Search by BoMiProt ID - Bomi6978

Primary Information

BoMiProt ID Bomi6978
Protein Name Matrix metalloproteinase-23
Organism Bos taurus
Uniprot IdQ2TBM7
Milk Fractionwhey
Ref Sequence Id NP_001033645.1
Aminoacid Length 393
Molecular Weight 43964
Fasta Sequence
Gene Name MMP23
Gene Id 527590
Protein Existence Status Reviewed

Secondary Information

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
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.
Significance in milk able to degrade the extracellular matrix, triggering the involution and immune function of cow mammary gland.
PTMs N-glycosylation,Proteolytic cleavage
Site(s) of PTM(s)

N-glycosylation, O-glycosylation,
Predicted Disorder Regions 7-13, 65-79, 305-308
DisProt Annotation
TM Helix Prediction 1TMH; (21-39)
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.
Linking IDs
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). 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.