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Q9Y5R2

- MMP24_HUMAN

UniProt

Q9Y5R2 - MMP24_HUMAN

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Protein

Matrix metalloproteinase-24

Gene

MMP24

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli

Functioni

Metalloprotease that mediates cleavage of N-cadherin (CDH2) and acts as a regulator of neuro-immune interactions and neural stem cell quiescence. 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. 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. May play a role in axonal growth. 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 (By similarity).By similarity

Cofactori

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi139 – 1391Zinc; in inhibited formBy similarity
Metal bindingi282 – 2821Zinc; catalyticPROSITE-ProRule annotation
Active sitei283 – 2831PROSITE-ProRule annotation
Metal bindingi286 – 2861Zinc; catalyticPROSITE-ProRule annotation
Metal bindingi292 – 2921Zinc; catalyticPROSITE-ProRule annotation
Sitei581 – 5822Cleavage; by furinBy similarity

GO - Molecular functioni

  1. calcium ion binding Source: InterPro
  2. enzyme activator activity Source: ProtInc
  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. positive regulation of catalytic activity Source: GOC
  7. proteolysis Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Biological processi

Cell adhesion

Keywords - Ligandi

Calcium, Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_118682. Activation of Matrix Metalloproteinases.

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):
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:MT5MMP
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 20

Organism-specific databases

HGNCiHGNC:7172. MMP24.

Subcellular locationi

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

GO - Cellular componenti

  1. extracellular vesicular exosome Source: UniProt
  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

Organism-specific databases

PharmGKBiPA30881.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 5252Sequence AnalysisAdd
BLAST
Propeptidei53 – 155103By similarityPRO_0000028846Add
BLAST
Chaini156 – 645490Matrix metalloproteinase-24PRO_0000028847Add
BLAST
Chaini156 – 581426Processed matrix metalloproteinase-24By similarityPRO_0000302758Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi380 ↔ 569By similarity

Post-translational modificationi

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

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Zymogen

Proteomic databases

PaxDbiQ9Y5R2.
PRIDEiQ9Y5R2.

PTM databases

PhosphoSiteiQ9Y5R2.

Expressioni

Tissue specificityi

Predominantly expressed in brain, kidney, pancreas and lung. Overexpressed in a series of brain tumors, including astrocytomas and glioblastomas.1 Publication

Gene expression databases

BgeeiQ9Y5R2.
CleanExiHS_MMP24.
ExpressionAtlasiQ9Y5R2. baseline and differential.
GenevestigatoriQ9Y5R2.

Organism-specific databases

HPAiHPA049280.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

IntActiQ9Y5R2. 1 interaction.
MINTiMINT-7897838.
STRINGi9606.ENSP00000246186.

Structurei

3D structure databases

ProteinModelPortaliQ9Y5R2.
SMRiQ9Y5R2. Positions 111-548.
ModBaseiSearch...
MobiDBiSearch...

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini53 – 602550ExtracellularSequence AnalysisAdd
BLAST
Topological domaini624 – 64522CytoplasmicSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei603 – 62321HelicalSequence AnalysisAdd
BLAST

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati377 – 42549Hemopexin 1Add
BLAST
Repeati426 – 47146Hemopexin 2Add
BLAST
Repeati473 – 52149Hemopexin 3Add
BLAST
Repeati522 – 56948Hemopexin 4Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi137 – 1448Cysteine switchBy similarity
Motifi643 – 6453PDZ-binding

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi149 – 1524Poly-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.By similarity

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.
InParanoidiQ9Y5R2.
KOiK08002.
OMAiFKNKAGP.
OrthoDBiEOG7XPZ57.
PhylomeDBiQ9Y5R2.
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.

