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Protein

Meprin A subunit alpha

Gene

Mep1a

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

Functioni

Catalytic activityi

Hydrolysis of protein and peptide substrates preferentially on carboxyl side of hydrophobic residues.2 Publications

Cofactori

Zn2+By similarityNote: Binds 1 zinc ion per subunit.By similarity

Enzyme regulationi

Inhibited by metal ion chelators EDTA and 1,10-phenanthroline, bradykinin analogs, cysteine, CONA65, and several hydroxamate compounds, particularly tyrosine hydroxamate. Not inhibited by 3,4-dichloroisocourmarin, soybean trypsin inhibitor, or the cysteine proteinase inhibitors iodoacetic acid and E-64.3 Publications

Kineticsi

  1. KM=29.6 µM for GRP3 Publications
  2. KM=67.2 µM for PTH 12-343 Publications
  3. KM=111 µM for secretin3 Publications
  4. KM=30.6 µM for substance P3 Publications
  5. KM=156 µM for LHRH3 Publications
  6. KM=22.3 µM for alpha-MSH3 Publications
  7. KM=101 µM for bradykinin3 Publications
  8. KM=290 µM for Arg-Pro-Pro-Gly-Npa-Ser-Pro-Phe-Arg3 Publications
  9. KM=331 µM for Arg-Pro-Pro-Gly-Npa-Ala-Pro-Phe-Arg3 Publications
  10. KM=174 µM for Arg-Pro-Pro-Gly-Npa-Arg-Pro-Phe-Arg3 Publications
  11. KM=226 µM for Arg-Pro-Pro-Gly-Npa-Phe-Pro-Phe-Arg3 Publications
  12. KM=182 µM for Arg-Pro-Pro-Gly-Npa-Lys-Pro-Phe-Arg3 Publications
  13. KM=339 µM for Arg-Pro-Pro-Gly-Npa-Glu-Pro-Phe-Arg3 Publications
  14. KM=366 µM for 2ABz-Arg-Pro-Gly-Phe-Ser-Pro-Npa-Arg3 Publications
  15. KM=296 µM for 2ABz-Arg-Pro-Ile-Phe-Ser-Pro-Npa-Arg3 Publications
  16. KM=183 µM for 2ABz-Arg-Hyp-Gly-Phe-Ser-Pro-Npa-Arg3 Publications
  17. KM=220 µM for 2ABz-Arg-Gly-Pro-Phe-Ser-Pro-Npa-Arg3 Publications
  18. KM=1380 µM for 2ABz-Arg-Pro-Gly-Ala-Ser-Pro-Npa-Arg3 Publications
  19. KM=1220 µM for 2ABz-Arg-Pro-Gly-Glu-Ser-Pro-Npa-Arg3 Publications
  20. KM=402 µM for 2ABz-Arg-Pro-Gly-Lys-Ser-Pro-Npa-Arg3 Publications
  21. KM=2460 µM for 2ABz-Arg-Pro-Gly-Leu-Ser-Pro-Npa-Arg3 Publications

    Temperature dependencei

    The half-life at 58 degrees Celsius is 50 minutes.3 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi57 – 571Zinc; catalyticPROSITE-ProRule annotation
    Metal bindingi154 – 1541Zinc; via tele nitrogen; catalyticBy similarity
    Active sitei155 – 1551PROSITE-ProRule annotation
    Metal bindingi158 – 1581Zinc; via tele nitrogen; catalyticBy similarity
    Metal bindingi164 – 1641Zinc; via tele nitrogen; catalyticBy similarity

    GO - Molecular functioni

    Complete GO annotation...

    Keywords - Molecular functioni

    Hydrolase, Metalloprotease, Protease

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    BRENDAi3.4.24.18. 3474.

    Protein family/group databases

    MEROPSiM12.002.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Meprin A subunit alpha (EC:3.4.24.18)
    Alternative name(s):
    Endopeptidase-2
    MEP-1
    Gene namesi
    Name:Mep1a
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    Proteomesi
    • UP000000589 Componenti: Chromosome 17

    Organism-specific databases

    MGIiMGI:96963. Mep1a.

