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Q9Y5R2 (MMP24_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 135. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | 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-24

Short name=MMP-24
EC=3.4.24.-
Alternative name(s):
Membrane-type matrix metalloproteinase 5
Short name=MT-MMP 5
Short name=MTMMP5
Membrane-type-5 matrix metalloproteinase
Short name=MT5-MMP
Short name=MT5MMP

Cleaved into the following chain:

  1. Processed matrix metalloproteinase-24
Gene names
Name:MMP24
Synonyms:MT5MMP
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length645 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Activates progelatinase A. May also be a proteoglycanase involved in degradation of proteoglycans, such as dermatan sulfate and chondroitin sulfate proteoglycans. Cleaves partially fibronectin, but not collagen type I, nor laminin By similarity.

Cofactor

Binds 1 zinc ion per subunit By similarity.

Calcium By similarity.

Subcellular location

Cell membrane; Single-pass type I membrane protein; Extracellular side By similarity.

Processed matrix metalloproteinase-24: Secretedextracellular spaceextracellular matrix By similarity. Note: Also shed from cell surface as soluble proteinase, by a proteolytic cleavage By similarity.

Tissue specificity

Predominantly expressed in brain, kidney, pancreas and lung. Overexpressed in a series of brain tumors, including astrocytomas and glioblastomas.

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 repeats.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 5252 Potential
Propeptide53 – 155103 By similarity
PRO_0000028846
Chain156 – 645490Matrix metalloproteinase-24
PRO_0000028847
Chain156 – ?Processed matrix metalloproteinase-24PRO_0000302758

Regions

Topological domain53 – 602550Extracellular Potential
Transmembrane603 – 62321Helical; Potential
Topological domain624 – 64522Cytoplasmic Potential
Repeat377 – 42549Hemopexin 1
Repeat426 – 47146Hemopexin 2
Repeat473 – 52149Hemopexin 3
Repeat522 – 56948Hemopexin 4
Motif137 – 1448Cysteine switch By similarity
Compositional bias149 – 1524Poly-Arg

Sites

Active site2831 By similarity
Metal binding1391Zinc; in inhibited form By similarity
Metal binding2821Zinc; catalytic By similarity
Metal binding2861Zinc; catalytic By similarity
Metal binding2921Zinc; catalytic By similarity

Amino acid modifications

Disulfide bond380 ↔ 569 By similarity

Natural variations

Natural variant5641R → H.
Corresponds to variant rs751887 [ dbSNP | Ensembl ].
VAR_060166

Sequences

Sequence LengthMass (Da)Tools
Q9Y5R2 [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: 06B2B76EA3DABB9D

FASTA64573,231
        10         20         30         40         50         60 
MPRSRGGRAA PGPPPPPPPP GQAPRWSRWR VPGRLLLLLL PALCCLPGAA RAAAAAAGAG 

        70         80         90        100        110        120 
NRAAVAVAVA RADEAEAPFA GQNWLKSYGY LLPYDSRASA LHSAKALQSA VSTMQQFYGI 

       130        140        150        160        170        180 
PVTGVLDQTT IEWMKKPRCG VPDHPHLSRR RRNKRYALTG QKWRQKHITY SIHNYTPKVG 

       190        200        210        220        230        240 
ELDTRKAIRQ AFDVWQKVTP LTFEEVPYHE IKSDRKEADI MIFFASGFHG DSSPFDGEGG 

       250        260        270        280        290        300 
FLAHAYFPGP GIGGDTHFDS DEPWTLGNAN HDGNDLFLVA VHELGHALGL EHSSDPSAIM 

       310        320        330        340        350        360 
APFYQYMETH NFKLPQDDLQ GIQKIYGPPA EPLEPTRPLP TLPVRRIHSP SERKHERQPR 

       370        380        390        400        410        420 
PPRPPLGDRP STPGTKPNIC DGNFNTVALF RGEMFVFKDR WFWRLRNNRV QEGYPMQIEQ 

       430        440        450        460        470        480 
FWKGLPARID AAYERADGRF VFFKGDKYWV FKEVTVEPGY PHSLGELGSC LPREGIDTAL 