Q9Y5R2-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MPRSRGGRAA PGPPPPPPPP GQAPRWSRWR VPGRLLLLLL PALCCLPGAA
60 70 80 90 100
RAAAAAAGAG NRAAVAVAVA RADEAEAPFA GQNWLKSYGY LLPYDSRASA
110 120 130 140 150
LHSAKALQSA VSTMQQFYGI PVTGVLDQTT IEWMKKPRCG VPDHPHLSRR
160 170 180 190 200
RRNKRYALTG QKWRQKHITY SIHNYTPKVG ELDTRKAIRQ AFDVWQKVTP
210 220 230 240 250
LTFEEVPYHE IKSDRKEADI MIFFASGFHG DSSPFDGEGG FLAHAYFPGP
260 270 280 290 300
GIGGDTHFDS DEPWTLGNAN HDGNDLFLVA VHELGHALGL EHSSDPSAIM
310 320 330 340 350
APFYQYMETH NFKLPQDDLQ GIQKIYGPPA EPLEPTRPLP TLPVRRIHSP
360 370 380 390 400
SERKHERQPR PPRPPLGDRP STPGTKPNIC DGNFNTVALF RGEMFVFKDR
410 420 430 440 450
WFWRLRNNRV QEGYPMQIEQ FWKGLPARID AAYERADGRF VFFKGDKYWV
460 470 480 490 500
FKEVTVEPGY PHSLGELGSC LPREGIDTAL RWEPVGKTYF FKGERYWRYS
510 520 530 540 550
EERRATDPGY PKPITVWKGI PQAPQGAFIS KEGYYTYFYK GRDYWKFDNQ
560 570 580 590 600
KLSVEPGYPR NILRDWMGCN QKEVERRKER RLPQDDVDIM VTINDVPGSV
610 620 630 640
NAVAVVIPCI LSLCILVLVY TIFQFKNKTG PQPVTYYKRP VQEWV
Length:645
Mass (Da):73,231
Last modified:November 1, 1999 - v1
Checksum:i06B2B76EA3DABB9D
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti564 – 5641R → H.
Corresponds to variant rs751887 [ dbSNP | Ensembl ].
VAR_060166

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF131284 mRNA. Translation: AAD42962.1.
AB021227 mRNA. Translation: BAA82967.1.
AL121753 Genomic DNA. Translation: CAX12722.1.
CCDSiCCDS46593.1.
RefSeqiNP_006681.1. NM_006690.3.
UniGeneiHs.715494.

Genome annotation databases

EnsembliENST00000246186; ENSP00000246186; ENSG00000125966.
GeneIDi10893.
KEGGihsa:10893.
UCSCiuc002xbu.2. human.

Polymorphism databases

DMDMi12585280.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF131284 mRNA. Translation: AAD42962.1 .
AB021227 mRNA. Translation: BAA82967.1 .
AL121753 Genomic DNA. Translation: CAX12722.1 .
CCDSi CCDS46593.1.
RefSeqi NP_006681.1. NM_006690.3.
UniGenei Hs.715494.

3D structure databases

ProteinModelPortali Q9Y5R2.
SMRi Q9Y5R2. Positions 111-548.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi Q9Y5R2. 1 interaction.
MINTi MINT-7897838.
STRINGi 9606.ENSP00000246186.

Chemistry

BindingDBi Q9Y5R2.
ChEMBLi CHEMBL5050.
DrugBanki DB00786. Marimastat.

Protein family/group databases

MEROPSi M10.023.

PTM databases

PhosphoSitei Q9Y5R2.

Polymorphism databases

DMDMi 12585280.

Proteomic databases

PaxDbi Q9Y5R2.
PRIDEi Q9Y5R2.

Protocols and materials databases

DNASUi 10893.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000246186 ; ENSP00000246186 ; ENSG00000125966 .
GeneIDi 10893.
KEGGi hsa:10893.
UCSCi uc002xbu.2. human.

Organism-specific databases

CTDi 10893.
GeneCardsi GC20P033814.
HGNCi HGNC:7172. MMP24.
HPAi HPA049280.
MIMi 604871. gene.
neXtProti NX_Q9Y5R2.
PharmGKBi PA30881.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG295915.
GeneTreei ENSGT00760000118870.
HOGENOMi HOG000217928.
HOVERGENi HBG052484.
InParanoidi Q9Y5R2.
KOi K08002.
OMAi FKNKAGP.
OrthoDBi EOG7XPZ57.
PhylomeDBi Q9Y5R2.
TreeFami TF352396.

Enzyme and pathway databases

Reactomei REACT_118682. Activation of Matrix Metalloproteinases.

Miscellaneous databases

GeneWikii MMP24.
GenomeRNAii 10893.
NextBioi 41363.
PROi Q9Y5R2.
SOURCEi Search...

Gene expression databases

Bgeei Q9Y5R2.
CleanExi HS_MMP24.
ExpressionAtlasi Q9Y5R2. baseline and differential.
Genevestigatori Q9Y5R2.

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 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 SPECIFICITY.
    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.
    , 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].

Entry informationi

Entry nameiMMP24_HUMAN
AccessioniPrimary (citable) accession number: Q9Y5R2
Secondary accession number(s): B7ZBG8, Q9H440
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 24, 2001
Last sequence update: November 1, 1999
Last modified: October 29, 2014
This is version 141 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 20
    Human chromosome 20: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. Peptidase families
    Classification of peptidase families and list of entries
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3