    Subcellular locationi

    Topology

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini65 – 713649ExtracellularSequence analysisAdd
    BLAST
    Transmembranei714 – 74128HelicalSequence analysisAdd
    BLAST
    Topological domaini742 – 7476CytoplasmicSequence analysis

    GO - Cellular componenti

    • extracellular exosome Source: MGI
    • integral component of membrane Source: UniProtKB-KW
    • membrane Source: MGI
    Complete GO annotation...

    Keywords - Cellular componenti

    Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi139 – 1391N → Q: Increased susceptibility to heat-inactivation. Forms homodimers and oligomers; when associated with Q-221. Inactive, impaired ability to form homodimers or oligomers; when associated with Q-257 or Q-221 and Q-257. 1 Publication
    Mutagenesisi141 – 1411S → A: Impaired ability to form homodimers or oligomers; when associated with A-259. 1 Publication
    Mutagenesisi221 – 2211N → Q: Increased susceptibility to heat-inactivation. Forms homodimers and oligomers; when associated with Q-139 or Q-257. Inactive, impaired ability to form homodimers or oligomers; when associated with Q-139 and Q-257. 1 Publication
    Mutagenesisi257 – 2571N → Q: Increased susceptibility to heat-inactivation. Forms homodimers and oligomers; when associated with Q-221. Inactive, impaired ability to form homodimers or oligomers; when associated with Q-139 or Q-139 and Q-221. 1 Publication
    Mutagenesisi259 – 2591T → A: Impaired ability to form homodimers or oligomers; when associated with A-141. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 20201 PublicationAdd
    BLAST
    Propeptidei21 – 64443 PublicationsPRO_0000028879Add
    BLAST
    Chaini65 – 747683Meprin A subunit alphaPRO_0000028880Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi28 – 281N-linked (GlcNAc...)1 Publication
    Disulfide bondi106 ↔ 258PROSITE-ProRule annotation
    Disulfide bondi127 ↔ 146PROSITE-ProRule annotation
    Glycosylationi139 – 1391N-linked (GlcNAc...)1 Publication
    Glycosylationi221 – 2211N-linked (GlcNAc...)1 Publication
    Glycosylationi257 – 2571N-linked (GlcNAc...)1 Publication
    Disulfide bondi268 ↔ 430PROSITE-ProRule annotation
    Disulfide bondi276 – 276InterchainPROSITE-ProRule annotation
    Disulfide bondi307 – 307InterchainPROSITE-ProRule annotation
    Glycosylationi317 – 3171N-linked (GlcNAc...)1 Publication
    Glycosylationi413 – 4131N-linked (GlcNAc...)1 Publication
    Glycosylationi439 – 4391N-linked (GlcNAc...)1 Publication
    Glycosylationi533 – 5331N-linked (GlcNAc...)1 Publication
    Glycosylationi540 – 5401N-linked (GlcNAc...)1 Publication
    Disulfide bondi675 ↔ 686PROSITE-ProRule annotation
    Disulfide bondi680 ↔ 695PROSITE-ProRule annotation
    Disulfide bondi697 ↔ 710PROSITE-ProRule annotation

    Post-translational modificationi

    N-glycosylated; contains GlcNAc, galactose, mannose and a small amount of fucose.2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei601 – 6011Not glycosylated

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Zymogen

    Proteomic databases

    MaxQBiP28825.
    PaxDbiP28825.
    PRIDEiP28825.

    PTM databases

    iPTMnetiP28825.
    PhosphoSiteiP28825.

    Miscellaneous databases

    PMAP-CutDBQ91WH9.

    Expressioni

    Tissue specificityi

    Kidney, intestinal brush borders and salivary ducts.

    Gene expression databases

    BgeeiP28825.
    CleanExiMM_MEP1A.
    GenevisibleiP28825. MM.

