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Q9H239

- MMP28_HUMAN

UniProt

Q9H239 - MMP28_HUMAN

Protein

Matrix metalloproteinase-28

Gene

MMP28

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 135 (01 Oct 2014)
      Sequence version 2 (03 Oct 2003)
      Previous versions | rss
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    Functioni

    Can degrade casein. Could play a role in tissues homeostasis and repair.

    Cofactori

    Binds 1 zinc ion per subunit.By similarity
    Calcium.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi91 – 911Zinc; in inhibited formBy similarity
    Metal bindingi240 – 2401Zinc; catalyticPROSITE-ProRule annotation
    Active sitei241 – 2411PROSITE-ProRule annotation
    Metal bindingi244 – 2441Zinc; catalyticPROSITE-ProRule annotation
    Metal bindingi250 – 2501Zinc; catalyticPROSITE-ProRule annotation

    GO - Molecular functioni

    1. calcium ion binding Source: InterPro
    2. metalloendopeptidase activity Source: UniProtKB
    3. zinc ion binding Source: InterPro

    Keywords - Molecular functioni

    Hydrolase, Metalloprotease, Protease

    Keywords - Ligandi

    Calcium, Metal-binding, Zinc

    Protein family/group databases

    MEROPSiM10.030.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Matrix metalloproteinase-28 (EC:3.4.24.-)
    Short name:
    MMP-28
    Alternative name(s):
    Epilysin
    Gene namesi
    Name:MMP28
    Synonyms:MMP25
    ORF Names:UNQ1893/PRO4339
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:14366. MMP28.

    Subcellular locationi

    GO - Cellular componenti

    1. proteinaceous extracellular matrix Source: UniProtKB

    Keywords - Cellular componenti

    Extracellular matrix, Secreted

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA30885.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2222Sequence AnalysisAdd
    BLAST
    Propeptidei23 – 122100By similarityPRO_0000028857Add
    BLAST
    Chaini123 – 520398Matrix metalloproteinase-28PRO_0000028858Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi164 – 1641N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi324 ↔ 510By similarity
    Glycosylationi355 – 3551N-linked (GlcNAc...)Sequence Analysis

    Post-translational modificationi

    The precursor is cleaved by a furin endopeptidase.By similarity

    Keywords - PTMi

    Cleavage on pair of basic residues, Disulfide bond, Glycoprotein, Zymogen

    Proteomic databases

    PaxDbiQ9H239.
    PRIDEiQ9H239.

    Expressioni

    Tissue specificityi

    Expressed at high levels in testes and lung. Low levels are detected in kidney, pancreas and skin. Also expressed in fetal lung, brain, skeletal muscle and kidney. Expressed selectively in keratinocytes. Widely expressed in several carcinomas as well. Is up-regulated in response to injury in the skin.

    Gene expression databases

    ArrayExpressiQ9H239.
    BgeeiQ9H239.
    CleanExiHS_MMP25.
    HS_MMP28.
    GenevestigatoriQ9H239.

    Interactioni

    Protein-protein interaction databases

    STRINGi9606.ENSP00000250144.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9H239.
    SMRiQ9H239. Positions 33-510.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati325 – 36945Hemopexin 1Add
    BLAST
    Repeati370 – 40940Hemopexin 2Add
    BLAST
    Repeati415 – 46349Hemopexin 3Add
    BLAST
    Repeati464 – 51047Hemopexin 4Add
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi89 – 968Cysteine switchBy similarity

    Domaini

    The conserved cysteine present in the cysteine-switch motif binds the catalytic zinc ion, thus inhibiting the enzyme. The dissociation of the cysteine from the zinc ion upon the activation-peptide release activates the enzyme.

    Sequence similaritiesi

    Belongs to the peptidase M10A family.Curated
    Contains 4 hemopexin repeats.Curated

    Keywords - Domaini

    Repeat, Signal

    Phylogenomic databases

    eggNOGiNOG254923.
    HOGENOMiHOG000217927.
    HOVERGENiHBG052484.
    InParanoidiQ9H239.
    KOiK08006.
    OMAiFEAWDPH.
    PhylomeDBiQ9H239.

