Q80Z19 · MUC2_MOUSE
- ProteinMucin-2
- GeneMuc2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids4576 (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 (PubMed:18806221, PubMed:19432394, PubMed:33093110).
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:18806221, PubMed:19432394, PubMed:33093110).
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:18806221, PubMed:19432394).
Acts as a divalent copper chaperone that protects intestinal cells from copper toxicity and facilitates nutritional copper unptake into cells (By similarity).
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 (By similarity).
MUC2-bound Cu1+ is protected from oxidation in aerobic environments, and can be released for nutritional delivery to cells (By similarity).
Mucin gels store antimicrobial molecules that participate in innate immunity (PubMed:18806221, PubMed:19432394).
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:33093110).
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 (PubMed:33093110).
'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 (PubMed:33093110).
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:18806221, PubMed:19432394, PubMed:33093110).
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:18806221, PubMed:19432394).
Acts as a divalent copper chaperone that protects intestinal cells from copper toxicity and facilitates nutritional copper unptake into cells (By similarity).
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 (By similarity).
MUC2-bound Cu1+ is protected from oxidation in aerobic environments, and can be released for nutritional delivery to cells (By similarity).
Mucin gels store antimicrobial molecules that participate in innate immunity (PubMed:18806221, PubMed:19432394).
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:33093110).
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 (PubMed:33093110).
'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 (PubMed:33093110).
Features
Showing features for binding site, 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 | 275 | Cu2+ (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 322 | Cu2+ (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 324 | Cu+ (UniProtKB | ChEBI) | ||||
Sequence: M | ||||||
Binding site | 401 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 528 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 530 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 532 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: L | ||||||
Binding site | 535 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 536 | Ca2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 871 | Ca2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 992 | Ca2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 994 | Ca2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 999 | Ca2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 1000 | Ca2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 1305 | Ca2+ 5 (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 1308 | Ca2+ 4 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 1315 | Ca2+ 4 (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 1316 | Ca2+ 5 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 1318 | Ca2+ 5 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 1375 | Ca2+ 5 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 1376 | Ca2+ 5 (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Site | 3887-3888 | Cleavage; by autolysis; in vitro | ||||
Sequence: DP |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | collagen-containing extracellular matrix | |
Cellular Component | extracellular matrix | |
Cellular Component | extracellular space | |
Cellular Component | inner mucus layer | |
Cellular Component | mucus layer | |
Cellular Component | outer mucus layer | |
Molecular Function | cupric ion binding | |
Molecular Function | cuprous ion binding | |
Molecular Function | extracellular matrix structural constituent | |
Molecular Function | identical protein binding | |
Biological Process | apoptotic process | |
Biological Process | detoxification of copper ion | |
Biological Process | glandular epithelial cell development | |
Biological Process | host-mediated regulation of intestinal microbiota composition | |
Biological Process | maintenance of gastrointestinal epithelium | |
Biological Process | mucus secretion | |
Biological Process | negative regulation of cell migration | |
Biological Process | negative regulation of cell population proliferation | |
Biological Process | positive regulation of apoptotic process |
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
- Strains
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ80Z19
- Secondary accessions
Proteomes
Organism-specific databases
Phenotypes & Variants
Disruption phenotype
Aberrant intestinal crypt morphology and altered cell maturation and migration (PubMed:11872843).
Frequent development of adenomas in the small intestine which progress to invasive adenocarcinomas, as well as rectal tumors (PubMed:11872843).
Absence of inner and outer mucus layers in the colon so that bacteria are in direct contact with the colon epithelium and enter into the cells and crypts in contrast to wild-type animals which are devoid of bacteria in the inner mucus layer (PubMed:18806221).
Frequent development of adenomas in the small intestine which progress to invasive adenocarcinomas, as well as rectal tumors (PubMed:11872843).
Absence of inner and outer mucus layers in the colon so that bacteria are in direct contact with the colon epithelium and enter into the cells and crypts in contrast to wild-type animals which are devoid of bacteria in the inner mucus layer (PubMed:18806221).
