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UniProtKB/Swiss-Prot entry Q9Y5R2


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name MMP24_HUMAN
Primary accession number Q9Y5R2
Secondary accession number Q9H440
Integrated into Swiss-Prot on January 24, 2001
Sequence was last modified on November 1, 1999 (Sequence version 1)
Annotations were last modified on    June 16, 2009 (Entry version 91)
Name and origin of the protein
Protein name Matrix metalloproteinase-24 [Precursor]
Synonyms MMP-24
EC 3.4.24.-
Membrane-type matrix metalloproteinase 5
MT-MMP 5
Membrane-type-5 matrix metalloproteinase
MT5-MMP
Contains Processed matrix metalloproteinase-24
Gene name
Name: MMP24
Synonyms: MT5MMP
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Brain;
PubMed=10363975 [NCBI, ExPASy, EBI, Israel, Japan]
Llano E., Pendas A.M., Freije J.P., Nakano A., Knaeuper V., Murphy G., Lopez-Otin C.;
"Identification and characterization of human MT5-MMP, a new membrane-bound activator of progelatinase a overexpressed in brain tumors.";
Cancer Res. 59:2570-2576(1999).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
Seiki M.;
"Identification of a new membrane-type matrix metalloproteinase, MT5-MMP, that is expressed predominantly in cerebellum.";
Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/414865a; PubMed=11780052 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"The DNA sequence and comparative analysis of human chromosome 20.";
Nature 414:865-871(2001).
[4]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-629, AND MASS SPECTROMETRY.
DOI=10.2116/analsci.24.161; PubMed=18187866 [NCBI, ExPASy, EBI, Israel, Japan]
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Anal. Sci. 24:161-166(2008).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AF131284; AAD42962.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AB021227; BAA82967.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL121753; -; NOT_ANNOTATED_CDS; Genomic_DNA.[EMBL / GenBank / DDBJ]
IPI IPI00001729; -.
RefSeq NP_006681.1; -.
UniGene Hs.567417
3D structure databases
HSSP P50281; 1BQQ. [HSSP ENTRY / PDB]
SMR Q9Y5R2; 160-328.
ModBase Q9Y5R2.
Protein family/group databases
MEROPS M10.023; -.
PTM databases
PhosphoSite Q9Y5R2; -.
Organism-specific databases
GeneCards GC20P033278; -.
H-InvDB HIX0019627; -.
HGNC HGNC:7172; MMP24.
GenAtlas MMP24.
MIM 604871; gene. [NCBI / EBI]
PharmGKB PA30881; -.
Gene expression databases
ArrayExpress Q9Y5R2; -.
Bgee Q9Y5R2; -.
CleanEx HS_MMP24; -.
GermOnline ENSG00000125966; Homo sapiens.
Ontologies
GO
GO:0005615; Cellular component: extracellular space (inferred from electronic annotation from UniProtKB-SubCell).
GO:0005887; Cellular component: integral to plasma membrane (traceable author statement from ProtInc).
GO:0005578; Cellular component: proteinaceous extracellular matrix (inferred from electronic annotation from UniProtKB-SubCell).
GO:0005509; Molecular function: calcium ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0008047; Molecular function: enzyme activator activity (traceable author statement from ProtInc).
GO:0004222; Molecular function: metalloendopeptidase activity (traceable author statement from ProtInc).
GO:0008270; Molecular function: zinc ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0006508; Biological process: proteolysis (traceable author statement from ProtInc).
QuickGo view.
Family and domain databases
InterPro IPR000585; Hemopexin/matrixin.
IPR018486; Hemopexin/matrixin_CS.
IPR018487; Hemopexin/matrixin_repeat.
IPR001818; Pept_M10A_M12B.
IPR016293; Pept_M10A_matrix.
IPR006025; Pept_M_Zn_BS.
IPR006026; Peptidase_M.
IPR002477; Peptidoglycan-bd-like.
Graphical view of domain structure.
Gene3D G3DSA:2.110.10.10; Hemopexin; 1.
Pfam PF00045; Hemopexin; 4.
PF00413; Peptidase_M10; 1.
PF01471; PG_binding_1; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF001191; Peptidase_M10A_matrix; 1.
PRINTS PR00138; MATRIXIN.
SMART SM00120; HX; 4.
SM00235; ZnMc; 1.
SMART graphical view of domain structure.
PROSITE PS00546; CYSTEINE_SWITCH; FALSE_NEG.
PS00024; HEMOPEXIN; 1.
PS00142; ZINC_PROTEASE; 1.
Proteomic databases
PRIDE Q9Y5R2; -.
Genome annotation databases
Ensembl ENSG00000125966; Homo sapiens. [Contig view]
GeneID 10893; -.
KEGG hsa:10893; -.
NMPDR fig|9606.3.peg.20141; -.
Phylogenomic databases
HOGENOM Q9Y5R2; -.
HOVERGEN Q9Y5R2; -.
Other
NextBio 41363; -.
SOURCE MMP24; Homo sapiens.
ProtoNet Q9Y5R2.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Calcium; Cell membrane; Cleavage on pair of basic residues; Disulfide bond; Extracellular matrix; Hydrolase; Membrane; Metal-binding; Metalloprotease; Phosphoprotein; Protease; Repeat; Secreted; Signal; Transmembrane; Zinc; Zymogen.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
SIGNAL   1    52  52     Potential. 
PROPEP   53   155  103     By similarity. PRO_0000028846
CHAIN   156   645  490     Matrix metalloproteinase-24. PRO_0000028847
CHAIN   156     ?        Processed matrix metalloproteinase-24. PRO_0000302758
TOPO_DOM   53   602  550     Extracellular (Potential). 
TRANSMEM   603   623  21     Potential. 
TOPO_DOM   624   645  22     Cytoplasmic (Potential). 
DOMAIN   384   427  44     Hemopexin-like 1. 
DOMAIN   429   473  45     Hemopexin-like 2. 
DOMAIN   476   522  47     Hemopexin-like 3. 
DOMAIN   524   569  46     Hemopexin-like 4. 
MOTIF   137   144  8     Cysteine switch (By similarity). 
COMPBIAS   149   152  4     Poly-Arg. 
ACT_SITE   283   283        By similarity. 
METAL   139   139        Zinc; in inhibited form (By similarity). 
METAL   282   282        Zinc; catalytic (By similarity). 
METAL   286   286        Zinc; catalytic (By similarity). 
METAL   292   292        Zinc; catalytic (By similarity). 
MOD_RES   629   629        Phosphothreonine. 
DISULFID   380   569        By similarity. 
Sequence information
Length: 645 AA [This is the length of the unprocessed precursor] Molecular weight: 73231 Da [This is the MW of the unprocessed precursor] CRC64: 06B2B76EA3DABB9D [This is a checksum on the sequence]
        10         20         30         40         50         60 
MPRSRGGRAA PGPPPPPPPP GQAPRWSRWR VPGRLLLLLL PALCCLPGAA RAAAAAAGAG 

