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Q9ULZ9

- MMP17_HUMAN

UniProt

Q9ULZ9 - MMP17_HUMAN

Protein

Matrix metalloproteinase-17

Gene

MMP17

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 143 (01 Oct 2014)
      Sequence version 4 (18 May 2010)
      Previous versions | rss
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    Functioni

    Endopeptidase that degrades various components of the extracellular matrix, such as fibrin. May be involved in the activation of membrane-bound precursors of growth factors or inflammatory mediators, such as tumor necrosis factor-alpha. May also be involved in tumoral process. Not obvious if able to proteolytically activate progelatinase A. Does not hydrolyze collagen types I, II, III, IV and V, gelatin, fibronectin, laminin, decorin nor alpha1-antitrypsin.

    Catalytic activityi

    Cleaves pro-TNF-alpha at the 74-Ala-|-Gln-75 site.

    Cofactori

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi110 – 1101Zinc; in inhibited formBy similarity
    Metal bindingi248 – 2481Zinc; catalyticPROSITE-ProRule annotation
    Active sitei249 – 2491PROSITE-ProRule annotation
    Metal bindingi252 – 2521Zinc; catalyticPROSITE-ProRule annotation
    Metal bindingi258 – 2581Zinc; catalyticPROSITE-ProRule annotation

    GO - Molecular functioni

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

    GO - Biological processi

    1. positive regulation of catalytic activity Source: GOC

    Keywords - Molecular functioni

    Hydrolase, Metalloprotease, Protease

    Keywords - Ligandi

    Calcium, Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_118682. Activation of Matrix Metalloproteinases.

    Protein family/group databases

    MEROPSiM10.017.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Matrix metalloproteinase-17 (EC:3.4.24.-)
    Short name:
    MMP-17
    Alternative name(s):
    Membrane-type matrix metalloproteinase 4
    Short name:
    MT-MMP 4
    Short name:
    MTMMP4
    Membrane-type-4 matrix metalloproteinase
    Short name:
    MT4-MMP
    Short name:
    MT4MMP
    Gene namesi
    Name:MMP17
    Synonyms:MT4MMP
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:7163. MMP17.

    Subcellular locationi

    GO - Cellular componenti

    1. anchored component of membrane Source: UniProtKB-KW
    2. integral component of plasma membrane Source: ProtInc
    3. proteinaceous extracellular matrix Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell membrane, Extracellular matrix, Membrane, Secreted

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA30875.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 3535Sequence AnalysisAdd
    BLAST
    Propeptidei36 – 12590By similarityPRO_0000028818Add
    BLAST
    Chaini126 – 565440Matrix metalloproteinase-17PRO_0000028819Add
    BLAST
    Propeptidei566 – 60338Removed in mature formSequence AnalysisPRO_0000028820Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi137 – 1371N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi318 – 3181N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi332 ↔ 523By similarity
    Lipidationi565 – 5651GPI-anchor amidated serineSequence 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, GPI-anchor, Lipoprotein, Zymogen

    Proteomic databases

    PaxDbiQ9ULZ9.
    PRIDEiQ9ULZ9.

    PTM databases

    PhosphoSiteiQ9ULZ9.

    Expressioni

    Tissue specificityi

    Expressed in brain, leukocytes, colon, ovary testis and breast cancer. Expressed also in many transformed and non-transformed cell types.

    Gene expression databases

    ArrayExpressiQ9ULZ9.
    BgeeiQ9ULZ9.
    CleanExiHS_MMP17.
    GenevestigatoriQ9ULZ9.

    Interactioni

    Protein-protein interaction databases

    BioGridi110469. 1 interaction.
    STRINGi9606.ENSP00000353767.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9ULZ9.
    SMRiQ9ULZ9. Positions 39-523.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati333 – 37846Hemopexin 1Add
    BLAST
    Repeati382 – 42746Hemopexin 2Add
    BLAST
    Repeati428 – 47548Hemopexin 3Add
    BLAST
    Repeati476 – 52348Hemopexin 4Add
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi108 – 1158Cysteine switchBy similarity

