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Q9R0S2

- MMP24_MOUSE

UniProt

Q9R0S2 - MMP24_MOUSE

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Protein
Matrix metalloproteinase-24
Gene
Mmp24, Mmp21, Mt5mmp
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.1 Publication

Cofactori

Binds 1 zinc ion per subunit By similarity.
Calcium By similarity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi112 – 1121Zinc; in inhibited form By similarity
Metal bindingi255 – 2551Zinc; catalytic By similarity
Active sitei256 – 2561
Metal bindingi259 – 2591Zinc; catalytic By similarity
Metal bindingi265 – 2651Zinc; catalytic By similarity

GO - Molecular functioni

  1. calcium ion binding Source: InterPro
  2. metalloendopeptidase activity Source: InterPro
  3. zinc ion binding Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Calcium, Metal-binding, Zinc

Protein family/group databases

MEROPSiM10.023.

Names & Taxonomyi

Protein namesi
Recommended name:
Matrix metalloproteinase-24 (EC:3.4.24.-)
Short name:
MMP-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:
Gene namesi
Name:Mmp24
Synonyms:Mmp21, Mt5mmp
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 2

Organism-specific databases

MGIiMGI:1341867. Mmp24.

Subcellular locationi

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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini42 – 575534Extracellular Reviewed prediction
Add
BLAST
Transmembranei576 – 59621Helical; Reviewed prediction
Add
BLAST
Topological domaini597 – 61822Cytoplasmic Reviewed prediction
Add
BLAST

GO - Cellular componenti

  1. integral component of plasma membrane Source: InterPro
  2. proteinaceous extracellular matrix Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Extracellular matrix, Membrane, Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi256 – 2561E → A: Inactive against progelatinase A. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 4141 Reviewed prediction
Add
BLAST
Propeptidei42 – 12887 By similarity
PRO_0000028848Add
BLAST
Chaini129 – 618490Matrix metalloproteinase-24
PRO_0000028849Add
BLAST
Chaini129 – ?Processed matrix metalloproteinase-24PRO_0000302759

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi353 ↔ 542 By similarity

Post-translational modificationi

The precursor is cleaved by a furin endopeptidase By similarity.

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Zymogen

Proteomic databases

PaxDbiQ9R0S2.
PRIDEiQ9R0S2.

PTM databases

PhosphoSiteiQ9R0S2.

Miscellaneous databases

PMAP-CutDBQ9R0S2.

Expressioni

Tissue specificityi

Expressed in brain. Expressed at low level in testis.

Developmental stagei

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

Gene expression databases

ArrayExpressiQ9R0S2.
BgeeiQ9R0S2.
CleanExiMM_MMP21.
MM_MMP24.
GenevestigatoriQ9R0S2.

Structurei

3D structure databases

ProteinModelPortaliQ9R0S2.
SMRiQ9R0S2. Positions 84-521.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati350 – 39849Hemopexin 1
Add
BLAST
Repeati399 – 44446Hemopexin 2
Add
BLAST
Repeati446 – 49449Hemopexin 3
Add
BLAST
Repeati495 – 54248Hemopexin 4
Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi110 – 1178Cysteine switch By similarity

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi122 – 1254Poly-Arg

Domaini

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 similaritiesi

Belongs to the peptidase M10A family.
Contains 4 hemopexin repeats.

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG295915.
GeneTreeiENSGT00750000117332.
HOGENOMiHOG000217928.
HOVERGENiHBG052484.
InParanoidiA2AUV7.
KOiK08002.
OMAiFKNKAGP.
OrthoDBiEOG7XPZ57.
TreeFamiTF352396.

Family and domain databases

Gene3Di2.110.10.10. 1 hit.
3.40.390.10. 1 hit.
InterProiIPR000585. 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]
PANTHERiPTHR10201:SF138. PTHR10201:SF138. 1 hit.
PfamiPF11857. DUF3377. 1 hit.
PF00045. Hemopexin. 4 hits.
PF00413. Peptidase_M10. 1 hit.
PF01471. PG_binding_1. 1 hit.
[Graphical view]
PIRSFiPIRSF001191. Peptidase_M10A_matrix. 1 hit.
PRINTSiPR00138. MATRIXIN.
SMARTiSM00120. HX. 4 hits.
SM00235. ZnMc. 1 hit.
[Graphical view]
SUPFAMiSSF47090. SSF47090. 1 hit.
SSF50923. SSF50923. 1 hit.
PROSITEiPS00024. HEMOPEXIN. 1 hit.
PS51642. HEMOPEXIN_2. 4 hits.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9R0S2-1 [UniParc]FASTAAdd to Basket

« Hide

MPRSRGGRAA PGQASRWSGW RAPGRLLPLL PALCCLAAAA GAGKPAGADA    50
PFAGQNWLKS YGYLLPYESR ASALHSGKAL QSAVSTMQQF YGIPVTGVLD 100
QTTIEWMKKP RCGVPDHPHL SRRRRNKRYA LTGQKWRQKH ITYSIHNYTP 150
KVGELDTRKA IRQAFDVWQK VTPLTFEEVP YHEIKSDRKE ADIMIFFASG 200
FHGDSSPFDG EGGFLAHAYF PGPGIGGDTH FDSDEPWTLG NANHDGNDLF 250
LVAVHELGHA LGLEHSNDPS AIMAPFYQYM ETHNFKLPQD DLQGIQKIYG 300
PPAEPLEPTR PLPTLPVRRI HSPSERKHER HPRPPRPPLG DRPSTPGAKP 350
NICDGNFNTV ALFRGEMFVF KDRWFWRLRN NRVQEGYPMQ IEQFWKGLPA 400
RIDAAYERAD GRFVFFKGDK YWVFKEVTVE PGYPHSLGEL GSCLPREGID 450
TALRWEPVGK TYFFKGERYW RYSEERRATD PGYPKPITVW KGIPQAPQGA 500
FISKEGYYTY FYKGRDYWKF DNQKLSVEPG YPRNILRDWM GCKQKEVERR 550
KERRLPQDDV DIMVTIDDVP GSVNAVAVVV PCTLSLCLLV LLYTIFQFKN 600
KAGPQPVTYY KRPVQEWV 618
Length:618
Mass (Da):70,460
Last modified:July 27, 2011 - v2
Checksum:i51C8E61B187264F5
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti7 – 2822GRAAP…GRLLP → AALRRARPRAGALAGPGAAA in CAA09055. 1 Publication
Add
BLAST
Sequence conflicti44 – 507KPAGADA → SRPGR in CAA09055. 1 Publication
Sequence conflicti46 – 461A → T in BAA82966. 1 Publication
Sequence conflicti306 – 3083LEP → SGA in CAA09055. 1 Publication
Sequence conflicti326 – 3261R → K in CAA09055. 1 Publication
Sequence conflicti337 – 3415PPLGD → RPWG in CAA09055. 1 Publication
Sequence conflicti449 – 4491I → KP in CAA09055. 1 Publication
Sequence conflicti502 – 5021I → L in CAA09055. 1 Publication
Sequence conflicti589 – 5891L → R in CAA09055. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB021226 mRNA. Translation: BAA82966.1.
AJ010262 mRNA. Translation: CAA09055.1.
AL929233 Genomic DNA. Translation: CAM22837.1.
CCDSiCCDS16955.1.
RefSeqiNP_034938.3. NM_010808.3.
UniGeneiMm.330707.
Mm.389325.

Genome annotation databases

EnsembliENSMUST00000029141; ENSMUSP00000029141; ENSMUSG00000027612.
GeneIDi17391.
KEGGimmu:17391.
UCSCiuc008nlj.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB021226 mRNA. Translation: BAA82966.1 .
AJ010262 mRNA. Translation: CAA09055.1 .
AL929233 Genomic DNA. Translation: CAM22837.1 .
CCDSi CCDS16955.1.
RefSeqi NP_034938.3. NM_010808.3.
UniGenei Mm.330707.
Mm.389325.

3D structure databases

ProteinModelPortali Q9R0S2.
SMRi Q9R0S2. Positions 84-521.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

MEROPSi M10.023.

PTM databases

PhosphoSitei Q9R0S2.

Proteomic databases

PaxDbi Q9R0S2.
PRIDEi Q9R0S2.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000029141 ; ENSMUSP00000029141 ; ENSMUSG00000027612 .
GeneIDi 17391.
KEGGi mmu:17391.
UCSCi uc008nlj.1. mouse.

Organism-specific databases

CTDi 10893.
MGIi MGI:1341867. Mmp24.

Phylogenomic databases

eggNOGi NOG295915.
GeneTreei ENSGT00750000117332.
HOGENOMi HOG000217928.
HOVERGENi HBG052484.
InParanoidi A2AUV7.
KOi K08002.
OMAi FKNKAGP.
OrthoDBi EOG7XPZ57.
TreeFami TF352396.

Miscellaneous databases

NextBioi 292016.
PMAP-CutDB Q9R0S2.
PROi Q9R0S2.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9R0S2.
Bgeei Q9R0S2.
CleanExi MM_MMP21.
MM_MMP24.
Genevestigatori Q9R0S2.

Family and domain databases

Gene3Di 2.110.10.10. 1 hit.
3.40.390.10. 1 hit.
InterProi IPR000585. 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 ]
PANTHERi PTHR10201:SF138. PTHR10201:SF138. 1 hit.
Pfami PF11857. DUF3377. 1 hit.
PF00045. Hemopexin. 4 hits.
PF00413. Peptidase_M10. 1 hit.
PF01471. PG_binding_1. 1 hit.
[Graphical view ]
PIRSFi PIRSF001191. Peptidase_M10A_matrix. 1 hit.
PRINTSi PR00138. MATRIXIN.
SMARTi SM00120. HX. 4 hits.
SM00235. ZnMc. 1 hit.
[Graphical view ]
SUPFAMi SSF47090. SSF47090. 1 hit.
SSF50923. SSF50923. 1 hit.
PROSITEi PS00024. HEMOPEXIN. 1 hit.
PS51642. HEMOPEXIN_2. 4 hits.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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.

Entry informationi

Entry nameiMMP24_MOUSE
AccessioniPrimary (citable) accession number: Q9R0S2
Secondary accession number(s): A2AUV7, Q9Z0J9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 24, 2001
Last sequence update: July 27, 2011
Last modified: September 3, 2014
This is version 129 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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