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Protein

Matrix metalloproteinase-14

Gene

Mmp14

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

Seems to specifically activate progelatinase A. May thus trigger invasion by tumor cells by activating progelatinase A on the tumor cell surface. 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 similarity

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

  • calcium ion binding Source: InterPro
  • integrin binding Source: RGD
  • metalloendopeptidase activity Source: UniProtKB
  • peptidase activator activity Source: RGD
  • zinc ion binding Source: InterPro

GO - Biological processi

  • angiogenesis Source: RGD
  • astrocyte cell migration Source: RGD
  • branching morphogenesis of an epithelial tube Source: Ensembl
  • chondrocyte proliferation Source: Ensembl
  • collagen catabolic process Source: Ensembl
  • craniofacial suture morphogenesis Source: Ensembl
  • embryonic cranial skeleton morphogenesis Source: Ensembl
  • endochondral ossification Source: Ensembl
  • endodermal cell differentiation Source: Ensembl
  • endothelial cell proliferation Source: RGD
  • lung development Source: Ensembl
  • male gonad development Source: RGD
  • negative regulation of focal adhesion assembly Source: RGD
  • negative regulation of Notch signaling pathway Source: UniProtKB
  • ossification Source: RGD
  • ovarian follicle development Source: RGD
  • positive regulation of B cell differentiation Source: UniProtKB
  • positive regulation of cell growth Source: Ensembl
  • positive regulation of cell migration Source: Ensembl
  • positive regulation of myotube differentiation Source: UniProtKB
  • response to estrogen Source: RGD
  • response to hormone Source: RGD
  • response to hypoxia Source: RGD
  • response to mechanical stimulus Source: RGD
  • response to odorant Source: RGD
  • response to organic cyclic compound Source: RGD
  • response to oxidative stress Source: RGD
  • tissue remodeling Source: RGD
  • zymogen activation Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Calcium, Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-RNO-1442490. Collagen degradation.
R-RNO-1474228. Degradation of the extracellular matrix.
R-RNO-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):
Membrane-type matrix metalloproteinase 1
Short name:
MT-MMP 1
Short name:
MTMMP1
Membrane-type-1 matrix metalloproteinase
Short name:
MT-MMP
Short name:
MT1-MMP
Short name:
MT1MMP
Gene namesi
Name:Mmp14
Synonyms:Mtmmp
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 15

Organism-specific databases

RGDi620198. 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_000002880621 – 111Activation peptideAdd BLAST91
ChainiPRO_0000028807112 – 582Matrix metalloproteinase-14Add BLAST471

Amino acid modifications

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

Post-translational modificationi

Tyrosine phosphorylated by PKDCC/VLK.By similarity

Keywords - PTMi

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

Proteomic databases

PaxDbiQ10739.
PRIDEiQ10739.

PTM databases

iPTMnetiQ10739.
PhosphoSitePlusiQ10739.

Expressioni

Gene expression databases

BgeeiENSRNOG00000010947.
GenevisibleiQ10739. RN.

Interactioni

Subunit structurei

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

GO - Molecular functioni

  • integrin binding Source: RGD

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000049168.

Structurei

3D structure databases

ProteinModelPortaliQ10739.
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.
InParanoidiQ10739.
KOiK07763.
OMAiNPESWLQ.
OrthoDBiEOG091G03DP.
PhylomeDBiQ10739.
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.

Q10739-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSPAPRPSRS LLLPLLTLGT TLASLGWAQS SNFSPEAWLQ QYGYLPPGDL
60 70 80 90 100
RTHTQRSPQS LSAAIAAMQR FYGLQVTGKA DSDTMKAMRR 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
SRPSVPDKPR NPTYGPNICD 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):66,080
Last modified:May 1, 2007 - v2
Checksum:i48F1A8E3065E1AE8
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti68M → I in CAA58521 (PubMed:7708715).Curated1
Sequence conflicti255A → D in CAA58521 (PubMed:7708715).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X83537 mRNA. Translation: CAA58521.1.
X91785 mRNA. Translation: CAA62897.1.
BC072509 mRNA. Translation: AAH72509.1.
PIRiI84471.
RefSeqiNP_112318.1. NM_031056.1.
UniGeneiRn.10371.

Genome annotation databases

EnsembliENSRNOT00000075610; ENSRNOP00000065434; ENSRNOG00000010947.
GeneIDi81707.
KEGGirno:81707.
UCSCiRGD:620198. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X83537 mRNA. Translation: CAA58521.1.
X91785 mRNA. Translation: CAA62897.1.
BC072509 mRNA. Translation: AAH72509.1.
PIRiI84471.
RefSeqiNP_112318.1. NM_031056.1.
UniGeneiRn.10371.

3D structure databases

ProteinModelPortaliQ10739.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000049168.

Protein family/group databases

MEROPSiM10.014.

PTM databases

iPTMnetiQ10739.
PhosphoSitePlusiQ10739.

Proteomic databases

PaxDbiQ10739.
PRIDEiQ10739.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000075610; ENSRNOP00000065434; ENSRNOG00000010947.
GeneIDi81707.
KEGGirno:81707.
UCSCiRGD:620198. rat.

Organism-specific databases

CTDi4323.
RGDi620198. Mmp14.

Phylogenomic databases

eggNOGiKOG1565. Eukaryota.
ENOG410XQ5D. LUCA.
GeneTreeiENSGT00760000118870.
HOGENOMiHOG000217928.
HOVERGENiHBG052484.
InParanoidiQ10739.
KOiK07763.
OMAiNPESWLQ.
OrthoDBiEOG091G03DP.
PhylomeDBiQ10739.
TreeFamiTF352396.

Enzyme and pathway databases

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

Miscellaneous databases

PROiQ10739.

Gene expression databases

BgeeiENSRNOG00000010947.
GenevisibleiQ10739. RN.

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_RAT
AccessioniPrimary (citable) accession number: Q10739
Secondary accession number(s): Q6IN06
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: May 1, 2007
Last modified: November 30, 2016
This is version 146 of the entry and version 2 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. Peptidase families
    Classification of peptidase families and list of entries
  2. 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.