    Interactioni

    Subunit structurei

    Homotetramer consisting of disulfide-linked alpha subunits, homooligomer consisting of disulfide-linked alpha subunit homodimers, or heterotetramer of two alpha and two beta subunits formed by non-covalent association of two disulfide-linked heterodimers. Genetic factors determine which oligomer(s) will be formed (strain-specific). Interacts with MBL2 through its carbohydrate moiety. This interaction may inhibit its catalytic activity.3 Publications

    Protein-protein interaction databases

    BioGridi201396. 2 interactions.
    IntActiP28825. 3 interactions.
    MINTiMINT-4121349.
    STRINGi10090.ENSMUSP00000024707.

    Structurei

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1IAFmodel-A65-261[»]
    ProteinModelPortaliP28825.
    SMRiP28825. Positions 31-605.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini263 – 432170MAMPROSITE-ProRule annotationAdd
    BLAST
    Domaini433 – 594162MATHPROSITE-ProRule annotationAdd
    BLAST
    Domaini671 – 71141EGF-likePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni65 – 262198MetalloproteaseAdd
    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

    eggNOGiKOG3714. Eukaryota.
    ENOG410ZPX7. LUCA.
    GeneTreeiENSGT00760000119227.
    HOGENOMiHOG000043106.
    HOVERGENiHBG052457.
    InParanoidiP28825.
    KOiK01395.
    OrthoDBiEOG73V6MT.
    PhylomeDBiP28825.
    TreeFamiTF315280.

    Family and domain databases

    Gene3Di2.60.210.10. 1 hit.
    3.40.390.10. 1 hit.
    InterProiIPR013320. ConA-like_dom.
    IPR000742. EGF-like_dom.
    IPR000998. MAM_dom.
    IPR002083. MATH/TRAF_dom.
    IPR008294. Meprin.
    IPR024079. MetalloPept_cat_dom.
    IPR001506. Peptidase_M12A.
    IPR006026. Peptidase_Metallo.
    IPR008974. TRAF-like.
    [Graphical view]
    PANTHERiPTHR10127:SF311. PTHR10127:SF311. 1 hit.
    PfamiPF01400. Astacin. 1 hit.
    PF00008. EGF. 1 hit.
    PF00629. MAM. 1 hit.
    [Graphical view]
    PIRSFiPIRSF001196. Meprin. 1 hit.
    PRINTSiPR00480. ASTACIN.
    PR00020. MAMDOMAIN.
    SMARTiSM00137. 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]

    Sequencei

    Sequence statusi: Complete.

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

    P28825-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MLWIQPACLL SLIFSAHIAA VSIKHLLNGS DHDTDVGEQK DIFEINLAAG
    60 70 80 90 100
    LNLFQGDILL PRTRNAMRDP SSRWKLPIPY ILADNLELNA KGAILHAFEM
    110 120 130 140 150
    FRLKSCVDFK PYEGESSYII FQKLSGCWSM IGDQQVGQNI SIGEGCDFKA
    160 170 180 190 200
    TIEHEILHAL GFFHEQSRTD RDDYVNIWWD QIITDYEHNF NTYDDNTITD
    210 220 230 240 250
    LNTPYDYESL MHYGPFSFNK NESIPTITTK IPEFNTIIGQ LPDFSAIDLI
    260 270 280 290 300
    RLNRMYNCTA THTLLDHCDF EKTNVCGMIQ GTRDDADWAH GDSSQPEQVD
    310 320 330 340 350
    HTLVGQCKGA GYFMFFNTSL GARGEAALLE SRILYPKRKQ QCLQFFYKMT
    360 370 380 390 400
    GSPADRFEVW VRRDDNAGKV RQLAKIQTFQ GDSDHNWKIA HVTLNEEKKF
    410 420 430 440 450
    RYVFLGTKGD PGNSSGGIYL DDITLTETPC PAGVWTIRNI SQILENTVKG
    460 470 480 490 500
    DKLVSPRFYN SEGYGVGVTL YPNGRITSNS GFLGLTFHLY SGDNDAILEW
    510 520 530 540 550
    PVENRQAIMT ILDQEADTRN RMSLTLMFTT SKNQTSSAIN GSVIWDRPSK
    560 570 580 590 600
    VGVYDKDCDC FRSLDWGWGQ AISHQLLKRR NFLKGDSLII FVDFKDLTHL
    610 620 630 640 650
    NRTEVPASAR STMPRGLLLQ GQESPALGES SRKAMLEESL PSSLGQRHPS
    660 670 680 690 700
    RQKRSVENTG PMEDHNWPQY FRDPCDPNPC QNEGTCVNVK GMASCRCVSG
    710 720 730 740
    HAFFYAGERC QAMHVHGSLL GLLIGCIAGL IFLTFVTFST TNGKLRQ
    Length:747
    Mass (Da):84,231
    Last modified:July 13, 2010 - v4
    Checksum:i2A1A268043559953
    GO

