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Q10739 (MMP14_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 121. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Matrix metalloproteinase-14

Short name=MMP-14
EC=3.4.24.80
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 names
Name:Mmp14
Synonyms:Mtmmp
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length582 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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.

Catalytic activity

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.

Cofactor

Binds 1 zinc ion per subunit By similarity.

Calcium By similarity.

Subunit structure

Interacts (via C-terminal cytoplasmic tail) with BST2 By similarity.

Subcellular location

Membrane; Single-pass type I membrane protein Potential. Melanosome By similarity. Cytoplasm By similarity. Note: Forms a complex with BST2 and localizes to the cytoplasm By similarity.

Domain

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 similarities

Belongs to the peptidase M10A family.

Contains 4 hemopexin repeats.

Ontologies

Keywords
   Cellular componentCytoplasm
Membrane
   DomainRepeat
Signal
Transmembrane
Transmembrane helix
   LigandCalcium
Metal-binding
Zinc
   Molecular functionHydrolase
Metalloprotease
Protease
   PTMCleavage on pair of basic residues
Disulfide bond
Zymogen
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processangiogenesis

Inferred from expression pattern PubMed 14766216. Source: RGD

astrocyte cell migration

Inferred from expression pattern PubMed 16265672. Source: RGD

branching morphogenesis of an epithelial tube

Inferred from electronic annotation. Source: Ensembl

endothelial cell proliferation

Inferred from expression pattern PubMed 14766216. Source: RGD

lung development

Inferred from electronic annotation. Source: Ensembl

male gonad development

Inferred from expression pattern PubMed 22152881. Source: RGD

negative regulation of focal adhesion assembly

Inferred from direct assay PubMed 15044209. Source: RGD

ossification

Inferred from expression pattern PubMed 15883642. Source: RGD

ovarian follicle development

Inferred from expression pattern PubMed 15617683. Source: RGD

positive regulation of cell growth

Inferred from electronic annotation. Source: Ensembl

positive regulation of cell migration

Inferred from electronic annotation. Source: Ensembl

proteolysis

Inferred from electronic annotation. Source: UniProtKB-KW

response to estrogen

Inferred from expression pattern PubMed 15053235. Source: RGD

response to hypoxia

Inferred from expression pattern PubMed 16980344. Source: RGD

response to mechanical stimulus

Inferred from expression pattern PubMed 15350851. Source: RGD

response to oxidative stress

Inferred from expression pattern PubMed 15642321. Source: RGD

tissue remodeling

Inferred from direct assay PubMed 16740171. Source: RGD

zymogen activation

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcytoplasm

Inferred from direct assay PubMed 16740171. Source: RGD

extracellular matrix

Inferred from electronic annotation. Source: InterPro

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

melanosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functioncalcium ion binding

Inferred from electronic annotation. Source: InterPro

metalloendopeptidase activity

Inferred from electronic annotation. Source: InterPro

peptidase activator activity

Inferred from mutant phenotype PubMed 14668206. Source: RGD

sequence-specific DNA binding transcription factor activity

Inferred from electronic annotation. Source: Ensembl

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 Potential
Propeptide21 – 11191Activation peptide
PRO_0000028806
Chain112 – 582471Matrix metalloproteinase-14
PRO_0000028807

Regions

Topological domain112 – 541430Extracellular Potential
Transmembrane542 – 56221Helical; Potential
Topological domain563 – 58220Cytoplasmic Potential
Repeat316 – 36449Hemopexin 1
Repeat365 – 41046Hemopexin 2
Repeat412 – 46049Hemopexin 3
Repeat461 – 50848Hemopexin 4
Motif91 – 988Cysteine switch By similarity

Sites

Active site2401 By similarity
Metal binding931Zinc; in inhibited form By similarity
Metal binding2391Zinc; catalytic By similarity
Metal binding2431Zinc; catalytic By similarity
Metal binding2491Zinc; catalytic By similarity

Amino acid modifications

Disulfide bond319 ↔ 508 By similarity

Experimental info

Sequence conflict681M → I in CAA58521. Ref.1
Sequence conflict2551A → D in CAA58521. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q10739 [UniParc].

