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Matrix metalloproteinase-24 (MMP-24) (EC 3.4.24.-) (Matrix metalloproteinase-21) (MMP-21) (Membrane-type matrix metalloproteinase 5) (MT-MMP 5) (MTMMP5) (Membrane-type-5 matrix metalloproteinase) (MT5-MMP) (MT5MMP) [Cleaved into: Processed matrix metalloproteinase-24]

 MMP24_MOUSE             Reviewed;         618 AA.
Q9R0S2; A2AUV7; Q9Z0J9;
24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
27-JUL-2011, sequence version 2.
05-DEC-2018, entry version 163.
RecName: Full=Matrix metalloproteinase-24;
Short=MMP-24;
EC=3.4.24.-;
AltName: Full=Matrix metalloproteinase-21;
Short=MMP-21;
AltName: Full=Membrane-type matrix metalloproteinase 5;
Short=MT-MMP 5;
Short=MTMMP5;
AltName: Full=Membrane-type-5 matrix metalloproteinase;
Short=MT5-MMP;
Short=MT5MMP;
Contains:
RecName: Full=Processed matrix metalloproteinase-24;
Flags: Precursor;
Name=Mmp24; Synonyms=Mmp21, Mt5mmp;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
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.
[2]
NUCLEOTIDE SEQUENCE [MRNA], MUTAGENESIS OF GLU-256, AND ACTIVE SITE.
STRAIN=BALB/cJ; TISSUE=Brain;
PubMed=10085137; DOI=10.1074/jbc.274.13.8925;
Pei D.Q.;
"Identification and characterization of the fifth membrane-type matrix
metalloproteinase MT5-MMP.";
J. Biol. Chem. 274:8925-8932(1999).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[4]
FUNCTION.
PubMed=10622708; DOI=10.1016/S0014-5793(99)01534-3;
Wang X., Yi J., Lei J., Pei D.Q.;
"Expression, purification and characterization of recombinant mouse
MT5-MMP protein products.";
FEBS Lett. 462:261-266(1999).
[5]
SUBCELLULAR LOCATION, PROTEOLYTIC PROCESSING, AND MUTAGENESIS OF
GLU-256 AND 549-ARG--ARG-555.
PubMed=11470782; DOI=10.1074/jbc.M103680200;
Wang X., Pei D.;
"Shedding of membrane type matrix metalloproteinase 5 by a furin-type
convertase: a potential mechanism for down-regulation.";
J. Biol. Chem. 276:35953-35960(2001).
[6]
FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
PubMed=11714638;
Hayashita-Kinoh H., Kinoh H., Okada A., Komori K., Itoh Y., Chiba T.,
Kajita M., Yana I., Seiki M.;
"Membrane-type 5 matrix metalloproteinase is expressed in
differentiated neurons and regulates axonal growth.";
Cell Growth Differ. 12:573-580(2001).
[7]
SUBCELLULAR LOCATION, INTERACTION WITH APBA3, AND MUTAGENESIS OF
616-GLU--VAL-618.
PubMed=14990567; DOI=10.1074/jbc.M400264200;
Wang P., Wang X., Pei D.;
"Mint-3 regulates the retrieval of the internalized membrane-type
matrix metalloproteinase, MT5-MMP, to the plasma membrane by binding
to its carboxyl end motif EWV.";
J. Biol. Chem. 279:20461-20470(2004).
[8]
FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
PubMed=19805319; DOI=10.1073/pnas.0908507106;
Folgueras A.R., Valdes-Sanchez T., Llano E., Menendez L., Baamonde A.,
Denlinger B.L., Belmonte C., Juarez L., Lastra A., Garcia-Suarez O.,
Astudillo A., Kirstein M., Pendas A.M., Farinas I., Lopez-Otin C.;
"Metalloproteinase MT5-MMP is an essential modulator of neuro-immune
interactions in thermal pain stimulation.";
Proc. Natl. Acad. Sci. U.S.A. 106:16451-16456(2009).
[9]
FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
PubMed=24952463; DOI=10.1038/ncb2993;
Porlan E., Marti-Prado B., Morante-Redolat J.M., Consiglio A.,
Delgado A.C., Kypta R., Lopez-Otin C., Kirstein M., Farinas I.;
"MT5-MMP regulates adult neural stem cell functional quiescence
through the cleavage of N-cadherin.";
Nat. Cell Biol. 16:629-638(2014).
-!- FUNCTION: 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).
{ECO:0000269|PubMed:10622708, ECO:0000269|PubMed:11714638,
ECO:0000269|PubMed:19805319, ECO:0000269|PubMed:24952463}.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
Note=Binds 1 zinc ion per subunit. {ECO:0000250};
-!- COFACTOR:
Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
-!- SUBUNIT: Interacts with GRIP1 and GRIP2 (By similarity). Interacts
(via PDZ-binding motif) with APBA3 (via PDZ domain). {ECO:0000250,
ECO:0000269|PubMed:14990567}.
-!- SUBCELLULAR LOCATION: Matrix metalloproteinase-24: Cell membrane;
Single-pass type I membrane protein. Golgi apparatus, trans-Golgi
network membrane; Single-pass type I membrane protein.
Note=Recycled back to the plasma membrane through the trans-Golgi
network via interaction with APBA3. {ECO:0000269|PubMed:14990567}.
-!- SUBCELLULAR LOCATION: Processed matrix metalloproteinase-24:
Secreted, extracellular space, extracellular matrix. Note=Also
shed from cell surface as soluble proteinase, by a proteolytic
cleavage. {ECO:0000269|PubMed:11470782}.
-!- TISSUE SPECIFICITY: 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.
{ECO:0000269|PubMed:11714638, ECO:0000269|PubMed:19805319,
ECO:0000269|PubMed:24952463}.
-!- DEVELOPMENTAL STAGE: 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. {ECO:0000269|PubMed:11714638}.
-!- 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.
-!- DOMAIN: The PDZ-binding motif (also named EWV motif) is required
for interaction with PDZ domains of APBA3 and recycling through
the trans-Golgi network. {ECO:0000269|PubMed:14990567}.
-!- PTM: Cleaved by a furin endopeptidase in the trans-Golgi network.
-!- DISRUPTION PHENOTYPE: 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). {ECO:0000269|PubMed:19805319,
ECO:0000269|PubMed:24952463}.
-!- SIMILARITY: Belongs to the peptidase M10A family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AB021226; BAA82966.1; -; mRNA.
EMBL; AJ010262; CAA09055.1; -; mRNA.
EMBL; AL929233; -; NOT_ANNOTATED_CDS; Genomic_DNA.
CCDS; CCDS16955.1; -.
RefSeq; NP_034938.3; NM_010808.4.
UniGene; Mm.389325; -.
ProteinModelPortal; Q9R0S2; -.
SMR; Q9R0S2; -.
STRING; 10090.ENSMUSP00000029141; -.
MEROPS; M10.023; -.
iPTMnet; Q9R0S2; -.
PhosphoSitePlus; Q9R0S2; -.
MaxQB; Q9R0S2; -.
PaxDb; Q9R0S2; -.
PRIDE; Q9R0S2; -.
Ensembl; ENSMUST00000029141; ENSMUSP00000029141; ENSMUSG00000027612.
GeneID; 17391; -.
KEGG; mmu:17391; -.
UCSC; uc008nlj.1; mouse.
CTD; 10893; -.
MGI; MGI:1341867; Mmp24.
eggNOG; KOG1565; Eukaryota.
eggNOG; ENOG410XQ5D; LUCA.
GeneTree; ENSGT00940000158315; -.
HOGENOM; HOG000217928; -.
HOVERGEN; HBG052484; -.
InParanoid; Q9R0S2; -.
KO; K08002; -.
OMA; GYPHSLV; -.
OrthoDB; EOG091G03DP; -.
TreeFam; TF352396; -.
Reactome; R-MMU-1592389; Activation of Matrix Metalloproteinases.
ChiTaRS; Mmp24; mouse.
PMAP-CutDB; Q9R0S2; -.
PRO; PR:Q9R0S2; -.
Proteomes; UP000000589; Chromosome 2.
Bgee; ENSMUSG00000027612; Expressed in 176 organ(s), highest expression level in cerebellum.
CleanEx; MM_MMP21; -.
CleanEx; MM_MMP24; -.
Genevisible; Q9R0S2; MM.
GO; GO:0031012; C:extracellular matrix; IEA:InterPro.
GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
GO; GO:0032588; C:trans-Golgi network membrane; IDA:UniProtKB.
GO; GO:0045296; F:cadherin binding; IPI:UniProtKB.
GO; GO:0004222; F:metalloendopeptidase activity; IDA:UniProtKB.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0044331; P:cell-cell adhesion mediated by cadherin; IDA:UniProtKB.
GO; GO:0098742; P:cell-cell adhesion via plasma-membrane adhesion molecules; IMP:UniProtKB.
GO; GO:0050965; P:detection of temperature stimulus involved in sensory perception of pain; IMP:UniProtKB.
GO; GO:0010001; P:glial cell differentiation; IDA:UniProtKB.
GO; GO:0097150; P:neuronal stem cell population maintenance; IDA:UniProtKB.
GO; GO:0006508; P:proteolysis; IMP:UniProtKB.
CDD; cd00094; HX; 1.
CDD; cd04278; ZnMc_MMP; 1.
Gene3D; 2.110.10.10; -; 1.
Gene3D; 3.40.390.10; -; 1.
InterPro; IPR000585; Hemopexin-like_dom.
InterPro; IPR036375; Hemopexin-like_dom_sf.
InterPro; IPR018487; Hemopexin-like_repeat.
InterPro; IPR018486; Hemopexin_CS.
InterPro; IPR033739; M10A_MMP.
InterPro; IPR024079; MetalloPept_cat_dom_sf.
InterPro; IPR028723; MMP24.
InterPro; IPR001818; Pept_M10_metallopeptidase.
InterPro; IPR021190; Pept_M10A.
InterPro; IPR021805; Pept_M10A_metallopeptidase_C.
InterPro; IPR006026; Peptidase_Metallo.
InterPro; IPR002477; Peptidoglycan-bd-like.
InterPro; IPR036365; PGBD-like_sf.
PANTHER; PTHR10201:SF138; PTHR10201:SF138; 1.
Pfam; PF11857; DUF3377; 1.
Pfam; PF00045; Hemopexin; 4.
Pfam; PF00413; Peptidase_M10; 1.
Pfam; PF01471; PG_binding_1; 1.
PIRSF; PIRSF001191; Peptidase_M10A_matrix; 1.
PRINTS; PR00138; MATRIXIN.
SMART; SM00120; HX; 4.
SMART; SM00235; ZnMc; 1.
SUPFAM; SSF47090; SSF47090; 1.
SUPFAM; SSF50923; SSF50923; 1.
PROSITE; PS00024; HEMOPEXIN; 1.
PROSITE; PS51642; HEMOPEXIN_2; 4.
PROSITE; PS00142; ZINC_PROTEASE; 1.
1: Evidence at protein level;
Calcium; Cell adhesion; Cell membrane;
Cleavage on pair of basic residues; Complete proteome; Disulfide bond;
Extracellular matrix; Golgi apparatus; Hydrolase; Membrane;
Metal-binding; Metalloprotease; Protease; Reference proteome; Repeat;
Secreted; Signal; Transmembrane; Transmembrane helix; Zinc; Zymogen.
SIGNAL 1 41 {ECO:0000255}.
PROPEP 42 128 {ECO:0000250}.
/FTId=PRO_0000028848.
CHAIN 129 618 Matrix metalloproteinase-24.
/FTId=PRO_0000028849.
CHAIN 129 554 Processed matrix metalloproteinase-24.
{ECO:0000305}.
/FTId=PRO_0000302759.
TOPO_DOM 42 575 Extracellular. {ECO:0000255}.
TRANSMEM 576 596 Helical. {ECO:0000255}.
TOPO_DOM 597 618 Cytoplasmic. {ECO:0000255}.
REPEAT 350 398 Hemopexin 1.
REPEAT 399 444 Hemopexin 2.
REPEAT 446 494 Hemopexin 3.
