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Protein

Matrix metalloproteinase-14

Gene

Mmp14

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. Activates progelatinase A. Essential for pericellular collagenolysis and modeling of skeletal and extraskeletal connective tissues during development. May be involved in actin cytoskeleton reorganization by cleaving PTK7 (By similarity). Acts as a positive regulator of cell growth and migration via activation of MMP15. Involved in the formation of the fibrovascular tissues (By similarity).By similarity1 Publication

Catalytic activityi

Endopeptidase activity. Activates progelatinase A by cleavage of the propeptide at 37-Asn-|-Leu-38. Other bonds hydrolyzed include 35-Gly-|-Ile-36 in the propeptide of collagenase 3, and 341-Asn-|-Phe-342, 441-Asp-|-Leu-442 and 354-Gln-|-Thr-355 in the aggrecan interglobular domain.

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 bindingi93Zinc; in inhibited formBy similarity1
Metal bindingi239Zinc; catalyticPROSITE-ProRule annotation1
Active sitei240PROSITE-ProRule annotation1
Metal bindingi243Zinc; catalyticPROSITE-ProRule annotation1
Metal bindingi249Zinc; catalyticPROSITE-ProRule annotation1

GO - Molecular functioni

GO - Biological processi

  • angiogenesis Source: Ensembl
  • astrocyte cell migration Source: Ensembl
  • bone development Source: MGI
  • branching morphogenesis of an epithelial tube Source: MGI
  • cell migration 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
  • endodermal cell differentiation Source: Ensembl
  • endothelial cell proliferation Source: Ensembl
  • lung development Source: MGI
  • male gonad development Source: Ensembl
  • negative regulation of focal adhesion assembly Source: Ensembl
  • negative regulation of Notch signaling pathway Source: UniProtKB
  • ossification Source: MGI
  • ovarian follicle development Source: Ensembl
  • positive regulation of B cell differentiation Source: UniProtKB
  • positive regulation of cell growth Source: MGI
  • positive regulation of cell migration Source: MGI
  • positive regulation of myotube differentiation Source: UniProtKB
  • proteolysis Source: MGI
  • response to estrogen Source: Ensembl
  • response to hormone Source: Ensembl
  • response to hypoxia Source: Ensembl
  • response to mechanical stimulus Source: Ensembl
  • response to organic cyclic compound Source: Ensembl
  • response to oxidative stress Source: Ensembl
  • tissue remodeling Source: Ensembl
  • zymogen activation 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-1442490. Collagen degradation.
R-MMU-1474228. Degradation of the extracellular matrix.
R-MMU-1592389. Activation of Matrix Metalloproteinases.

Protein family/group databases

MEROPSiM10.014.

Names & Taxonomyi

Protein namesi
Recommended name:
Matrix metalloproteinase-14 (EC:3.4.24.80)
Short name:
MMP-14
Alternative name(s):
MMP-X1
MT-MMP
Membrane-type matrix metalloproteinase 1
Short name:
MT-MMP 1
Short name:
MTMMP1
Membrane-type-1 matrix metalloproteinase
Short name:
MT1-MMP
Short name:
MT1MMP
Gene namesi
Name:Mmp14
Synonyms:Mtmmp
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 14

Organism-specific databases

MGIiMGI:101900. Mmp14.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini112 – 541ExtracellularSequence analysisAdd BLAST430
Transmembranei542 – 562HelicalSequence analysisAdd BLAST21
Topological domaini563 – 582CytoplasmicSequence analysisAdd BLAST20

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 20Sequence analysisAdd BLAST20
PropeptideiPRO_000002880021 – 111By similarityAdd BLAST91
ChainiPRO_0000028801112 – 582Matrix metalloproteinase-14Add BLAST471

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi319 ↔ 508By similarity
Modified residuei399Phosphotyrosine; by PKDCCBy similarity1

Post-translational modificationi

The precursor is cleaved by a furin endopeptidase.By similarity
Tyrosine phosphorylated by PKDCC/VLK.By similarity

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Phosphoprotein, Zymogen

Proteomic databases

MaxQBiP53690.
PaxDbiP53690.
PeptideAtlasiP53690.
PRIDEiP53690.