    Sequence cautioni

    The sequence AAA75354.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
    The sequence AAH15258.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti482 – 4821F → L in AAA75354 (PubMed:1374387).Curated
    Sequence conflicti533 – 5331N → I AA sequence (PubMed:1894622).Curated
    Sequence conflicti540 – 5401N → S AA sequence (PubMed:1894622).Curated
    Sequence conflicti545 – 5451W → T AA sequence (PubMed:1894622).Curated

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    M74897 mRNA. Translation: AAA75354.1. Different initiation.
    CT010585 Genomic DNA. Translation: CAQ11110.1.
    BC015258 mRNA. Translation: AAH15258.1. Different initiation.
    U62765 Genomic DNA. Translation: AAC53194.1.
    PIRiA40195.
    RefSeqiNP_032611.2. NM_008585.2.
    XP_006523814.1. XM_006523751.2.
    UniGeneiMm.5346.

    Genome annotation databases

    EnsembliENSMUST00000117137; ENSMUSP00000113838; ENSMUSG00000023914.
    GeneIDi17287.
    KEGGimmu:17287.
    UCSCiuc008cpc.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    M74897 mRNA. Translation: AAA75354.1. Different initiation.
    CT010585 Genomic DNA. Translation: CAQ11110.1.
    BC015258 mRNA. Translation: AAH15258.1. Different initiation.
    U62765 Genomic DNA. Translation: AAC53194.1.
    PIRiA40195.
    RefSeqiNP_032611.2. NM_008585.2.
    XP_006523814.1. XM_006523751.2.
    UniGeneiMm.5346.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1IAFmodel-A65-261[»]
    ProteinModelPortaliP28825.
    SMRiP28825. Positions 31-605.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi201396. 2 interactions.
    IntActiP28825. 3 interactions.
    MINTiMINT-4121349.
    STRINGi10090.ENSMUSP00000024707.

    Protein family/group databases

    MEROPSiM12.002.

    PTM databases

    iPTMnetiP28825.
    PhosphoSiteiP28825.

    Proteomic databases

    MaxQBiP28825.
    PaxDbiP28825.
    PRIDEiP28825.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENSMUST00000117137; ENSMUSP00000113838; ENSMUSG00000023914.
    GeneIDi17287.
    KEGGimmu:17287.
    UCSCiuc008cpc.1. mouse.

    Organism-specific databases

    CTDi4224.
    MGIiMGI:96963. Mep1a.

    Phylogenomic databases

    eggNOGiKOG3714. Eukaryota.
    ENOG410ZPX7. LUCA.
    GeneTreeiENSGT00760000119227.
    HOGENOMiHOG000043106.
    HOVERGENiHBG052457.
    InParanoidiP28825.
    KOiK01395.
    OrthoDBiEOG73V6MT.
    PhylomeDBiP28825.
    TreeFamiTF315280.

    Enzyme and pathway databases

    BRENDAi3.4.24.18. 3474.

    Miscellaneous databases

    ChiTaRSiMep1a. mouse.
    PMAP-CutDBQ91WH9.
    PROiP28825.
    SOURCEiSearch...

    Gene expression databases

    BgeeiP28825.
    CleanExiMM_MEP1A.
    GenevisibleiP28825. MM.

