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Q9WTR0 (MMP16_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 129. 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-16

Short name=MMP-16
EC=3.4.24.-
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 names
Name:Mmp16
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length607 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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. 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 By similarity.

Cofactor

Binds 1 zinc ion per subunit By similarity.

Calcium By similarity.

Subunit structure

Interacts with CSPG4 through CSPG4 chondroitin sulfate glycosaminoglycan By similarity.

Subcellular location

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

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.

Ontologies

Keywords
   Biological processCollagen degradation
   Cellular componentCell membrane
Membrane
   DomainRepeat
Signal
Transmembrane
Transmembrane helix
   LigandCalcium
Metal-binding
Zinc
   Molecular functionHydrolase
Metalloprotease
Protease
   PTMCleavage on pair of basic residues
Disulfide bond
Glycoprotein
Zymogen
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processbone development

Inferred from genetic interaction PubMed 18022611. Source: MGI

chondrocyte proliferation

Inferred from genetic interaction PubMed 18022611. Source: MGI

collagen catabolic process

Inferred from direct assay PubMed 18022611. Source: MGI

craniofacial suture morphogenesis

Inferred from genetic interaction PubMed 18022611. Source: MGI

embryonic cranial skeleton morphogenesis

Inferred from genetic interaction PubMed 18022611. Source: MGI

endochondral ossification

Inferred from genetic interaction PubMed 18022611. Source: MGI

ossification

Inferred from genetic interaction PubMed 18022611. Source: MGI

proteolysis

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentextracellular matrix

Inferred from electronic annotation. Source: InterPro

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functioncalcium ion binding

Inferred from electronic annotation. Source: InterPro

metalloendopeptidase activity

Inferred from electronic annotation. Source: InterPro

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3131 Potential
Propeptide32 – 11988 By similarity
PRO_0000028814
Chain120 – 607488Matrix metalloproteinase-16
PRO_0000028815

Regions

Topological domain120 – 564445Extracellular Potential
Transmembrane565 – 58521Helical; Potential
Topological domain586 – 60722Cytoplasmic Potential
Repeat340 – 38849Hemopexin 1
Repeat389 – 43446Hemopexin 2
Repeat436 – 48449Hemopexin 3
Repeat485 – 53248Hemopexin 4
Motif99 – 1068Cysteine switch By similarity

Sites

Active site2471 By similarity
Metal binding1011Zinc 1; in inhibited form By similarity
Metal binding1831Calcium 1; via carbonyl oxygen By similarity
Metal binding1931Zinc 1 By similarity
Metal binding1951Zinc 1 By similarity
Metal binding2001Calcium 2 By similarity
Metal binding2011Calcium 2; via carbonyl oxygen By similarity
Metal binding2031Calcium 2; via carbonyl oxygen By similarity
Metal binding2051Calcium 2; via carbonyl oxygen By similarity
Metal binding2151Calcium 1; via carbonyl oxygen By similarity
Metal binding2171Calcium 1; via carbonyl oxygen By similarity
Metal binding2191Calcium 1 By similarity
Metal binding2231Calcium 2 By similarity
Metal binding2261Calcium 2 By similarity
Metal binding2461Zinc 2; catalytic By similarity
Metal binding2501Zinc 2; catalytic By similarity
Metal binding2561Zinc 2; catalytic By similarity

Amino acid modifications

Glycosylation831N-linked (GlcNAc...) Potential
Disulfide bond343 ↔ 532 By similarity

Experimental info

Sequence conflict171R → H in BAA78420. Ref.1
Sequence conflict191G → V in AAG17704. Ref.2
Sequence conflict1961S → R in AAG17704. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q9WTR0 [UniParc].

Last modified July 27, 2011. Version 3.
Checksum: C4CB54F75B26A296

FASTA60769,571
        10         20         30         40         50         60 
MILLAFSSGR RLDFVHRSGV FFLQTLLWIL CATVCGTEQY FNVEVWLQKY GYLPPTDPRM 

        70         80         90        100        110        120 
SVLRSAETMQ SALAAMQQFY GINMTGKVDR NTIDWMKKPR CGVPDQTRGS SKFNIRRKRY 

       130        140        150        160        170        180 
ALTGQKWQHK HITYSIKNVT PKVGDPETRR AIRRAFDVWQ NVTPLTFEEV PYSELENGKR 