       490        500        510        520        530        540 
RWEPVGKTYF FKGERYWRYS EERRATDPGY PKPITVWKGI PQAPQGAFIS KEGYYTYFYK 

       550        560        570        580        590        600 
GRDYWKFDNQ KLSVEPGYPR NILRDWMGCN QKEVERRKER RLPQDDVDIM VTINDVPGSV 

       610        620        630        640 
NAVAVVIPCI LSLCILVLVY TIFQFKNKTG PQPVTYYKRP VQEWV 

« Hide

References

« Hide 'large scale' references
[1]"Identification and characterization of human MT5-MMP, a new membrane-bound activator of progelatinase a overexpressed in brain tumors."
Llano E., Pendas A.M., Freije J.P., Nakano A., Knaeuper V., Murphy G., Lopez-Otin C.
Cancer Res. 59:2570-2576(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Brain.
[2]"Identification of a new membrane-type matrix metalloproteinase, MT5-MMP, that is expressed predominantly in cerebellum."
Seiki M.
Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"The DNA sequence and comparative analysis of human chromosome 20."
Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E. expand/collapse author list , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF131284 mRNA. Translation: AAD42962.1.
AB021227 mRNA. Translation: BAA82967.1.
AL121753 Genomic DNA. Translation: CAX12722.1.
RefSeqNP_006681.1. NM_006690.3.
UniGeneHs.715494.

3D structure databases

ProteinModelPortalQ9Y5R2.
SMRQ9Y5R2. Positions 62-571.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ9Y5R2. 1 interaction.
MINTMINT-7897838.
STRING9606.ENSP00000246186.

Chemistry

BindingDBQ9Y5R2.
ChEMBLCHEMBL5050.

Protein family/group databases

MEROPSM10.023.

PTM databases

PhosphoSiteQ9Y5R2.

Polymorphism databases

DMDM12585280.

Proteomic databases

PaxDbQ9Y5R2.
PRIDEQ9Y5R2.

Protocols and materials databases

DNASU10893.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000246186; ENSP00000246186; ENSG00000125966.
GeneID10893.
KEGGhsa:10893.
UCSCuc002xbu.2. human.

Organism-specific databases

CTD10893.
GeneCardsGC20P033814.
HGNCHGNC:7172. MMP24.
HPAHPA049280.
MIM604871. gene.
neXtProtNX_Q9Y5R2.
PharmGKBPA30881.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG295915.
HOGENOMHOG000217928.
HOVERGENHBG052484.
InParanoidQ9Y5R2.
KOK08002.
OMAFKNKAGP.
OrthoDBEOG7XPZ57.
PhylomeDBQ9Y5R2.
TreeFamTF352396.

Enzyme and pathway databases

ReactomeREACT_118779. Extracellular matrix organization.

Gene expression databases

ArrayExpressQ9Y5R2.
BgeeQ9Y5R2.
CleanExHS_MMP24.
GenevestigatorQ9Y5R2.

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.
IPR028723. MMP24.
IPR001818. Pept_M10_metallopeptidase.
IPR021190. Pept_M10A.
IPR021805. Pept_M10A_metallopeptidase_C.
IPR016293. Pept_M10A_stromelysin-type.
IPR006026. Peptidase_Metallo.
IPR002477. Peptidoglycan-bd-like.
[Graphical view]
PANTHERPTHR10201. PTHR10201. 1 hit.
PTHR10201:SF27. PTHR10201:SF27. 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.
PROSITEPS00024. HEMOPEXIN. 1 hit.
PS51642. HEMOPEXIN_2. 4 hits.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiMMP24.
GenomeRNAi10893.
NextBio41363.
PROQ9Y5R2.
SOURCESearch...

Entry information

Entry nameMMP24_HUMAN
AccessionPrimary (citable) accession number: Q9Y5R2
Secondary accession number(s): B7ZBG8, Q9H440
Entry history
Integrated into UniProtKB/Swiss-Prot: January 24, 2001
Last sequence update: November 1, 1999
Last modified: April 16, 2014
This is version 135 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 20

Human chromosome 20: entries, gene names and cross-references to MIM