Primary Information |
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| BoMiProt ID | Bomi6978 |
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| Protein Name | Matrix metalloproteinase-23 |
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| Organism | Bos taurus |
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| Uniprot ID | Q2TBM7 |
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| Milk Fraction | whey |
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| Ref Sequence ID | NP_001033645.1 |
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| Aminoacid Length | 393 |
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| Molecular Weight | 43964 |
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| FASTA Sequence |
Download |
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| Gene Name | MMP23 |
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| Gene ID | 527590 |
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| Protein Existence Status | Reviewed |
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Secondary Information |
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| Protein Function | These are zinc-dependent endopeptidases that function at neutral pH to degrade extracellular matrix proteins, cleave cell-surface receptors, release apoptotic ligands, and activate chemokines and cytokines.Involved in a wide range of cellular processes, including tissue remodeling, cell proliferation, cell migration, differentiation, angiogenesis, apoptosis, and the immune response |
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| Biochemical Properties | MMP23 is a membrane-anchored protein of 391 amino acid residues and four separate domains.The N-terminal pro-domain of MMP23 lacks the enzymatic inhibitory sequence motif and folded globular structure.known to modulate voltage-gated potassium (Kv1) activity by regulating the intracellular trafficking of the channels. MMP23 also contains a toxin-like domain (TxD) that has been shown to block Kv1 channels. In addition, the C-terminal hemopexin domain common to other MMPs is replaced by an immunoglobulin-like cell adhesion molecule (IgCAM) domain of unknown function in MMP23.The highly conserved pro-domain possesses a ‘cysteine-switch’ motif (PRCGXPD) containing a cysteine residue that coordinates with the catalytic zinc ion.They have a common architecture comprised of three α-helices and a five-stranded β-sheet, and typically contain four metal ions (two calcium and two zinc) in highly conserved calcium- and zinc-binding sites. |
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| Significance in milk | able to degrade the extracellular matrix, triggering the involution and immune function of cow mammary gland. |
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| PTMs | N-glycosylation,Proteolytic cleavage |
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Site(s) of PTM(s)
N-glycosylation,
O-glycosylation,
Phosphorylation
| >sp|Q2TBM7|MMP23_BOVIN Matrix metalloproteinase-23 OS=Bos taurus OX=9913 GN=MMP23 PE=2 SV=1
MGRGACVPSAASGAGDRARQLGAVLGALCLFPALVLLAWPGTPANGAGARVAQGDAAPQT
SGVLASGSLGPPHPPVPRRRRYTLTPARLRWEHFN*95LTYKILSFPRNLLSPSETRRGLAAA
FRMWSDVSPFSFREVAPEQPSDLRIGFYPVN*151HTDCLVSPLHHCFDGPTGELAHAFFPPHG
GIHFDDSEYWVLGRTRYSWKKGVWLTDLVHVAAHEIGHALGLMHSQHGRALMHLN*235ATLRG
WKALSQDELWGLHRLYGCLDRLFVCASWARRGFCDTRRRLMKRLCPSSCDFCYEFPFPTV
AATPPPPRTKTKLVPEGRN*319VTFRCGQKILHKKGKVYWYKDQEPLEFSYPGYLALGEAHLS
IIANAINEGTYTCVVRRRQRVLSTYSWRIRVRS
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| Predicted Disorder Regions | 7-13, 65-79, 305-308 |
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| DisProt Annotation | |
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| TM Helix Prediction | 1TMH; (21-39) |
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| Significance of PTMs | Regulated by a single proteolytic cleavage for both activation and secretion. It is a type II membrane-anchored zymogen that is proteolytically processed at a conserved motif and converted into a secretory and mature enzyme.From N-terminal sequencing,it has been reported that L20GAALSGLCLLSALALL36 is retained with CA-MMP as a signal-anchor.N-glycosylated, is important for protein residing in the lumen of the secretory pathway.There are 4 N-glycosylation sites (Asn93, Asn149, Asn233, and Asn317)-are located downstream of the signal anchor,the carboxyl side must reside in the lumen in order to beingN-glycosylated. |
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| Linking IDs | |
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| Bibliography | 1.Galea, C.A., Nguyen, H.M., George Chandy, K. et al. Domain structure and function of matrix metalloprotease 23 (MMP23): role in potassium channel trafficking. Cell. Mol. Life Sci. 71, 1191–1210 (2014). https://doi.org/10.1007/s00018-013-1431-0 2.Pei D, Kang T, Qi H. Cysteine array matrix metalloproteinase (CA-MMP)/MMP-23 is a type II transmembrane matrix metalloproteinase regulated by a single cleavage for both secretion and activation. J Biol Chem. 2000 Oct 27;275(43):33988-97. doi: 10.1074/jbc.M006493200. PMID: 10945999. |
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