Skip Header

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

Reviewed, UniProtKB/Swiss-Prot Q9GLE4 (MMP14_BOVIN)

Last modified January 19, 2010. Version 58. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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
Gene names
Name: MMP14
OrganismBos taurus (Bovine)
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

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 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.

Subcellular location

Membrane; Single-pass type I membrane protein Potential. Melanosome 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.

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 – 11090Activation peptide
PRO_0000289295
Chain111 – 582472Matrix metalloproteinase-14
PRO_0000289296

Regions

Topological domain111 – 541431Extracellular Potential
Transmembrane542 – 56221 Potential
Topological domain563 – 58220Cytoplasmic Potential
Domain322 – 36544Hemopexin-like 1
Domain367 – 41145Hemopexin-like 2
Domain414 – 46047Hemopexin-like 3
Domain462 – 50746Hemopexin-like 4
Motif90 – 978Cysteine switch By similarity

Sites

Active site2391 By similarity
Metal binding921Zinc; in inhibited form By similarity
Metal binding2381Zinc; catalytic By similarity
Metal binding2421Zinc; catalytic By similarity
Metal binding2481Zinc; catalytic By similarity

Amino acid modifications

Disulfide bond318 ↔ 507 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9GLE4-1 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: 65174CE65D4040E1

FASTA58265,883
        10         20         30         40         50         60 
MSPAPRPACS LLLPVLTLAS ALASLSSAQS SFSPEAWLQQ HGYLPPGDLR THTQRSPQSL 

        70         80         90        100        110        120 
SAAIAAMQRF YGLRVTGKAD ADTMKAMRRP RCGVPDKFGA EIKANVRRKR YAIQGLKWQH 

       130        140        150        160        170        180 
NEITFCIQNY TPNVGEYATF EAIRKAFRVW ESATPLRFRE VPYAYIREGH EKQADIMIFF 

       190        200        210        220        230        240 
AEGFHGDSTP FDGEGGFLAH AYFPGPNIGG DTHFDSAEPW TVRNEDLNGN DIFLVAVHEL 

       250        260        270        280        290        300 
GHALGLEHSN DPSAIMAPFY QWMDTENFVL PDDDRRGIQQ LYGSKSGSPT KMPPQPRTTS 

       310        320        330        340        350        360 
RPSVPDKPKN PTYGPNICDG NFDTVAMLRG EMFVFKERWF WRVRKNQVMD GYPMPIGQFW 

       370        380        390        400        410        420 
RGLPASINTA YERKDGKFVF FKGDKHWVFD EASLEPGYPK HIKELGRGLP TDRIDAALFW 

       430        440        450        460        470        480 
MPNGKTYFFR GNKYYRFNEE LRIVESEYPK NIKVWEGIPE SPRGSFMGSD EVFTYFYKGN 

       490        500        510        520        530        540 
KYWKFNNQKL KVEPGYPKSA LRDWMGCPSS GGQPDEGTEE ETEVIIIEVD EEGSGAVSAA 

       550        560        570        580 
AVVLPVLLLL LVLAVGLAVF FFRRHGTPKR LLYCQRSLLD KV 

« Hide

References

[1]"Molecular cloning and biological characterization of bovine membrane-type matrix metalloprotease 1 (bMT1-MMP)."
Zhang B., Yan L., Moses M.A., Fang J., Miao H., Tsang P.
Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF290429 mRNA. Translation: AAG28170.1.
IPIIPI00692043.
RefSeqNP_776815.1.
UniGeneBt.7046

3D structure databases

HSSPHSSP built from PDB template 1BQQ based on UniProtKB P50281.
SMRQ9GLE4. Positions 113-286, 315-507.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ9GLE4.

Protein family/group databases

MEROPSM10.014.

Genome annotation databases

EnsemblENSBTAT00000019744; ENSBTAP00000019744; ENSBTAG00000014824; Bos taurus. [Genome view]
GeneID281915.
KEGGbta:281915.

Organism-specific databases

CTD281915.

Phylogenomic databases

HOVERGENQ9GLE4.
InParanoidQ9GLE4.

Enzyme and pathway databases

BRENDA3.4.24.80. 251.

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...

Entry information

Entry nameMMP14_BOVIN
AccessionPrimary (citable) accession number: Q9GLE4
Entry history
Integrated into UniProtKB/Swiss-Prot: May 29, 2007
Last sequence update: March 1, 2001
Last modified: January 19, 2010
This is version 58 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

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