc...) (Potential). 
CARBOHYD   540   540        N-linked (GlcNAc...) (Potential). 
CARBOHYD   601   601        N-linked (GlcNAc...) (Potential). 
DISULFID   307   307        Interchain (with C-306 in MEP1B) (By similarity). 
DISULFID   675   686        By similarity. 
DISULFID   680   695        By similarity. 
DISULFID   697   710        By similarity. 
STRAND   66    68  3      
HELIX   70    72  3      
STRAND   76    82  7      
HELIX   88   104  17      
STRAND   108   111  4      
STRAND   119   122  4      
STRAND   124   128  5      
STRAND   138   142  5      
HELIX   149   160  12      
HELIX   171   173  3      
STRAND   175   177  3      
HELIX   179   181  3      
HELIX   184   187  4      
HELIX   188   190  3      
STRAND   196   199  4      
STRAND   218   220  3      
TURN   221   223  3      
STRAND   226   231  6      
HELIX   246   253  8      
Sequence information
Length: 747 AA [This is the length of the unprocessed precursor] Molecular weight: 84197 Da [This is the MW of the unprocessed precursor] CRC64: 2A18242A43505633 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MLWIQPACLL SLIFSAHIAA VSIKHLLNGS DHDTDVGEQK DIFEINLAAG LNLFQGDILL 

        70         80         90        100        110        120 
PRTRNAMRDP SSRWKLPIPY ILADNLELNA KGAILHAFEM FRLKSCVDFK PYEGESSYII 

       130        140        150        160        170        180 
FQKLSGCWSM IGDQQVGQNI SIGEGCDFKA TIEHEILHAL GFFHEQSRTD RDDYVNIWWD 

       190        200        210        220        230        240 
QIITDYEHNF NTYDDNTITD LNTPYDYESL MHYGPFSFNK NESIPTITTK IPEFNTIIGQ 

       250        260        270        280        290        300 
LPDFSAIDLI RLNRMYNCTA THTLLDHCDF EKTNVCGMIQ GTRDDADWAH GDSSQPEQVD 

       310        320        330        340        350        360 
HTLVGQCKGA GYFMFFNTSL GARGEAALLE SRILYPKRKQ QCLQFFYKMT GSPADRFEVW 

       370        380        390        400        410        420 
VRRDDNAGKV RQLAKIQTFQ GDSDHNWKIA HVTLNEEKKF RYVFLGTKGD PGNSSGGIYL 

       430        440        450        460        470        480 
DDITLTETPC PAGVWTIRNI SQILENTVKG DKLVSPRFYN SEGYGVGVTL YPNGRITSNS 

       490        500        510        520        530        540 
GLLGLTFHLY SGDNDAILEW PVENRQAIMT ILDQEADTRN RMSLTLMFTT SKNQTSSAIN 

       550        560        570        580        590        600 
GSVIWDRPSK VGVYDKDCDC FRSLDWGWGQ AISHQLLKRR NFLKGDSLII FVDFKDLTHL 

       610        620        630        640        650        660 
NRTEVPASAR STMPRGLLLQ GQESPALGES SRKAMLEESL PSSLGQRHPS RQKRSVENTG 

       670        680        690        700        710        720 
PMEDHNWPQY FRDPCDPNPC QNEGTCVNVK GMASCRCVSG HAFFYAGERC QAMHVHGSLL 

       730        740 
GLLIGCIAGL IFLTFVTFST TNGKLRQ 

P28825 in FASTA format

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