    Family and domain databases

    Gene3Di1.10.101.10. 1 hit.
    2.110.10.10. 1 hit.
    3.40.390.10. 1 hit.
    InterProiIPR000585. Hemopexin-like_dom.
    IPR018487. Hemopexin-like_repeat.
    IPR024079. MetalloPept_cat_dom.
    IPR028735. MMP28.
    IPR001818. Pept_M10_metallopeptidase.
    IPR021190. Pept_M10A.
    IPR016293. Pept_M10A_stromelysin-type.
    IPR006026. Peptidase_Metallo.
    IPR002477. Peptidoglycan-bd-like.
    [Graphical view]
    PANTHERiPTHR10201:SF16. PTHR10201:SF16. 1 hit.
    PfamiPF00045. Hemopexin. 2 hits.
    PF00413. Peptidase_M10. 1 hit.
    PF01471. PG_binding_1. 1 hit.
    [Graphical view]
    PIRSFiPIRSF001191. Peptidase_M10A_matrix. 1 hit.
    PRINTSiPR00138. MATRIXIN.
    SMARTiSM00120. HX. 4 hits.
    SM00235. ZnMc. 1 hit.
    [Graphical view]
    SUPFAMiSSF47090. SSF47090. 1 hit.
    SSF50923. SSF50923. 1 hit.
    PROSITEiPS51642. HEMOPEXIN_2. 4 hits.
    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 splicing. Align

    Isoform 1 (identifier: Q9H239-1) [UniParc]FASTAAdd to Basket

    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

    MVARVGLLLR ALQLLLWGHL DAQPAERGGQ ELRKEAEAFL EKYGYLNEQV    50
    PKAPTSTRFS DAIRAFQWVS QLPVSGVLDR ATLRQMTRPR CGVTDTNSYA 100
    AWAERISDLF ARHRTKMRRK KRFAKQGNKW YKQHLSYRLV NWPEHLPEPA 150
    VRGAVRAAFQ LWSNVSALEF WEAPATGPAD IRLTFFQGDH NDGLGNAFDG 200
    PGGALAHAFL PRRGEAHFDQ DERWSLSRRR GRNLFVVLAH EIGHTLGLTH 250
    SPAPRALMAP YYKRLGRDAL LSWDDVLAVQ SLYGKPLGGS VAVQLPGKLF 300
    TDFETWDSYS PQGRRPETQG PKYCHSSFDA ITVDRQQQLY IFKGSHFWEV 350
    AADGNVSEPR PLQERWVGLP PNIEAAAVSL NDGDFYFFKG GRCWRFRGPK 400
    PVWGLPQLCR AGGLPRHPDA ALFFPPLRRL ILFKGARYYV LARGGLQVEP 450
    YYPRSLQDWG GIPEEVSGAL PRPDGSIIFF RDDRYWRLDQ AKLQATTSGR 500
    WATELPWMGC WHANSGSALF 520
    Length:520
    Mass (Da):58,939
    Last modified:October 3, 2003 - v2
    Checksum:iE85D7ADA3069B063
    GO
    Isoform 2 (identifier: Q9H239-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         128-130: NKW → EHC
         131-520: Missing.

    Show »
    Length:130
    Mass (Da):14,927
    Checksum:i8A037DC95502660C
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti487 – 4871R → C in AAG41981. (PubMed:11255011)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei128 – 1303NKW → EHC in isoform 2. 1 PublicationVSP_040552
    Alternative sequencei131 – 520390Missing in isoform 2. 1 PublicationVSP_040553Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF315683 mRNA. Translation: AAG41981.1.
    AF219624 mRNA. Translation: AAK01480.1.
    AF330002 mRNA. Translation: AAK01706.1.
    AY358987 mRNA. Translation: AAQ89346.1.
    AC006237 Genomic DNA. No translation available.
    AC015849 Genomic DNA. No translation available.
    BC011774 mRNA. Translation: AAH11774.1.
    CCDSiCCDS45651.1. [Q9H239-2]
    RefSeqiNP_001027449.1. NM_001032278.2. [Q9H239-2]
    NP_077278.1. NM_024302.4. [Q9H239-1]
    NP_116568.1. NM_032950.3.
    UniGeneiHs.380710.

    Genome annotation databases

    EnsembliENST00000605424; ENSP00000473853; ENSG00000271447. [Q9H239-1]
    GeneIDi79148.
    KEGGihsa:79148.
    UCSCiuc002hjy.1. human. [Q9H239-1]
    uc002hka.3. human. [Q9H239-2]

    Polymorphism databases

    DMDMi37538314.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF315683 mRNA. Translation: AAG41981.1 .
    AF219624 mRNA. Translation: AAK01480.1 .
    AF330002 mRNA. Translation: AAK01706.1 .
    AY358987 mRNA. Translation: AAQ89346.1 .
    AC006237 Genomic DNA. No translation available.
    AC015849 Genomic DNA. No translation available.
    BC011774 mRNA. Translation: AAH11774.1 .
    CCDSi CCDS45651.1. [Q9H239-2 ]
    RefSeqi NP_001027449.1. NM_001032278.2. [Q9H239-2 ]
    NP_077278.1. NM_024302.4. [Q9H239-1 ]
    NP_116568.1. NM_032950.3.
    UniGenei Hs.380710.

