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Details on Person UniProt:P98088 MUC5AC
Class:Id
ReferenceGeneProduct:59697
_chainChangeLog
signal peptide:1-27 added on Fri February 6 2015;chain:28-5030 added on Fri February 6 2015;chain:28-5030 removed on Fri May 8 2015;chain:28-5654 added on Fri May 8 2015
_displayName
UniProt:P98088 MUC5AC
_timestamp
2024-11-03 19:42:04
chain
signal peptide:1-27 chain:28-5654
checksum
13217A8257E8E2DE
comment
FUNCTION Gel-forming glycoprotein of gastric and respiratory tract epithelia that protects the mucosa from infection and chemical damage by binding to inhaled microorganisms and particles that are subsequently removed by the mucociliary system (PubMed:14535999, PubMed:14718370). Interacts with H.pylori in the gastric epithelium, Barrett's esophagus as well as in gastric metaplasia of the duodenum (GMD) (PubMed:14535999).SUBUNIT Homomultimer; disulfide-linked (PubMed:14718370). The N- and C-terminus mediate their assembly into higher order structures to form filaments (By similarity). The CTCK domains of two polypeptides associate in the endoplasmic reticulum to generate intermolecularly disulfide-bonded dimers (By similarity). These dimers progress to the Golgi apparatus, which is a more acidic environment than the endoplasmic reticulum. Under acidic conditions, the N-termini form non-covalent intermolecular interactions that juxtapose assemblies from different CTCK-linked dimers to produce long, disulfide-linked polymers that remain highly compact until secretion (By similarity).SUBCELLULAR LOCATION Highly expressed in surface mucosal cells of respiratory tract and stomach epithelia. Overexpressed in a number of carcinomas. Also expressed in Barrett's esophagus epithelium and in the proximal duodenum.DEVELOPMENTAL STAGE In airway epithelial cells, expression increases significantly during cell differentiation (at protein level).INDUCTION By IL4.DOMAIN The cysteine residues in the Cys-rich subdomain repeats are not involved in disulfide bonding.DOMAIN The CTCK domain mediates interchain disulfide bonds with another molecule of MUC5AC.PTM C-, O- and N-glycosylated (PubMed:14718370). O-glycosylated on the second and last Thr of the Thr-/Ser-rich tandem repeats TTPSPVPTTSTTSA (PubMed:14718370, PubMed:22186971, PubMed:25939779). One form of glycosylation is also known as Lewis B (LeB) blood group antigen, a tetrasaccharide consisting of N-acetylglucosamine having a fucosyl residue attached (PubMed:14535999). It has a role as an epitope and antigen and functions as a receptor for H.pylori binding and facilitates infection (PubMed:14535999). C-mannosylation in the Cys-rich subdomains may be required for proper folding of these regions and for export from the endoplasmic reticulum during biosynthesis (PubMed:14718370).PTM Proteolytic cleavage in the C-terminal is initiated early in the secretory pathway and does not involve a serine protease. The extent of cleavage is increased in the acidic parts of the secretory pathway. Cleavage generates a reactive group which could link the protein to a primary amide.SEQUENCE CAUTION Truncated C-terminus.
3D-structure Copper Direct protein sequencing Disulfide bond Glycoprotein Metal-binding Proteomics identification Reference proteome Repeat Secreted Signal
