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Protein

Matrix metalloproteinase-17

Gene

Mmp17

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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.1 Publication

Catalytic activityi

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

Cofactori

Protein has several cofactor binding sites:
  • Zn2+By similarityNote: Binds 1 zinc ion per subunit.By similarity
  • Ca2+By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi109 – 1091Zinc; in inhibited formBy similarity
Metal bindingi247 – 2471Zinc; catalyticPROSITE-ProRule annotation
Active sitei248 – 2481
Metal bindingi251 – 2511Zinc; catalyticPROSITE-ProRule annotation
Metal bindingi257 – 2571Zinc; catalyticPROSITE-ProRule annotation

GO - Molecular functioni

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

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Calcium, Metal-binding, Zinc

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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 5

Organism-specific databases

MGIiMGI:1346076. Mmp17.

Subcellular locationi

GO - Cellular componenti

  1. anchored component of membrane Source: UniProtKB-KW
  2. plasma membrane Source: UniProtKB-SubCell
  3. proteinaceous extracellular matrix Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Extracellular matrix, Membrane, Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi248 – 2481E → A: Loss of activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3939Sequence AnalysisAdd
BLAST
Propeptidei40 – 12485By similarityPRO_0000028821Add
BLAST
Chaini125 – 558434Matrix metalloproteinase-17PRO_0000028822Add
BLAST
Propeptidei559 – 57820Removed in mature formSequence AnalysisPRO_0000028823Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi136 – 1361N-linked (GlcNAc...)Sequence Analysis
Glycosylationi322 – 3221N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi336 ↔ 527By similarity
Lipidationi558 – 5581GPI-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

PaxDbiQ9R0S3.
PRIDEiQ9R0S3.

2D gel databases

REPRODUCTION-2DPAGEQ9R0S3.

PTM databases

PhosphoSiteiQ9R0S3.

Expressioni

Tissue specificityi

Expressed by monocytes and macrophages.

Gene expression databases

BgeeiQ9R0S3.
CleanExiMM_MMP17.
GenevestigatoriQ9R0S3.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000031390.

Structurei

3D structure databases

ProteinModelPortaliQ9R0S3.
SMRiQ9R0S3. Positions 47-559.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati333 – 38250Hemopexin 1Add
BLAST
Repeati386 – 43247Hemopexin 2Add
BLAST
Repeati436 – 47944Hemopexin 3Add
BLAST
Repeati480 – 52748Hemopexin 4Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi107 – 1148Cysteine 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

eggNOGiNOG295915.
GeneTreeiENSGT00760000118870.
HOGENOMiHOG000217928.
HOVERGENiHBG052484.
InParanoidiQ9R0S3.
KOiK07997.
OMAiAHNDRTY.
OrthoDBiEOG7XPZ57.
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]

Sequencei

Sequence statusi: Complete.