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 165 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for signal, modified residue, chain, disulfide bond, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-20 | |||||
Sequence: MGLPLARLVAACLVLALAKG | ||||||
Modified residue | 21 | Phosphoserine | ||||
Sequence: S | ||||||
Chain | PRO_5030002787 | 21-4576 | Mucin-2 | |||
Sequence: SELQKEARSRNHVCSTWGDFHYKTFDGDVYRFPGLCDYNFASDCRDSYKEFAVHLKRGLGEAGGHSQIESILITIKDDTIYLTHKLAVVNGAMVSTPHYSSGLLIEKNDAYTKVYSRAGLSLMWNREDALMVELDSRFQNHTCGLCGDFNGMQTNYEFLSEEGIQFSAIEFGNMQKINKPEVQCEDPEAVQEPESCSEHRAECERLLTSAAFEDCQTRVPVESYVRACMHDRCQCPKGGACECSTLAEFSRQCSHAGGRPENWRTASLCPKKCPNNMVYLESSSPCVDTCSHLEVSSLCEEHYMDGCFCPEGTVYDDITGSGCIPVSQCHCKLHGHLYMPGQEFTNDCEQCVCNAGRWVCKDLPCPETCALEGGSHITTFDGKKFTFHGDCYYVLTKSEHNDSYALLGELASCGSTDKQTCLKTVVLLTDDKKNVVAFKSGGSVLLNEMEVTLPHVAASFSIFQPSSYHIVVNTKFGLRLQIQLLPVMQLFVTLDQAAQGQVQGLCGNFNGLESDDFMTSGGMVEATGAGFANTWKAQSSCHDKLDWLDDPCSLNIESANYAEHWCSLLKRSETPFARCHLAVDPTEYYKRCKYDTCNCQNNEDCMCAALSSYARACAAKGVMLWGWRERVCNKDVHACPSSQIFMYNLTTCQQTCRSLSEGDSHCLKGFAPVEGCGCPDHTFMDEKGRCVPLAKCSCYHHGLYLEAGDVILRQEERCICRNGRLQCTQVKLIGHTCQYPKILVDCNNLTALAVRKPRPTSCQTLVAGYYHTECISGCVCPDGLLDDGRGGCVEEDKCPCIHNKDLYSSGESIKLDCNNTCTCQKGRWECTRYACHSTCSIYGSGHYITFDGKHYDFDGHCSYVAVQDYCGQNSTGSFSIITENVPCGTTGVTCSKAIKIFIGGTELKLVDKHRVVKQLEEGHHVPYITREVGQYLVVEASSGIIVIWDKKTTIFIKLDPSYKGTVCGLCGNFDDQTKNDFTTRDHMVVTSELDFGNSWKEASTCPDVSHNPDPCSLNPHRRSWAEKQCSIIKSRVFKVCHSKVDPTVFYEACVHDSCSCDTGGDCDCFCSAVASYAQECTKAEACVFWRTPDLCPIFCDYYNPPDECEWHYEPCGNRSFETCRTLNGIHSNISVSYLEGCYPRCPEDRPIYDEDLKKCVTGDKCGCYIEDTRYPPGGSVPTDEICKSCTCTNTSKIECHPDEGKILNMTQDGIFCYWEFCGPNGTVGQHFNICGSSTAIPSTTTSFTTISTPISTTPISTTITTTTVTMTTEQVPCCFWSDWINKYHPTKENGGDRETFTHVCSAPEDIECRAATDPKLSWEELGQKVQCNVSTGLICNNEDQYGIGEFELCYDYEIRVNCCYPMEYCTPSTISPTTSTTTLSTTPPTSSPTTLPTSSPVTSSATLPTTSSITSTISPTTSPTTPLTTSPTTSPTTSPTTPSTTSPTTPTTTSPTTPSTTSPTTPSTTPSTTSPTTPSTTSPTTPTSTSPNTQSTTSPTTSPTTPSTTSPTTSPTTPSTTSPTISTTTSTISPTTPSTTSPNTPSTTSSTIPSTTSPTTPSTTSPTISTTTSTTSPTTPSTTSPTTPSTTSPTTPSTTSPTISTTTLTTSPTTPSTTSPTTPSTTSPTTPSTTSPTISITTSTISPTTPSTTSPTTLSTTSPTTPSTTSPTISTTTSTSPTTPSTTSPTTPSTPSSTTPSTTSPTTPSTTSPTISTTSSTISPTTPSTTSPTTPSTTSPTTPSTTSPTISTTTSTISPTTPSTTSPTTPSTTSPTTPSTTSPTISTTTSTISPTTPSTTSPTTPSTTSPNTPSTTSTTTSTTSPTTPSTTSPTISTTTSTTSPTTPSTTSPTISTTTSTTSPTTPSTTSPTTPSTTSPTTPSTTSPTTPSTTSPTISTTSSTISPTTPSTTSPTTPSTTSPTTPSTTSPTISTTTSTTSPTTPSTTSPTISTTTSTISPTTPSTSSPTTPSTTSPTTPSTTSPTISTTTSTTSPTTPSTTSPTTPSTTSPTISTTTSTTSPTTPSTTSPTISTTTSTTSPTTPSTTSPTTPSTTSPTTPSTTSPTTPSTTSPTISTTSSTISPTTPSTTSPTTPSTTSPTTPSTTSPTISTTTSTTSPTTPSTTSPTISTTTSTTSPTTPSTTSPTTPSTTSPTTPSTTSPTTPSTTSPTISTTSSTISPTTPSTTSPTTPSTTSPTTPSTTSPTISTTTSTTSPTTPSTTSPTISTTTSTISPTTPSTTSPITPSTTSPTTPSTTSPTISTTTSTTSPTTPSTTSPTISTTTSTISPTTPSTTSPITPSTTSPTTPSTTSPTISTTTSTISPTTPSTTSPTTPSTTSPTTLSTTSPTISTTTSTISPTTPSTTSPTTPSTTSPTTPSTTSPTTPSTTSPTISTTTSTISPTTSPTTPSTTSPTTHSTTSPTTPSTTSPTISTTTSTISPTTPSTTSLTTPSTTSPTTPSTTSPTTPSTTSPTISTTTSTISPTTPSTTSPTTPSTTSPTTPSTTSPNISTTTSTISPTTPSTTSPTTPSTTSPTTPSTTSPTISTTTSTISPTTPSTTSPTTPSTTSPTTPSTTSPTTPSTTSPTISTTTSTISPTTPSTTSPTTPSTTSPTTQSTTSPTISTNTPSTTSPTTPSTTSPTISTTTSTISPTTPSTTSPTTPSTTSPTTSSTTSPTISTTTSTISPTTPSTTSPTTPSTTSPTTPLTTSPTISTTTSTISPTTPSTTSPTTPSTTSPTTPSTTSPTTPSTTSPTISTTTSTISPTTPSTTSPTTSPTTPSTTSPTTSSTATQTISVTTSQTSSSATPPNSSPTSSATTSPTTSSGTSTATSPSTSPTTSSTFTTPPSTTCIDDCKWTGWLDSGKPTYDIKSGDFELIKGVCEPHWEVQNISCRAVMHSNIPLDQLGQIVVCNKEVGLVCKNEDQEIGGIIPMRMCLNYEINVYCCNPICFTSTPSSTTTETPTTTSTTKTSILTSTTTQTPSPSPTTTVTPTPAPTTTQIPTSTSTTTQTTTPTPITETSTPTSTISQTPSPASTTTVTPATTSTTTETSTSTSTTTQTTSPTPTVTETSTPRSTTTQTPSPVPTTTVTSTPTPTIGETTTPTTTITETFTPRSTTTQTSSPVPSTTVTPTPTPITTETSTSTPTTTQTTTPTPITETSTPISTTTHTPSPSSTTSTTSTQTPTPTTTGPSTSTSTTIQTTTPTPITETFTPTSTTTQTPSSTPTTTVTPTPTTTETSTSTSTTTQTTTPTPITETFTPTSTTTQTPSPTPTTTVNPTPTPTTIGPSTSTSTTTQTTTPTPTGTETSTPTSTTTQTPSPTPTTTVTPTPSPTTTETSTSTTTQTTTPTPTGTETSTPTSTTTQTPSPTPTTTVTPTPSPTTTETSTSTTTQTTTPTPITETSTPTSTTTQTPSPTPTTTVTPTSTPTTTGTSTSTSTTTQTTTPTPTGTETFTPRSTTTQTPSSSSTTSGTPTPTPTTTHTSTLTSTTEASTPTPIIETSTPKSTTIQTPSPSPTTTVTSPTTPTTTVKETSTPTNTVPTTGSTSSKPPTESSTPVTSQSTPSPPTESTTLSSTPVTTATSSTASSPGTTSPFVTSSAGSTPSSPPGSTPGPTTSSGMPTSSKTTTGPTSPTTRPPSTSTPTSFTVPTETTTQTRPLSTTPTTLETTRTSSWGTFSSTSPITSPSTVWTHTETQVTCCVLNEMFYGPGELVYNSTHGGTCFYVNCSLDCHLQFFNWSCPSTPSTPTPSTPTPTPSQTTTPSTTSSKSTPSTPQSTSPKSTLSTPTKTTPYGCPDFDPPRQVNETWWLCNCTMAICNHDNVVEIVPLKCDPPPMPTCANGLKPVRVPDADNCCWHWECDCYCTGWGDPHFVTFDGLYYSYQGNCTYVLVEEITPTVDNFGVYIDNYHCDANDKVSCPRTLIVRHETQEVQIKTVRMMPIEVEVQVNKQLVALPYKKYGLEVYESGINIVVNISRLEAKISYNGLSFSIRLPYKLFGNNTKGQCGTCTNNTADDCILPSGKIISDCEIAADEWLVNDPSKPHCPHKGLTTKRPATTTPGLSLNNCTVSPVCHLIMDSLFSQCHAFVPPKHYYEACLFDSCYVPGSNMECASVQAYATLCAKEGVCIDWRNHTQGVCSVKCPPHKQYQACGPEEEPTCQPSSSQNSTLLVEGCFCPEGTTKFAPGYDVCVKTCGCVGPDNVPREFGEHFEFDCKDCVCREGGSGIVCQPKKCSGGNQTTCEEDGTYLVVETNPDDKCCNITSCKCDTKRCKAERPTCLLGFEVKTEIVPGKCCPVYSCVPKGVCVHQNAEYQPGSPVYSNKCQDCVCTNILDNSTQLNVISCTHVPCNISCSSGFELVDVPGECCKKCQQTHCIIEGPKQQYIILKPGEIHKNPSNKCTFFSCMKINNQLISSVSNITCPDFNPSDCVSGSITYMPNGCCKTCIPQNQTRVPCSAVSVMKEISYNGCTKNISMNYCFGSCGTFAMYSAQVQGLDHRCSCCKEEKTSVRSVTLECPDGSELSHTYTHIESCLCQDTVCGLPQAQQVRTRRSSPRFLGRK | ||||||
Disulfide bond | 34↔166 | |||||
Sequence: CSTWGDFHYKTFDGDVYRFPGLCDYNFASDCRDSYKEFAVHLKRGLGEAGGHSQIESILITIKDDTIYLTHKLAVVNGAMVSTPHYSSGLLIEKNDAYTKVYSRAGLSLMWNREDALMVELDSRFQNHTCGLC | ||||||
Disulfide bond | 56↔204 | |||||
Sequence: CDYNFASDCRDSYKEFAVHLKRGLGEAGGHSQIESILITIKDDTIYLTHKLAVVNGAMVSTPHYSSGLLIEKNDAYTKVYSRAGLSLMWNREDALMVELDSRFQNHTCGLCGDFNGMQTNYEFLSEEGIQFSAIEFGNMQKINKPEVQC | ||||||
Disulfide bond | 64↔163 | |||||
Sequence: CRDSYKEFAVHLKRGLGEAGGHSQIESILITIKDDTIYLTHKLAVVNGAMVSTPHYSSGLLIEKNDAYTKVYSRAGLSLMWNREDALMVELDSRFQNHTC | ||||||
Glycosylation | 160 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 216↔253 | |||||
Sequence: CSEHRAECERLLTSAAFEDCQTRVPVESYVRACMHDRC | ||||||
Disulfide bond | 223↔248 | |||||
Sequence: CERLLTSAAFEDCQTRVPVESYVRAC | ||||||
