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Q9R0S2

- MMP24_MOUSE

UniProt

Q9R0S2 - MMP24_MOUSE

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Protein

Matrix metalloproteinase-24

Gene

Mmp24

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Metalloprotease that mediates cleavage of N-cadherin (CDH2) and acts as a regulator of neuro-immune interactions and neural stem cell quiescence (PubMed:19805319, PubMed:24952463). Involved in cell-cell interactions between nociceptive neurites and mast cells, possibly by mediating cleavage of CDH2, thereby acting as a mediator of peripheral thermal nociception and inflammatory hyperalgesia (PubMed:19805319). Key regulator of neural stem cells quiescence by mediating cleavage of CDH2, affecting CDH2-mediated anchorage of neural stem cells to ependymocytes in the adult subependymal zone, leading to modulate their quiescence (PubMed:24952463). May play a role in axonal growth (PubMed:11714638). Able to activate 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 (PubMed:10622708).4 Publications

Cofactori

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi112 – 1121Zinc; in inhibited formBy similarity
Metal bindingi255 – 2551Zinc; catalyticPROSITE-ProRule annotation
Active sitei256 – 25611 PublicationPROSITE-ProRule annotation
Metal bindingi259 – 2591Zinc; catalyticPROSITE-ProRule annotation
Metal bindingi265 – 2651Zinc; catalyticPROSITE-ProRule annotation
Sitei554 – 5552Cleavage; by furin

GO - Molecular functioni

  1. cadherin binding Source: UniProtKB
  2. calcium ion binding Source: InterPro
  3. metalloendopeptidase activity Source: UniProtKB
  4. zinc ion binding Source: InterPro

GO - Biological processi

  1. cell-cell adhesion Source: UniProtKB
  2. cell-cell adhesion mediated by cadherin Source: UniProtKB
  3. detection of temperature stimulus involved in sensory perception of pain Source: UniProtKB
  4. glial cell differentiation Source: UniProtKB
  5. neuronal stem cell maintenance Source: UniProtKB
  6. proteolysis Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Biological processi

Cell adhesion

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 Matrix metalloproteinase-24 : Cell membrane; Single-pass type I membrane protein. Golgi apparatustrans-Golgi network membrane; Single-pass type I membrane protein
Note: Recycled back to the plasma membrane through the trans-Golgi network via interaction with APBA3.1 Publication
Chain Processed matrix metalloproteinase-24 : Secretedextracellular spaceextracellular matrix
Note: Also shed from cell surface as soluble proteinase, by a proteolytic cleavage.1 Publication

GO - Cellular componenti

  1. extracellular vesicular exosome Source: Ensembl
  2. integral component of plasma membrane Source: UniProtKB
  3. proteinaceous extracellular matrix Source: UniProtKB-KW
  4. trans-Golgi network membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Extracellular matrix, Golgi apparatus, Membrane, Secreted

Pathology & Biotechi

Disruption phenotypei

No visible phenotype. Mice are viable, develop normally and are fertile. They however display enhanced sensitivity to noxious thermal stimuli under basal conditions characterized by an absence of thermal inflammatory hyperalgesia (PubMed:19805319). In subependymal zone, more intense signal is observed for extracellular N-cadherin (Cdh2) as well as increased levels of full-length Cdh2 without changes in Cdh2 messenger RNA levels (PubMed:24952463).2 Publications

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi256 – 2561E → A: Loss of function. Does not prevent proteolytic processing. 2 Publications
Mutagenesisi549 – 5546Missing: Abolishes proteolytic processing. Gain of function mutant.
Mutagenesisi616 – 6183Missing: Impaired recycling affecting its internalization, leading to decreased activity on the plasma surface. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 4141Sequence AnalysisAdd
BLAST
Propeptidei42 – 12887By similarityPRO_0000028848Add
BLAST
Chaini129 – 618490Matrix metalloproteinase-24PRO_0000028849Add
BLAST
Chaini129 – 554426Processed matrix metalloproteinase-24CuratedPRO_0000302759Add
BLAST

Amino acid modifications

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

Post-translational modificationi

Cleaved by a furin endopeptidase in the trans-Golgi network.

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Zymogen

Proteomic databases

MaxQBiQ9R0S2.
PaxDbiQ9R0S2.
PRIDEiQ9R0S2.

PTM databases

PhosphoSiteiQ9R0S2.

Miscellaneous databases

PMAP-CutDBQ9R0S2.

Expressioni

Tissue specificityi

Mainly expressed in neuronal cells of both central and peripheral nervous systems. Expressed by CGRP-containing peptidergic nociceptors in dorsal root ganglia (PubMed:19805319). Expressed in adult neural stem cell and ependymocytes (PubMed:24952463). Expressed at low level in testis.3 Publications

Developmental stagei

Expressed at day 11 until day 15, before dropping around day 17 before birth. Expressed in the cerebrum in embryos, but it declines after birth, while expression in the cerebellum starts to increase postnatally and continues thereafter.1 Publication

Gene expression databases

BgeeiQ9R0S2.
CleanExiMM_MMP21.
MM_MMP24.
ExpressionAtlasiQ9R0S2. baseline.
GenevestigatoriQ9R0S2.

Interactioni

Subunit structurei

Interacts with GRIP1 and GRIP2 (By similarity). Interacts (via PDZ-binding motif) with APBA3 (via PDZ domain).By similarity1 Publication

Structurei

3D structure databases

ProteinModelPortaliQ9R0S2.
SMRiQ9R0S2. Positions 84-521.
ModBaseiSearch...
MobiDBiSearch...