Last modified May 1, 2007. Version 2.
Checksum: 48F1A8E3065E1AE8

FASTA58266,080
        10         20         30         40         50         60 
MSPAPRPSRS LLLPLLTLGT TLASLGWAQS SNFSPEAWLQ QYGYLPPGDL RTHTQRSPQS 

        70         80         90        100        110        120 
LSAAIAAMQR FYGLQVTGKA DSDTMKAMRR PRCGVPDKFG TEIKANVRRK RYAIQGLKWQ 

       130        140        150        160        170        180 
HNEITFCIQN YTPKVGEYAT FEAIRKAFRV WESATPLRFR EVPYAYIREG HEKQADIMIL 

       190        200        210        220        230        240 
FAEGFHGDST PFDGEGGFLA HAYFPGPNIG GDTHFDSAEP WTVQNEDLNG NDIFLVAVHE 

       250        260        270        280        290        300 
LGHALGLEHS NDPSAIMAPF YQWMDTENFV LPDDDRRGIQ QLYGSKSGSP TKMPPQPRTT 

       310        320        330        340        350        360 
SRPSVPDKPR NPTYGPNICD GNFDTVAMLR GEMFVFKERW FWRVRNNQVM DGYPMPIGQF 

       370        380        390        400        410        420 
WRGLPASINT AYERKDGKFV FFKGDKHWVF DEASLEPGYP KHIKELGRGL PTDKIDAALF 

       430        440        450        460        470        480 
WMPNGKTYFF RGNKYYRFNE EFRAVDSEYP KNIKVWEGIP ESPRGSFMGS DEVFTYFYKG 

       490        500        510        520        530        540 
NKYWKFNNQK LKVEPGYPKS ALRDWMGCPS GGRPDEGTEE ETEVIIIEVD EEGSGAVSAA 

       550        560        570        580 
AVVLPVLLLL LVLAVGLAVF FFRRHGTPKR LLYCQRSLLD KV 

« Hide

References

« Hide 'large scale' references
[1]"Membrane-type matrix metalloproteinase (MT-MMP) gene is expressed in stromal cells of human colon, breast, and head and neck carcinomas."
Okada A., Bellocq J.-P., Rouyer N., Chenard M.P., Rio M.C., Chambon P., Basset P.
Proc. Natl. Acad. Sci. U.S.A. 92:2730-2734(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Expression and function of MT-MMP in glial cells."
Cossins J., Clements J., Catlin G., Wells G.
Submitted (SEP-1995) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"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].
Tissue: Heart.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X83537 mRNA. Translation: CAA58521.1.
X91785 mRNA. Translation: CAA62897.1.
BC072509 mRNA. Translation: AAH72509.1.
PIRI84471.
RefSeqNP_112318.1. NM_031056.1.
UniGeneRn.10371.

3D structure databases

ProteinModelPortalQ10739.
SMRQ10739. Positions 114-287.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10116.ENSRNOP00000049168.

Protein family/group databases

MEROPSM10.014.

PTM databases

PhosphoSiteQ10739.

Proteomic databases

PRIDEQ10739.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000042938; ENSRNOP00000049168; ENSRNOG00000010947.
ENSRNOT00000075610; ENSRNOP00000065434; ENSRNOG00000010947.
GeneID81707.
KEGGrno:81707.
UCSCRGD:620198. rat.

Organism-specific databases

CTD4323.
RGD620198. Mmp14.

Phylogenomic databases

eggNOGNOG295915.
GeneTreeENSGT00740000115381.
HOGENOMHOG000217928.
HOVERGENHBG052484.
InParanoidQ10739.
KOK07763.
OMAWMGCPSG.
OrthoDBEOG7XPZ57.
TreeFamTF352396.

Gene expression databases

GenevestigatorQ10739.

Family and domain databases

Gene3D2.110.10.10. 1 hit.
3.40.390.10. 1 hit.
InterProIPR000585. Hemopexin-like_dom.
IPR018487. Hemopexin-like_repeat.
IPR018486. Hemopexin_CS.
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]
PANTHERPTHR10201. PTHR10201. 1 hit.
PTHR10201:SF24. PTHR10201:SF24. 1 hit.
PfamPF11857. DUF3377. 1 hit.
PF00045. Hemopexin. 4 hits.
PF00413. Peptidase_M10. 1 hit.
PF01471. PG_binding_1. 1 hit.
[Graphical view]
PIRSFPIRSF001191. Peptidase_M10A_matrix. 1 hit.
PRINTSPR00138. MATRIXIN.
SMARTSM00120. HX. 4 hits.
SM00235. ZnMc. 1 hit.
[Graphical view]
SUPFAMSSF47090. SSF47090. 1 hit.
SSF50923. SSF50923. 1 hit.
PROSITEPS00546. CYSTEINE_SWITCH. 1 hit.
PS00024. HEMOPEXIN. 1 hit.
PS51642. HEMOPEXIN_2. 4 hits.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio615328.
PROQ10739.

Entry information

Entry nameMMP14_RAT
AccessionPrimary (citable) accession number: Q10739
Secondary accession number(s): Q6IN06
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: May 1, 2007
Last modified: March 19, 2014
This is version 121 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries