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Q8N119

- MMP21_HUMAN

UniProt

Q8N119 - MMP21_HUMAN

Protein

Matrix metalloproteinase-21

Gene

MMP21

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 108 (01 Oct 2014)
      Sequence version 2 (11 Jan 2011)
      Previous versions | rss
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    Functioni

    May have an important and specific function in tumor progression and embryogenesis. Cleaves alpha-1-antitrypsin.

    Cofactori

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi117 – 1171Zinc; in inhibited formBy similarity
    Metal bindingi283 – 2831Zinc; catalyticPROSITE-ProRule annotation
    Active sitei284 – 2841PROSITE-ProRule annotation
    Metal bindingi287 – 2871Zinc; catalyticPROSITE-ProRule annotation
    Metal bindingi293 – 2931Zinc; catalyticPROSITE-ProRule annotation

    GO - Molecular functioni

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

    Keywords - Molecular functioni

    Hydrolase, Metalloprotease, Protease

    Keywords - Ligandi

    Calcium, Metal-binding, Zinc

    Protein family/group databases

    MEROPSiM10.026.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Matrix metalloproteinase-21 (EC:3.4.24.-)
    Short name:
    MMP-21
    Gene namesi
    Name:MMP21
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 10

    Organism-specific databases

    HGNCiHGNC:14357. MMP21.

    Subcellular locationi

    Secreted Curated

    GO - Cellular componenti

    1. extracellular matrix Source: InterPro
    2. extracellular region Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA134885721.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2424Sequence AnalysisAdd
    BLAST
    Propeptidei25 – 144120By similarityPRO_0000028839Add
    BLAST
    Chaini145 – 569425Matrix metalloproteinase-21PRO_0000028840Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi329 ↔ 560By similarity
    Glycosylationi372 – 3721N-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

    PaxDbiQ8N119.
    PRIDEiQ8N119.

    PTM databases

    PhosphoSiteiQ8N119.

    Expressioni

    Tissue specificityi

    Identified in fetal brain, kidney and liver. In adult tissues found primarily in ovary, kidney, liver, lung, placenta, brain and peripheral blood leukocytes. Expressed as well in various cancer cell lines.2 Publications

    Gene expression databases

    BgeeiQ8N119.
    CleanExiHS_MMP21.
    GenevestigatoriQ8N119.

    Organism-specific databases

    HPAiHPA024429.

    Interactioni

    Protein-protein interaction databases

    STRINGi9606.ENSP00000357798.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8N119.
    SMRiQ8N119. Positions 76-564.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati330 – 38960Hemopexin 1Add
    BLAST
    Repeati391 – 44757Hemopexin 2Add
    BLAST
    Repeati448 – 49649Hemopexin 3Add
    BLAST
    Repeati503 – 55957Hemopexin 4Add
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi115 – 1228Cysteine 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

    eggNOGiNOG115777.
    HOGENOMiHOG000113608.
    HOVERGENiHBG052483.
    InParanoidiQ8N119.
    KOiK08000.
    OMAiLYENRNN.
    OrthoDBiEOG7X9G6K.
    PhylomeDBiQ8N119.
    TreeFamiTF315428.

    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.
    IPR001818. Pept_M10_metallopeptidase.
    IPR021190. Pept_M10A.
    IPR016293. Pept_M10A_stromelysin-type.
    IPR006026. Peptidase_Metallo.
    IPR002477. Peptidoglycan-bd-like.
    [Graphical view]
    PfamiPF00045. Hemopexin. 3 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]

    Sequencei

    Sequence statusi: Complete.

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

    Q8N119-1 [UniParc]FASTAAdd to Basket

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    MLAASIFRPT LLLCWLAAPW PTQPESLFHS RDRSDLEPSP LRQAKPIADL    50
    HAAQRFLSRY GWSGVWAAWG PSPEGPPETP KGAALAEAVR RFQRANALPA 100
    SGELDAATLA AMNRPRCGVP DMRPPPPSAP PSPPGPPPRA RSRRSPRAPL 150
    SLSRRGWQPR GYPDGGAAQA FSKRTLSWRL LGEALSSQLS VADQRRIVAL 200
    AFRMWSEVTP LDFREDLAAP GAAVDIKLGF GRGRHLGCPR AFDGSGQEFA 250
    HAWRLGDIHF DDDEHFTPPT SDTGISLLKV AVHEIGHVLG LPHTYRTGSI 300
    MQPNYIPQEP AFELDWSDRK AIQKLYGSCE GSFDTAFDWI RKERNQYGEV 350
    MVRFSTYFFR NSWYWLYENR NNRTRYGDPI QILTGWPGIP THNIDAFVHI 400
    WTWKRDERYF FQGNQYWRYD SDKDQALTED EQGKSYPKLI SEGFPGIPSP 450
    LDTAFYDRRQ KLIYFFKESL VFAFDVNRNR VLNSYPKRIT EVFPAVIPQN 500
    HPFRNIDSAY YSYAYNSIFF FKGNAYWKVV NDKDKQQNSW LPANGLFPKK 550
    FISEKWFDVC DVHISTLNM 569
    Length:569
    Mass (Da):65,043
    Last modified:January 11, 2011 - v2
    Checksum:i6785EF34F5B5105E
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti95 – 951A → E.1 Publication
    Corresponds to variant rs28381282 [ dbSNP | Ensembl ].
    VAR_022291
    Natural varianti115 – 1151P → Q.1 Publication
    Corresponds to variant rs28381284 [ dbSNP | Ensembl ].
    VAR_022292
    Natural varianti191 – 1911V → A.2 Publications
    Corresponds to variant rs10901425 [ dbSNP | Ensembl ].
    VAR_019393
    Natural varianti263 – 2631D → E.
    Corresponds to variant rs34811493 [ dbSNP | Ensembl ].
    VAR_032824
    Natural varianti311 – 3111A → T.
    Corresponds to variant rs17173746 [ dbSNP | Ensembl ].
    VAR_057803
    Natural varianti349 – 3491E → G.1 Publication
    Corresponds to variant rs28381302 [ dbSNP | Ensembl ].
    VAR_022293
    Natural varianti360 – 3601R → H.
    Corresponds to variant rs17153524 [ dbSNP | Ensembl ].
    VAR_057804
    Natural varianti454 – 4541A → V.1 Publication
    Corresponds to variant rs28381319 [ dbSNP | Ensembl ].
    VAR_022294

