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Q9R0S2 (MMP24_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 128. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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):
Matrix metalloproteinase-21
Short name=MMP-21
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:Mmp21, Mt5mmp
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length618 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein 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. Ref.4

Cofactor

Binds 1 zinc ion per subunit By similarity.

Calcium By similarity.

Subcellular location

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

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

Tissue specificity

Expressed in brain. Expressed at low level in testis.

Developmental stage

Expressed at day 11 until day 15, before dropping around day 17 before birth.

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 – 4141 Potential
Propeptide42 – 12887 By similarity
PRO_0000028848
Chain129 – 618490Matrix metalloproteinase-24
PRO_0000028849
Chain129 – ?Processed matrix metalloproteinase-24PRO_0000302759

Regions

Topological domain42 – 575534Extracellular Potential
Transmembrane576 – 59621Helical; Potential
Topological domain597 – 61822Cytoplasmic Potential
Repeat350 – 39849Hemopexin 1
Repeat399 – 44446Hemopexin 2
Repeat446 – 49449Hemopexin 3
Repeat495 – 54248Hemopexin 4
Motif110 – 1178Cysteine switch By similarity
Compositional bias122 – 1254Poly-Arg

Sites

Active site2561
Metal binding1121Zinc; in inhibited form By similarity
Metal binding2551Zinc; catalytic By similarity
Metal binding2591Zinc; catalytic By similarity
Metal binding2651Zinc; catalytic By similarity

Amino acid modifications

Disulfide bond353 ↔ 542 By similarity

Experimental info

Mutagenesis2561E → A: Inactive against progelatinase A. Ref.2
Sequence conflict7 – 2822GRAAP…GRLLP → AALRRARPRAGALAGPGAAA in CAA09055. Ref.2
Sequence conflict44 – 507KPAGADA → SRPGR in CAA09055. Ref.2
Sequence conflict461A → T in BAA82966. Ref.1
Sequence conflict306 – 3083LEP → SGA in CAA09055. Ref.2
Sequence conflict3261R → K in CAA09055. Ref.2
Sequence conflict337 – 3415PPLGD → RPWG in CAA09055. Ref.2
Sequence conflict4491I → KP in CAA09055. Ref.2
Sequence conflict5021I → L in CAA09055. Ref.2
Sequence conflict5891L → R in CAA09055. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q9R0S2 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: 51C8E61B187264F5

FASTA61870,460
        10         20         30         40         50         60 
MPRSRGGRAA PGQASRWSGW RAPGRLLPLL PALCCLAAAA GAGKPAGADA PFAGQNWLKS 

        70         80         90        100        110        120 
YGYLLPYESR ASALHSGKAL QSAVSTMQQF YGIPVTGVLD QTTIEWMKKP RCGVPDHPHL 

       130        140        150        160        170        180 
SRRRRNKRYA LTGQKWRQKH ITYSIHNYTP KVGELDTRKA IRQAFDVWQK VTPLTFEEVP 

       190        200        210        220        230        240 
YHEIKSDRKE ADIMIFFASG FHGDSSPFDG EGGFLAHAYF PGPGIGGDTH FDSDEPWTLG 

       250        260        270        280        290        300 
NANHDGNDLF LVAVHELGHA LGLEHSNDPS AIMAPFYQYM ETHNFKLPQD DLQGIQKIYG 

       310        320        330        340        350        360 
PPAEPLEPTR PLPTLPVRRI HSPSERKHER HPRPPRPPLG DRPSTPGAKP NICDGNFNTV 

       370        380        390        400        410        420 
ALFRGEMFVF KDRWFWRLRN NRVQEGYPMQ IEQFWKGLPA RIDAAYERAD GRFVFFKGDK 

       430        440        450        460        470        480 
YWVFKEVTVE PGYPHSLGEL GSCLPREGID TALRWEPVGK TYFFKGERYW RYSEERRATD 

       490        500        510        520        530        540 
PGYPKPITVW KGIPQAPQGA FISKEGYYTY FYKGRDYWKF DNQKLSVEPG YPRNILRDWM 

       550        560        570        580        590        600 
GCKQKEVERR KERRLPQDDV DIMVTIDDVP GSVNAVAVVV PCTLSLCLLV LLYTIFQFKN 

       610 
KAGPQPVTYY KRPVQEWV 

« Hide

References

« Hide 'large scale' references
[1]"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].
[2]"Identification and characterization of the fifth membrane-type matrix metalloproteinase MT5-MMP."
Pei D.Q.
J. Biol. Chem. 274:8925-8932(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], MUTAGENESIS OF GLU-256.
Strain: BALB/c.
Tissue: Brain.
[3]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[4]"Expression, purification and characterization of recombinant mouse MT5-MMP protein products."
Wang X., Yi J., Lei J., Pei D.Q.
FEBS Lett. 462:261-266(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB021226 mRNA. Translation: BAA82966.1.
AJ010262 mRNA. Translation: CAA09055.1.
AL929233 Genomic DNA. Translation: CAM22837.1.
CCDSCCDS16955.1.
RefSeqNP_034938.3. NM_010808.3.
UniGeneMm.330707.
Mm.389325.

3D structure databases

ProteinModelPortalQ9R0S2.
SMRQ9R0S2. Positions 84-521.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

MEROPSM10.023.

PTM databases

PhosphoSiteQ9R0S2.

Proteomic databases

PaxDbQ9R0S2.
PRIDEQ9R0S2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000029141; ENSMUSP00000029141; ENSMUSG00000027612.
GeneID17391.
KEGGmmu:17391.
UCSCuc008nlj.1. mouse.

Organism-specific databases

CTD10893.
MGIMGI:1341867. Mmp24.

Phylogenomic databases

eggNOGNOG295915.
GeneTreeENSGT00750000117332.
HOGENOMHOG000217928.
HOVERGENHBG052484.
InParanoidA2AUV7.
KOK08002.
OMAFKNKAGP.
OrthoDBEOG7XPZ57.
TreeFamTF352396.

Gene expression databases

ArrayExpressQ9R0S2.
BgeeQ9R0S2.
CleanExMM_MMP21.
MM_MMP24.
GenevestigatorQ9R0S2.

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:SF138. PTHR10201:SF138. 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

NextBio292016.
PMAP-CutDBQ9R0S2.
PROQ9R0S2.
SOURCESearch...

Entry information

Entry nameMMP24_MOUSE
AccessionPrimary (citable) accession number: Q9R0S2
Secondary accession number(s): A2AUV7, Q9Z0J9
Entry history
Integrated into UniProtKB/Swiss-Prot: January 24, 2001
Last sequence update: July 27, 2011
Last modified: July 9, 2014
This is version 128 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

MGD cross-references

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