Disulfide bond | 235↔273 | |||||
Sequence: CQTRVPVESYVRACMHDRCQCPKGGACECSTLAEFSRQC | ||||||
Disulfide bond | 255↔261 | |||||
Sequence: CPKGGAC | ||||||
Disulfide bond | 263↔289 | |||||
Sequence: CSTLAEFSRQCSHAGGRPENWRTASLC | ||||||
Disulfide bond | 293↔327 | |||||
Sequence: CPNNMVYLESSSPCVDTCSHLEVSSLCEEHYMDGC | ||||||
Disulfide bond | 306↔319 | |||||
Sequence: CVDTCSHLEVSSLC | ||||||
Disulfide bond | 310↔349 | |||||
Sequence: CSHLEVSSLCEEHYMDGCFCPEGTVYDDITGSGCIPVSQC | ||||||
Disulfide bond | 329↔343 | |||||
Sequence: CPEGTVYDDITGSGC | ||||||
Disulfide bond | 351↔373 | |||||
Sequence: CKLHGHLYMPGQEFTNDCEQCVC | ||||||
Disulfide bond | 368↔385 | |||||
Sequence: CEQCVCNAGRWVCKDLPC | ||||||
Disulfide bond | 371↔380 | |||||
Sequence: CVCNAGRWVC | ||||||
Disulfide bond | 389↔526 | |||||
Sequence: CALEGGSHITTFDGKKFTFHGDCYYVLTKSEHNDSYALLGELASCGSTDKQTCLKTVVLLTDDKKNVVAFKSGGSVLLNEMEVTLPHVAASFSIFQPSSYHIVVNTKFGLRLQIQLLPVMQLFVTLDQAAQGQVQGLC | ||||||
Disulfide bond | 411↔561 | |||||
Sequence: CYYVLTKSEHNDSYALLGELASCGSTDKQTCLKTVVLLTDDKKNVVAFKSGGSVLLNEMEVTLPHVAASFSIFQPSSYHIVVNTKFGLRLQIQLLPVMQLFVTLDQAAQGQVQGLCGNFNGLESDDFMTSGGMVEATGAGFANTWKAQSSC | ||||||
Glycosylation | 421 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 433↔441 | |||||
Sequence: CGSTDKQTC | ||||||
Disulfide bond | 572↔617 | |||||
Sequence: CSLNIESANYAEHWCSLLKRSETPFARCHLAVDPTEYYKRCKYDTC | ||||||
Disulfide bond | 586↔612 | |||||
Sequence: CSLLKRSETPFARCHLAVDPTEYYKRC | ||||||
Disulfide bond | 599↔637 | |||||
Sequence: CHLAVDPTEYYKRCKYDTCNCQNNEDCMCAALSSYARAC | ||||||
Disulfide bond | 619↔625 | |||||
Sequence: CQNNEDC | ||||||
Disulfide bond | 627↔652 | |||||
Sequence: CAALSSYARACAAKGVMLWGWRERVC | ||||||
Disulfide bond | 659↔696 | |||||
Sequence: CPSSQIFMYNLTTCQQTCRSLSEGDSHCLKGFAPVEGC | ||||||
Glycosylation | 668 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 672↔686 | |||||
Sequence: CQQTCRSLSEGDSHC | ||||||
Disulfide bond | 676↔716 | |||||
Sequence: CRSLSEGDSHCLKGFAPVEGCGCPDHTFMDEKGRCVPLAKC | ||||||
Disulfide bond | 698↔710 | |||||
Sequence: CPDHTFMDEKGRC | ||||||
Disulfide bond | 718↔740 | |||||
Sequence: CYHHGLYLEAGDVILRQEERCIC | ||||||
Disulfide bond | 738↔747 | |||||
Sequence: CICRNGRLQC | ||||||
Glycosylation | 768 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 782↔818 | |||||
Sequence: CQTLVAGYYHTECISGCVCPDGLLDDGRGGCVEEDKC | ||||||
Disulfide bond | 800↔812 | |||||
Sequence: CPDGLLDDGRGGC | ||||||
Disulfide bond | 820↔843 | |||||
Sequence: CIHNKDLYSSGESIKLDCNNTCTC | ||||||
Disulfide bond | 837↔855 | |||||
Sequence: CNNTCTCQKGRWECTRYAC | ||||||
Glycosylation | 838 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 841↔850 | |||||
Sequence: CTCQKGRWEC | ||||||
Disulfide bond | 859↔990 | |||||
Sequence: CSIYGSGHYITFDGKHYDFDGHCSYVAVQDYCGQNSTGSFSIITENVPCGTTGVTCSKAIKIFIGGTELKLVDKHRVVKQLEEGHHVPYITREVGQYLVVEASSGIIVIWDKKTTIFIKLDPSYKGTVCGLC | ||||||
