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Protein

Meprin A subunit alpha

Gene

MEP1A

Organism
Homo sapiens (Human)
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.

Cofactori

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

Enzyme regulationi

Inhibited by several hydroxamate compounds, the most potent inhibitor is actinonin.1 Publication

Kineticsi

  1. KM=110 µM for GRP1 Publication
  2. KM=18.0 µM for PTH 12-341 Publication
  3. KM=33.9 µM for secretin1 Publication
  4. KM=41.3 µM for substance P1 Publication
  5. KM=56.5 µM for LHRH1 Publication
  6. KM=73.2 µM for orcokinin1 Publication
  7. KM=292 µM for alpha-MSH1 Publication
  8. KM=125 µM for bradykinin1 Publication
  9. KM=200 µM for gastrin1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi58 – 581Zinc; catalyticPROSITE-ProRule annotation
    Metal bindingi155 – 1551Zinc; via tele nitrogen; catalyticBy similarity
    Active sitei156 – 1561PROSITE-ProRule annotation
    Metal bindingi159 – 1591Zinc; via tele nitrogen; catalyticBy similarity
    Metal bindingi165 – 1651Zinc; via tele nitrogen; catalyticBy similarity

    GO - Molecular functioni

    • metalloendopeptidase activity Source: ProtInc
    • zinc ion binding Source: InterPro

    GO - Biological processi

    • digestion Source: ProtInc
    Complete GO annotation...

    Keywords - Molecular functioni

    Hydrolase, Metalloprotease, Protease

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    BRENDAi3.4.24.18. 2681.
    SignaLinkiQ16819.

    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
    N-benzoyl-L-tyrosyl-P-amino-benzoic acid hydrolase subunit alpha
    PABA peptide hydrolase
    PPH alpha
    Gene namesi
    Name:MEP1A
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640 Componenti: Chromosome 6

    Organism-specific databases

    HGNCiHGNC:7015. MEP1A.

    Subcellular locationi

    Topology

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini66 – 712647ExtracellularSequence AnalysisAdd
    BLAST
    Transmembranei713 – 74028HelicalSequence AnalysisAdd
    BLAST
    Topological domaini741 – 7466CytoplasmicSequence Analysis

    GO - Cellular componenti

    • extracellular exosome Source: UniProtKB
    • extracellular space Source: ProtInc
    • integral component of plasma membrane Source: ProtInc
    • meprin A complex Source: Ensembl
    Complete GO annotation...

    Keywords - Cellular componenti

    Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA30749.

    Polymorphism and mutation databases

    BioMutaiMEP1A.
    DMDMi205830902.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2121By similarityAdd
    BLAST
    Propeptidei22 – 6544By similarityPRO_0000028877Add
    BLAST
    Chaini66 – 746681Meprin A subunit alphaPRO_0000028878Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi107 ↔ 259PROSITE-ProRule annotation
    Disulfide bondi128 ↔ 147PROSITE-ProRule annotation
    Glycosylationi140 – 1401N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi222 – 2221N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi258 – 2581N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi269 ↔ 431PROSITE-ProRule annotation
    Disulfide bondi277 – 277InterchainPROSITE-ProRule annotation
    Disulfide bondi308 – 308InterchainPROSITE-ProRule annotation
    Glycosylationi414 – 4141N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi440 – 4401N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi447 – 4471N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi539 – 5391N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi674 ↔ 685PROSITE-ProRule annotation
    Disulfide bondi679 ↔ 694PROSITE-ProRule annotation
    Disulfide bondi696 ↔ 709PROSITE-ProRule annotation

    Post-translational modificationi

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

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Zymogen

    Proteomic databases

    PaxDbiQ16819.
    PRIDEiQ16819.

    PTM databases

    PhosphoSiteiQ16819.

    Expressioni

    Gene expression databases

    BgeeiQ16819.
    CleanExiHS_MEP1A.
    ExpressionAtlasiQ16819. baseline and differential.
    GenevisibleiQ16819. HS.

    Organism-specific databases

    HPAiCAB025163.
    HPA029416.

    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 (By similarity). Interacts with MBL2 through its carbohydrate moiety. This interaction may inhibit its catalytic activity (By similarity).By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    MMP9P147802EBI-8153734,EBI-1382326

    Protein-protein interaction databases

    BioGridi110387. 11 interactions.
    IntActiQ16819. 1 interaction.
    STRINGi9606.ENSP00000230588.

    Structurei

    3D structure databases

    ProteinModelPortaliQ16819.
    SMRiQ16819. Positions 62-259, 435-589.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini264 – 433170MAMPROSITE-ProRule annotationAdd
    BLAST
    Domaini434 – 593160MATHPROSITE-ProRule annotationAdd
    BLAST
    Domaini670 – 71041EGF-likePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni66 – 263198MetalloproteaseAdd
    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.
    HOVERGENiHBG052457.
    InParanoidiQ16819.
    KOiK01395.
    OrthoDBiEOG73V6MT.
    PhylomeDBiQ16819.
    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:SF311. PTHR10127:SF311. 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]

    Sequencei

    Sequence statusi: Complete.

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

    Q16819-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MAWIRSTCIL FFTLLFAHIA AVPIKYLPEE NVHDADFGEQ KDISEINLAA
    60 70 80 90 100
    GLDLFQGDIL LQKSRNGLRD PNTRWTFPIP YILADNLGLN AKGAILYAFE
    110 120 130 140 150
    MFRLKSCVDF KPYEGESSYI IFQQFDGCWS EVGDQHVGQN ISIGQGCAYK
    160 170 180 190 200
    AIIEHEILHA LGFYHEQSRT DRDDYVNIWW DQILSGYQHN FDTYDDSLIT
    210 220 230 240 250
    DLNTPYDYES LMHYQPFSFN KNASVPTITA KIPEFNSIIG QRLDFSAIDL
    260 270 280 290 300
    ERLNRMYNCT TTHTLLDHCT FEKANICGMI QGTRDDTDWA HQDSAQAGEV
    310 320 330 340 350
    DHTLLGQCTG AGYFMQFSTS SGSAEEAALL ESRILYPKRK QQCLQFFYKM
    360 370 380 390 400
    TGSPSDRLVV WVRRDDSTGN VRKLVKVQTF QGDDDHNWKI AHVVLKEEQK
    410 420 430 440 450
    FRYLFQGTKG DPQNSTGGIY LDDITLTETP CPTGVWTVRN FSQVLENTSK
    460 470 480 490 500
    GDKLQSPRFY NSEGYGFGVT LYPNSRESSG YLRLAFHVCS GENDAILEWP
    510 520 530 540 550
    VENRQVIITI LDQEPDVRNR MSSSMVFTTS KSHTSPAIND TVIWDRPSRV
    560 570 580 590 600
    GTYHTDCNCF RSIDLGWSGF ISHQMLKRRS FLKNDDLIIF VDFEDITHLS
    610 620 630 640 650
    QTEVPTKGKR LSPQGLILQG QEQQVSEEGS GKAMLEEALP VSLSQGQPSR
    660 670 680 690 700
    QKRSVENTGP LEDHNWPQYF RDPCDPNPCQ NDGICVNVKG MASCRCISGH
    710 720 730 740
    AFFYTGERCQ AVQVHGSVLG MVIGGTAGVI FLTFSIIAIL SQRPRK
    Length:746
    Mass (Da):84,419
    Last modified:July 22, 2008 - v2
    Checksum:iB5F0812F2850F958
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti26 – 261Y → H in AAA21338 (Ref. 1) Curated
    Sequence conflicti162 – 1621G → V in AAL85339 (Ref. 2) Curated
    Sequence conflicti306 – 3061G → E in BAF98731 (PubMed:14702039).Curated
    Sequence conflicti426 – 4261L → P in BAF98731 (PubMed:14702039).Curated
    Sequence conflicti518 – 5181R → Q in BAG37669 (PubMed:14702039).Curated
    Sequence conflicti546 – 5461R → S in BAF98731 (PubMed:14702039).Curated
    Sequence conflicti638 – 6381A → V in BAF98731 (PubMed:14702039).Curated
    Sequence conflicti711 – 7133AVQ → SAE in AAA21338 (Ref. 1) Curated
    Sequence conflicti711 – 7133AVQ → SAE no nucleotide entry (PubMed:8262185).Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti469 – 4691V → L.2 Publications
    Corresponds to variant rs2274658 [ dbSNP | Ensembl ].
    VAR_020056
    Natural varianti476 – 4761R → G.1 Publication
    Corresponds to variant rs12197930 [ dbSNP | Ensembl ].
    VAR_033492
    Natural varianti606 – 6061T → S.2 Publications
    Corresponds to variant rs2297020 [ dbSNP | Ensembl ].
    VAR_051583
    Natural varianti634 – 6341M → V.
    Corresponds to variant rs2297019 [ dbSNP | Ensembl ].
    VAR_021846
    Natural varianti726 – 7261T → M.1 Publication
    Corresponds to variant rs1804211 [ dbSNP | Ensembl ].
    VAR_033493

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    M82962 mRNA. Translation: AAA21338.1.
    AF478685 mRNA. Translation: AAL85339.1.
    AK290282 mRNA. Translation: BAF82971.1.
    AK315246 mRNA. Translation: BAG37669.1.
    AK315840 mRNA. Translation: BAF98731.1.
    AL161618 Genomic DNA. Translation: CAC21508.1.
    CH471081 Genomic DNA. Translation: EAX04306.1.
    BC131714 mRNA. Translation: AAI31715.1.
    CCDSiCCDS4918.1.
    PIRiS60193. HYHUMA.
    RefSeqiNP_005579.2. NM_005588.2.
    UniGeneiHs.179704.