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

Q9R0S3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGRRPRGPGS PRGPGPPRPG PGLPPLLLVL ALAAHGGCAA PAPRAEDLSL
60 70 80 90 100
GVEWLSRFGY LPPADPASGQ LQTQEELSKA ITAMQQFGGL ETTGILDEAT
110 120 130 140 150
LALMKTPRCS LPDLPPGAQS RRKRQTPPPT KWSKRNLSWR VRTFPRDSPL
160 170 180 190 200
GRDTVRALMY YALKVWSDIT PLNFHEVAGN AADIQIDFSK ADHNDGYPFD
210 220 230 240 250
GPGGTVAHAF FPGDHHTAGD THFDDDEPWT FRSSDAHGMD LFAVAVHEFG
260 270 280 290 300
HAIGLSHVAA PSSIMQPYYQ GPVGDPLRYG LPYEDRVRVW QLYGVRESVS
310 320 330 340 350
PTAQLDTPEP EEPPLLPEPP NNRSSTPPQK DVPHRCTAHF DAVAQIRGEA
360 370 380 390 400
FFFKGKYFWR LTRDRHLVSL QPAQMHRFWR GLPLHLDSVD AVYERTSDHK
410 420 430 440 450
IVFFKGDRYW VFKDNNVEEG YPRPVSDFSL PPGGIDAVFS WAHNDRTYFF
460 470 480 490 500
KDQLYWRYDD HTRRMDPGYP AQGPLWRGVP SMLDDAMRWS DGASYFFRGQ
510 520 530 540 550
EYWKVLDGEL EAAPGYPQST ARDWLVCGEP LADAEDVGPG PQGRSGAQDG
560 570
LAVCSCTSDA HRLALPSLLL LTPLLWGL
Length:578
Mass (Da):64,333
Last modified:July 27, 2011 - v3
Checksum:i168C933B63A1EB7B
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti45 – 451A → G in CAB92315 (PubMed:10799478).Curated
Sequence conflicti277 – 2771L → V in BAA82708 (PubMed:10471807).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB021224 mRNA. Translation: BAA82708.2.
AJ010731 mRNA. Translation: CAB92315.1.
CH466529 Genomic DNA. Translation: EDL19513.1.
BC051917 mRNA. Translation: AAH51917.1.
CCDSiCCDS19695.1.
RefSeqiNP_035976.3. NM_011846.4.
UniGeneiMm.42047.

Genome annotation databases

EnsembliENSMUST00000031390; ENSMUSP00000031390; ENSMUSG00000029436.
GeneIDi23948.
KEGGimmu:23948.
UCSCiuc008zsy.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB021224 mRNA. Translation: BAA82708.2.
AJ010731 mRNA. Translation: CAB92315.1.
CH466529 Genomic DNA. Translation: EDL19513.1.
BC051917 mRNA. Translation: AAH51917.1.
CCDSiCCDS19695.1.
RefSeqiNP_035976.3. NM_011846.4.
UniGeneiMm.42047.

3D structure databases

ProteinModelPortaliQ9R0S3.
SMRiQ9R0S3. Positions 47-559.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000031390.

Protein family/group databases

MEROPSiM10.017.

PTM databases

PhosphoSiteiQ9R0S3.

2D gel databases

REPRODUCTION-2DPAGEQ9R0S3.

Proteomic databases

PaxDbiQ9R0S3.
PRIDEiQ9R0S3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000031390; ENSMUSP00000031390; ENSMUSG00000029436.
GeneIDi23948.
KEGGimmu:23948.
UCSCiuc008zsy.1. mouse.

Organism-specific databases

CTDi4326.
MGIiMGI:1346076. Mmp17.

Phylogenomic databases

eggNOGiNOG295915.
GeneTreeiENSGT00760000118870.
HOGENOMiHOG000217928.
HOVERGENiHBG052484.
InParanoidiQ9R0S3.
KOiK07997.
OMAiAHNDRTY.
OrthoDBiEOG7XPZ57.
TreeFamiTF315428.

Miscellaneous databases

NextBioi303765.
PROiQ9R0S3.
SOURCEiSearch...

Gene expression databases

BgeeiQ9R0S3.
CleanExiMM_MMP17.
GenevestigatoriQ9R0S3.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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].
    Tissue: Embryonic brain.
  2. Seiki M.
    Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION TO C-TERMINUS.
  3. "Membrane type 4 matrix metalloproteinase (MMP17) has tumor necrosis factor-alpha convertase activity but does not activate pro-MMP2."
    English W.R., Puente X.S., Freije J.M.P., Knaeuper V., Amour A., Merryweather A., Lopez-Otin C., Murphy G.
    J. Biol. Chem. 275:14046-14055(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
    Tissue: Brain.
  4. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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].
    Strain: C57BL/6.
    Tissue: Embryonic brain.
  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, MUTAGENESIS OF GLU-248.

Entry informationi

Entry nameiMMP17_MOUSE
AccessioniPrimary (citable) accession number: Q9R0S3
Secondary accession number(s): Q80UM9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 24, 2001
Last sequence update: July 27, 2011
Last modified: January 7, 2015
This is version 133 of the entry and version 3 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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.