Reviewed, UniProtKB/Swiss-Prot Q9Y5R2 (MMP24_HUMAN)

Names and origin

Protein names

Recommended name:
    Matrix metalloproteinase-24
      Short name=MMP-24
    EC=3.4.24.-
Alternative name(s):
    Membrane-type matrix metalloproteinase 5
      Short name=MT-MMP 5
    Membrane-type-5 matrix metalloproteinase
      Short name=MT5-MMP
Cleaved into the following chain:
    1- Recommended name:
            Processed matrix metalloproteinase-24

Gene names

Name:	MMP24
Synonyms:	MT5MMP

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	645 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	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.
Cofactor	Binds 1 zinc ion per subunit By similarity. Calcium By similarity.
Subcellular location	Cell membrane; Single-pass type I membrane protein; Extracellular side By similarity. Processed matrix metalloproteinase-24: Secreted › extracellular space › extracellular matrix By similarity. Note: Also shed from cell surface as soluble proteinase, by a proteolytic cleavage By similarity.
Tissue specificity	Predominantly expressed in brain, kidney, pancreas and lung. Overexpressed in a series of brain tumors, including astrocytomas and glioblastomas.
Domain	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.
Post-translational modification	The precursor is cleaved by a furin endopeptidase By similarity.
Sequence similarities	Belongs to the peptidase M10A family. Contains 4 hemopexin-like domains.

Ontologies

Keywords
Cellular component	Cell membrane Extracellular matrix Membrane Secreted
Coding sequence diversity	Polymorphism
Domain	Repeat Signal Transmembrane
Ligand	Calcium Metal-binding Zinc
Molecular function	Hydrolase Metalloprotease Protease
PTM	Cleavage on pair of basic residues Disulfide bond Phosphoprotein Zymogen
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	proteolysis Ref.1 Traceable author statement. Source: ProtInc
Cellular component	external side of plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to plasma membrane Ref.1 Traceable author statement. Source: ProtInc proteinaceous extracellular matrix Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	calcium ion binding Inferred from electronic annotation. Source: UniProtKB-KW enzyme activator activity Ref.1 Traceable author statement. Source: ProtInc metalloendopeptidase activity Ref.1 Traceable author statement. Source: ProtInc zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 52	52	Potential
	Propeptide	53 – 155	103	By similarity		PRO_0000028846
	Chain	156 – 645	490	Matrix metalloproteinase-24		PRO_0000028847
	Chain	156 – ?		Processed matrix metalloproteinase-24		PRO_0000302758
Regions
	Topological domain	53 – 602	550	Extracellular Potential
	Transmembrane	603 – 623	21	Potential
	Topological domain	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
	Compositional bias	149 – 152	4	Poly-Arg
Sites
	Active site	283	1	By similarity
	Metal binding	139	1	Zinc; in inhibited form By similarity
	Metal binding	282	1	Zinc; catalytic By similarity
	Metal binding	286	1	Zinc; catalytic By similarity
	Metal binding	292	1	Zinc; catalytic By similarity
Amino acid modifications
	Modified residue	629	1	Phosphothreonine Ref.4
	Disulfide bond	380 ↔ 569		By similarity
Natural variations
	Natural variant	564	1	R → H: dbSNP rs751887.		VAR_060166

Sequences

	Sequence		Length	Mass (Da)
	Q9Y5R2-1 [UniParc]. Last modified November 1, 1999. Version 1. Checksum: 06B2B76EA3DABB9D	FASTA	645	73,231
	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

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 10363975] [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: 11780052] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column." Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y. Anal. Sci. 24:161-166(2008) [PubMed: 18187866] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-629, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF131284 mRNA. Translation: AAD42962.1. AB021227 mRNA. Translation: BAA82967.1. AL121753 Genomic DNA. Translation: CAX12722.1.
IPI	IPI00001729.
RefSeq	NP_006681.1.
UniGene	Hs.567417
3D structure databases
HSSP	HSSP built from PDB template 1BQQ based on UniProtKB P50281.
SMR	Q9Y5R2. Positions 160-328.
ModBase	Search...
Protein-protein interaction databases
STRING	Q9Y5R2.
Protein family/group databases
MEROPS	M10.023.
PTM databases
PhosphoSite	Q9Y5R2.
Proteomic databases
PRIDE	Q9Y5R2.
Genome annotation databases
Ensembl	ENST00000246186; ENSP00000246186; ENSG00000125966; Homo sapiens. [Genome view]
GeneID	10893.
KEGG	hsa:10893.
NMPDR	fig|9606.3.peg.20141.
UCSC	uc002xbu.1. human.
Organism-specific databases
CTD	10893.
GeneCards	GC20P033278.
H-InvDB	HIX0019627.
HGNC	HGNC:7172. MMP24.
MIM	604871. gene.
PharmGKB	PA30881.
GenAtlas	Search...
Phylogenomic databases
HOGENOM	Q9Y5R2.
HOVERGEN	Q9Y5R2.
Gene expression databases
ArrayExpress	Q9Y5R2.
Bgee	Q9Y5R2.
CleanEx	HS_MMP24.
Genevestigator	Q9Y5R2.
GermOnline	ENSG00000125966. Homo sapiens.
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]
Gene3D	G3DSA:2.110.10.10. Hemopexin. 1 hit.
Pfam	PF00045. Hemopexin. 4 hits. PF00413. Peptidase_M10. 1 hit. PF01471. PG_binding_1. 1 hit. [Graphical view]
PIRSF	PIRSF001191. Peptidase_M10A_matrix. 1 hit.
PRINTS	PR00138. MATRIXIN.
SMART	SM00120. HX. 4 hits. SM00235. ZnMc. 1 hit. [Graphical view]
PROSITE	PS00546. CYSTEINE_SWITCH. False negative. PS00024. HEMOPEXIN. 1 hit. PS00142. ZINC_PROTEASE. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	41363.
SOURCE	Search...

Entry information

Entry name

MMP24_HUMAN

Accession

Primary (citable) accession number: Q9Y5R2
Secondary accession number(s): B7ZBG8, Q9H440

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 24, 2001
Last sequence update:	November 1, 1999
Last modified:	October 13, 2009
This is version 96 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any 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.