Disulfide bond | 881↔1025 | |||||
Sequence: CSYVAVQDYCGQNSTGSFSIITENVPCGTTGVTCSKAIKIFIGGTELKLVDKHRVVKQLEEGHHVPYITREVGQYLVVEASSGIIVIWDKKTTIFIKLDPSYKGTVCGLCGNFDDQTKNDFTTRDHMVVTSELDFGNSWKEASTC | ||||||
Disulfide bond | 890↔987 | |||||
Sequence: CGQNSTGSFSIITENVPCGTTGVTCSKAIKIFIGGTELKLVDKHRVVKQLEEGHHVPYITREVGQYLVVEASSGIIVIWDKKTTIFIKLDPSYKGTVC | ||||||
Glycosylation | 893 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 907↔914 | |||||
Sequence: CGTTGVTC | ||||||
Disulfide bond | 1035↔1078 | |||||
Sequence: CSLNPHRRSWAEKQCSIIKSRVFKVCHSKVDPTVFYEACVHDSC | ||||||
Disulfide bond | 1049↔1073 | |||||
Sequence: CSIIKSRVFKVCHSKVDPTVFYEAC | ||||||
Disulfide bond | 1060↔1100 | |||||
Sequence: CHSKVDPTVFYEACVHDSCSCDTGGDCDCFCSAVASYAQEC | ||||||
Disulfide bond | 1080↔1088 | |||||
Sequence: CDTGGDCDC | ||||||
Disulfide bond | 1086 | Interchain | ||||
Sequence: C | ||||||
Disulfide bond | 1090↔1115 | |||||
Sequence: CSAVASYAQECTKAEACVFWRTPDLC | ||||||
Disulfide bond | 1106↔1135 | |||||
Sequence: CVFWRTPDLCPIFCDYYNPPDECEWHYEPC | ||||||
Disulfide bond | 1119↔1161 | |||||
Sequence: CDYYNPPDECEWHYEPCGNRSFETCRTLNGIHSNISVSYLEGC | ||||||
Disulfide bond | 1128 | Interchain | ||||
Sequence: C | ||||||
Glycosylation | 1137 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 1143↔1185 | |||||
Sequence: CRTLNGIHSNISVSYLEGCYPRCPEDRPIYDEDLKKCVTGDKC | ||||||
Glycosylation | 1152 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 1165↔1179 | |||||
Sequence: CPEDRPIYDEDLKKC | ||||||
Disulfide bond | 1187↔1211 | |||||
Sequence: CYIEDTRYPPGGSVPTDEICKSCTC | ||||||
Disulfide bond | 1206↔1236 | |||||
Sequence: CKSCTCTNTSKIECHPDEGKILNMTQDGIFC | ||||||
Disulfide bond | 1209↔1219 | |||||
Sequence: CTCTNTSKIEC | ||||||
Glycosylation | 1213 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 1228 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 1244 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 1265 | O-linked (GalNAc) threonine | ||||
Sequence: T | ||||||
Glycosylation | 1268 | O-linked (GalNAc) threonine | ||||
Sequence: T | ||||||
Glycosylation | 1269 | O-linked (GalNAc) threonine | ||||
Sequence: T | ||||||
Glycosylation | 1281 | O-linked (GalNAc) threonine | ||||
Sequence: T | ||||||
Glycosylation | 1292 | O-linked (GalNAc) threonine | ||||
Sequence: T | ||||||
Glycosylation | 1352 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 2529 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 2910 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 3734 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 3745 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 3756 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 3823 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 3830 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 3882↔4023 | |||||
Sequence: CTGWGDPHFVTFDGLYYSYQGNCTYVLVEEITPTVDNFGVYIDNYHCDANDKVSCPRTLIVRHETQEVQIKTVRMMPIEVEVQVNKQLVALPYKKYGLEVYESGINIVVNISRLEAKISYNGLSFSIRLPYKLFGNNTKGQC | ||||||
Glycosylation | 3903 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 3904↔4062 | |||||
Sequence: CTYVLVEEITPTVDNFGVYIDNYHCDANDKVSCPRTLIVRHETQEVQIKTVRMMPIEVEVQVNKQLVALPYKKYGLEVYESGINIVVNISRLEAKISYNGLSFSIRLPYKLFGNNTKGQCGTCTNNTADDCILPSGKIISDCEIAADEWLVNDPSKPHC | ||||||
Disulfide bond | 3928↔3936 | |||||
Sequence: CDANDKVSC | ||||||
Glycosylation | 3991 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 4017 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 4028 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 4083 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 4149 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 4183 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 4254 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 4277 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 4351 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 4366 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 4434 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 4465 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 4471↔4518 | |||||
Sequence: CSAVSVMKEISYNGCTKNISMNYCFGSCGTFAMYSAQVQGLDHRCSCC | ||||||
Disulfide bond | 4485↔4532 | |||||
Sequence: CTKNISMNYCFGSCGTFAMYSAQVQGLDHRCSCCKEEKTSVRSVTLEC | ||||||
Glycosylation | 4488 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 4494↔4548 | |||||
Sequence: CFGSCGTFAMYSAQVQGLDHRCSCCKEEKTSVRSVTLECPDGSELSHTYTHIESC | ||||||
Disulfide bond | 4498↔4550 | |||||
Sequence: CGTFAMYSAQVQGLDHRCSCCKEEKTSVRSVTLECPDGSELSHTYTHIESCLC |
Post-translational modification
O-glycosylated (PubMed:9886986).
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 (PubMed:33093110).
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 (PubMed:33093110).
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
Proteomic databases
PTM databases
Expression
Tissue specificity
Highly expressed in goblet cells of the colon with lower levels in the small intestine and no expression in the stomach (at protein level).
Gene expression databases
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 (By similarity).
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 (By similarity).
The VWD3 assemblies then become disulfide bonded to one another to produce long, disulfide-linked polymers that remain highly compact until secretion (By similarity).
Interacts with FCGBP (PubMed:19432394).
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 (By similarity).
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 (By similarity).
The VWD3 assemblies then become disulfide bonded to one another to produce long, disulfide-linked polymers that remain highly compact until secretion (By similarity).
Interacts with FCGBP (PubMed:19432394).
Interacts with AGR2; disulfide-linked (By similarity).
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain, repeat, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 32-205 | VWFD 1 | ||||
Sequence: HVCSTWGDFHYKTFDGDVYRFPGLCDYNFASDCRDSYKEFAVHLKRGLGEAGGHSQIESILITIKDDTIYLTHKLAVVNGAMVSTPHYSSGLLIEKNDAYTKVYSRAGLSLMWNREDALMVELDSRFQNHTCGLCGDFNGMQTNYEFLSEEGIQFSAIEFGNMQKINKPEVQCE | ||||||
Domain | 293-349 | TIL | ||||
Sequence: CPNNMVYLESSSPCVDTCSHLEVSSLCEEHYMDGCFCPEGTVYDDITGSGCIPVSQC | ||||||
Domain | 387-562 | VWFD 2 | ||||
Sequence: ETCALEGGSHITTFDGKKFTFHGDCYYVLTKSEHNDSYALLGELASCGSTDKQTCLKTVVLLTDDKKNVVAFKSGGSVLLNEMEVTLPHVAASFSIFQPSSYHIVVNTKFGLRLQIQLLPVMQLFVTLDQAAQGQVQGLCGNFNGLESDDFMTSGGMVEATGAGFANTWKAQSSCH | ||||||
Domain | 857-1026 | VWFD 3 | ||||
Sequence: STCSIYGSGHYITFDGKHYDFDGHCSYVAVQDYCGQNSTGSFSIITENVPCGTTGVTCSKAIKIFIGGTELKLVDKHRVVKQLEEGHHVPYITREVGQYLVVEASSGIIVIWDKKTTIFIKLDPSYKGTVCGLCGNFDDQTKNDFTTRDHMVVTSELDFGNSWKEASTCP | ||||||
Repeat | 1395-1415 | 1 | ||||
Sequence: SPTTSTTTLSTTPPTSSPTTL | ||||||
Region | 1395-2866 | Disordered | ||||
Sequence: SPTTSTTTLSTTPPTSSPTTLPTSSPVTSSATLPTTSSITSTISPTTSPTTPLTTSPTTSPTTSPTTPSTTSPTTPTTTSPTTPSTTSPTTPSTTPSTTSPTTPSTTSPTTPTSTSPNTQSTTSPTTSPTTPSTTSPTTSPTTPSTTSPTISTTTSTISPTTPSTTSPNTPSTTSSTIPSTTSPTTPSTTSPTISTTTSTTSPTTPSTTSPTTPSTTSPTTPSTTSPTISTTTLTTSPTTPSTTSPTTPSTTSPTTPSTTSPTISITTSTISPTTPSTTSPTTLSTTSPTTPSTTSPTISTTTSTSPTTPSTTSPTTPSTPSSTTPSTTSPTTPSTTSPTISTTSSTISPTTPSTTSPTTPSTTSPTTPSTTSPTISTTTSTISPTTPSTTSPTTPSTTSPTTPSTTSPTISTTTSTISPTTPSTTSPTTPSTTSPNTPSTTSTTTSTTSPTTPSTTSPTISTTTSTTSPTTPSTTSPTISTTTSTTSPTTPSTTSPTTPSTTSPTTPSTTSPTTPSTTSPTISTTSSTISPTTPSTTSPTTPSTTSPTTPSTTSPTISTTTSTTSPTTPSTTSPTISTTTSTISPTTPSTSSPTTPSTTSPTTPSTTSPTISTTTSTTSPTTPSTTSPTTPSTTSPTISTTTSTTSPTTPSTTSPTISTTTSTTSPTTPSTTSPTTPSTTSPTTPSTTSPTTPSTTSPTISTTSSTISPTTPSTTSPTTPSTTSPTTPSTTSPTISTTTSTTSPTTPSTTSPTISTTTSTTSPTTPSTTSPTTPSTTSPTTPSTTSPTTPSTTSPTISTTSSTISPTTPSTTSPTTPSTTSPTTPSTTSPTISTTTSTTSPTTPSTTSPTISTTTSTISPTTPSTTSPITPSTTSPTTPSTTSPTISTTTSTTSPTTPSTTSPTISTTTSTISPTTPSTTSPITPSTTSPTTPSTTSPTISTTTSTISPTTPSTTSPTTPSTTSPTTLSTTSPTISTTTSTISPTTPSTTSPTTPSTTSPTTPSTTSPTTPSTTSPTISTTTSTISPTTSPTTPSTTSPTTHSTTSPTTPSTTSPTISTTTSTISPTTPSTTSLTTPSTTSPTTPSTTSPTTPSTTSPTISTTTSTISPTTPSTTSPTTPSTTSPTTPSTTSPNISTTTSTISPTTPSTTSPTTPSTTSPTTPSTTSPTISTTTSTISPTTPSTTSPTTPSTTSPTTPSTTSPTTPSTTSPTISTTTSTISPTTPSTTSPTTPSTTSPTTQSTTSPTISTNTPSTTSPTTPSTTSPTISTTTSTISPTTPSTTSPTTPSTTSPTTSSTTSPTISTTTSTISPTTPSTTSPTTPSTTSPTTPLTTSPTISTTTSTISPTTPSTTSPTTPSTTSPTTPSTTSPTTPSTTSPTISTTTSTISPTTPSTTSPTTSPTTPSTTSPTTSSTATQTISVTTSQTSSSATPPNSSPTSSATTSPTTSSGTSTATSPSTSPTTSSTFTTP | ||||||