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini42 – 575534ExtracellularSequence AnalysisAdd
BLAST
Topological domaini597 – 61822CytoplasmicSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei576 – 59621HelicalSequence AnalysisAdd
BLAST

Family & Domainsi

Domains and Repeats

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

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi110 – 1178Cysteine switchBy similarity
Motifi616 – 6183PDZ-binding

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.
The PDZ-binding motif (also named EWV motif) is required for interaction with PDZ domains of APBA3 and recycling through the trans-Golgi network.1 Publication

Sequence similaritiesi

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

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG295915.
GeneTreeiENSGT00760000118870.
HOGENOMiHOG000217928.
HOVERGENiHBG052484.
InParanoidiQ9R0S2.
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

        10         20         30         40         50
MPRSRGGRAA PGQASRWSGW RAPGRLLPLL PALCCLAAAA GAGKPAGADA
60 70 80 90 100
PFAGQNWLKS YGYLLPYESR ASALHSGKAL QSAVSTMQQF YGIPVTGVLD
110 120 130 140 150
QTTIEWMKKP RCGVPDHPHL SRRRRNKRYA LTGQKWRQKH ITYSIHNYTP
160 170 180 190 200
KVGELDTRKA IRQAFDVWQK VTPLTFEEVP YHEIKSDRKE ADIMIFFASG
210 220 230 240 250
FHGDSSPFDG EGGFLAHAYF PGPGIGGDTH FDSDEPWTLG NANHDGNDLF
260 270 280 290 300
LVAVHELGHA LGLEHSNDPS AIMAPFYQYM ETHNFKLPQD DLQGIQKIYG
310 320 330 340 350
PPAEPLEPTR PLPTLPVRRI HSPSERKHER HPRPPRPPLG DRPSTPGAKP
360 370 380 390 400
NICDGNFNTV ALFRGEMFVF KDRWFWRLRN NRVQEGYPMQ IEQFWKGLPA
410 420 430 440 450
RIDAAYERAD GRFVFFKGDK YWVFKEVTVE PGYPHSLGEL GSCLPREGID
460 470 480 490 500
TALRWEPVGK TYFFKGERYW RYSEERRATD PGYPKPITVW KGIPQAPQGA
510 520 530 540 550
FISKEGYYTY FYKGRDYWKF DNQKLSVEPG YPRNILRDWM GCKQKEVERR
560 570 580 590 600
KERRLPQDDV DIMVTIDDVP GSVNAVAVVV PCTLSLCLLV LLYTIFQFKN
610
KAGPQPVTYY KRPVQEWV
Length:618
Mass (Da):70,460
Last modified:July 27, 2011 - v2
Checksum:i51C8E61B187264F5
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti7 – 2822GRAAP…GRLLP → AALRRARPRAGALAGPGAAA in CAA09055. (PubMed:10085137)CuratedAdd
BLAST
Sequence conflicti44 – 507KPAGADA → SRPGR in CAA09055. (PubMed:10085137)Curated
Sequence conflicti46 – 461A → T in BAA82966. 1 PublicationCurated
Sequence conflicti306 – 3083LEP → SGA in CAA09055. (PubMed:10085137)Curated
Sequence conflicti326 – 3261R → K in CAA09055. (PubMed:10085137)Curated
Sequence conflicti337 – 3415PPLGD → RPWG in CAA09055. (PubMed:10085137)Curated
Sequence conflicti449 – 4491I → KP in CAA09055. (PubMed:10085137)Curated
Sequence conflicti502 – 5021I → L in CAA09055. (PubMed:10085137)Curated
Sequence conflicti589 – 5891L → R in CAA09055. (PubMed:10085137)Curated

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

MaxQBi Q9R0S2.
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 ENSGT00760000118870.
HOGENOMi HOG000217928.
HOVERGENi HBG052484.
InParanoidi Q9R0S2.
KOi K08002.
OMAi FKNKAGP.
OrthoDBi EOG7XPZ57.
TreeFami TF352396.

Miscellaneous databases

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

Gene expression databases

Bgeei Q9R0S2.
CleanExi MM_MMP21.
MM_MMP24.
ExpressionAtlasi Q9R0S2. baseline.
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, ACTIVE SITE.
    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.
  5. "Shedding of membrane type matrix metalloproteinase 5 by a furin-type convertase: a potential mechanism for down-regulation."
    Wang X., Pei D.
    J. Biol. Chem. 276:35953-35960(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, PROTEOLYTIC PROCESSING, MUTAGENESIS OF GLU-256 AND 549-ARG--ARG-555.
  6. "Membrane-type 5 matrix metalloproteinase is expressed in differentiated neurons and regulates axonal growth."
    Hayashita-Kinoh H., Kinoh H., Okada A., Komori K., Itoh Y., Chiba T., Kajita M., Yana I., Seiki M.
    Cell Growth Differ. 12:573-580(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
  7. "Mint-3 regulates the retrieval of the internalized membrane-type matrix metalloproteinase, MT5-MMP, to the plasma membrane by binding to its carboxyl end motif EWV."
    Wang P., Wang X., Pei D.
    J. Biol. Chem. 279:20461-20470(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, INTERACTION WITH APBA3, MUTAGENESIS OF 616-GLU--VAL-618.
  8. Cited for: FUNCTION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE.
  9. "MT5-MMP regulates adult neural stem cell functional quiescence through the cleavage of N-cadherin."
    Porlan E., Marti-Prado B., Morante-Redolat J.M., Consiglio A., Delgado A.C., Kypta R., Lopez-Otin C., Kirstein M., Farinas I.
    Nat. Cell Biol. 16:629-638(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE.

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: October 29, 2014
This is version 131 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