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Details on Person UniProt:Q02817 MUC2
| Class:Id | ReferenceGeneProduct:59703 |
|---|---|
| _chainChangeLog | signal peptide:1-20 added on Fri February 6 2015;chain:21-5179 added on Fri February 6 2015;chain:21-5179 for 59703 removed on Fri May 5 2023;chain:21-5289 for 59703 added on Fri May 5 2023 |
| _displayName | UniProt:Q02817 MUC2 |
| _timestamp | 2024-11-03 19:42:02 |
| chain | signal peptide:1-20 chain:21-5289 |
| checksum | 7AFBC09DA626F0A5 |
| comment | FUNCTION Coats the epithelia of the intestines and other mucus membrane-containing organs to provide a protective, lubricating barrier against particles and infectious agents at mucosal surfaces (PubMed:17058067, PubMed:19432394, PubMed:33031746). Major constituent of the colon mucus, which is mainly formed by large polymeric networks of MUC2 secreted by goblet cells that cover the exposed surfaces of intestine (PubMed:19432394, PubMed:33031746). MUC2 networks form hydrogels that guard the underlying epithelium from pathogens and other hazardous matter entering from the outside world, while permitting nutrient absorption and gas exchange (PubMed:33031746, PubMed:36206754). Acts as a divalent copper chaperone that protects intestinal cells from copper toxicity and facilitates nutritional copper unptake into cells (PubMed:36206754). Binds both Cu(2+) and its reduced form, Cu(1+), at two juxtaposed binding sites: Cu(2+), once reduced to Cu(1+) by vitamin C (ascorbate) or other dietary antioxidants, transits to the other binding site (PubMed:36206754). MUC2-bound Cu(1+) is protected from oxidation in aerobic environments, and can be released for nutritional delivery to cells (PubMed:36206754). Mucin gels store antimicrobial molecules that participate in innate immunity (PubMed:33031746). Mucin glycoproteins also house and feed the microbiome, lubricate tissue surfaces, and may facilitate the removal of contaminants and waste products from the body (PubMed:33031746). Goblet cells synthesize two forms of MUC2 mucin that differ in branched chain O-glycosylation and the site of production in the colon: a (1) 'thick' mucus that wraps the microbiota to form fecal pellets is produced in the proximal, ascending colon (By similarity). 'Thick' mucus transits along the descending colon and is lubricated by a (2) 'thin' MUC2 mucus produced in the distal colon which adheres to the 'thick' mucus (By similarity).SUBUNIT Homomultimer; disulfide-linked (PubMed:12374796, PubMed:31310764, PubMed:33031746, PubMed:35377815). The N- and C-terminus mediate their assembly into higher order structures to form filaments (PubMed:33031746, PubMed:35377815). 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 (PubMed:33031746). Under acidic conditions, the N-termini form non-covalent intermolecular interactions that juxtapose assemblies of the third VWD domain (VWD3) from different CTCK-linked dimers (PubMed:33031746). The VWD3 assemblies then become disulfide bonded to one another to produce long, disulfide-linked polymers that remain highly compact until secretion (PubMed:33031746). Interacts with FCGBP (PubMed:19432394). Interacts with AGR2; disulfide-linked (PubMed:19359471).SUBUNIT (Microbial infection) Interacts in vitro with L.monocytogenes internalin proteins InlB, InlC and InlJ; for InlC binding is slightly better at pH 5.5, (the pH of the intestine) than at pH 7.4.INTERACTION In the intestine, secreted into the inner and outer mucus layers (By similarity). Before secretion, mucin polymers are stored in dedicated secretory vesicles (PubMed:33031746).TISSUE SPECIFICITY Colon, small intestine, colonic tumors, bronchus, cervix and gall bladder.DOMAIN The CTCK domain mediates interchain disulfide bonds with another molecule of MUC2.PTM O-glycosylated (PubMed:11445551, PubMed:33031746). O-glycosylation is required for mucin assembly (PubMed:33031746). Goblet cells synthesize two forms of mucin that differ in branched chain O-glycosylation and the site of production in the colon (By similarity).PTM May undergo proteolytic cleavage in the outer mucus layer of the colon, contributing to the expanded volume and loose nature of this layer which allows for bacterial colonization in contrast to the inner mucus layer which is dense and devoid of bacteria.PTM At low pH of 6 and under, undergoes autocatalytic cleavage in vitro in the N-terminal region of the fourth VWD domain. It is likely that this also occurs in vivo and is triggered by the low pH of the late secretory pathway.POLYMORPHISM The number of repeats is highly polymorphic and varies among different alleles. |
