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Q9R0S3 (MMP17_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 126. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Matrix metalloproteinase-17

Short name=MMP-17
EC=3.4.24.-
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 names
Name:Mmp17
Synonyms:Mt4mmp
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length578 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.3

Catalytic activity

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

Cofactor

Binds 1 zinc ion per subunit By similarity.

Calcium By similarity.

Subcellular location

Cell membrane; Lipid-anchorGPI-anchor; Extracellular side. Secretedextracellular spaceextracellular matrix Ref.6.

Tissue specificity

Expressed by monocytes and macrophages.

Domain

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.

Post-translational modification

The precursor is cleaved by a furin endopeptidase By similarity.

Sequence similarities

Belongs to the peptidase M10A family.

Contains 4 hemopexin repeats.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3939 Potential
Propeptide40 – 12485 By similarity
PRO_0000028821
Chain125 – 558434Matrix metalloproteinase-17
PRO_0000028822
Propeptide559 – 57820Removed in mature form Potential
PRO_0000028823

Regions

Repeat333 – 38250Hemopexin 1
Repeat386 – 43247Hemopexin 2
Repeat436 – 47944Hemopexin 3
Repeat480 – 52748Hemopexin 4
Motif107 – 1148Cysteine switch By similarity

Sites

Active site2481
Metal binding1091Zinc; in inhibited form By similarity
Metal binding2471Zinc; catalytic By similarity
Metal binding2511Zinc; catalytic By similarity
Metal binding2571Zinc; catalytic By similarity

Amino acid modifications

Lipidation5581GPI-anchor amidated serine Potential
Glycosylation1361N-linked (GlcNAc...) Potential
Glycosylation3221N-linked (GlcNAc...) Potential
Disulfide bond336 ↔ 527 By similarity

Experimental info

Mutagenesis2481E → A: Loss of activity. Ref.6
Sequence conflict451A → G in CAB92315. Ref.3
Sequence conflict2771L → V in BAA82708. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9R0S3 [UniParc].

Last modified July 27, 2011. Version 3.
Checksum: 168C933B63A1EB7B

FASTA57864,333
        10         20         30         40         50         60 
MGRRPRGPGS PRGPGPPRPG PGLPPLLLVL ALAAHGGCAA PAPRAEDLSL GVEWLSRFGY 

        70         80         90        100        110        120 
LPPADPASGQ LQTQEELSKA ITAMQQFGGL ETTGILDEAT LALMKTPRCS LPDLPPGAQS 

       130        140        150        160        170        180 
RRKRQTPPPT KWSKRNLSWR VRTFPRDSPL GRDTVRALMY YALKVWSDIT PLNFHEVAGN 

       190        200        210        220        230        240 
AADIQIDFSK ADHNDGYPFD GPGGTVAHAF FPGDHHTAGD THFDDDEPWT FRSSDAHGMD 

       250        260        270        280        290        300 
LFAVAVHEFG HAIGLSHVAA PSSIMQPYYQ GPVGDPLRYG LPYEDRVRVW QLYGVRESVS 

       310        320        330        340        350        360 
PTAQLDTPEP EEPPLLPEPP NNRSSTPPQK DVPHRCTAHF DAVAQIRGEA FFFKGKYFWR 

       370        380        390        400        410        420 
LTRDRHLVSL QPAQMHRFWR GLPLHLDSVD AVYERTSDHK IVFFKGDRYW VFKDNNVEEG 

       430        440        450        460        470        480 
YPRPVSDFSL PPGGIDAVFS WAHNDRTYFF KDQLYWRYDD HTRRMDPGYP AQGPLWRGVP 

       490        500        510        520        530        540 
SMLDDAMRWS DGASYFFRGQ EYWKVLDGEL EAAPGYPQST ARDWLVCGEP LADAEDVGPG 

       550        560        570 
PQGRSGAQDG LAVCSCTSDA HRLALPSLLL LTPLLWGL 

« Hide

References

« Hide 'large scale' references
[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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB021224 mRNA. Translation: BAA82708.2.
AJ010731 mRNA. Translation: CAB92315.1.
CH466529 Genomic DNA. Translation: EDL19513.1.
BC051917 mRNA. Translation: AAH51917.1.
RefSeqNP_035976.3. NM_011846.4.
UniGeneMm.42047.

3D structure databases

ProteinModelPortalQ9R0S3.
SMRQ9R0S3. Positions 45-559.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000031390.

Protein family/group databases

MEROPSM10.017.

PTM databases

PhosphoSiteQ9R0S3.

2D gel databases

REPRODUCTION-2DPAGEQ9R0S3.

Proteomic databases

PaxDbQ9R0S3.
PRIDEQ9R0S3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000031390; ENSMUSP00000031390; ENSMUSG00000029436.
GeneID23948.
KEGGmmu:23948.
UCSCuc008zsy.1. mouse.

Organism-specific databases

CTD4326.
MGIMGI:1346076. Mmp17.

Phylogenomic databases

eggNOGNOG295915.
GeneTreeENSGT00750000117336.
HOGENOMHOG000217928.
HOVERGENHBG052484.
InParanoidQ80UM9.
KOK07997.
OMAAHNDRTY.
OrthoDBEOG7XPZ57.
TreeFamTF315428.

Gene expression databases

BgeeQ9R0S3.
CleanExMM_MMP17.
GenevestigatorQ9R0S3.

Family and domain databases

Gene3D2.110.10.10. 1 hit.
3.40.390.10. 1 hit.
InterProIPR000585. 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]
PANTHERPTHR10201. PTHR10201. 1 hit.
PTHR10201:SF21. PTHR10201:SF21. 1 hit.
PfamPF00045. Hemopexin. 4 hits.
PF00413. Peptidase_M10. 1 hit.
PF01471. PG_binding_1. 1 hit.
[Graphical view]
PIRSFPIRSF001191. Peptidase_M10A_matrix. 1 hit.
PRINTSPR00138. MATRIXIN.
SMARTSM00120. HX. 4 hits.
SM00235. ZnMc. 1 hit.
[Graphical view]
SUPFAMSSF47090. SSF47090. 1 hit.
SSF50923. SSF50923. 1 hit.
PROSITEPS51642. HEMOPEXIN_2. 4 hits.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio303765.
PROQ9R0S3.
SOURCESearch...

Entry information

Entry nameMMP17_MOUSE
AccessionPrimary (citable) accession number: Q9R0S3
Secondary accession number(s): Q80UM9
Entry history
Integrated into UniProtKB/Swiss-Prot: January 24, 2001
Last sequence update: July 27, 2011
Last modified: April 16, 2014
This is version 126 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot