Q62635 · MUC2_RAT
- ProteinMucin-2
- GeneMuc2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1513 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
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. 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. 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. Acts as a divalent copper chaperone that protects intestinal cells from copper toxicity and facilitates nutritional copper unptake into cells. Binds both Cu2+ and its reduced form, Cu1+, at two juxtaposed binding sites: Cu2+, once reduced to Cu1+ by vitamin C (ascorbate) or other dietary antioxidants, transits to the other binding site. MUC2-bound Cu1+ is protected from oxidation in aerobic environments, and can be released for nutritional delivery to cells. Mucin gels store antimicrobial molecules that participate in innate immunity. Mucin glycoproteins also house and feed the microbiome, lubricate tissue surfaces, and may facilitate the removal of contaminants and waste products from the body (By similarity).
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. '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).
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. '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).
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 46 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 143 | Cu+ (UniProtKB | ChEBI) | ||||
Sequence: M | ||||||
Binding site | 151 | Cu+ (UniProtKB | ChEBI) | ||||
Sequence: M | ||||||
Binding site | 153 | Cu2+ (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 168 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 170 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 177 | Ca2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 274 | Cu2+ (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 321 | Cu2+ (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 323 | Cu+ (UniProtKB | ChEBI) | ||||
Sequence: M | ||||||
Binding site | 400 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 527 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 529 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 531 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: L | ||||||
Binding site | 534 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 535 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 870 | Ca2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 991 | Ca2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 993 | Ca2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 998 | Ca2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 999 | Ca2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 1303 | Ca2+ 5 (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 1306 | Ca2+ 4 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 1309 | Ca2+ 4 (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 1313 | Ca2+ 4 (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 1314 | Ca2+ 5 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 1316 | Ca2+ 5 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 1373 | Ca2+ 5 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 1374 | Ca2+ 5 (UniProtKB | ChEBI) | ||||
Sequence: Y |
GO annotations
Keywords
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameMucin-2
- Short namesMUC-2
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Rattus
Accessions
- Primary accessionQ62635
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: In the intestine, secreted into the inner and outer mucus layers (By similarity).
Before secretion, mucin polymers are stored in dedicated secretory vesicles (By similarity).
Before secretion, mucin polymers are stored in dedicated secretory vesicles (By similarity).
Keywords
- Cellular component
PTM/Processing
Features
Showing features for signal, chain, disulfide bond, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-20 | |||||
Sequence: MGLPLARLVAVCLVLALAKG | ||||||
Chain | PRO_0000019282 | 21-1513 | Mucin-2 | |||
Sequence: LELQKEARSRNHVCSTWGDFHYKTFDGDVFRFPGLCDYNFASDCRDSYKEFAVHLKRGLDKAGGHSSIESVLITIKDDTIYLTHKLAVVNGAMVSTPHYSSGLLIEKNDAYTKVYSRAGLSLMWNREDALMVELDGRFQNHTCGLCGDFNGMQANNEFLSDGIRFSAIEFGNMQKINKPEVVCEDPEEVQEPESCSEHRAECERLLTSTAFEDCQARVPVELYVLACMHDRCQCPQGGACECSTLAEFSRQCSHAGGRPENWRTASLCPKKCPGNMVYLESGSPWLDTCSHLEVSSLCEEHYMDGCFCPEGTVYDDITGSGCIPVSQCHCKLHGHLYMPGQEITNDCEQCVCNAGRWMCKDLPCPETCALEGGSHITTFDGKKFTFHGDCYYVLTKTKYNDSYALLGELASCGSTDKQTCLKTVVLLTDNKKNVVAFKSGGSVLLNEMEVSLPHVAASFSIFKPSSYHIVVNTMFGLRLQIQLVPVMQLFVTLDQSAQGQVQGLCGNFNGLESDDFMTSGGMVEATGAGFANTWKAQSSCHDKLDWLDDPCPLNIESANYAEHWCSLLKRSETPFARCHLAVDPTEYYKRCKYDTCNCQNNEDCMCAALSSYARACAAKGVMLWGWRESVCNKDVHACPSSQIFMYNLTTCQQTCRSISEGDTHCLKGFAPVEGCGCPDHTFMDEKGRCVPLSKCSCYHHGLYLEAGDVILRQEERCICRNGRLQCTQVKLIGHTCLSPQILVDCNNLTALAIREPRPTSCQTLVARYYHTECISGCVCPDGLLDNGRGGCVVEDECPCIHNKQFYDSGKSIKLDCNNTCTCQKGRWECTRYACHSTCSIYGSGHYITFDGKHYDFDGHCSYVAVQDYCGQNSTGSFSIITENVPCGTTGVTCSKAIKIFIGGTELKLVDKHRVVKQLEEGHHVPFITREVGLYLVVEVSSGIIVIWDKKTTIFIKLDPSYKGNVCGLCGNFDDQTKNDFTTRDHMVVASELDFGNSWKEASTCPDVSHNPDPCSLNPHRRSWAEKQCSIIKSDVFLACHGKVDPTVFYDACVHDSCSCDTGGDCECFCSAVASYAQECTKAEACVFWRTPDLCPVFCDYYNPPDECEWHYEPCGNRSFETCRTLNGIHSNISVSYLEGCYPRCPEDRPIYDEDLKKCVSGDKCGCYIEDTRYPPGGSVPTDEICMSCTCTNTSEIICRPDEGKIINQTQDGIFCYWETCGSNGTVEKHFEICVSSTLSPTSMTSFTTTSTPISTTPISTTITTTSATATTTVPCCFWSDWINNNHPTSGNGGDRENFEHVCSAPENIECRAATDPKLDWTELGQKVQCNVSEGLICNNEDQYGTGQFELCYDYEIRVNCCFPMEYCLSTVSPTTSTPISSTPQPTSSPTTLPTTSPLTSSATSPTTSHITSTVSPTTSPTTSTTSPTTSPTTSTTSPTTSTTSPTPSPTTSTTSPTPSPTTSTTSPTPSPTTSTTSPTTSPITSPTTSTTSP | ||||||
Disulfide bond | 34↔166 | |||||
Sequence: CSTWGDFHYKTFDGDVFRFPGLCDYNFASDCRDSYKEFAVHLKRGLDKAGGHSSIESVLITIKDDTIYLTHKLAVVNGAMVSTPHYSSGLLIEKNDAYTKVYSRAGLSLMWNREDALMVELDGRFQNHTCGLC | ||||||
Disulfide bond | 56↔203 | |||||
Sequence: CDYNFASDCRDSYKEFAVHLKRGLDKAGGHSSIESVLITIKDDTIYLTHKLAVVNGAMVSTPHYSSGLLIEKNDAYTKVYSRAGLSLMWNREDALMVELDGRFQNHTCGLCGDFNGMQANNEFLSDGIRFSAIEFGNMQKINKPEVVC | ||||||
Disulfide bond | 64↔163 | |||||
Sequence: CRDSYKEFAVHLKRGLDKAGGHSSIESVLITIKDDTIYLTHKLAVVNGAMVSTPHYSSGLLIEKNDAYTKVYSRAGLSLMWNREDALMVELDGRFQNHTC | ||||||
Glycosylation | 160 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 215↔252 | |||||
Sequence: CSEHRAECERLLTSTAFEDCQARVPVELYVLACMHDRC | ||||||
Disulfide bond | 222↔247 | |||||
Sequence: CERLLTSTAFEDCQARVPVELYVLAC | ||||||
Disulfide bond | 234↔272 | |||||
Sequence: CQARVPVELYVLACMHDRCQCPQGGACECSTLAEFSRQC | ||||||
Disulfide bond | 254↔260 | |||||
Sequence: CPQGGAC | ||||||
Disulfide bond | 262↔288 | |||||
Sequence: CSTLAEFSRQCSHAGGRPENWRTASLC | ||||||
Disulfide bond | 292↔326 | |||||
Sequence: CPGNMVYLESGSPWLDTCSHLEVSSLCEEHYMDGC | ||||||
Disulfide bond | 309↔348 | |||||
Sequence: CSHLEVSSLCEEHYMDGCFCPEGTVYDDITGSGCIPVSQC | ||||||
Disulfide bond | 328↔342 | |||||
Sequence: CPEGTVYDDITGSGC | ||||||
Disulfide bond | 350↔372 | |||||
Sequence: CKLHGHLYMPGQEITNDCEQCVC | ||||||
Disulfide bond | 367↔384 | |||||
Sequence: CEQCVCNAGRWMCKDLPC | ||||||
Disulfide bond | 370↔379 | |||||
Sequence: CVCNAGRWMC | ||||||
Disulfide bond | 388↔525 | |||||
Sequence: CALEGGSHITTFDGKKFTFHGDCYYVLTKTKYNDSYALLGELASCGSTDKQTCLKTVVLLTDNKKNVVAFKSGGSVLLNEMEVSLPHVAASFSIFKPSSYHIVVNTMFGLRLQIQLVPVMQLFVTLDQSAQGQVQGLC | ||||||
Disulfide bond | 410↔560 | |||||
Sequence: CYYVLTKTKYNDSYALLGELASCGSTDKQTCLKTVVLLTDNKKNVVAFKSGGSVLLNEMEVSLPHVAASFSIFKPSSYHIVVNTMFGLRLQIQLVPVMQLFVTLDQSAQGQVQGLCGNFNGLESDDFMTSGGMVEATGAGFANTWKAQSSC | ||||||
Glycosylation | 420 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 432↔440 | |||||
Sequence: CGSTDKQTC | ||||||
Disulfide bond | 571↔616 | |||||
Sequence: CPLNIESANYAEHWCSLLKRSETPFARCHLAVDPTEYYKRCKYDTC | ||||||
Disulfide bond | 585↔611 | |||||
Sequence: CSLLKRSETPFARCHLAVDPTEYYKRC | ||||||
Disulfide bond | 598↔636 | |||||
Sequence: CHLAVDPTEYYKRCKYDTCNCQNNEDCMCAALSSYARAC | ||||||
Disulfide bond | 618↔624 | |||||
Sequence: CQNNEDC | ||||||
Disulfide bond | 626↔651 | |||||
Sequence: CAALSSYARACAAKGVMLWGWRESVC | ||||||
Disulfide bond | 658↔695 | |||||
Sequence: CPSSQIFMYNLTTCQQTCRSISEGDTHCLKGFAPVEGC | ||||||
Glycosylation | 667 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 671↔685 | |||||
Sequence: CQQTCRSISEGDTHC | ||||||
Disulfide bond | 675↔715 | |||||
Sequence: CRSISEGDTHCLKGFAPVEGCGCPDHTFMDEKGRCVPLSKC | ||||||
Disulfide bond | 697↔709 | |||||
Sequence: CPDHTFMDEKGRC | ||||||
Disulfide bond | 717↔739 | |||||
Sequence: CYHHGLYLEAGDVILRQEERCIC | ||||||
Disulfide bond | 737↔746 | |||||
Sequence: CICRNGRLQC | ||||||
Glycosylation | 767 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 781↔817 | |||||
Sequence: CQTLVARYYHTECISGCVCPDGLLDNGRGGCVVEDEC | ||||||
Disulfide bond | 799↔811 | |||||
Sequence: CPDGLLDNGRGGC | ||||||
Disulfide bond | 819↔842 | |||||
Sequence: CIHNKQFYDSGKSIKLDCNNTCTC | ||||||
Disulfide bond | 836↔854 | |||||
Sequence: CNNTCTCQKGRWECTRYAC | ||||||
Glycosylation | 837 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 840↔849 | |||||
Sequence: CTCQKGRWEC | ||||||
Disulfide bond | 858↔989 | |||||
Sequence: CSIYGSGHYITFDGKHYDFDGHCSYVAVQDYCGQNSTGSFSIITENVPCGTTGVTCSKAIKIFIGGTELKLVDKHRVVKQLEEGHHVPFITREVGLYLVVEVSSGIIVIWDKKTTIFIKLDPSYKGNVCGLC | ||||||
Disulfide bond | 880↔1024 | |||||
Sequence: CSYVAVQDYCGQNSTGSFSIITENVPCGTTGVTCSKAIKIFIGGTELKLVDKHRVVKQLEEGHHVPFITREVGLYLVVEVSSGIIVIWDKKTTIFIKLDPSYKGNVCGLCGNFDDQTKNDFTTRDHMVVASELDFGNSWKEASTC | ||||||
Disulfide bond | 889↔986 | |||||
Sequence: CGQNSTGSFSIITENVPCGTTGVTCSKAIKIFIGGTELKLVDKHRVVKQLEEGHHVPFITREVGLYLVVEVSSGIIVIWDKKTTIFIKLDPSYKGNVC | ||||||
Glycosylation | 892 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 906↔913 | |||||
Sequence: CGTTGVTC | ||||||
Disulfide bond | 1034↔1077 | |||||
Sequence: CSLNPHRRSWAEKQCSIIKSDVFLACHGKVDPTVFYDACVHDSC | ||||||