        70         80         90        100        110        120 
NRAAVAVAVA RADEAEAPFA GQNWLKSYGY LLPYDSRASA LHSAKALQSA VSTMQQFYGI 

       130        140        150        160        170        180 
PVTGVLDQTT IEWMKKPRCG VPDHPHLSRR RRNKRYALTG QKWRQKHITY SIHNYTPKVG 

       190        200        210        220        230        240 
ELDTRKAIRQ AFDVWQKVTP LTFEEVPYHE IKSDRKEADI MIFFASGFHG DSSPFDGEGG 

       250        260        270        280        290        300 
FLAHAYFPGP GIGGDTHFDS DEPWTLGNAN HDGNDLFLVA VHELGHALGL EHSSDPSAIM 

       310        320        330        340        350        360 
APFYQYMETH NFKLPQDDLQ GIQKIYGPPA EPLEPTRPLP TLPVRRIHSP SERKHERQPR 

       370        380        390        400        410        420 
PPRPPLGDRP STPGTKPNIC DGNFNTVALF RGEMFVFKDR WFWRLRNNRV QEGYPMQIEQ 

       430        440        450        460        470        480 
FWKGLPARID AAYERADGRF VFFKGDKYWV FKEVTVEPGY PHSLGELGSC LPREGIDTAL 

       490        500        510        520        530        540 
RWEPVGKTYF FKGERYWRYS EERRATDPGY PKPITVWKGI PQAPQGAFIS KEGYYTYFYK 

       550        560        570        580        590        600 
GRDYWKFDNQ KLSVEPGYPR NILRDWMGCN QKEVERRKER RLPQDDVDIM VTINDVPGSV 

       610        620        630        640 
NAVAVVIPCI LSLCILVLVY TIFQFKNKTG PQPVTYYKRP VQEWV 

Q9Y5R2 in FASTA format

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