| description | recommendedName: fullName evidence="21"Mucin-2 shortName evidence="20"MUC-2 alternativeName: fullName evidence="21"Intestinal mucin-2 |
| geneName | MUC2 SMUC |
| identifier | Q02817 |
| isSequenceChanged | FALSE |
| keyword | 3D-structure Autocatalytic cleavage Calcium Copper Disulfide bond Glycoprotein Phosphoprotein Proteomics identification Reference proteome Repeat Secreted Signal |
| modified | [InstanceEdit:84067] Schmidt, EE, 2003-12-18 04:29:09 [InstanceEdit:143527] Schmidt, EE, 2004-11-12 07:45:10 [InstanceEdit:217385] Schmidt, EE, 2008-03-27 06:23:53 [InstanceEdit:354386] Schmidt, EE, 2008-06-18 04:45:12 [InstanceEdit:384350] Kanapin, AA, 2008-11-26 14:00:39 [InstanceEdit:392885] Kanapin, AA, 2009-03-09 12:07:18 [InstanceEdit:400710] Schmidt, EE, 2009-03-25 05:33:35 [InstanceEdit:423310] Kanapin, AA [InstanceEdit:435478] Kanapin, AA [InstanceEdit:435871] Kanapin, AA [InstanceEdit:447347] Kanapin, AA [InstanceEdit:525883] Kanapin, AA [InstanceEdit:613449] Kanapin, AA [InstanceEdit:797602] Kanapin, AA [InstanceEdit:937368] Yung, CK [InstanceEdit:1042053] Yung, CK [InstanceEdit:1220657] Yung, CK [InstanceEdit:1300696] Yung, CK [InstanceEdit:1301627] Yung, CK [InstanceEdit:1551960] Weiser, JD [InstanceEdit:1995863] Weiser, JD [InstanceEdit:2132304] Weiser, JD [InstanceEdit:2265580] Weiser, JD [InstanceEdit:5433710] Weiser, JD [InstanceEdit:5618415] Weiser, JD [InstanceEdit:5634237] Weiser, JD [InstanceEdit:5673015] Weiser, JD [InstanceEdit:9037114] Weiser, JD [InstanceEdit:9637257] Weiser, JD [InstanceEdit:9666080] Weiser, JD [InstanceEdit:9676415] Weiser, JD [InstanceEdit:9715482] Weiser, JD [InstanceEdit:9834092] Weiser, Joel [InstanceEdit:9841277] Weiser, Joel [InstanceEdit:9852000] Weiser, Joel, 2023-11-03 [InstanceEdit:9926675] Weiser, Joel, 2024-11-03 |
| name | MUC2 |
| referenceDatabase | [ReferenceDatabase:2] UniProt |
| secondaryIdentifier | MUC2_HUMAN Q14878 |
| sequenceLength | 5289 |
| species | [Species:48887] Homo sapiens |
| (referenceEntity) | [EntityWithAccessionedSequence:913640] MUC2 [Golgi lumen] [Homo sapiens] [EntityWithAccessionedSequence:1462171] Core 7 (MUC2) [Golgi lumen] [Homo sapiens] [EntityWithAccessionedSequence:1462185] Core 6 (MUC2) [Golgi lumen] [Homo sapiens] [EntityWithAccessionedSequence:1462200] T-antigen (MUC2) [Golgi lumen] [Homo sapiens] [EntityWithAccessionedSequence:1462225] Core 5 (MUC2) [Golgi lumen] [Homo sapiens] [EntityWithAccessionedSequence:1462232] Core 2 (MUC2) [Golgi lumen] [Homo sapiens] [EntityWithAccessionedSequence:1462281] Core 4 (MUC2) [Golgi lumen] [Homo sapiens] [EntityWithAccessionedSequence:1462340] Core 8 (MUC2) [Golgi lumen] [Homo sapiens] [EntityWithAccessionedSequence:1462363] Core 3 (MUC2) [Golgi lumen] [Homo sapiens] [EntityWithAccessionedSequence:1463437] GalNAc-MUC2 [Golgi lumen] [Homo sapiens] |
| (referenceSequence) | [ModifiedResidue:913629] O-(N-acetylamino)galactosyl-L-threonine at unknown position [ModifiedResidue:913655] O-(N-acetylamino)galactosyl-L-serine at unknown position [GroupModifiedResidue:1462111] O-(N-acetylamino)galactosyl-L-serine (beta-D-Galactosyl-1,3-N-acetyl-alpha-D-galactosaminyl group) at unknown position [GroupModifiedResidue:1462125] O-(N-acetylamino)galactosyl-L-serine (GlcNAc-alpha1,3-GalNAc-alpha group) at unknown position [GroupModifiedResidue:1462126] O-(N-acetylamino)galactosyl-L-serine (GlcNAc-beta1,6-GalNAc-alpha group) at unknown position [GroupModifiedResidue:1462169] O-(N-acetylamino)galactosyl-L-serine (GlcNAc-beta1,3(GlcNAc-beta1,6)GalNac-alpha group) at unknown position [GroupModifiedResidue:1462210] O-(N-acetylamino)galactosyl-L-serine (GlcNAc-beta1,3-GalNAc-alpha group) at unknown position [GroupModifiedResidue:1462237] O-(N-acetylamino)galactosyl-L-serine (Gal-beta1,3(GlcNAc-beta1,6)GalNAc-alpha group) at unknown position [GroupModifiedResidue:1462275] O-(N-acetylamino)galactosyl-L-serine (GalNAc-alpha1,6-GalNAc-alpha group) at unknown position [GroupModifiedResidue:1462360] O-(N-acetylamino)galactosyl-L-serine (Gal-alpha1,3-GalNAc-alpha group) at unknown position |
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No pathways have been reviewed or authored by UniProt:Q02817 MUC2 (59703)
