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Protein

Matrix metalloproteinase-14

Gene

Mmp14

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: -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. Acts as a positive regulator of cell growth and migration via activation of MMP15 in association with pro-MMP2. Involved in the formation of the fibrovascular tissues in association with pro-MMP2. Cleaves ADGRB1 to release vasculostatin-40 which inhibits angiogenesis.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

  • metalloaminopeptidase activity Source: Ensembl
  • 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
  • head development Source: Ensembl
  • 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 macrophage 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

Keywordsi

Molecular functionHydrolase, Metalloprotease, Protease
LigandCalcium, 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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 15

Organism-specific databases

RGDi620198 Mmp14

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

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

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

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

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

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

Family and domain databases

CDDicd00094 HX, 1 hit
cd04278 ZnMc_MMP, 1 hit
Gene3Di1.10.101.10, 1 hit
2.110.10.10, 1 hit
3.40.390.10, 1 hit
InterProiView protein in InterPro
IPR000585 Hemopexin-like_dom
IPR036375 Hemopexin-like_dom_sf
IPR018487 Hemopexin-like_repeat
IPR018486 Hemopexin_CS
IPR033739 M10A_MMP
IPR024079 MetalloPept_cat_dom_sf
IPR028693 MMP14
IPR001818 Pept_M10_metallopeptidase
IPR021190 Pept_M10A
IPR021805 Pept_M10A_metallopeptidase_C
IPR021158 Pept_M10A_Zn_BS
IPR006026 Peptidase_Metallo
IPR002477 Peptidoglycan-bd-like
IPR036365 PGBD-like_sf
IPR036366 PGBDSf
PANTHERiPTHR10201:SF24 PTHR10201:SF24, 1 hit
PfamiView protein in Pfam
PF11857 DUF3377, 1 hit
PF00045 Hemopexin, 4 hits
PF00413 Peptidase_M10, 1 hit
PF01471 PG_binding_1, 1 hit
PIRSFiPIRSF001191 Peptidase_M10A_matrix, 1 hit
PRINTSiPR00138 MATRIXIN
SMARTiView protein in SMART
SM00120 HX, 4 hits
SM00235 ZnMc, 1 hit
SUPFAMiSSF47090 SSF47090, 1 hit
SSF50923 SSF50923, 1 hit
PROSITEiView protein in PROSITE
PS00546 CYSTEINE_SWITCH, 1 hit
PS00024 HEMOPEXIN, 1 hit
PS51642 HEMOPEXIN_2, 4 hits
PS00142 ZINC_PROTEASE, 1 hit

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

Similar proteinsi

Entry informationi

Entry nameiMMP14_RAT
AccessioniPrimary (citable) accession number: Q10739
Secondary accession number(s): Q6IN06
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: May 1, 2007
Last modified: May 23, 2018
This is version 158 of the entry and version 2 of the sequence. See 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

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