Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Matrix metalloproteinase-16

Gene

Mmp16

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

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. 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).By similarity

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 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

GO - Biological processi

  • bone development Source: MGI
  • chondrocyte proliferation Source: MGI
  • collagen catabolic process Source: MGI
  • craniofacial suture morphogenesis Source: MGI
  • embryonic cranial skeleton morphogenesis Source: MGI
  • endochondral ossification Source: MGI
  • ossification Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Biological processi

Collagen degradation

Keywords - Ligandi

Calcium, Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_332323. Activation of Matrix Metalloproteinases.

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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 4

Organism-specific databases

MGIiMGI:1276107. Mmp16.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini120 – 564445ExtracellularSequence AnalysisAdd
BLAST
Transmembranei565 – 58521HelicalSequence AnalysisAdd
BLAST
Topological domaini586 – 60722CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3131Sequence AnalysisAdd
BLAST
Propeptidei32 – 11988By similarityPRO_0000028814Add
BLAST
Chaini120 – 607488Matrix metalloproteinase-16PRO_0000028815Add
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

PRIDEiQ9WTR0.

PTM databases

PhosphoSiteiQ9WTR0.

Expressioni

Gene expression databases

BgeeiQ9WTR0.
CleanExiMM_MMP16.
ExpressionAtlasiQ9WTR0. baseline and differential.
GenevisibleiQ9WTR0. MM.

Interactioni

Subunit structurei

Interacts with CSPG4 through CSPG4 chondroitin sulfate glycosaminoglycan.By similarity

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000029881.

Structurei

3D structure databases

ProteinModelPortaliQ9WTR0.
SMRiQ9WTR0. Positions 85-561.
ModBaseiSearch...
MobiDBiSearch...

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.
GeneTreeiENSGT00760000118870.
HOGENOMiHOG000217928.
HOVERGENiHBG052484.
InParanoidiQ9WTR0.
KOiK07996.
OMAiVPYIELE.
OrthoDBiEOG7XPZ57.
TreeFamiTF352396.

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]

Sequencei

Sequence statusi: Complete.

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

Q9WTR0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MILLAFSSGR RLDFVHRSGV FFLQTLLWIL CATVCGTEQY FNVEVWLQKY
60 70 80 90 100
GYLPPTDPRM SVLRSAETMQ SALAAMQQFY GINMTGKVDR NTIDWMKKPR
110 120 130 140 150
CGVPDQTRGS SKFNIRRKRY ALTGQKWQHK HITYSIKNVT PKVGDPETRR
160 170 180 190 200
AIRRAFDVWQ NVTPLTFEEV PYSELENGKR DVDITIIFAS GFHGDSSPFD
210 220 230 240 250
GEGGFLAHAY FPGPGIGGDT HFDSDEPWTL GNPNHDGNDL FLVAVHELGH
260 270 280 290 300
ALGLEHSNDP TAIMAPFYQY METDNFKLPN DDLQGIQKIY GPPDKIPPPT
310 320 330 340 350
RPLPTVPPHR SVPPADPRRH DRPKPPRPPT GRPSYPGAKP NICDGNFNTL
360 370 380 390 400
AILRREMFVF KDQWFWRVRN NRVMDGYPMQ ITYFWRGLPP SIDAVYENSD
410 420 430 440 450
GNFVFFKGNK YWVFKDTTLQ PGYPHDLITL GNGIPPHGID SAIWWEDVGK
460 470 480 490 500
TYFFKGDRYW RYSEEMKTMD PGYPKPITIW KGIPESPQGA FVHKENGFTY
510 520 530 540 550
FYKGKEYWKF NNQILKVEPG YPRSILKDFM GCDGPTDRDK EGLSPPDDVD
560 570 580 590 600
IVIKLDNTAS TVKAIAIVIP CILALCLLVL VYTVFQFKRK GTPRHILYCK

RSMQEWV
Length:607
Mass (Da):69,571
Last modified:July 27, 2011 - v3
Checksum:iC4CB54F75B26A296
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti17 – 171R → H in BAA78420 (Ref. 1) Curated
Sequence conflicti19 – 191G → V in AAG17704 (Ref. 2) Curated
Sequence conflicti196 – 1961S → R in AAG17704 (Ref. 2) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS17989.1.
RefSeqiNP_062698.2. NM_019724.3.
UniGeneiMm.187315.

Genome annotation databases

EnsembliENSMUST00000029881; ENSMUSP00000029881; ENSMUSG00000028226.
GeneIDi17389.
KEGGimmu:17389.
UCSCiuc008sbw.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS17989.1.
RefSeqiNP_062698.2. NM_019724.3.
UniGeneiMm.187315.

3D structure databases

ProteinModelPortaliQ9WTR0.
SMRiQ9WTR0. Positions 85-561.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000029881.

Protein family/group databases

MEROPSiM10.016.

PTM databases

PhosphoSiteiQ9WTR0.

Proteomic databases

PRIDEiQ9WTR0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000029881; ENSMUSP00000029881; ENSMUSG00000028226.
GeneIDi17389.
KEGGimmu:17389.
UCSCiuc008sbw.2. mouse.

Organism-specific databases

CTDi4325.
MGIiMGI:1276107. Mmp16.

Phylogenomic databases

eggNOGiNOG295915.
GeneTreeiENSGT00760000118870.
HOGENOMiHOG000217928.
HOVERGENiHBG052484.
InParanoidiQ9WTR0.
KOiK07996.
OMAiVPYIELE.
OrthoDBiEOG7XPZ57.
TreeFamiTF352396.

Enzyme and pathway databases

ReactomeiREACT_332323. Activation of Matrix Metalloproteinases.

Miscellaneous databases

ChiTaRSiMmp16. mouse.
NextBioi292008.
PROiQ9WTR0.
SOURCEiSearch...

Gene expression databases

BgeeiQ9WTR0.
CleanExiMM_MMP16.
ExpressionAtlasiQ9WTR0. baseline and differential.
GenevisibleiQ9WTR0. MM.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. 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.

Entry informationi

Entry nameiMMP16_MOUSE
AccessioniPrimary (citable) accession number: Q9WTR0
Secondary accession number(s): Q6PEQ6, Q9ERT6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 24, 2001
Last sequence update: July 27, 2011
Last modified: July 22, 2015
This is version 140 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.