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O35548

- MMP16_RAT

UniProt

O35548 - MMP16_RAT

Protein

Matrix metalloproteinase-16

Gene

Mmp16

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 130 (01 Oct 2014)
      Sequence version 1 (01 Jan 1998)
      Previous versions | rss
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    Functioni

    Endopeptidase that degrades various components of the extracellular matrix, such as collagen type III and fibronectin. Activates progelatinase A. Involved in the matrix remodeling of blood vessels. The short isoform efficiently converts progelatinase A to the intermediate form but not to the mature one. It has no effect on type I, II, IV and V collagen. However, upon interaction with CSPG4, it may be involved in degradation and invasion of type I collagen by melanoma cells.

    Cofactori

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi101 – 1011Zinc 1; in inhibited formBy similarity
    Metal bindingi183 – 1831Calcium 1; via carbonyl oxygenBy similarity
    Metal bindingi193 – 1931Zinc 1By similarity
    Metal bindingi195 – 1951Zinc 1By similarity
    Metal bindingi200 – 2001Calcium 2By similarity
    Metal bindingi201 – 2011Calcium 2; via carbonyl oxygenBy similarity
    Metal bindingi203 – 2031Calcium 2; via carbonyl oxygenBy similarity
    Metal bindingi205 – 2051Calcium 2; via carbonyl oxygenBy similarity
    Metal bindingi215 – 2151Calcium 1; via carbonyl oxygenBy similarity
    Metal bindingi217 – 2171Calcium 1; via carbonyl oxygenBy similarity
    Metal bindingi219 – 2191Calcium 1By similarity
    Metal bindingi223 – 2231Calcium 2By similarity
    Metal bindingi226 – 2261Calcium 2By similarity
    Metal bindingi246 – 2461Zinc 2; catalyticBy similarity
    Active sitei247 – 2471PROSITE-ProRule annotation
    Metal bindingi250 – 2501Zinc 2; catalyticBy similarity
    Metal bindingi256 – 2561Zinc 2; catalyticBy similarity

    GO - Molecular functioni

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

    GO - Biological processi

    1. collagen catabolic process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Hydrolase, Metalloprotease, Protease

    Keywords - Biological processi

    Collagen degradation

    Keywords - Ligandi

    Calcium, Metal-binding, Zinc

    Protein family/group databases

    MEROPSiM10.016.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Matrix metalloproteinase-16 (EC:3.4.24.-)
    Short name:
    MMP-16
    Alternative name(s):
    Membrane-type matrix metalloproteinase 3
    Short name:
    MT-MMP 3
    Short name:
    MTMMP3
    Membrane-type-3 matrix metalloproteinase
    Short name:
    MT3-MMP
    Short name:
    MT3MMP
    Gene namesi
    Name:Mmp16
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Unplaced

    Organism-specific databases

    RGDi620199. Mmp16.

    Subcellular locationi

    Cell membrane Curated; Single-pass type I membrane protein Curated; Extracellular side Curated
    Note: Localized at the cell surface of melanoma cells.By similarity

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Cell membrane, Extracellular matrix, Membrane, Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 3131Sequence AnalysisAdd
    BLAST
    Propeptidei32 – 11988By similarityPRO_0000028816Add
    BLAST
    Chaini120 – 607488Matrix metalloproteinase-16PRO_0000028817Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi83 – 831N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi343 ↔ 532By similarity

    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

    PaxDbiO35548.
    PRIDEiO35548.

    PTM databases

    PhosphoSiteiO35548.

    Expressioni

    Tissue specificityi

    Strongly expressed in the lung, brain and smooth muscle cells. Weakly detectable in the spleen and liver and indetectable in the heart, skeletal muscle and kidney.

    Gene expression databases

    GenevestigatoriO35548.

    Interactioni

    Subunit structurei

    Interacts with CSPG4 through CSPG4 chondroitin sulfate glycosaminoglycan.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliO35548.
    SMRiO35548. Positions 124-292.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini120 – 564445ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini586 – 60722CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei565 – 58521HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati340 – 38849Hemopexin 1Add
    BLAST
    Repeati389 – 43446Hemopexin 2Add
    BLAST
    Repeati436 – 48449Hemopexin 3Add
    BLAST
    Repeati485 – 53248Hemopexin 4Add
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi99 – 1068Cysteine 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, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG295915.
    HOGENOMiHOG000217928.
    HOVERGENiHBG052484.
    KOiK07996.
    PhylomeDBiO35548.

