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Reviewed (UniProtKB/Swiss-Prot)

Note: Proteins listed in ProtBank™ database are NOT off-the-shelf [catalog] proteins. Customized protein production request can be made for any protein in this database by clicking on the corresponding button under "Quick Quote". Please ensure sequence accuracy and/or make any necessary modifications prior to submitting your quote request

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Reviewed (UniProtKB/Swiss-Prot)


Name Gene Symbol Rec Full Name Protein Information Quick Quote  Price,
Turnaround
MMP24_RAT, Rattus norvegicus (Norway rat) Mmp24 Membrane-type-5 matrix metalloproteinase Functions
wild_type
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Protein Domains
mutant
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Protein Names | ProteinIDs  | Organism | Gene Names  | GeneID | Genome Annotation(Ensembl) |  Protein Sequence | 
General annotation |  References | Order
Protein Names
Recommended name:
 Matrix metalloproteinase-24;
Alternative name(s):
 Membrane-type matrix metalloproteinase 5
Membrane-type-5 matrix metalloproteinase
Processed matrix metalloproteinase-24
Protein IDs
(Accession numbers)
UniProtKB
 Q99PW6
NCBI RefSeq

NP_113945.1, NM_031757.1.
Organism
Latin Name/
(Common Name)
Rattus norvegicus (Rat).
Taxonomic Identifier (NCBI)
 10116
Gene Names
 Mmp24 [GenPool]
GeneID

83513
Genome
Annotation (Ensembl)
Protein Sequence
 
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
General annotation
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
 Calcium (By similarity).
Subunit structure
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
Induction
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 (Bysimilarity).
Involvement in disease

References

  • "Molecular cloning and characterization of rat MT5-MMP.";,Sekine-Aizawa Y.;,Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases.

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Protein Domain Databases | 3D Structure Database  | Sequence Annotation | Protein-protein Interaction Databases  | 
Binary Interactions | Enzyme and Pathway Databases |  Phylogenomic Database | Proteomics Database | 
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Protein Domain Databases
InterPro

IPR000585, Hemopexin/matrixin.

IPR018486, Hemopexin/matrixin_CS.

IPR018487, Hemopexin/matrixin_repeat.

IPR001818, Pept_M10_metallopeptidase.

IPR016293, Pept_M10A_matrix_strom.

IPR021190, Pept_M10A_matrixin.

IPR021805, Pept_M10A_metallopeptidase_C.

IPR006026, Peptidase_Metallo.

IPR002477, Peptidoglycan-bd-like.
Gene3D

G3DSA:2.110.10.10, Hemopexin; 1.
PANTHER
Pfam

PF11857, DUF3377; 1.

PF00045, Hemopexin; 4.

PF00413, Peptidase_M10; 1.

PF01471, PG_binding_1; 1.
PRINTS

PR00138, MATRIXIN.
SUPFAM

SSF50923, Hemopexin; 1.

SSF47090, PGBD_like; 1.
PROSITE

PS00024, HEMOPEXIN; 1.

PS00142, ZINC_PROTEASE; 1.
3D Structure
Database (PDB)
Entry
Method
Resolution (A)
Chain
Positions
PDBsum
Sequence
Annotation
Feature key
Position(s)
Length
Description
Signal sequence 1 - 41 41 Potential.
Propeptide 42 - 128 87 By similarity. /FTId=PRO_0000028850.
Polypeptide chain 129 - 618 490 Matrix metalloproteinase-24. /FTId=PRO_0000028851.
Polypeptide chain 129 - ? -128 Processed matrix metalloproteinase-24. /FTId=PRO_0000302760.
Topological domain 42 - 575 534 Extracellular (Potential).
Topological domain 597 - 618 22 Cytoplasmic (Potential).
Transmembrane region 576 - 596 21 Helical; (Potential).
Domain 357 - 400 44 Hemopexin-like 1.
Domain 402 - 446 45 Hemopexin-like 2.
Domain 449 - 495 47 Hemopexin-like 3.
Domain 497 - 542 46 Hemopexin-like 4.
Sequence motif 110 - 117 8 Cysteine switch (By similarity).
Amino acid(s) 256 1 By similarity.
Metal ion 112 1 Zinc; in inhibited form (By similarity).
Metal ion 255 1 Zinc; catalytic (By similarity).
Metal ion 259 1 Zinc; catalytic (By similarity).
Metal ion 265 1 Zinc; catalytic (By similarity).
Posttranslational modification of a residue 602 1 Phosphothreonine (By similarity).
Disulfide bond 353 - 542 190 By similarity.
Protein-protein
Interaction
Databases
DIP
IntAct
MINT
STRING
Binary Interactions
With
Entry
#Exp.
IntAct
Enzyme and Pathway Databases
Pathway
Interaction DB
Reactome
Phylogenomic Database
HOVERGEN

HBG052484
InParanoid
OMA
OrthoDB
Proteomics
Database (PRIDE)
Comparative
Toxicogenomics
Database (CTD)

10893
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