    Family and domain databases

    Gene3Di2.60.210.10. 1 hit.
    3.40.390.10. 1 hit.
    InterProiIPR013320. ConA-like_dom.
    IPR000742. EGF-like_dom.
    IPR000998. MAM_dom.
    IPR002083. MATH/TRAF_dom.
    IPR008294. Meprin.
    IPR024079. MetalloPept_cat_dom.
    IPR001506. Peptidase_M12A.
    IPR006026. Peptidase_Metallo.
    IPR008974. TRAF-like.
    [Graphical view]
    PANTHERiPTHR10127:SF311. PTHR10127:SF311. 1 hit.
    PfamiPF01400. Astacin. 1 hit.
    PF00008. EGF. 1 hit.
    PF00629. MAM. 1 hit.
    [Graphical view]
    PIRSFiPIRSF001196. Meprin. 1 hit.
    PRINTSiPR00480. ASTACIN.
    PR00020. MAMDOMAIN.
    SMARTiSM00137. 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]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "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."
      Jiang W., Gorbea C.M., Flannery A.V., Beynon R.J., Grant G.A., Bond J.S.
      J. Biol. Chem. 267:9185-9193(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 65-103; 107-122; 273-292; 314-348; 370-375; 377-386; 389-398 AND 527-557.
      Strain: C3H/He and C57BL/6.
      Tissue: Kidney.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    3. "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].
      Strain: FVB/N.
      Tissue: Kidney.
    4. "Characterization of the soluble, secreted form of urinary meprin."
      Beynon R.J., Oliver S., Robertson D.H.L.
      Biochem. J. 315:461-465(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 21-25 AND 65-69.
    5. "Correlation of the exon/intron organization to the secondary structures of the protease domain of mouse meprin alpha subunit."
      Jiang W., Flannery A.V.
      Gene 189:65-71(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 62-258.
      Strain: 129.
    6. "The astacin family of metalloendopeptidases."
      Dumermuth E., Sterchi E.E., Jiang W., Wolz R.L., Bond J.S., Flannery A.V., Beynon R.J.
      J. Biol. Chem. 266:21381-21385(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 64-262.
    7. "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 65-72; 315-348 AND 529-546, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, GLYCOSYLATION.
      Strain: ICR.
      Tissue: Kidney.
    8. "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.
    9. "Mapping the active site of meprin-A with peptide substrates and inhibitors."
      Wolz R.L., Harris R.B., Bond J.S.
      Biochemistry 30:8488-8493(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES.
    10. "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.
    11. "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.
    12. "Protease domain glycans affect oligomerization, disulfide bond formation, and stability of the meprin A metalloprotease homo-oligomer."
      Ishmael S.S., Ishmael F.T., Jones A.D., Bond J.S.
      J. Biol. Chem. 281:37404-37415(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBUNIT, GLYCOSYLATION AT ASN-28; ASN-139; ASN-221; ASN-257; ASN-317; ASN-413; ASN-439; ASN-533 AND ASN-540, MUTAGENESIS OF ASN-139; SER-141; ASN-221; ASN-257 AND THR-259.
    13. "Human and mouse homo-oligomeric meprin A metalloendopeptidase: substrate and inhibitor specificities."
      Bylander J.E., Bertenshaw G.P., Matters G.L., Hubbard S.J., Bond J.S.
      Biol. Chem. 388:1163-1172(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES.
    14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Kidney.
    15. "Implications of the three-dimensional structure of astacin for the structure and function of the astacin family of zinc-endopeptidases."
      Stoecker W., Gomis-Rueth F.-X., Bode W., Zwilling R.
      Eur. J. Biochem. 214:215-231(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: 3D-STRUCTURE MODELING.

    Entry informationi

    Entry nameiMEP1A_MOUSE
    AccessioniPrimary (citable) accession number: P28825
    Secondary accession number(s): B0V2P9, Q91WH9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 1992
    Last sequence update: July 13, 2010
    Last modified: June 8, 2016
    This is version 159 of the entry and version 4 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

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

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.