Disulfide bond | 1048↔1072 | |||||
Sequence: CSIIKSDVFLACHGKVDPTVFYDAC | ||||||
Disulfide bond | 1059↔1099 | |||||
Sequence: CHGKVDPTVFYDACVHDSCSCDTGGDCECFCSAVASYAQEC | ||||||
Disulfide bond | 1079↔1087 | |||||
Sequence: CDTGGDCEC | ||||||
Disulfide bond | 1085 | Interchain | ||||
Sequence: C | ||||||
Disulfide bond | 1089↔1114 | |||||
Sequence: CSAVASYAQECTKAEACVFWRTPDLC | ||||||
Disulfide bond | 1105↔1134 | |||||
Sequence: CVFWRTPDLCPVFCDYYNPPDECEWHYEPC | ||||||
Disulfide bond | 1118↔1160 | |||||
Sequence: CDYYNPPDECEWHYEPCGNRSFETCRTLNGIHSNISVSYLEGC | ||||||
Disulfide bond | 1127 | Interchain | ||||
Sequence: C | ||||||
Glycosylation | 1136 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 1142↔1184 | |||||
Sequence: CRTLNGIHSNISVSYLEGCYPRCPEDRPIYDEDLKKCVSGDKC | ||||||
Glycosylation | 1151 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 1164↔1178 | |||||
Sequence: CPEDRPIYDEDLKKC | ||||||
Disulfide bond | 1186↔1210 | |||||
Sequence: CYIEDTRYPPGGSVPTDEICMSCTC | ||||||
Disulfide bond | 1205↔1235 | |||||
Sequence: CMSCTCTNTSEIICRPDEGKIINQTQDGIFC | ||||||
Disulfide bond | 1208↔1218 | |||||
Sequence: CTCTNTSEIIC | ||||||
Glycosylation | 1212 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 1227 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 1243 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 1264 | O-linked (GalNAc) threonine | ||||
Sequence: T | ||||||
Glycosylation | 1267 | O-linked (GalNAc) threonine | ||||
Sequence: T | ||||||
Glycosylation | 1268 | O-linked (GalNAc) threonine | ||||
Sequence: T | ||||||
Glycosylation | 1280 | O-linked (GalNAc) threonine | ||||
Sequence: T | ||||||
Glycosylation | 1286 | O-linked (GalNAc) serine | ||||
Sequence: S | ||||||
Glycosylation | 1290 | O-linked (GalNAc) threonine | ||||
Sequence: T | ||||||
Glycosylation | 1350 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Post-translational modification
O-glycosylated. O-glycosylation is required for mucin assembly (By similarity).
Goblet cells synthesize two forms of mucin that differ in branched chain O-glycosylation and the site of production in the colon (By similarity).
Goblet cells synthesize two forms of mucin that differ in branched chain O-glycosylation and the site of production in the colon (By similarity).
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.
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.
Keywords
- PTM
PTM databases
Expression
Tissue specificity
Expressed in intestine and airway.
Interaction
Subunit
Homomultimer; disulfide-linked. 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 of the third VWD domain (VWD3) from different CTCK-linked dimers. The VWD3 assemblies then become disulfide bonded to one another to produce long, disulfide-linked polymers that remain highly compact until secretion. Interacts with FCGBP. Interacts with AGR2; disulfide-linked (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 of the third VWD domain (VWD3) from different CTCK-linked dimers. The VWD3 assemblies then become disulfide bonded to one another to produce long, disulfide-linked polymers that remain highly compact until secretion. Interacts with FCGBP. Interacts with AGR2; disulfide-linked (By similarity).