PTM databases

iPTMnetiP53690.
PhosphoSitePlusiP53690.
SwissPalmiP53690.

Expressioni

Tissue specificityi

Highly expressed in placenta, kidney, heart, lung, embryonic skeletal and periskeletal tissues.

Developmental stagei

Not detected before day 10.5. At day 12.5, prominently expressed in large arteries and the umbilical arteries, expressed at lower levels in the myocardium, craniofacial mesenchyme, nasal epithelium and liver capsule. At days 14.5 and 17.5, expressed in the musculoskeletal system, and ossification areas, with continued expression in the arterial tunica media.

Gene expression databases

BgeeiENSMUSG00000000957.
CleanExiMM_MMP14.
ExpressionAtlasiP53690. baseline and differential.
GenevisibleiP53690. MM.

Interactioni

Subunit structurei

Interacts (via C-terminal cytoplasmic tail) with BST2. Interacts with DLL1; inhibits DLL1-induced Notch signaling.By similarity

Protein-protein interaction databases

IntActiP53690. 1 interactor.
STRINGi10090.ENSMUSP00000087119.

Structurei

3D structure databases

ProteinModelPortaliP53690.
SMRiP53690.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati316 – 364Hemopexin 1Add BLAST49
Repeati365 – 410Hemopexin 2Add BLAST46
Repeati412 – 460Hemopexin 3Add BLAST49
Repeati461 – 508Hemopexin 4Add BLAST48

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi91 – 98Cysteine 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.
InParanoidiP53690.
KOiK07763.
OMAiNPESWLQ.
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.
IPR028693. MMP14.
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:SF24. PTHR10201:SF24. 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.

P53690-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSPAPRPSRS LLLPLLTLGT ALASLGWAQG SNFSPEAWLQ QYGYLPPGDL
60 70 80 90 100
RTHTQRSPQS LSAAIAAMQK FYGLQVTGKA DLATMMAMRR PRCGVPDKFG
110 120 130 140 150
TEIKANVRRK RYAIQGLKWQ HNEITFCIQN YTPKVGEYAT FEAIRKAFRV
160 170 180 190 200
WESATPLRFR EVPYAYIREG HEKQADIMIL FAEGFHGDST PFDGEGGFLA
210 220 230 240 250
HAYFPGPNIG GDTHFDSAEP WTVQNEDLNG NDIFLVAVHE LGHALGLEHS
260 270 280 290 300
NDPSAIMAPF YQWMDTENFV LPDDDRRGIQ QLYGSKSGSP TKMPPQPRTT
310 320 330 340 350
SRPSVPDKPK NPAYGPNICD GNFDTVAMLR GEMFVFKERW FWRVRNNQVM
360 370 380 390 400
DGYPMPIGQF WRGLPASINT AYERKDGKFV FFKGDKHWVF DEASLEPGYP
410 420 430 440 450
KHIKELGRGL PTDKIDAALF WMPNGKTYFF RGNKYYRFNE EFRAVDSEYP
460 470 480 490 500
KNIKVWEGIP ESPRGSFMGS DEVFTYFYKG NKYWKFNNQK LKVEPGYPKS
510 520 530 540 550
ALRDWMGCPS GGRPDEGTEE ETEVIIIEVD EEGSGAVSAA AVVLPVLLLL
560 570 580
LVLAVGLAVF FFRRHGTPKR LLYCQRSLLD KV
Length:582
Mass (Da):65,919
Last modified:July 27, 2011 - v3
Checksum:i6CA95CFD5811B093
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti133P → S in AAB86602 (PubMed:9325265).Curated1
Sequence conflicti255A → D in CAA58520 (PubMed:7708715).Curated1
Sequence conflicti258A → S in CAA58520 (PubMed:7708715).Curated1
Sequence conflicti258A → S in AAB51753 (PubMed:9648071).Curated1
Sequence conflicti341F → L in CAA58520 (PubMed:7708715).Curated1
Sequence conflicti346N → P in AAB86602 (PubMed:9325265).Curated1
Sequence conflicti378K → T in CAA58520 (PubMed:7708715).Curated1
Sequence conflicti390 – 391FD → CV in CAA58520 (PubMed:7708715).Curated2
Sequence conflicti400 – 401PK → AN in CAA58520 (PubMed:7708715).Curated2
Sequence conflicti407G → V in CAA58520 (PubMed:7708715).Curated1
Sequence conflicti412T → S in CAA58520 (PubMed:7708715).Curated1
Sequence conflicti417A → T in CAA58520 (PubMed:7708715).Curated1
Sequence conflicti512G → R in AAB51753 (PubMed:9648071).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X83536 mRNA. Translation: CAA58520.2.
AF022432
, AF022424, AF022425, AF022426, AF022427, AF022428, AF022429, AF022430, AF022431 Genomic DNA. Translation: AAB86602.1.
U54984 mRNA. Translation: AAB51753.1.
DQ249870 mRNA. Translation: ABB45784.1.
AK088476 mRNA. Translation: BAC40377.1.
AK138611 mRNA. Translation: BAE23719.1.
AK149907 mRNA. Translation: BAE29158.1.
AK149988 mRNA. Translation: BAE29216.1.
AK165014 mRNA. Translation: BAE38000.1.
CH466535 Genomic DNA. Translation: EDL36348.1.
CCDSiCCDS36922.1.
PIRiI48673.
RefSeqiNP_032634.3. NM_008608.4.
UniGeneiMm.280175.
Mm.486486.