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi122 – 1254Poly-Arg

    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

    eggNOGiNOG295915.
    HOVERGENiHBG052484.
    InParanoidiQ9ULZ9.
    KOiK07997.
    OMAiAHNDRTY.
    OrthoDBiEOG7XPZ57.
    PhylomeDBiQ9ULZ9.
    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.
    IPR024079. MetalloPept_cat_dom.
    IPR028726. MMP17.
    IPR001818. Pept_M10_metallopeptidase.
    IPR021190. Pept_M10A.
    IPR016293. Pept_M10A_stromelysin-type.
    IPR006026. Peptidase_Metallo.
    IPR002477. Peptidoglycan-bd-like.
    [Graphical view]
    PANTHERiPTHR10201:SF118. PTHR10201:SF118. 1 hit.
    PfamiPF00045. 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.
    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 Long (identifier: Q9ULZ9-1) [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

    MRRRAARGPG PPPPGPGLSR LPLPLLLLLA LGTRGGCAAP APAPRAEDLS    50
    LGVEWLSRFG YLPPADPTTG QLQTQEELSK AITAMQQFGG LEATGILDEA 100
    TLALMKTPRC SLPDLPVLTQ ARRRRQAPAP TKWNKRNLSW RVRTFPRDSP 150
    LGHDTVRALM YYALKVWSDI APLNFHEVAG SAADIQIDFS KADHNDGYPF 200
    DGPGGTVAHA FFPGHHHTAG DTHFDDDEAW TFRSSDAHGM DLFAVAVHEF 250
    GHAIGLSHVA AAHSIMRPYY QGPVGDPLRY GLPYEDKVRV WQLYGVRESV 300
    SPTAQPEEPP LLPEPPDNRS SAPPRKDVPH RCSTHFDAVA QIRGEAFFFK 350
    GKYFWRLTRD RHLVSLQPAQ MHRFWRGLPL HLDSVDAVYE RTSDHKIVFF 400
    KGDRYWVFKD NNVEEGYPRP VSDFSLPPGG IDAAFSWAHN DRTYFFKDQL 450
    YWRYDDHTRH MDPGYPAQSP LWRGVPSTLD DAMRWSDGAS YFFRGQEYWK 500
    VLDGELEVAP GYPQSTARDW LVCGDSQADG SVAAGVDAAE GPRAPPGQHD 550
    QSRSEDGYEV CSCTSGASSP PGAPGPLVAA TMLLLLPPLS PGALWTAAQA 600
    LTL 603
    Length:603
    Mass (Da):66,653
    Last modified:May 18, 2010 - v4
    Checksum:iBB297B21973C7A0B
    GO
    Isoform Short (identifier: Q9ULZ9-2) [UniParc]FASTAAdd to Basket

    Also known as: Puente

    The sequence of this isoform differs from the canonical sequence as follows:
         1-84: Missing.

    Show »
    Length:519
    Mass (Da):57,938
    Checksum:iEB74B32E8A7619C3
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti23 – 231L → LLPL in BAA82707. (PubMed:10471807)Curated
    Sequence conflicti23 – 231L → LLPL in CAA61753. 1 PublicationCurated
    Sequence conflicti182 – 1821A → T in BAA82707. (PubMed:10471807)Curated
    Sequence conflicti182 – 1821A → T in CAA61753. 1 PublicationCurated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 8484Missing in isoform Short. 1 PublicationVSP_005456Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB021225 mRNA. Translation: BAA82707.2.
    X89576 mRNA. Translation: CAA61753.1.
    AC131009 Genomic DNA. No translation available.
    CCDSiCCDS31927.1. [Q9ULZ9-1]
    RefSeqiNP_057239.4. NM_016155.4. [Q9ULZ9-1]
    UniGeneiHs.709245.

    Genome annotation databases

    EnsembliENST00000360564; ENSP00000353767; ENSG00000198598. [Q9ULZ9-1]
    ENST00000535291; ENSP00000441106; ENSG00000198598. [Q9ULZ9-2]
    GeneIDi4326.
    KEGGihsa:4326.
    UCSCiuc001ujc.1. human. [Q9ULZ9-1]

    Polymorphism databases

    DMDMi296439485.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB021225 mRNA. Translation: BAA82707.2 .
    X89576 mRNA. Translation: CAA61753.1 .
    AC131009 Genomic DNA. No translation available.
    CCDSi CCDS31927.1. [Q9ULZ9-1 ]
    RefSeqi NP_057239.4. NM_016155.4. [Q9ULZ9-1 ]
    UniGenei Hs.709245.

    3D structure databases

    ProteinModelPortali Q9ULZ9.
    SMRi Q9ULZ9. Positions 39-523.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110469. 1 interaction.
    STRINGi 9606.ENSP00000353767.