       190        200        210        220        230        240 
DVDITIIFAS GFHGDSSPFD GEGGFLAHAY FPGPGIGGDT HFDSDEPWTL GNPNHDGNDL 

       250        260        270        280        290        300 
FLVAVHELGH ALGLEHSNDP TAIMAPFYQY METDNFKLPN DDLQGIQKIY GPPDKIPPPT 

       310        320        330        340        350        360 
RPLPTVPPHR SVPPADPRRH DRPKPPRPPT GRPSYPGAKP NICDGNFNTL AILRREMFVF 

       370        380        390        400        410        420 
KDQWFWRVRN NRVMDGYPMQ ITYFWRGLPP SIDAVYENSD GNFVFFKGNK YWVFKDTTLQ 

       430        440        450        460        470        480 
PGYPHDLITL GNGIPPHGID SAIWWEDVGK TYFFKGDRYW RYSEEMKTMD PGYPKPITIW 

       490        500        510        520        530        540 
KGIPESPQGA FVHKENGFTY FYKGKEYWKF NNQILKVEPG YPRSILKDFM GCDGPTDRDK 

       550        560        570        580        590        600 
EGLSPPDDVD IVIKLDNTAS TVKAIAIVIP CILALCLLVL VYTVFQFKRK GTPRHILYCK 


RSMQEWV 

« Hide

References

« Hide 'large scale' references
[1]Seiki M., Kinoh H.
Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Differential localization and Triton X-100 solubility of membrane-type matrix metalloproteinases 1-3."
Budde P., Gatsios P., Nienaber N.T., Li H., Staege M.S., Graeve L., Heinrich P.C., Frey J.
Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: C57BL/6.
Tissue: Brain.
[3]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[4]Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
Submitted (SEP-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: 129.
Tissue: Mammary tumor.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB021228 mRNA. Translation: BAA78420.1.
AF282844 mRNA. Translation: AAG17704.1.
AL683877, AL805957 Genomic DNA. Translation: CAM13981.1.
AL805957, AL683877 Genomic DNA. Translation: CAM18851.1.
CH466538 Genomic DNA. Translation: EDL05585.1.
CH466538 Genomic DNA. Translation: EDL05587.1.
BC057926 mRNA. Translation: AAH57926.1.
RefSeqNP_062698.2. NM_019724.3.
XP_006537704.1. XM_006537641.1.
UniGeneMm.187315.

3D structure databases

ProteinModelPortalQ9WTR0.
SMRQ9WTR0. Positions 42-561.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000029881.

Protein family/group databases

MEROPSM10.016.

PTM databases

PhosphoSiteQ9WTR0.

Proteomic databases

PRIDEQ9WTR0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000029881; ENSMUSP00000029881; ENSMUSG00000028226.
GeneID17389.
KEGGmmu:17389.
UCSCuc008sbw.2. mouse.

Organism-specific databases

CTD4325.
MGIMGI:1276107. Mmp16.

Phylogenomic databases

eggNOGNOG295915.
GeneTreeENSGT00750000117332.
HOGENOMHOG000217928.
HOVERGENHBG052484.
InParanoidQ6PEQ6.
KOK07996.
OMAVPPHRSV.
OrthoDBEOG7XPZ57.
TreeFamTF352396.

Gene expression databases

ArrayExpressQ9WTR0.
BgeeQ9WTR0.
CleanExMM_MMP16.
GenevestigatorQ9WTR0.

Family and domain databases

Gene3D2.110.10.10. 1 hit.
3.40.390.10. 1 hit.
InterProIPR000585. 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]
PANTHERPTHR10201. PTHR10201. 1 hit.
PTHR10201:SF26. PTHR10201:SF26. 1 hit.
PfamPF11857. DUF3377. 1 hit.
PF00045. 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.
PROSITEPS00546. CYSTEINE_SWITCH. 1 hit.
PS00024. HEMOPEXIN. 1 hit.
PS51642. HEMOPEXIN_2. 4 hits.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSMMP16. mouse.
NextBio292008.
PROQ9WTR0.
SOURCESearch...

Entry information

Entry nameMMP16_MOUSE
AccessionPrimary (citable) accession number: Q9WTR0
Secondary accession number(s): Q6PEQ6, Q9ERT6
Entry history
Integrated into UniProtKB/Swiss-Prot: January 24, 2001
Last sequence update: July 27, 2011
Last modified: April 16, 2014
This is version 129 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