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P51511

- MMP15_HUMAN

UniProt

P51511 - MMP15_HUMAN

Protein

Matrix metalloproteinase-15

Gene

MMP15

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 150 (01 Oct 2014)
      Sequence version 1 (01 Oct 1996)
      Previous versions | rss
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    Functioni

    Endopeptidase that degrades various components of the extracellular matrix. May activate progelatinase A.1 Publication

    Cofactori

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi111 – 1111Zinc; in inhibited formBy similarity
    Metal bindingi259 – 2591Zinc; catalyticPROSITE-ProRule annotation
    Active sitei260 – 2601PROSITE-ProRule annotation
    Metal bindingi263 – 2631Zinc; catalyticPROSITE-ProRule annotation
    Metal bindingi269 – 2691Zinc; catalyticPROSITE-ProRule annotation

    GO - Molecular functioni

    1. calcium ion binding Source: InterPro
    2. enzyme activator activity Source: ProtInc
    3. metalloendopeptidase activity Source: ProtInc
    4. protein binding Source: IntAct
    5. zinc ion binding Source: ProtInc

    GO - Biological processi

    1. cellular protein modification process Source: ProtInc
    2. collagen catabolic process Source: Reactome
    3. extracellular matrix disassembly Source: Reactome
    4. extracellular matrix organization Source: Reactome
    5. positive regulation of catalytic activity Source: GOC
    6. response to estradiol Source: Ensembl

    Keywords - Molecular functioni

    Hydrolase, Metalloprotease, Protease

    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

    MEROPSiM10.015.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Matrix metalloproteinase-15 (EC:3.4.24.-)
    Short name:
    MMP-15
    Alternative name(s):
    Membrane-type matrix metalloproteinase 2
    Short name:
    MT-MMP 2
    Short name:
    MTMMP2
    Membrane-type-2 matrix metalloproteinase
    Short name:
    MT2-MMP
    Short name:
    MT2MMP
    SMCP-2
    Gene namesi
    Name:MMP15
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 16

    Organism-specific databases

    HGNCiHGNC:7161. MMP15.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular matrix Source: InterPro
    2. integral component of plasma membrane Source: ProtInc
    3. plasma membrane Source: Reactome

    Keywords - Cellular componenti

    Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA30873.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 4141Or 45Sequence AnalysisAdd
    BLAST
    Propeptidei42 – 13190By similarityPRO_0000028808Add
    BLAST
    Chaini132 – 669538Matrix metalloproteinase-15PRO_0000028809Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi150 – 1501N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi370 ↔ 559By similarity
    Modified residuei589 – 5891Phosphoserine1 Publication

    Post-translational modificationi

    The precursor is cleaved by a furin endopeptidase.By similarity

    Keywords - PTMi

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

    Proteomic databases

    MaxQBiP51511.
    PaxDbiP51511.
    PRIDEiP51511.

    PTM databases

    PhosphoSiteiP51511.

    Expressioni

    Tissue specificityi

    Appeared to be synthesized preferentially in liver, placenta, testis, colon and intestine. Substantial amounts are also detected in pancreas, kidney, lung, heart and skeletal muscle.

    Gene expression databases

    BgeeiP51511.
    CleanExiHS_MMP15.
    GenevestigatoriP51511.

    Organism-specific databases

    HPAiCAB002611.
    HPA040390.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    PROCP040702EBI-1383043,EBI-1383018

    Protein-protein interaction databases

    BioGridi110467. 1 interaction.
    IntActiP51511. 2 interactions.
    MINTiMINT-7897770.
    STRINGi9606.ENSP00000219271.

    Structurei

    3D structure databases

    ProteinModelPortaliP51511.
    SMRiP51511. Positions 83-559.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini132 – 625494ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini647 – 66923CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei626 – 64621HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati367 – 41549Hemopexin 1Add
    BLAST
    Repeati416 – 46146Hemopexin 2Add
    BLAST
    Repeati463 – 51149Hemopexin 3Add
    BLAST
    Repeati512 – 55948Hemopexin 4Add
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi109 – 1168Cysteine switchBy similarity

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi331 – 34010Poly-Pro

    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, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG295915.
    HOGENOMiHOG000217928.
    HOVERGENiHBG052484.
    InParanoidiP51511.
    KOiK07995.
    OMAiVQMQRKG.
    OrthoDBiEOG7XPZ57.
    PhylomeDBiP51511.
    TreeFamiTF352396.

