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Q9Y5R2

- MMP24_HUMAN

UniProt

Q9Y5R2 - MMP24_HUMAN

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Protein
Matrix metalloproteinase-24
Gene
MMP24, MT5MMP
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at transcript 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 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 form By similarity
Metal bindingi282 – 2821Zinc; catalytic By similarity
Active sitei283 – 2831 By similarity
Metal bindingi286 – 2861Zinc; catalytic By similarity
Metal bindingi292 – 2921Zinc; catalytic By similarity

GO - Molecular functioni

  1. calcium ion binding Source: InterPro
  2. enzyme activator activity Source: ProtInc
  3. metalloendopeptidase activity Source: ProtInc
  4. zinc ion binding Source: InterPro

GO - Biological processi

  1. positive regulation of catalytic activity Source: GOC
  2. proteolysis Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini53 – 602550Extracellular Reviewed prediction
Add
BLAST
Transmembranei603 – 62321Helical; Reviewed prediction
Add
BLAST
Topological domaini624 – 64522Cytoplasmic Reviewed prediction
Add
BLAST

GO - Cellular componenti

  1. extracellular vesicular exosome Source: UniProt
  2. integral component of plasma membrane Source: ProtInc
  3. proteinaceous extracellular matrix Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Extracellular matrix, Membrane, Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA30881.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 5252 Reviewed prediction
Add
BLAST
Propeptidei53 – 155103 By similarity
PRO_0000028846Add
BLAST
Chaini156 – 645490Matrix metalloproteinase-24
PRO_0000028847Add
BLAST
Chaini156 – ?Processed matrix metalloproteinase-24PRO_0000302758

Amino acid modifications

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

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.

Gene expression databases

ArrayExpressiQ9Y5R2.
BgeeiQ9Y5R2.
CleanExiHS_MMP24.
GenevestigatoriQ9Y5R2.

Organism-specific databases

HPAiHPA049280.

Interactioni

Protein-protein interaction databases

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

Structurei

3D structure databases

ProteinModelPortaliQ9Y5R2.
SMRiQ9Y5R2. Positions 111-548.

Family & Domainsi

Domains and Repeats

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

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi137 – 1448Cysteine switch By similarity

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.

Sequence similaritiesi

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

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG295915.
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

MPRSRGGRAA PGPPPPPPPP GQAPRWSRWR VPGRLLLLLL PALCCLPGAA    50
RAAAAAAGAG NRAAVAVAVA RADEAEAPFA GQNWLKSYGY LLPYDSRASA 100
LHSAKALQSA VSTMQQFYGI PVTGVLDQTT IEWMKKPRCG VPDHPHLSRR 150
RRNKRYALTG QKWRQKHITY SIHNYTPKVG ELDTRKAIRQ AFDVWQKVTP 200
LTFEEVPYHE IKSDRKEADI MIFFASGFHG DSSPFDGEGG FLAHAYFPGP 250
GIGGDTHFDS DEPWTLGNAN HDGNDLFLVA VHELGHALGL EHSSDPSAIM 300
APFYQYMETH NFKLPQDDLQ GIQKIYGPPA EPLEPTRPLP TLPVRRIHSP 350
SERKHERQPR PPRPPLGDRP STPGTKPNIC DGNFNTVALF RGEMFVFKDR 400
WFWRLRNNRV QEGYPMQIEQ FWKGLPARID AAYERADGRF VFFKGDKYWV 450
FKEVTVEPGY PHSLGELGSC LPREGIDTAL RWEPVGKTYF FKGERYWRYS 500
EERRATDPGY PKPITVWKGI PQAPQGAFIS KEGYYTYFYK GRDYWKFDNQ 550
KLSVEPGYPR NILRDWMGCN QKEVERRKER RLPQDDVDIM VTINDVPGSV 600
NAVAVVIPCI LSLCILVLVY TIFQFKNKTG PQPVTYYKRP VQEWV 645
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.

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.
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

ArrayExpressi Q9Y5R2.
Bgeei Q9Y5R2.
CleanExi HS_MMP24.
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: 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: September 3, 2014
This is version 139 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

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