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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)DescriptionActionsGraphical viewLength
Metal bindingi101Zinc 1; in inhibited formBy similarity1
Metal bindingi183Calcium 1; via carbonyl oxygenBy similarity1
Metal bindingi193Zinc 1By similarity1
Metal bindingi195Zinc 1By similarity1
Metal bindingi200Calcium 2By similarity1
Metal bindingi201Calcium 2; via carbonyl oxygenBy similarity1
Metal bindingi203Calcium 2; via carbonyl oxygenBy similarity1
Metal bindingi205Calcium 2; via carbonyl oxygenBy similarity1
Metal bindingi215Calcium 1; via carbonyl oxygenBy similarity1
Metal bindingi217Calcium 1; via carbonyl oxygenBy similarity1
Metal bindingi219Calcium 1By similarity1
Metal bindingi223Calcium 2By similarity1
Metal bindingi226Calcium 2By similarity1
Metal bindingi246Zinc 2; catalyticBy similarity1
Active sitei247PROSITE-ProRule annotation1
Metal bindingi250Zinc 2; catalyticBy similarity1
Metal bindingi256Zinc 2; catalyticBy similarity1

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
  • protein processing Source: MGI
  • proteolysis 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

ReactomeiR-MMU-1592389. 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
Proteomesi
  • UP000000589 Componenti: Chromosome 4

Organism-specific databases

MGIiMGI:1276107. Mmp16.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini120 – 564ExtracellularSequence analysisAdd BLAST445
Transmembranei565 – 585HelicalSequence analysisAdd BLAST21
Topological domaini586 – 607CytoplasmicSequence analysisAdd BLAST22

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 31Sequence analysisAdd BLAST31
PropeptideiPRO_000002881432 – 119By similarityAdd BLAST88
ChainiPRO_0000028815120 – 607Matrix metalloproteinase-16Add BLAST488

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi83N-linked (GlcNAc...)Sequence analysis1
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

PaxDbiQ9WTR0.
PRIDEiQ9WTR0.

PTM databases

PhosphoSitePlusiQ9WTR0.

Expressioni

Gene expression databases

BgeeiENSMUSG00000028226.
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.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati340 – 388Hemopexin 1Add BLAST49
Repeati389 – 434Hemopexin 2Add BLAST46
Repeati436 – 484Hemopexin 3Add BLAST49
Repeati485 – 532Hemopexin 4Add BLAST48

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi99 – 106Cysteine switchBy similarity8

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

eggNOGiKOG1565. Eukaryota.
ENOG410XQ5D. LUCA.
GeneTreeiENSGT00760000118870.
HOGENOMiHOG000217928.
HOVERGENiHBG052484.
InParanoidiQ9WTR0.
KOiK07996.
OMAiVPYIELE.
OrthoDBiEOG091G03DP.
TreeFamiTF352396.

Family and domain databases

CDDicd00094. HX. 1 hit.
cd04278. ZnMc_MMP. 1 hit.
Gene3Di2.110.10.10. 1 hit.
3.40.390.10. 1 hit.
InterProiIPR000585. Hemopexin-like_dom.
IPR018487. Hemopexin-like_repeat.
IPR018486. Hemopexin_CS.
IPR033739. M10A_MMP.
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. 2 hits.
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)DescriptionActionsGraphical viewLength
Sequence conflicti17R → H in BAA78420 (Ref. 1) Curated1
Sequence conflicti19G → V in AAG17704 (Ref. 2) Curated1
Sequence conflicti196S → R in AAG17704 (Ref. 2) Curated1

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_019724.4.
XP_017175506.1. XM_017320017.1.
UniGeneiMm.187315.
Mm.487950.

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_019724.4.
XP_017175506.1. XM_017320017.1.
UniGeneiMm.187315.
Mm.487950.

3D structure databases

ProteinModelPortaliQ9WTR0.
SMRiQ9WTR0.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000029881.

Protein family/group databases

MEROPSiM10.016.

PTM databases

PhosphoSitePlusiQ9WTR0.

Proteomic databases

PaxDbiQ9WTR0.
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

eggNOGiKOG1565. Eukaryota.
ENOG410XQ5D. LUCA.
GeneTreeiENSGT00760000118870.
HOGENOMiHOG000217928.
HOVERGENiHBG052484.
InParanoidiQ9WTR0.
KOiK07996.
OMAiVPYIELE.
OrthoDBiEOG091G03DP.
TreeFamiTF352396.

Enzyme and pathway databases

ReactomeiR-MMU-1592389. Activation of Matrix Metalloproteinases.

Miscellaneous databases

ChiTaRSiMmp16. mouse.
PROiQ9WTR0.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000028226.
CleanExiMM_MMP16.
ExpressionAtlasiQ9WTR0. baseline and differential.
GenevisibleiQ9WTR0. MM.

Family and domain databases

CDDicd00094. HX. 1 hit.
cd04278. ZnMc_MMP. 1 hit.
Gene3Di2.110.10.10. 1 hit.
3.40.390.10. 1 hit.
InterProiIPR000585. Hemopexin-like_dom.
IPR018487. Hemopexin-like_repeat.
IPR018486. Hemopexin_CS.
IPR033739. M10A_MMP.
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. 2 hits.
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...

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: November 30, 2016
This is version 151 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

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 one 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.