Skip Header

Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot P53690 (MMP14_MOUSE)

Last modified February 9, 2010. Version 95. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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=MT1-MMP
      Short name=MT1MMP
    MMP-X1
    MT-MMP
Gene names
Name: Mmp14
Synonyms: Mtmmp
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMus

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

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. Ref.5

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.

Subcellular location

Membrane; Single-pass type I membrane protein; Extracellular side Potential. Melanosome By similarity.

Tissue specificity

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

Developmental stage

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.

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.

Post-translational modification

The precursor is cleaved by a furin endopeptidase By similarity.

Sequence similarities

Belongs to the peptidase M10A family.

Contains 4 hemopexin-like domains.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 Potential
Propeptide21 – 11191 By similarity
PRO_0000028800
Chain112 – 582471Matrix metalloproteinase-14
PRO_0000028801

Regions

Topological domain112 – 541430Extracellular Potential
Transmembrane542 – 56221 Potential
Topological domain563 – 58220Cytoplasmic Potential
Domain323 – 36644Hemopexin-like 1
Domain368 – 41245Hemopexin-like 2
Domain415 – 46147Hemopexin-like 3
Domain463 – 50846Hemopexin-like 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 conflict1331P → S in AAB86602. Ref.3
Sequence conflict2551A → D in CAA58520. Ref.1
Sequence conflict2581S → A in AAB86602. Ref.3
Sequence conflict3411F → L in CAA58520. Ref.1
Sequence conflict3461N → P in AAB86602. Ref.3
Sequence conflict3781K → T in CAA58520. Ref.1
Sequence conflict390 – 3912FD → CV in CAA58520. Ref.1
Sequence conflict400 – 4012PK → AN in CAA58520. Ref.1
Sequence conflict4071G → V in CAA58520. Ref.1
Sequence conflict4121T → S in CAA58520. Ref.1
Sequence conflict4171A → T in CAA58520. Ref.1
Sequence conflict5121G → R in AAB51753. Ref.4

Sequences

Sequence LengthMass (Da)Tools
P53690-1 [UniParc].

Last modified January 24, 2001. Version 2.
Checksum: 3AB355158D4DD175

FASTA58265,935
        10         20         30         40         50         60 
MSPAPRPSRS LLLPLLTLGT ALASLGWAQG SNFSPEAWLQ QYGYLPPGDL RTHTQRSPQS 

        70         80         90        100        110        120 
LSAAIAAMQK FYGLQVTGKA DLATMMAMRR 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 NDPSAIMSPF YQWMDTENFV LPDDDRRGIQ QLYGSKSGSP TKMPPQPRTT 

       310        320        330        340        350        360 
SRPSVPDKPK NPAYGPNICD 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

[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: 7708715] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]Odaka A.
Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION.
[3]"The matrix metalloproteinase-14 (MMP-14) gene is structurally distinct from other MMP genes and is co-expressed with the TIMP-2 gene during mouse embryogenesis."
Apte S.S., Fukai N., Beier D.R., Olsen B.R.
J. Biol. Chem. 272:25511-25517(1997) [PubMed: 9325265] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: 129/Sv.
[4]"Cloning of murine membrane-type-1-matrix metalloproteinase (MT-1-MMP) and its metanephric developmental regulation with respect to MMP-2 and its inhibitor."
Ota K., Stetler-Stevenson W.G., Yang Q., Kumar A., Wada J., Kashihara N., Wallner E.I., Kanwar Y.S.
Kidney Int. 54:131-142(1998) [PubMed: 9648071] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: CD-1.
Tissue: Kidney.
[5]"MT1-MMP-deficient mice develop dwarfism, osteopenia, arthritis, and connective tissue disease due to inadequate collagen turnover."
Holmbeck K., Bianco P., Caterina J., Yamada S., Kromer M., Kuznetsov S.A., Mankani M., Robey P.G., Poole A.R., Pidoux I., Ward J.M., Birkedal-Hansen H.
Cell 99:81-92(1999) [PubMed: 10520996] [Abstract]
Cited for: FUNCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X83536 mRNA. Translation: CAA58520.2.
AF022432 expand/collapse EMBL AC list , AF022424, AF022425, AF022426, AF022427, AF022428, AF022429, AF022430, AF022431 Genomic DNA. Translation: AAB86602.1.
U54984 mRNA. Translation: AAB51753.1.
IPIIPI00133725.
PIRI48673.
UniGeneMm.280175

3D structure databases

SMRP53690. Positions 114-287, 315-508.
ModBaseSearch...

Protein-protein interaction databases

STRINGP53690.

Protein family/group databases

MEROPSM10.014.

PTM databases

PhosphoSiteP53690.

Proteomic databases

PRIDEP53690.

Genome annotation databases

EnsemblENSMUST00000089688; ENSMUSP00000087119; ENSMUSG00000000957; Mus musculus. [Genome view]

Organism-specific databases

MGIMGI:101900. Mmp14.

Phylogenomic databases

eggNOGmaNOG06003.
HOGENOMHBG747685.
HOVERGENP53690.
InParanoidP53690.

Enzyme and pathway databases

BRENDA3.4.24.80. 244.

Gene expression databases

ArrayExpressP53690.
BgeeP53690.
CleanExMM_MMP14.
GenevestigatorP53690.
GermOnlineENSMUSG00000000957. Mus musculus.

Family and domain databases

InterProIPR000585. Hemopexin/matrixin.
IPR018486. Hemopexin/matrixin_CS.
IPR018487. Hemopexin/matrixin_repeat.
IPR001818. Pept_M10A_M12B.
IPR016293. Pept_M10A_matrix.
IPR006026. Peptidase_M.
IPR002477. Peptidoglycan-bd-like.
[Graphical view]
Gene3DG3DSA:2.110.10.10. Hemopexin. 1 hit.
PfamPF00045. 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]
PROSITEPS00546. CYSTEINE_SWITCH. 1 hit.
PS00024. HEMOPEXIN. 1 hit.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

SOURCESearch...

Entry information

Entry nameMMP14_MOUSE
AccessionPrimary (citable) accession number: P53690
Secondary accession number(s): O08645, O35369
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: January 24, 2001
Last modified: February 9, 2010
This is version 95 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents