{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"Q02817","secondaryAccessions":["Q14878"],"uniProtkbId":"MUC2_HUMAN","entryAudit":{"firstPublicDate":"1994-06-01","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2023-02-22","entryVersion":200,"sequenceVersion":3},"annotationScore":5.0,"organism":{"scientificName":"Homo sapiens","commonName":"Human","taxonId":9606,"lineage":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"8300571"}],"value":"Mucin-2"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"1885763"}],"value":"MUC-2"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"8300571"}],"value":"Intestinal mucin-2"}}],"flag":"Precursor"},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"8300571"},{"evidenceCode":"ECO:0000312","source":"HGNC","id":"HGNC:7512"}],"value":"MUC2"},"synonyms":[{"value":"SMUC"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q80Z19"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17058067"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19432394"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33031746"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"36206754"}],"value":"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)"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q9HC84"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12374796"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19359471"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19432394"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"31310764"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33031746"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"35377815"}],"value":"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)"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18327567"}],"value":"(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"}],"commentType":"SUBUNIT"},{"commentType":"INTERACTION","interactions":[{"interactantOne":{"uniProtKBAccession":"Q02817","intActId":"EBI-2105803"},"interactantTwo":{"uniProtKBAccession":"O95994","geneName":"AGR2","intActId":"EBI-712648"},"numberOfExperiments":3,"organismDiffer":false}]},{"commentType":"SUBCELLULAR LOCATION","note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q80Z19"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"33031746"}],"value":"In the intestine, secreted into the inner and outer mucus layers (By similarity). 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STAPIAELTTSNPPPESSTPQTSRSTSSPLTESTTLLSTLPPAIEMTSTAPPSTPTAPTTTSGGHTLSPPPSTTTSPPGTPTRGTTTGSSSAPTPSTVQTTTTSAWTPTPTPLSTPSIIRTTGLRPYPSSVLICCVLNDTYYAPGEEVYNGTYGDTCYFVNCSLSCTLEFYNWSCPSTPSPTPTPSKSTPTPSKPSSTPSKPTPGTKPPECPDFDPPRQENETWWLCDCFMATCKYNNTVEIVKVECEPPPMPTCSNGLQPVRVEDPDGCCWHWECDCYCTGWGDPHYVTFDGLYYSYQGNCTYVLVEEISPSVDNFGVYIDNYHCDPNDKVSCPRTLIVRHETQEVLIKTVHMMPMQVQVQVNRQAVALPYKKYGLEVYQSGINYVVDIPELGVLVSYNGLSFSVRLPYHRFGNNTKGQCGTCTNTTSDDCILPSGEIVSNCEAAADQWLVNDPSKPHCPHSSSTTKRPAVTVPGGGKTTPHKDCTPSPLCQLIKDSLFAQCHALVPPQHYYDACVFDSCFMPGSSLECASLQAYAALCAQQNICLDWRNHTHGACLVECPSHREYQACGPAEEPTCKSSSSQQNNTVLVEGCFCPEGTMNYAPGFDVCVKTCGCVGPDNVPREFGEHFEFDCKNCVCLEGGSGIICQPKRCSQKPVTHCVEDGTYLATEVNPADTCCNITVCKCNTSLCKEKPSVCPLGFEVKSKMVPGRCCPFYWCESKGVCVHGNAEYQPGSPVYSSKCQDCVCTDKVDNNTLLNVIACTHVPCNTSCSPGFELMEAPGECCKKCEQTHCIIKRPDNQHVILKPGDFKSDPKNNCTFFSCVKIHNQLISSVSNITCPNFDASICIPGSITFMPNGCCKTCTPRNETRVPCSTVPVTTEVSYAGCTKTVLMNHCSGSCGTFVMYSAKAQALDHSCSCCKEEKTSQREVVLSCPNGGSLTHTYTHIESCQCQDTVCGLPTGTSRRARRSPRHLGSG","length":5289,"molWeight":550850,"crc64":"7AFBC09DA626F0A5","md5":"FD57044300E62B9B215B68EEC0413B92"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"SUBUNIT":2,"INTERACTION":1,"SUBCELLULAR LOCATION":1,"TISSUE SPECIFICITY":1,"DOMAIN":1,"PTM":3,"POLYMORPHISM":1,"WEB RESOURCE":2},"countByFeatureType":{"Signal":1,"Chain":1,"Domain":8,"Repeat":21,"Region":6,"Compositional bias":14,"Binding site":35,"Site":1,"Modified residue":1,"Glycosylation":45,"Disulfide bond":59,"Natural variant":11,"Mutagenesis":9,"Sequence conflict":111,"Beta strand":136,"Turn":25,"Helix":64},"uniParcId":"UPI00087801BC"}}