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Protein

Matrix metalloproteinase-24

Gene

Mmp24

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: 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

Protein has several cofactor binding sites:
  • Zn2+By similarityNote: Binds 1 zinc ion per subunit.By similarity
  • Ca2+By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi112Zinc; in inhibited formBy similarity1
Metal bindingi255Zinc; catalyticPROSITE-ProRule annotation1
Active sitei256PROSITE-ProRule annotation1 Publication1
Metal bindingi259Zinc; catalyticPROSITE-ProRule annotation1
Metal bindingi265Zinc; catalyticPROSITE-ProRule annotation1

GO - Molecular functioni

  • cadherin binding Source: UniProtKB
  • calcium ion binding Source: InterPro
  • metalloendopeptidase activity Source: UniProtKB
  • zinc ion binding Source: InterPro

GO - Biological processi

  • cell-cell adhesion Source: UniProtKB
  • cell-cell adhesion mediated by cadherin Source: UniProtKB
  • detection of temperature stimulus involved in sensory perception of pain Source: UniProtKB
  • glial cell differentiation Source: UniProtKB
  • neuronal stem cell population maintenance Source: UniProtKB
  • 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
Proteomesi
  • UP000000589 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:1341867. Mmp24.

Subcellular locationi

Matrix metalloproteinase-24 :
Processed matrix metalloproteinase-24 :
  • Secretedextracellular spaceextracellular matrix

  • Note: Also shed from cell surface as soluble proteinase, by a proteolytic cleavage.1 Publication

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini42 – 575ExtracellularSequence analysisAdd BLAST534
Transmembranei576 – 596HelicalSequence analysisAdd BLAST21
Topological domaini597 – 618CytoplasmicSequence analysisAdd BLAST22

GO - Cellular componenti

  • extracellular exosome Source: MGI
  • integral component of plasma membrane Source: UniProtKB
  • proteinaceous extracellular matrix Source: UniProtKB-SubCell
  • 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)DescriptionActionsGraphical viewLength
Mutagenesisi256E → A: Loss of function. Does not prevent proteolytic processing. 2 Publications1
Mutagenesisi549 – 554Missing : Abolishes proteolytic processing. Gain of function mutant. 6
Mutagenesisi616 – 618Missing : Impaired recycling affecting its internalization, leading to decreased activity on the plasma surface. 1 Publication3

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 41Sequence analysisAdd BLAST41
PropeptideiPRO_000002884842 – 128By similarityAdd BLAST87
ChainiPRO_0000028849129 – 618Matrix metalloproteinase-24Add BLAST490
ChainiPRO_0000302759129 – 554Processed matrix metalloproteinase-24CuratedAdd BLAST426

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi353 ↔ 542By similarity

Post-translational modificationi

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei554 – 555Cleavage; by furin2

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Zymogen

Proteomic databases

MaxQBiQ9R0S2.
PaxDbiQ9R0S2.
PRIDEiQ9R0S2.

PTM databases

iPTMnetiQ9R0S2.
PhosphoSitePlusiQ9R0S2.

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

BgeeiENSMUSG00000027612.
CleanExiMM_MMP21.
MM_MMP24.
GenevisibleiQ9R0S2. MM.

Interactioni

Subunit structurei

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

GO - Molecular functioni

  • cadherin binding Source: UniProtKB

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000029141.

Structurei

3D structure databases

ProteinModelPortaliQ9R0S2.
SMRiQ9R0S2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati350 – 398Hemopexin 1Add BLAST49
Repeati399 – 444Hemopexin 2Add BLAST46
Repeati446 – 494Hemopexin 3Add BLAST49
Repeati495 – 542Hemopexin 4Add BLAST48

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi110 – 117Cysteine switchBy similarity8
Motifi616 – 618PDZ-binding3

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi122 – 125Poly-Arg4

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

eggNOGiKOG1565. Eukaryota.
ENOG410XQ5D. LUCA.
GeneTreeiENSGT00760000118870.
HOGENOMiHOG000217928.
HOVERGENiHBG052484.
InParanoidiQ9R0S2.
KOiK08002.
OMAiFQFKNKA.
OrthoDBiEOG091G03DP.
TreeFamiTF352396.

Family and domain databases

CDDicd00094. HX. 1 hit.
cd04278. ZnMc_MMP. 1 hit.
Gene3Di2.110.10.10. 1 hit.
3.40.390.10. 1 hit.
InterProiIPR000585. Hemopexin-like_dom.
IPR018487. Hemopexin-like_repeat.
IPR018486. Hemopexin_CS.
IPR033739. M10A_MMP.
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. 2 hits.
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)DescriptionActionsGraphical viewLength
Sequence conflicti7 – 28GRAAP…GRLLP → AALRRARPRAGALAGPGAAA in CAA09055 (PubMed:10085137).CuratedAdd BLAST22
Sequence conflicti44 – 50KPAGADA → SRPGR in CAA09055 (PubMed:10085137).Curated7
Sequence conflicti46A → T in BAA82966 (Ref. 1) Curated1
Sequence conflicti306 – 308LEP → SGA in CAA09055 (PubMed:10085137).Curated3
Sequence conflicti326R → K in CAA09055 (PubMed:10085137).Curated1
Sequence conflicti337 – 341PPLGD → RPWG in CAA09055 (PubMed:10085137).Curated5
Sequence conflicti449I → KP in CAA09055 (PubMed:10085137).Curated1
Sequence conflicti502I → L in CAA09055 (PubMed:10085137).Curated1
Sequence conflicti589L → R in CAA09055 (PubMed:10085137).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB021226 mRNA. Translation: BAA82966.1.
AJ010262 mRNA. Translation: CAA09055.1.
AL929233 Genomic DNA. Translation: CAM22837.1.
CCDSiCCDS16955.1.
RefSeqiNP_034938.3. NM_010808.4.
UniGeneiMm.389325.

Genome annotation databases

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

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB021226 mRNA. Translation: BAA82966.1.
AJ010262 mRNA. Translation: CAA09055.1.
AL929233 Genomic DNA. Translation: CAM22837.1.
CCDSiCCDS16955.1.
RefSeqiNP_034938.3. NM_010808.4.
UniGeneiMm.389325.

3D structure databases

ProteinModelPortaliQ9R0S2.
SMRiQ9R0S2.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000029141.

Protein family/group databases

MEROPSiM10.023.

PTM databases

iPTMnetiQ9R0S2.
PhosphoSitePlusiQ9R0S2.

Proteomic databases

MaxQBiQ9R0S2.
PaxDbiQ9R0S2.
PRIDEiQ9R0S2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi10893.
MGIiMGI:1341867. Mmp24.

Phylogenomic databases

eggNOGiKOG1565. Eukaryota.
ENOG410XQ5D. LUCA.
GeneTreeiENSGT00760000118870.
HOGENOMiHOG000217928.
HOVERGENiHBG052484.
InParanoidiQ9R0S2.
KOiK08002.
OMAiFQFKNKA.
OrthoDBiEOG091G03DP.
TreeFamiTF352396.

Miscellaneous databases

ChiTaRSiMmp24. mouse.
PMAP-CutDBQ9R0S2.
PROiQ9R0S2.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000027612.
CleanExiMM_MMP21.
MM_MMP24.
GenevisibleiQ9R0S2. MM.

Family and domain databases

CDDicd00094. HX. 1 hit.
cd04278. ZnMc_MMP. 1 hit.
Gene3Di2.110.10.10. 1 hit.
3.40.390.10. 1 hit.
InterProiIPR000585. Hemopexin-like_dom.
IPR018487. Hemopexin-like_repeat.
IPR018486. Hemopexin_CS.
IPR033739. M10A_MMP.
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. 2 hits.
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]
ProtoNetiSearch...

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: November 30, 2016
This is version 146 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.