Genome annotation databases

EnsembliENSMUST00000089688; ENSMUSP00000087119; ENSMUSG00000000957.
GeneIDi17387.
KEGGimmu:17387.
UCSCiuc007twc.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X83536 mRNA. Translation: CAA58520.2.
AF022432
, AF022424, AF022425, AF022426, AF022427, AF022428, AF022429, AF022430, AF022431 Genomic DNA. Translation: AAB86602.1.
U54984 mRNA. Translation: AAB51753.1.
DQ249870 mRNA. Translation: ABB45784.1.
AK088476 mRNA. Translation: BAC40377.1.
AK138611 mRNA. Translation: BAE23719.1.
AK149907 mRNA. Translation: BAE29158.1.
AK149988 mRNA. Translation: BAE29216.1.
AK165014 mRNA. Translation: BAE38000.1.
CH466535 Genomic DNA. Translation: EDL36348.1.
CCDSiCCDS36922.1.
PIRiI48673.
RefSeqiNP_032634.3. NM_008608.4.
UniGeneiMm.280175.
Mm.486486.

3D structure databases

ProteinModelPortaliP53690.
SMRiP53690.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP53690. 1 interactor.
STRINGi10090.ENSMUSP00000087119.

Protein family/group databases

MEROPSiM10.014.

PTM databases

iPTMnetiP53690.
PhosphoSitePlusiP53690.
SwissPalmiP53690.

Proteomic databases

MaxQBiP53690.
PaxDbiP53690.
PeptideAtlasiP53690.
PRIDEiP53690.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000089688; ENSMUSP00000087119; ENSMUSG00000000957.
GeneIDi17387.
KEGGimmu:17387.
UCSCiuc007twc.2. mouse.

Organism-specific databases

CTDi4323.
MGIiMGI:101900. Mmp14.

Phylogenomic databases

eggNOGiKOG1565. Eukaryota.
ENOG410XQ5D. LUCA.
GeneTreeiENSGT00760000118870.
HOGENOMiHOG000217928.
HOVERGENiHBG052484.
InParanoidiP53690.
KOiK07763.
OMAiNPESWLQ.
OrthoDBiEOG091G03DP.
TreeFamiTF352396.

Enzyme and pathway databases

ReactomeiR-MMU-1442490. Collagen degradation.
R-MMU-1474228. Degradation of the extracellular matrix.
R-MMU-1592389. Activation of Matrix Metalloproteinases.

Miscellaneous databases

ChiTaRSiMmp14. mouse.
PROiP53690.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000000957.
CleanExiMM_MMP14.
ExpressionAtlasiP53690. baseline and differential.
GenevisibleiP53690. 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.
IPR028693. MMP14.
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:SF24. PTHR10201:SF24. 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...

Entry informationi

Entry nameiMMP14_MOUSE
AccessioniPrimary (citable) accession number: P53690
Secondary accession number(s): O08645, O35369, Q8BTX2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: July 27, 2011
Last modified: November 30, 2016
This is version 160 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.