Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P24347

- MMP11_HUMAN

UniProt

P24347 - MMP11_HUMAN

Protein

Stromelysin-3

Gene

MMP11

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 152 (01 Oct 2014)
      Sequence version 3 (11 Jan 2011)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    May play an important role in the progression of epithelial malignancies.

    Cofactori

    Binds 1 calcium ion per subunit.By similarity
    Binds 2 zinc ions per subunit.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi80 – 801Zinc 2; in inhibited formBy similarity
    Metal bindingi166 – 1661Zinc 1By similarity
    Metal bindingi171 – 1711CalciumBy similarity
    Metal bindingi172 – 1721Calcium; via carbonyl oxygenBy similarity
    Metal bindingi174 – 1741Calcium; via carbonyl oxygenBy similarity
    Metal bindingi176 – 1761Calcium; via carbonyl oxygenBy similarity
    Metal bindingi179 – 1791Zinc 1By similarity
    Metal bindingi192 – 1921Zinc 1By similarity
    Metal bindingi215 – 2151Zinc 2; catalyticBy similarity
    Active sitei216 – 2161PROSITE-ProRule annotation
    Metal bindingi219 – 2191Zinc 2; catalyticBy similarity
    Metal bindingi225 – 2251Zinc 2; catalyticBy similarity

    GO - Molecular functioni

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

    GO - Biological processi

    1. basement membrane organization Source: Ensembl
    2. collagen catabolic process Source: Reactome
    3. collagen fibril organization Source: Ensembl
    4. extracellular matrix disassembly Source: Reactome
    5. extracellular matrix organization Source: Reactome
    6. multicellular organismal development Source: ProtInc
    7. negative regulation of fat cell differentiation Source: Ensembl
    8. proteolysis Source: ProtInc

    Keywords - Molecular functioni

    Hydrolase, Metalloprotease, Protease

    Keywords - Biological processi

    Collagen degradation

    Keywords - Ligandi

    Calcium, Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_118572. Degradation of the extracellular matrix.
    REACT_118682. Activation of Matrix Metalloproteinases.
    REACT_150401. Collagen degradation.

    Protein family/group databases

    MEROPSiM10.007.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Stromelysin-3 (EC:3.4.24.-)
    Short name:
    SL-3
    Short name:
    ST3
    Alternative name(s):
    Matrix metalloproteinase-11
    Short name:
    MMP-11
    Gene namesi
    Name:MMP11
    Synonyms:STMY3
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 22

    Organism-specific databases

    HGNCiHGNC:7157. MMP11.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular matrix Source: MGI
    2. extracellular region Source: Reactome
    3. Golgi lumen Source: Reactome
    4. proteinaceous extracellular matrix Source: ProtInc

    Keywords - Cellular componenti

    Extracellular matrix, Secreted

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA30869.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 3131Sequence AnalysisAdd
    BLAST
    Propeptidei32 – 9766Activation peptideBy similarityPRO_0000028770Add
    BLAST
    Chaini98 – 488391Stromelysin-3PRO_0000028771Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi294 ↔ 480By similarity

    Post-translational modificationi

    The precursor is cleaved by a furin endopeptidase.By similarity

    Keywords - PTMi

    Cleavage on pair of basic residues, Disulfide bond, Zymogen

    Proteomic databases

    PaxDbiP24347.
    PRIDEiP24347.

    PTM databases

    PhosphoSiteiP24347.

    Expressioni

    Tissue specificityi

    Specifically expressed in stromal cells of breast carcinomas.

    Gene expression databases

    ArrayExpressiP24347.
    BgeeiP24347.
    CleanExiHS_MMP11.
    GenevestigatoriP24347.

    Organism-specific databases

    HPAiCAB002593.

    Interactioni

    Protein-protein interaction databases

    STRINGi9606.ENSP00000215743.

    Structurei

    3D structure databases

    ProteinModelPortaliP24347.
    SMRiP24347. Positions 75-460.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati291 – 33949Hemopexin 1Add
    BLAST
    Repeati340 – 38243Hemopexin 2Add
    BLAST
    Repeati384 – 43249Hemopexin 3Add
    BLAST
    Repeati433 – 48048Hemopexin 4Add
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi78 – 858Cysteine 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

    eggNOGiNOG236137.
    HOGENOMiHOG000217927.
    HOVERGENiHBG052484.
    InParanoidiP24347.
    KOiK07993.
    OMAiVDTNEIA.
    OrthoDBiEOG7XPZ57.
    PhylomeDBiP24347.
    TreeFamiTF315428.