    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.
    IPR028729. MMP15.
    IPR001818. Pept_M10_metallopeptidase.
    IPR021190. Pept_M10A.
    IPR021805. Pept_M10A_metallopeptidase_C.
    IPR016293. Pept_M10A_stromelysin-type.
    IPR021158. Pept_M10A_Zn_BS.
    IPR006026. Peptidase_Metallo.
    IPR002477. Peptidoglycan-bd-like.
    [Graphical view]
    PANTHERiPTHR10201:SF25. PTHR10201:SF25. 1 hit.
    PfamiPF11857. DUF3377. 1 hit.
    PF00045. Hemopexin. 4 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.
    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.

    P51511-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGSDPSAPGR PGWTGSLLGD REEAARPRLL PLLLVLLGCL GLGVAAEDAE    50
    VHAENWLRLY GYLPQPSRHM STMRSAQILA SALAEMQRFY GIPVTGVLDE 100
    ETKEWMKRPR CGVPDQFGVR VKANLRRRRK RYALTGRKWN NHHLTFSIQN 150
    YTEKLGWYHS MEAVRRAFRV WEQATPLVFQ EVPYEDIRLR RQKEADIMVL 200
    FASGFHGDSS PFDGTGGFLA HAYFPGPGLG GDTHFDADEP WTFSSTDLHG 250
    NNLFLVAVHE LGHALGLEHS SNPNAIMAPF YQWKDVDNFK LPEDDLRGIQ 300
    QLYGTPDGQP QPTQPLPTVT PRRPGRPDHR PPRPPQPPPP GGKPERPPKP 350
    GPPVQPRATE RPDQYGPNIC DGDFDTVAML RGEMFVFKGR WFWRVRHNRV 400
    LDNYPMPIGH FWRGLPGDIS AAYERQDGRF VFFKGDRYWL FREANLEPGY 450
    PQPLTSYGLG IPYDRIDTAI WWEPTGHTFF FQEDRYWRFN EETQRGDPGY 500
    PKPISVWQGI PASPKGAFLS NDAAYTYFYK GTKYWKFDNE RLRMEPGYPK 550
    SILRDFMGCQ EHVEPGPRWP DVARPPFNPH GGAEPGADSA EGDVGDGDGD 600
    FGAGVNKDGG SRVVVQMEEV ARTVNVVMVL VPLLLLLCVL GLTYALVQMQ 650
    RKGAPRVLLY CKRSLQEWV 669
    Length:669
    Mass (Da):75,807
    Last modified:October 1, 1996 - v1
    Checksum:iFE875EC0674B297F
    GO

    Sequence cautioni

    The sequence BAA13071.1 differs from that shown. Reason: Erroneous initiation.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti200 – 2001L → P.1 Publication
    Corresponds to variant rs41340745 [ dbSNP | Ensembl ].
    VAR_030523
    Natural varianti350 – 3501P → L.1 Publication
    Corresponds to variant rs41335851 [ dbSNP | Ensembl ].
    VAR_030524
    Natural varianti596 – 5961D → G.2 Publications
    Corresponds to variant rs41504346 [ dbSNP | Ensembl ].
    VAR_030525
    Natural varianti609 – 6091G → R.2 Publications
    Corresponds to variant rs3743563 [ dbSNP | Ensembl ].
    VAR_020055
    Natural varianti622 – 6221R → W.1 Publication
    Corresponds to variant rs41434246 [ dbSNP | Ensembl ].
    VAR_030526

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z48482 mRNA. Translation: CAA88373.1.
    EF032329 Genomic DNA. Translation: ABJ53423.1.
    BC036495 mRNA. Translation: AAH36495.1.
    BC055428 mRNA. Translation: AAH55428.1.
    D86331 mRNA. Translation: BAA13071.1. Different initiation.
    D85510 mRNA. Translation: BAA22225.1.
    CCDSiCCDS10792.1.
    PIRiI38029.
    RefSeqiNP_002419.1. NM_002428.2.
    UniGeneiHs.80343.

    Genome annotation databases

    EnsembliENST00000219271; ENSP00000219271; ENSG00000102996.
    GeneIDi4324.
    KEGGihsa:4324.
    UCSCiuc002ena.3. human.