REPEAT 495 542 Hemopexin 4.
MOTIF 110 117 Cysteine switch. {ECO:0000250}.
MOTIF 616 618 PDZ-binding.
COMPBIAS 122 125 Poly-Arg.
ACT_SITE 256 256 {ECO:0000255|PROSITE-ProRule:PRU10095,
ECO:0000269|PubMed:10085137}.
METAL 112 112 Zinc; in inhibited form. {ECO:0000250}.
METAL 255 255 Zinc; catalytic. {ECO:0000255|PROSITE-
ProRule:PRU10095}.
METAL 259 259 Zinc; catalytic. {ECO:0000255|PROSITE-
ProRule:PRU10095}.
METAL 265 265 Zinc; catalytic. {ECO:0000255|PROSITE-
ProRule:PRU10095}.
SITE 554 555 Cleavage; by furin.
DISULFID 353 542 {ECO:0000250}.
MUTAGEN 256 256 E->A: Loss of function. Does not prevent
proteolytic processing.
{ECO:0000269|PubMed:10085137,
ECO:0000269|PubMed:11470782}.
MUTAGEN 549 554 Missing: Abolishes proteolytic
processing. Gain of function mutant.
MUTAGEN 616 618 Missing: Impaired recycling affecting its
internalization, leading to decreased
activity on the plasma surface.
{ECO:0000269|PubMed:14990567}.
CONFLICT 7 28 GRAAPGQASRWSGWRAPGRLLP -> AALRRARPRAGALAG
PGAAA (in Ref. 2; CAA09055).
{ECO:0000305}.
CONFLICT 44 50 KPAGADA -> SRPGR (in Ref. 2; CAA09055).
{ECO:0000305}.
CONFLICT 46 46 A -> T (in Ref. 1; BAA82966).
{ECO:0000305}.
CONFLICT 306 308 LEP -> SGA (in Ref. 2; CAA09055).
{ECO:0000305}.
CONFLICT 326 326 R -> K (in Ref. 2; CAA09055).
{ECO:0000305}.
CONFLICT 337 341 PPLGD -> RPWG (in Ref. 2; CAA09055).
{ECO:0000305}.
CONFLICT 449 449 I -> KP (in Ref. 2; CAA09055).
{ECO:0000305}.
CONFLICT 502 502 I -> L (in Ref. 2; CAA09055).
{ECO:0000305}.
CONFLICT 589 589 L -> R (in Ref. 2; CAA09055).
{ECO:0000305}.
SEQUENCE 618 AA; 70460 MW; 51C8E61B187264F5 CRC64;
MPRSRGGRAA PGQASRWSGW RAPGRLLPLL PALCCLAAAA GAGKPAGADA PFAGQNWLKS
YGYLLPYESR ASALHSGKAL QSAVSTMQQF YGIPVTGVLD QTTIEWMKKP RCGVPDHPHL
SRRRRNKRYA LTGQKWRQKH ITYSIHNYTP KVGELDTRKA IRQAFDVWQK VTPLTFEEVP
YHEIKSDRKE ADIMIFFASG FHGDSSPFDG EGGFLAHAYF PGPGIGGDTH FDSDEPWTLG
NANHDGNDLF LVAVHELGHA LGLEHSNDPS AIMAPFYQYM ETHNFKLPQD DLQGIQKIYG
PPAEPLEPTR PLPTLPVRRI HSPSERKHER HPRPPRPPLG DRPSTPGAKP NICDGNFNTV
ALFRGEMFVF KDRWFWRLRN NRVQEGYPMQ IEQFWKGLPA RIDAAYERAD GRFVFFKGDK
YWVFKEVTVE PGYPHSLGEL GSCLPREGID TALRWEPVGK TYFFKGERYW RYSEERRATD
PGYPKPITVW KGIPQAPQGA FISKEGYYTY FYKGRDYWKF DNQKLSVEPG YPRNILRDWM
GCKQKEVERR KERRLPQDDV DIMVTIDDVP GSVNAVAVVV PCTLSLCLLV LLYTIFQFKN
KAGPQPVTYY KRPVQEWV


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