    Family and domain databases

    Gene3Di2.110.10.10. 1 hit.
    3.40.390.10. 1 hit.
    InterProiIPR000585. Hemopexin-like_dom.
    IPR018487. Hemopexin-like_repeat.
    IPR018486. Hemopexin_CS.
    IPR024079. MetalloPept_cat_dom.
    IPR001818. Pept_M10_metallopeptidase.
    IPR021190. Pept_M10A.
    IPR016293. Pept_M10A_stromelysin-type.
    IPR021158. Pept_M10A_Zn_BS.
    IPR006026. Peptidase_Metallo.
    IPR028705. Stromelysin-3.
    [Graphical view]
    PANTHERiPTHR10201:SF20. PTHR10201:SF20. 1 hit.
    PfamiPF00045. Hemopexin. 4 hits.
    PF00413. Peptidase_M10. 1 hit.
    [Graphical view]
    PIRSFiPIRSF001191. Peptidase_M10A_matrix. 1 hit.
    PRINTSiPR00138. MATRIXIN.
    SMARTiSM00120. HX. 4 hits.
    SM00235. ZnMc. 1 hit.
    [Graphical view]
    SUPFAMiSSF50923. SSF50923. 1 hit.
    PROSITEiPS00546. CYSTEINE_SWITCH. 1 hit.
    PS00024. HEMOPEXIN. 1 hit.
    PS51642. 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.

    P24347-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAPAAWLRSA AARALLPPML LLLLQPPPLL ARALPPDAHH LHAERRGPQP    50
    WHAALPSSPA PAPATQEAPR PASSLRPPRC GVPDPSDGLS ARNRQKRFVL 100
    SGGRWEKTDL TYRILRFPWQ LVQEQVRQTM AEALKVWSDV TPLTFTEVHE 150
    GRADIMIDFA RYWHGDDLPF DGPGGILAHA FFPKTHREGD VHFDYDETWT 200
    IGDDQGTDLL QVAAHEFGHV LGLQHTTAAK ALMSAFYTFR YPLSLSPDDC 250
    RGVQHLYGQP WPTVTSRTPA LGPQAGIDTN EIAPLEPDAP PDACEASFDA 300
    VSTIRGELFF FKAGFVWRLR GGQLQPGYPA LASRHWQGLP SPVDAAFEDA 350
    QGHIWFFQGA QYWVYDGEKP VLGPAPLTEL GLVRFPVHAA LVWGPEKNKI 400
    YFFRGRDYWR FHPSTRRVDS PVPRRATDWR GVPSEIDAAF QDADGYAYFL 450
    RGRLYWKFDP VKVKALEGFP RLVGPDFFGC AEPANTFL 488
    Length:488
    Mass (Da):54,590
    Last modified:January 11, 2011 - v3
    Checksum:iF03C537EE76706A9
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti38 – 381A → V.2 Publications
    Corresponds to variant rs738792 [ dbSNP | Ensembl ].
    VAR_022181
    Natural varianti44 – 441E → K.1 Publication
    Corresponds to variant rs28363646 [ dbSNP | Ensembl ].
    VAR_022182
    Natural varianti61 – 611P → L.1 Publication
    Corresponds to variant rs28363647 [ dbSNP | Ensembl ].
    VAR_022183
    Natural varianti86 – 861S → P.1 Publication
    Corresponds to variant rs28363648 [ dbSNP | Ensembl ].
    VAR_022184
    Natural varianti166 – 1661D → N in a colorectal cancer sample; somatic mutation. 1 Publication
    VAR_036140
    Natural varianti182 – 1821F → S.1 Publication
    Corresponds to variant rs17854940 [ dbSNP | Ensembl ].
    VAR_029659

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X57766 mRNA. Translation: CAA40918.1.
    AY899208 Genomic DNA. Translation: AAW65373.1.
    AP000349 Genomic DNA. No translation available.
    BC057788 mRNA. Translation: AAH57788.1.
    X84664 Genomic DNA. Translation: CAA59150.1.
    CCDSiCCDS13816.1.
    PIRiS13423.
    RefSeqiNP_005931.2. NM_005940.3.
    UniGeneiHs.143751.

    Genome annotation databases

    EnsembliENST00000215743; ENSP00000215743; ENSG00000099953.
    GeneIDi4320.
    KEGGihsa:4320.
    UCSCiuc002zxx.3. human.

    Polymorphism databases

    DMDMi317373418.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology
    NIEHS-SNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X57766 mRNA. Translation: CAA40918.1 .
    AY899208 Genomic DNA. Translation: AAW65373.1 .
    AP000349 Genomic DNA. No translation available.
    BC057788 mRNA. Translation: AAH57788.1 .
    X84664 Genomic DNA. Translation: CAA59150.1 .
    CCDSi CCDS13816.1.
    PIRi S13423.
    RefSeqi NP_005931.2. NM_005940.3.
    UniGenei Hs.143751.