    Polymorphism databases

    DMDMi1705988.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

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

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z48482 mRNA. Translation: CAA88373.1 .
    EF032329 Genomic DNA. Translation: ABJ53423.1 .
    BC036495 mRNA. Translation: AAH36495.1 .
    BC055428 mRNA. Translation: AAH55428.1 .
    D86331 mRNA. Translation: BAA13071.1 . Different initiation.
    D85510 mRNA. Translation: BAA22225.1 .
    CCDSi CCDS10792.1.
    PIRi I38029.
    RefSeqi NP_002419.1. NM_002428.2.
    UniGenei Hs.80343.

    3D structure databases

    ProteinModelPortali P51511.
    SMRi P51511. Positions 83-559.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110467. 1 interaction.
    IntActi P51511. 2 interactions.
    MINTi MINT-7897770.
    STRINGi 9606.ENSP00000219271.

    Chemistry

    BindingDBi P51511.
    ChEMBLi CHEMBL2963.

    Protein family/group databases

    MEROPSi M10.015.

    PTM databases

    PhosphoSitei P51511.

    Polymorphism databases

    DMDMi 1705988.

    Proteomic databases

    MaxQBi P51511.
    PaxDbi P51511.
    PRIDEi P51511.

    Protocols and materials databases

    DNASUi 4324.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000219271 ; ENSP00000219271 ; ENSG00000102996 .
    GeneIDi 4324.
    KEGGi hsa:4324.
    UCSCi uc002ena.3. human.

    Organism-specific databases

    CTDi 4324.
    GeneCardsi GC16P058060.
    HGNCi HGNC:7161. MMP15.
    HPAi CAB002611.
    HPA040390.
    MIMi 602261. gene.
    neXtProti NX_P51511.
    PharmGKBi PA30873.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG295915.
    HOGENOMi HOG000217928.
    HOVERGENi HBG052484.
    InParanoidi P51511.
    KOi K07995.
    OMAi VQMQRKG.
    OrthoDBi EOG7XPZ57.
    PhylomeDBi P51511.
    TreeFami TF352396.

    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 MMP15.
    GenomeRNAii 4324.
    NextBioi 17013.
    PROi P51511.
    SOURCEi Search...

    Gene expression databases

    Bgeei P51511.
    CleanExi HS_MMP15.
    Genevestigatori P51511.

    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.
    IPR028729. MMP15.
    IPR001818. Pept_M10_metallopeptidase.
    IPR021190. Pept_M10A.
    IPR021805. Pept_M10A_metallopeptidase_C.
    IPR016293. Pept_M10A_stromelysin-type.
    IPR021158. Pept_M10A_Zn_BS.
    IPR006026. Peptidase_Metallo.
    IPR002477. Peptidoglycan-bd-like.
    [Graphical view ]
    PANTHERi PTHR10201:SF25. PTHR10201:SF25. 1 hit.
    Pfami PF11857. DUF3377. 1 hit.
    PF00045. Hemopexin. 4 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 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. "cDNA sequence and mRNA tissue distribution of a novel human matrix metalloproteinase with a potential transmembrane segment."
      Will H., Hinzmann B.
      Eur. J. Biochem. 231:602-608(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Lung.
    2. NIEHS SNPs program
      Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS PRO-200; LEU-350; GLY-596; ARG-609 AND TRP-622.
    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].
      Tissue: Brain.
    4. "Assignment of the human genes for membrane-type-1, -2, and -3 matrix metalloproteinases (MMP14, MMP15, and MMP16) to 14q12.2, 16q12.2-q21, and 8q21, respectively, by in situ hybridization."
      Sato H., Tanaka M., Takino T., Inoue M., Seiki M.
      Genomics 39:412-413(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 94-669, VARIANT ARG-609.
    5. Shofuda K., Yasumitsu H., Nishihashi A., Miki K., Miyazaki K.
      Submitted (MAY-1996) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 163-669.
      Tissue: Placenta.
    6. "Membrane-type matrix metalloproteinases 1 and 2 exhibit broad-spectrum proteolytic capacities comparable to many matrix metalloproteinases."
      d'Ortho M.P., Will H., Atkinson S., Butler G., Messent A., Gavrilovic J., Smith B., Timpl R., Zardi L., Murphy G.
      Eur. J. Biochem. 250:751-757(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    7. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-589, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    8. Cited for: VARIANT [LARGE SCALE ANALYSIS] GLY-596.

    Entry informationi

    Entry nameiMMP15_HUMAN
    AccessioniPrimary (citable) accession number: P51511
    Secondary accession number(s): A0A2U6, Q14111
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: October 1, 1996
    Last modified: October 1, 2014
    This is version 150 of the entry and version 1 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 16
      Human chromosome 16: 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