    3D structure databases

    ProteinModelPortali Q9H239.
    SMRi Q9H239. Positions 33-510.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9606.ENSP00000250144.

    Protein family/group databases

    MEROPSi M10.030.

    Polymorphism databases

    DMDMi 37538314.

    Proteomic databases

    PaxDbi Q9H239.
    PRIDEi Q9H239.

    Protocols and materials databases

    DNASUi 79148.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000605424 ; ENSP00000473853 ; ENSG00000271447 . [Q9H239-1 ]
    GeneIDi 79148.
    KEGGi hsa:79148.
    UCSCi uc002hjy.1. human. [Q9H239-1 ]
    uc002hka.3. human. [Q9H239-2 ]

    Organism-specific databases

    CTDi 79148.
    GeneCardsi GC17M034092.
    HGNCi HGNC:14366. MMP28.
    MIMi 608417. gene.
    neXtProti NX_Q9H239.
    PharmGKBi PA30885.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG254923.
    HOGENOMi HOG000217927.
    HOVERGENi HBG052484.
    InParanoidi Q9H239.
    KOi K08006.
    OMAi FEAWDPH.
    PhylomeDBi Q9H239.

    Miscellaneous databases

    GeneWikii MMP28.
    GenomeRNAii 79148.
    NextBioi 68057.
    PROi Q9H239.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9H239.
    Bgeei Q9H239.
    CleanExi HS_MMP25.
    HS_MMP28.
    Genevestigatori Q9H239.

    Family and domain databases

    Gene3Di 1.10.101.10. 1 hit.
    2.110.10.10. 1 hit.
    3.40.390.10. 1 hit.
    InterProi IPR000585. Hemopexin-like_dom.
    IPR018487. Hemopexin-like_repeat.
    IPR024079. MetalloPept_cat_dom.
    IPR028735. MMP28.
    IPR001818. Pept_M10_metallopeptidase.
    IPR021190. Pept_M10A.
    IPR016293. Pept_M10A_stromelysin-type.
    IPR006026. Peptidase_Metallo.
    IPR002477. Peptidoglycan-bd-like.
    [Graphical view ]
    PANTHERi PTHR10201:SF16. PTHR10201:SF16. 1 hit.
    Pfami PF00045. Hemopexin. 2 hits.
    PF00413. Peptidase_M10. 1 hit.
    PF01471. PG_binding_1. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF001191. Peptidase_M10A_matrix. 1 hit.
    PRINTSi PR00138. MATRIXIN.
    SMARTi SM00120. HX. 4 hits.
    SM00235. ZnMc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47090. SSF47090. 1 hit.
    SSF50923. SSF50923. 1 hit.
    PROSITEi PS51642. HEMOPEXIN_2. 4 hits.
    PS00142. ZINC_PROTEASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "MMP-28, a new human matrix metalloproteinase with an unusual cysteine-switch sequence is widely expressed in tumors."
      Marchenko G.N., Strongin A.Y.
      Gene 265:87-93(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Lung.
    2. "Epilysin, a novel human matrix metalloproteinase (MMP-28) expressed in testis and keratinocytes and in response to injury."
      Lohi J., Wilson C.L., Roby J.D., Parks W.C.
      J. Biol. Chem. 276:10134-10144(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ALTERNATIVE SPLICING.
      Tissue: Testis.
    3. "Cloning and genomic localization of a novel matrix metalloprotease."
      Southan C., Hughes S.A.
      Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    5. "DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
      Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L.
      , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
      Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
      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] (ISOFORM 2).
      Tissue: Pancreas.

    Entry informationi

    Entry nameiMMP28_HUMAN
    AccessioniPrimary (citable) accession number: Q9H239
    Secondary accession number(s): Q96F04, Q96TE2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 1, 2001
    Last sequence update: October 3, 2003
    Last modified: October 1, 2014
    This is version 135 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 17
      Human chromosome 17: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. Peptidase families
      Classification of peptidase families and list of entries
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3