    3D structure databases

    ProteinModelPortali P24347.
    SMRi P24347. Positions 75-460.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9606.ENSP00000215743.

    Chemistry

    BindingDBi P24347.
    ChEMBLi CHEMBL2867.

    Protein family/group databases

    MEROPSi M10.007.

    PTM databases

    PhosphoSitei P24347.

    Polymorphism databases

    DMDMi 317373418.

    Proteomic databases

    PaxDbi P24347.
    PRIDEi P24347.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000215743 ; ENSP00000215743 ; ENSG00000099953 .
    GeneIDi 4320.
    KEGGi hsa:4320.
    UCSCi uc002zxx.3. human.

    Organism-specific databases

    CTDi 4320.
    GeneCardsi GC22P024110.
    H-InvDB HIX0203187.
    HGNCi HGNC:7157. MMP11.
    HPAi CAB002593.
    MIMi 185261. gene.
    neXtProti NX_P24347.
    PharmGKBi PA30869.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG236137.
    HOGENOMi HOG000217927.
    HOVERGENi HBG052484.
    InParanoidi P24347.
    KOi K07993.
    OMAi VDTNEIA.
    OrthoDBi EOG7XPZ57.
    PhylomeDBi P24347.
    TreeFami TF315428.

    Enzyme and pathway databases

    Reactomei REACT_118572. Degradation of the extracellular matrix.
    REACT_118682. Activation of Matrix Metalloproteinases.
    REACT_150401. Collagen degradation.

    Miscellaneous databases

    GeneWikii MMP11.
    GenomeRNAii 4320.
    NextBioi 16997.
    PROi P24347.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P24347.
    Bgeei P24347.
    CleanExi HS_MMP11.
    Genevestigatori P24347.

    Family and domain databases

    Gene3Di 2.110.10.10. 1 hit.
    3.40.390.10. 1 hit.
    InterProi IPR000585. Hemopexin-like_dom.
    IPR018487. Hemopexin-like_repeat.
    IPR018486. Hemopexin_CS.
    IPR024079. MetalloPept_cat_dom.
    IPR001818. Pept_M10_metallopeptidase.
    IPR021190. Pept_M10A.
    IPR016293. Pept_M10A_stromelysin-type.
    IPR021158. Pept_M10A_Zn_BS.
    IPR006026. Peptidase_Metallo.
    IPR028705. Stromelysin-3.
    [Graphical view ]
    PANTHERi PTHR10201:SF20. PTHR10201:SF20. 1 hit.
    Pfami PF00045. Hemopexin. 4 hits.
    PF00413. Peptidase_M10. 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 SSF50923. SSF50923. 1 hit.
    PROSITEi PS00546. CYSTEINE_SWITCH. 1 hit.
    PS00024. HEMOPEXIN. 1 hit.
    PS51642. HEMOPEXIN_2. 4 hits.
    PS00142. ZINC_PROTEASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "A novel metalloproteinase gene specifically expressed in stromal cells of breast carcinomas."
      Basset P., Bellocq J.-P., Wolf C., Stoll I., Hutin P., Limacher J.-M., Podhajcer O.L., Chenard M.P., Rio M.C., Chambon P.
      Nature 348:699-704(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT VAL-38.
    2. NIEHS SNPs program
      Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS VAL-38; LYS-44; LEU-61 AND PRO-86.
    3. "The DNA sequence of human chromosome 22."
      Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M.
      , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
      Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "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], VARIANT SER-182.
      Tissue: Placenta.
    5. "Structure and promoter characterization of the human stromelysin-3 gene."
      Anglard P., Melot T., Guerin E., Thomas G., Basset P.
      J. Biol. Chem. 270:20337-20344(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-36.
    6. "Furin-dependent intracellular activation of the human stromelysin-3 zymogen."
      Pei D., Weiss S.J.
      Nature 375:244-247(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 81-101.
    7. Cited for: VARIANT [LARGE SCALE ANALYSIS] ASN-166.

    Entry informationi

    Entry nameiMMP11_HUMAN
    AccessioniPrimary (citable) accession number: P24347
    Secondary accession number(s): Q5FX24, Q6PEZ6, Q9UC26
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 1, 1992
    Last sequence update: January 11, 2011
    Last modified: October 1, 2014
    This is version 152 of the entry and version 3 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, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 22
      Human chromosome 22: 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