    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.
    IPR028697. MMP16.
    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:SF26. PTHR10201:SF26. 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]

    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: O35548-1) [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

    MILLAFSSGR RLDFVHRSGV FFFQTLLWIL CATVCGTEQY FNVEVWLQKY    50
    GYLPPTDPRM SVLRSAETMQ SALAAMQQFY GINMTGKVDR NTIDWMKKPR 100
    CGVPDQTRGS SKFNIRRKRY ALTGQKWQHK HITYSIKNVT PKVGDPETRR 150
    AIRRAFDVWQ NVTPLTFEEV PYSELENGKR DVDITIIFAS GFHGDRSPFD 200
    GEGGFLAHAY FPGPGIGGDT HFDSDEPWTL GNPNHDGNDL FLVAVHELGH 250
    ALGLEHSNDP TAIMAPFYQY METDNFKLPN DDLQGIQKIY GPPDKIPPPT 300
    RPLPTVPPHR SVPPADPRKN DRPKPPRPPT GRPSYPGAKP NICDGNFNTL 350
    AILRREMFVF KDQWFWRVRN NRVMDGYPMQ ITYFWRGLPP SIDAVYENSD 400
    GNFVFFKGNK YWVFKDTTLQ PGYPHDLITL GNGIPPHGID SAIWWEDVGK 450
    TYFFKGDRYW RYSEEMKTMD PGYPKPITIW KGIPESPQGA FVHKENGFTY 500
    FYKGKEYWKF NNQILKVEPG YPRSILKDFM GCDGPTDRDK EGLSPPDDVD 550
    IVIKLDNTAS TVKAIAIVIP CILALCLLVL VYTVFQFKRK GTPRHILYCK 600
    RSMQEWV 607
    Length:607
    Mass (Da):69,624
    Last modified:January 1, 1998 - v1
    Checksum:i86BBCF8063441653
    GO
    Isoform Short (identifier: O35548-2) [UniParc]FASTAAdd to Basket

    Also known as: MT3-MMP-del

    The sequence of this isoform differs from the canonical sequence as follows:
         547-607: DDVDIVIKLDNTASTVKAIAIVIPCILALCLLVLVYTVFQFKRKGTPRHILYCKRSMQEWV → P

    Show »
    Length:547
    Mass (Da):62,775
    Checksum:i61CE63C123C3B9A5
    GO

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei547 – 60761DDVDI…MQEWV → P in isoform Short. CuratedVSP_005455Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D85509 mRNA. Translation: BAA22224.1.
    D63886 mRNA. Translation: BAA22223.1.
    RefSeqiNP_542954.1. NM_080776.1. [O35548-2]
    UniGeneiRn.208361.

    Genome annotation databases

    GeneIDi65205.
    KEGGirno:65205.
    UCSCiRGD:620199. rat. [O35548-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D85509 mRNA. Translation: BAA22224.1 .
    D63886 mRNA. Translation: BAA22223.1 .
    RefSeqi NP_542954.1. NM_080776.1. [O35548-2 ]
    UniGenei Rn.208361.

    3D structure databases

    ProteinModelPortali O35548.
    SMRi O35548. Positions 124-292.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    MEROPSi M10.016.

    PTM databases

    PhosphoSitei O35548.

    Proteomic databases

    PaxDbi O35548.
    PRIDEi O35548.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 65205.
    KEGGi rno:65205.
    UCSCi RGD:620199. rat. [O35548-1 ]

    Organism-specific databases

    CTDi 4325.
    RGDi 620199. Mmp16.

    Phylogenomic databases

    eggNOGi NOG295915.
    HOGENOMi HOG000217928.
    HOVERGENi HBG052484.
    KOi K07996.
    PhylomeDBi O35548.

    Miscellaneous databases

    NextBioi 614169.
    PROi O35548.

    Gene expression databases

    Genevestigatori O35548.

    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.
    IPR028697. MMP16.
    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:SF26. PTHR10201:SF26. 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. "Expression of three membrane-type matrix metalloproteinases (MT-MMPs) in rat vascular smooth muscle cells and characterization of MT3-MMPs with and without transmembrane domain."
      Shofuda K., Yasumitsu H., Nishihashi A., Miki K., Miyazaki K.
      J. Biol. Chem. 272:9749-9754(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], ALTERNATIVE SPLICING.
      Tissue: Smooth muscle.

    Entry informationi

    Entry nameiMMP16_RAT
    AccessioniPrimary (citable) accession number: O35548
    Secondary accession number(s): O35541
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1998
    Last sequence update: January 1, 1998
    Last modified: October 1, 2014
    This is version 130 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Peptidase families
      Classification of peptidase families and list of entries
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3