    Chemistry

    ChEMBLi CHEMBL2937.

    Protein family/group databases

    MEROPSi M10.017.

    PTM databases

    PhosphoSitei Q9ULZ9.

    Polymorphism databases

    DMDMi 296439485.

    Proteomic databases

    PaxDbi Q9ULZ9.
    PRIDEi Q9ULZ9.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000360564 ; ENSP00000353767 ; ENSG00000198598 . [Q9ULZ9-1 ]
    ENST00000535291 ; ENSP00000441106 ; ENSG00000198598 . [Q9ULZ9-2 ]
    GeneIDi 4326.
    KEGGi hsa:4326.
    UCSCi uc001ujc.1. human. [Q9ULZ9-1 ]

    Organism-specific databases

    CTDi 4326.
    GeneCardsi GC12P132312.
    H-InvDB HIX0036662.
    HGNCi HGNC:7163. MMP17.
    MIMi 602285. gene.
    neXtProti NX_Q9ULZ9.
    PharmGKBi PA30875.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG295915.
    HOVERGENi HBG052484.
    InParanoidi Q9ULZ9.
    KOi K07997.
    OMAi AHNDRTY.
    OrthoDBi EOG7XPZ57.
    PhylomeDBi Q9ULZ9.
    TreeFami TF315428.

    Enzyme and pathway databases

    Reactomei REACT_118682. Activation of Matrix Metalloproteinases.

    Miscellaneous databases

    GeneWikii MMP17.
    GenomeRNAii 4326.
    NextBioi 17023.
    PROi Q9ULZ9.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9ULZ9.
    Bgeei Q9ULZ9.
    CleanExi HS_MMP17.
    Genevestigatori Q9ULZ9.

    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.
    IPR024079. MetalloPept_cat_dom.
    IPR028726. MMP17.
    IPR001818. Pept_M10_metallopeptidase.
    IPR021190. Pept_M10A.
    IPR016293. Pept_M10A_stromelysin-type.
    IPR006026. Peptidase_Metallo.
    IPR002477. Peptidoglycan-bd-like.
    [Graphical view ]
    PANTHERi PTHR10201:SF118. PTHR10201:SF118. 1 hit.
    Pfami 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 PS51642. HEMOPEXIN_2. 4 hits.
    PS00142. ZINC_PROTEASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Human membrane type-4 matrix metalloproteinase (MT4-MMP) is encoded by a novel major transcript: isolation of complementary DNA clones for human and mouse mt4-mmp transcripts."
      Kajita M., Kinoh H., Ito N., Takamura A., Itoh Y., Okada A., Sato H., Seiki M.
      FEBS Lett. 457:353-356(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
      Tissue: Monocytic leukemia.
    2. Seiki M.
      Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION TO 41; 44; 202-207; 221 AND 225.
    3. "Molecular cloning of a novel membrane-type matrix metalloproteinase from a human breast carcinoma."
      Puente X.S., Pendas A.M., Llano E., Velasco G., Lopez-Otin C.
      Cancer Res. 56:944-949(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT).
      Tissue: Mammary carcinoma.
    4. "The finished DNA sequence of human chromosome 12."
      Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
      , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
      Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "Catalytic activities and substrate specificity of the human membrane type 4 matrix metalloproteinase catalytic domain."
      Wang Y., Johnson A.R., Ye Q.-Z., Dyer R.D.
      J. Biol. Chem. 274:33043-33049(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 126-299, CHARACTERIZATION.
    6. "Membrane type 4 matrix metalloproteinase (MT4-MMP, MMP-17) is a glycosylphosphatidylinositol-anchored proteinase."
      Itoh Y., Kajita M., Kinoh H., Mori H., Okada A., Seiki M.
      J. Biol. Chem. 274:34260-34266(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: GPI-ANCHOR.
    7. "Biochemical characterization of the catalytic domain of membrane-type 4 matrix metalloproteinase."
      Kolkenbrock H., Essers L., Ulbrich N., Will H.
      Biol. Chem. 380:1103-1108(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION.

    Entry informationi

    Entry nameiMMP17_HUMAN
    AccessioniPrimary (citable) accession number: Q9ULZ9
    Secondary accession number(s): Q14850
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 24, 2001
    Last sequence update: May 18, 2010
    Last modified: October 1, 2014
    This is version 143 of the entry and version 4 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 12
      Human chromosome 12: 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