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

 MMP24_RAT               Reviewed;         618 AA.
Q99PW6;
23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
01-JUN-2001, sequence version 1.
20-JUN-2018, entry version 125.
RecName: Full=Matrix metalloproteinase-24;
Short=MMP-24;
EC=3.4.24.-;
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=Mt5mmp;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Brain;
Sekine-Aizawa Y.;
"Molecular cloning and characterization of rat MT5-MMP.";
Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases.
[2]
TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
PubMed=10727639; DOI=10.1016/S0006-8993(00)02035-7;
Jaworski D.M.;
"Developmental regulation of membrane type-5 matrix metalloproteinase
(MT5-MMP) expression in the rat nervous system.";
Brain Res. 860:174-177(2000).
[3]
FUNCTION, SUBCELLULAR LOCATION, PROTEOLYTIC PROCESSING, INTERACTION
WITH GRIP1 AND GRIP2, AND MUTAGENESIS OF 616-GLU--VAL-618.
PubMed=16495457; DOI=10.1523/JNEUROSCI.3521-05.2006;
Monea S., Jordan B.A., Srivastava S., DeSouza S., Ziff E.B.;
"Membrane localization of membrane type 5 matrix metalloproteinase by
AMPA receptor binding protein and cleavage of cadherins.";
J. Neurosci. 26:2300-2312(2006).
-!- FUNCTION: 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.
{ECO:0000269|PubMed:16495457}.
-!- 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 (via PDZ-binding motif) with APBA3 (via PDZ
domain) (By similarity). Interacts with GRIP1 and GRIP2.
{ECO:0000250, ECO:0000269|PubMed:16495457}.
-!- SUBCELLULAR LOCATION: Matrix metalloproteinase-24: Cell membrane;
Single-pass type I membrane protein. Golgi apparatus, trans-Golgi
network membrane {ECO:0000250}; Single-pass type I membrane
protein {ECO:0000250}. Note=Recycled back to the plasma membrane
through the trans-Golgi network via interaction with APBA3.
{ECO:0000250}.
-!- SUBCELLULAR LOCATION: Processed matrix metalloproteinase-24:
Secreted, extracellular space, extracellular matrix {ECO:0000250}.
Note=Also shed from cell surface as soluble proteinase, by a
proteolytic cleavage. {ECO:0000250}.
-!- TISSUE SPECIFICITY: Predominantly expressed in the nervous system:
while enriched in the central nervous system, expression is also
detected in the peripheral nervous system, including the
trigeminal ganglion. Expression is not restricted to the nervous
system: it is also enriched in the thymus, with a lower level of
expression present in the aorta. In brain, high expression is
present in the brain parenchyma, particularly within the
neocortex. {ECO:0000269|PubMed:10727639}.
-!- DEVELOPMENTAL STAGE: Expression is first detected in embryonic day
16 (E16) brain, strongly increases at E20, and peaks at postnatal
day 0 (P0), within 24 hours of birth. The postnatal expression
declines steadily to reach adult levels at P60.
{ECO:0000269|PubMed:10727639}.
-!- 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:16495457}.
-!- 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.
-!- PTM: Cleaved by a furin endopeptidase in the trans-Golgi network.
-!- SIMILARITY: Belongs to the peptidase M10A family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AB023659; BAB32589.1; -; mRNA.
RefSeq; NP_113945.1; NM_031757.1.
UniGene; Rn.3117; -.
ProteinModelPortal; Q99PW6; -.
SMR; Q99PW6; -.
STRING; 10116.ENSRNOP00000067398; -.
MEROPS; M10.023; -.
PhosphoSitePlus; Q99PW6; -.
PaxDb; Q99PW6; -.
PRIDE; Q99PW6; -.
GeneID; 83513; -.
KEGG; rno:83513; -.
CTD; 10893; -.
RGD; 620202; Mmp24.
eggNOG; KOG1565; Eukaryota.
eggNOG; ENOG410XQ5D; LUCA.
HOVERGEN; HBG052484; -.
InParanoid; Q99PW6; -.
KO; K08002; -.
PhylomeDB; Q99PW6; -.
PRO; PR:Q99PW6; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0031012; C:extracellular matrix; IEA:InterPro.
GO; GO:0016021; C:integral component of membrane; TAS:RGD.
GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
GO; GO:0032588; C:trans-Golgi network membrane; ISS:UniProtKB.
GO; GO:0004222; F:metalloendopeptidase activity; ISS:UniProtKB.
GO; GO:0008233; F:peptidase activity; TAS:RGD.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0044331; P:cell-cell adhesion mediated by cadherin; ISS:UniProtKB.
GO; GO:0098742; P:cell-cell adhesion via plasma-membrane adhesion molecules; ISS:UniProtKB.
GO; GO:0050965; P:detection of temperature stimulus involved in sensory perception of pain; ISS:UniProtKB.
GO; GO:0010001; P:glial cell differentiation; ISS:UniProtKB.
GO; GO:0097150; P:neuronal stem cell population maintenance; ISS:UniProtKB.
GO; GO:0006508; P:proteolysis; ISS: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_0000028850.
CHAIN 129 618 Matrix metalloproteinase-24.
/FTId=PRO_0000028851.
CHAIN 129 554 Processed matrix metalloproteinase-24.
{ECO:0000250}.
/FTId=PRO_0000302760.
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.
ACT_SITE 256 256 {ECO:0000255|PROSITE-ProRule:PRU10095}.
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. {ECO:0000250}.
DISULFID 353 542 {ECO:0000250}.
MUTAGEN 616 618 Missing: Impaired interaction with GRIP1
and GRIP2. {ECO:0000269|PubMed:16495457}.
SEQUENCE 618 AA; 70465 MW; 614ED4EEC6B27F5F CRC64;
MPRSRGGRAA PGQAARWSGW 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 QPRPPRPPLG 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
KTGPQPVTYY KRPVQEWV


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