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF331526 mRNA. Translation: AAM92903.1.
    AY121358 Genomic DNA. Translation: AAM78033.1.
    AF520613 mRNA. Translation: AAM75352.1.
    AY885252 Genomic DNA. Translation: AAW62254.1.
    AL158835, AL360176 Genomic DNA. Translation: CAH73211.1.
    AL360176, AL158835 Genomic DNA. Translation: CAI12086.1.
    CCDSiCCDS7647.1.
    RefSeqiNP_671724.1. NM_147191.1.
    UniGeneiHs.314141.

    Genome annotation databases

    EnsembliENST00000368808; ENSP00000357798; ENSG00000154485.
    GeneIDi118856.
    KEGGihsa:118856.
    UCSCiuc001liu.3. human.

    Polymorphism databases

    DMDMi317373390.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    NIEHS-SNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF331526 mRNA. Translation: AAM92903.1 .
    AY121358 Genomic DNA. Translation: AAM78033.1 .
    AF520613 mRNA. Translation: AAM75352.1 .
    AY885252 Genomic DNA. Translation: AAW62254.1 .
    AL158835 , AL360176 Genomic DNA. Translation: CAH73211.1 .
    AL360176 , AL158835 Genomic DNA. Translation: CAI12086.1 .
    CCDSi CCDS7647.1.
    RefSeqi NP_671724.1. NM_147191.1.
    UniGenei Hs.314141.

    3D structure databases

    ProteinModelPortali Q8N119.
    SMRi Q8N119. Positions 76-564.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9606.ENSP00000357798.

    Protein family/group databases

    MEROPSi M10.026.

    PTM databases

    PhosphoSitei Q8N119.

    Polymorphism databases

    DMDMi 317373390.

    Proteomic databases

    PaxDbi Q8N119.
    PRIDEi Q8N119.

    Protocols and materials databases

    DNASUi 118856.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000368808 ; ENSP00000357798 ; ENSG00000154485 .
    GeneIDi 118856.
    KEGGi hsa:118856.
    UCSCi uc001liu.3. human.

    Organism-specific databases

    CTDi 118856.
    GeneCardsi GC10M127445.
    HGNCi HGNC:14357. MMP21.
    HPAi HPA024429.
    MIMi 608416. gene.
    neXtProti NX_Q8N119.
    PharmGKBi PA134885721.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG115777.
    HOGENOMi HOG000113608.
    HOVERGENi HBG052483.
    InParanoidi Q8N119.
    KOi K08000.
    OMAi LYENRNN.
    OrthoDBi EOG7X9G6K.
    PhylomeDBi Q8N119.
    TreeFami TF315428.

    Miscellaneous databases

    GeneWikii MMP21.
    GenomeRNAii 118856.
    NextBioi 80358.
    PROi Q8N119.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q8N119.
    CleanExi HS_MMP21.
    Genevestigatori Q8N119.

    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.
    IPR001818. Pept_M10_metallopeptidase.
    IPR021190. Pept_M10A.
    IPR016293. Pept_M10A_stromelysin-type.
    IPR006026. Peptidase_Metallo.
    IPR002477. Peptidoglycan-bd-like.
    [Graphical view ]
    Pfami PF00045. Hemopexin. 3 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. "Matrix metalloproteinase-21, the human orthologue for XMMP, is expressed during fetal development and in cancer."
      Ahokas K., Lohi J., Lohi H., Elomaa O., Karjalainen-Lindsberg M.-L., Kere J., Saarialho-Kere U.
      Gene 301:31-41(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
    2. "The structure and regulation of the human and mouse matrix metalloproteinase-21 gene and protein."
      Marchenko G.N., Marchenko N.D., Strongin A.Y.
      Biochem. J. 372:503-515(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], TISSUE SPECIFICITY, VARIANT ALA-191.
      Tissue: Kidney.
    3. NIEHS SNPs program
      Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS GLU-95; GLN-115; ALA-191; GLY-349 AND VAL-454.
    4. "The DNA sequence and comparative analysis of human chromosome 10."
      Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
      , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
      Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

    Entry informationi

    Entry nameiMMP21_HUMAN
    AccessioniPrimary (citable) accession number: Q8N119
    Secondary accession number(s): Q5VZP9, Q8NG02
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 19, 2004
    Last sequence update: January 11, 2011
    Last modified: October 1, 2014
    This is version 108 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 10
      Human chromosome 10: 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