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain, repeat, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 32-204 | VWFD 1 | ||||
Sequence: HVCSTWGDFHYKTFDGDVFRFPGLCDYNFASDCRDSYKEFAVHLKRGLDKAGGHSSIESVLITIKDDTIYLTHKLAVVNGAMVSTPHYSSGLLIEKNDAYTKVYSRAGLSLMWNREDALMVELDGRFQNHTCGLCGDFNGMQANNEFLSDGIRFSAIEFGNMQKINKPEVVCE | ||||||
Domain | 292-348 | TIL | ||||
Sequence: CPGNMVYLESGSPWLDTCSHLEVSSLCEEHYMDGCFCPEGTVYDDITGSGCIPVSQC | ||||||
Domain | 350-410 | VWFC | ||||
Sequence: CKLHGHLYMPGQEITNDCEQCVCNAGRWMCKDLPCPETCALEGGSHITTFDGKKFTFHGDC | ||||||
Domain | 386-561 | VWFD 2 | ||||
Sequence: ETCALEGGSHITTFDGKKFTFHGDCYYVLTKTKYNDSYALLGELASCGSTDKQTCLKTVVLLTDNKKNVVAFKSGGSVLLNEMEVSLPHVAASFSIFKPSSYHIVVNTMFGLRLQIQLVPVMQLFVTLDQSAQGQVQGLCGNFNGLESDDFMTSGGMVEATGAGFANTWKAQSSCH | ||||||
Domain | 856-1025 | VWFD 3 | ||||
Sequence: STCSIYGSGHYITFDGKHYDFDGHCSYVAVQDYCGQNSTGSFSIITENVPCGTTGVTCSKAIKIFIGGTELKLVDKHRVVKQLEEGHHVPFITREVGLYLVVEVSSGIIVIWDKKTTIFIKLDPSYKGNVCGLCGNFDDQTKNDFTTRDHMVVASELDFGNSWKEASTCP | ||||||
Repeat | 1392-1407 | 1 | ||||
Sequence: SPTTSTPISSTPQPTS | ||||||
Region | 1392-1513 | Approximate repeats | ||||
Sequence: SPTTSTPISSTPQPTSSPTTLPTTSPLTSSATSPTTSHITSTVSPTTSPTTSTTSPTTSPTTSTTSPTTSTTSPTPSPTTSTTSPTPSPTTSTTSPTPSPTTSTTSPTTSPITSPTTSTTSP | ||||||
Region | 1392-1513 | Disordered | ||||
Sequence: SPTTSTPISSTPQPTSSPTTLPTTSPLTSSATSPTTSHITSTVSPTTSPTTSTTSPTTSPTTSTTSPTTSTTSPTPSPTTSTTSPTPSPTTSTTSPTPSPTTSTTSPTTSPITSPTTSTTSP | ||||||
Repeat | 1408-1423 | 2 | ||||
Sequence: SPTTLPTTSPLTSSAT | ||||||
Repeat | 1424-1434 | 3 | ||||
Sequence: SPTTSHITSTV | ||||||
Repeat | 1435-1445 | 4 | ||||
Sequence: SPTTSPTTSTT | ||||||
Repeat | 1446-1456 | 5 | ||||
Sequence: SPTTSPTTSTT | ||||||
Repeat | 1457-1467 | 6 | ||||
Sequence: SPTTSTTSPTP | ||||||
Repeat | 1468-1478 | 7 | ||||
Sequence: SPTTSTTSPTP | ||||||
Repeat | 1479-1489 | 8 | ||||
Sequence: SPTTSTTSPTP | ||||||
Repeat | 1490-1500 | 9 | ||||
Sequence: SPTTSTTSPTT | ||||||
Repeat | 1501-1511 | 10 | ||||
Sequence: SPITSPTTSTT | ||||||
Repeat | 1512-1513 | 11 | ||||
Sequence: SP |
Domain
The CTCK domain mediates interchain disulfide bonds with another molecule of MUC2.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusFragment
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length1,513
- Mass (Da)166,038
- Last updated1996-11-01 v1
- Checksum26109DCA1BE7D008
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
M0R6C7 | M0R6C7_RAT | Muc2 | 4743 |
Features
Showing features for non-terminal residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Non-terminal residue | 1513 | |||||
Sequence: P |
Keywords
- Technical term