    Genome annotation databases

    EnsembliENST00000230588; ENSP00000230588; ENSG00000112818.
    GeneIDi4224.
    KEGGihsa:4224.
    UCSCiuc010jzh.1. human.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    M82962 mRNA. Translation: AAA21338.1.
    AF478685 mRNA. Translation: AAL85339.1.
    AK290282 mRNA. Translation: BAF82971.1.
    AK315246 mRNA. Translation: BAG37669.1.
    AK315840 mRNA. Translation: BAF98731.1.
    AL161618 Genomic DNA. Translation: CAC21508.1.
    CH471081 Genomic DNA. Translation: EAX04306.1.
    BC131714 mRNA. Translation: AAI31715.1.
    CCDSiCCDS4918.1.
    PIRiS60193. HYHUMA.
    RefSeqiNP_005579.2. NM_005588.2.
    UniGeneiHs.179704.

    3D structure databases

    ProteinModelPortaliQ16819.
    SMRiQ16819. Positions 62-259, 435-589.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi110387. 11 interactions.
    IntActiQ16819. 1 interaction.
    STRINGi9606.ENSP00000230588.

    Protein family/group databases

    MEROPSiM12.002.

    PTM databases

    PhosphoSiteiQ16819.

    Polymorphism and mutation databases

    BioMutaiMEP1A.
    DMDMi205830902.

    Proteomic databases

    PaxDbiQ16819.
    PRIDEiQ16819.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000230588; ENSP00000230588; ENSG00000112818.
    GeneIDi4224.
    KEGGihsa:4224.
    UCSCiuc010jzh.1. human.

    Organism-specific databases

    CTDi4224.
    GeneCardsiGC06P046807.
    H-InvDBHIX0032798.
    HGNCiHGNC:7015. MEP1A.
    HPAiCAB025163.
    HPA029416.
    MIMi600388. gene.
    neXtProtiNX_Q16819.
    PharmGKBiPA30749.
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiNOG322115.
    GeneTreeiENSGT00760000119227.
    HOVERGENiHBG052457.
    InParanoidiQ16819.
    KOiK01395.
    OrthoDBiEOG73V6MT.
    PhylomeDBiQ16819.
    TreeFamiTF315280.

    Enzyme and pathway databases

    BRENDAi3.4.24.18. 2681.
    SignaLinkiQ16819.

    Miscellaneous databases

    GeneWikiiMEP1A.
    GenomeRNAii4224.
    NextBioi16671.
    PROiQ16819.
    SOURCEiSearch...

    Gene expression databases

    BgeeiQ16819.
    CleanExiHS_MEP1A.
    ExpressionAtlasiQ16819. baseline and differential.
    GenevisibleiQ16819. HS.

    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:SF311. PTHR10127:SF311. 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]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. Sterchi E.E.
      Submitted (AUG-1994) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT SER-606.
      Tissue: Jejunum.
    2. "Expression of human meprin alpha."
      Haun R.S.
      Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Small intestine.
    3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANTS LEU-469 AND MET-726.
      Tissue: Colon and Small intestine.
    4. "The DNA sequence and analysis of human chromosome 6."
      Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
      , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
      Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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], VARIANTS LEU-469 AND GLY-476.
    7. "Cloning of the PABA peptide hydrolase alpha subunit (PPH alpha) from human small intestine and its expression in COS-1 cells."
      Dumermuth E., Eldering J.A., Gruenberg J., Jiang W., Sterchi E.E.
      FEBS Lett. 335:367-375(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 32-746, VARIANT SER-606.
      Tissue: Jejunum.
    8. "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.

    Entry informationi

    Entry nameiMEP1A_HUMAN
    AccessioniPrimary (citable) accession number: Q16819
    Secondary accession number(s): A2RRM4
    , B0AZP9, B2RCS2, Q8TDC9, Q9H1R1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: July 22, 2008
    Last modified: July 22, 2015
    This is version 153 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 6
      Human chromosome 6: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. Peptidase families
      Classification of peptidase families and list of entries
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3

    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 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.