Repeat | 1416-1427 | 2 | ||||
Sequence: PTSSPVTSSATL | ||||||
Repeat | 1428-1437 | 3 | ||||
Sequence: PTTSSITSTI | ||||||
Repeat | 1438-1453 | 4 | ||||
Sequence: SPTTSPTTPLTTSPTT | ||||||
Repeat | 1454-1460 | 5 | ||||
Sequence: SPTTSPT | ||||||
Repeat | 1478-1497 | 7B | ||||
Sequence: PSTTSPTTPSTTPSTTSPTT | ||||||
Repeat | 1498-1510 | 8A | ||||
Sequence: PSTTSPTTPTSTS | ||||||
Repeat | 1530-1556 | 9B | ||||
Sequence: SPTTSPTTPSTTSPTISTTTSTISPTT | ||||||
Repeat | 1557-1572 | 10A | ||||
Sequence: PSTTSPNTPSTTSSTI | ||||||
Repeat | 1573-1588 | 10B | ||||
Sequence: PSTTSPTTPSTTSPTI | ||||||
Repeat | 1589-1607 | 11A | ||||
Sequence: STTTSTTSPTTPSTTSPTT | ||||||
Repeat | 1608-1634 | 11B | ||||
Sequence: PSTTSPTTPSTTSPTISTTTLTTSPTT | ||||||
Repeat | 1635-1642 | 12 | ||||
Sequence: PSTTSPTT | ||||||
Repeat | 1665-1681 | 15 | ||||
Sequence: ISPTTPSTTSPTTLSTT | ||||||
Region | 2975-3706 | Disordered | ||||
Sequence: PSSTTTETPTTTSTTKTSILTSTTTQTPSPSPTTTVTPTPAPTTTQIPTSTSTTTQTTTPTPITETSTPTSTISQTPSPASTTTVTPATTSTTTETSTSTSTTTQTTSPTPTVTETSTPRSTTTQTPSPVPTTTVTSTPTPTIGETTTPTTTITETFTPRSTTTQTSSPVPSTTVTPTPTPITTETSTSTPTTTQTTTPTPITETSTPISTTTHTPSPSSTTSTTSTQTPTPTTTGPSTSTSTTIQTTTPTPITETFTPTSTTTQTPSSTPTTTVTPTPTTTETSTSTSTTTQTTTPTPITETFTPTSTTTQTPSPTPTTTVNPTPTPTTIGPSTSTSTTTQTTTPTPTGTETSTPTSTTTQTPSPTPTTTVTPTPSPTTTETSTSTTTQTTTPTPTGTETSTPTSTTTQTPSPTPTTTVTPTPSPTTTETSTSTTTQTTTPTPITETSTPTSTTTQTPSPTPTTTVTPTSTPTTTGTSTSTSTTTQTTTPTPTGTETFTPRSTTTQTPSSSSTTSGTPTPTPTTTHTSTLTSTTEASTPTPIIETSTPKSTTIQTPSPSPTTTVTSPTTPTTTVKETSTPTNTVPTTGSTSSKPPTESSTPVTSQSTPSPPTESTTLSSTPVTTATSSTASSPGTTSPFVTSSAGSTPSSPPGSTPGPTTSSGMPTSSKTTTGPTSPTTRPPSTSTPTSFTVPTETTTQTRPLSTTPTTLETTRTSSWGTFSSTSPITSPS | ||||||
Region | 3764-3806 | Disordered | ||||
Sequence: STPTPSTPTPTPSQTTTPSTTSSKSTPSTPQSTSPKSTLSTPT | ||||||
Compositional bias | 3776-3806 | Polar residues | ||||
Sequence: SQTTTPSTTSSKSTPSTPQSTSPKSTLSTPT | ||||||
Domain | 3880-4063 | VWFD 4 | ||||
Sequence: CYCTGWGDPHFVTFDGLYYSYQGNCTYVLVEEITPTVDNFGVYIDNYHCDANDKVSCPRTLIVRHETQEVQIKTVRMMPIEVEVQVNKQLVALPYKKYGLEVYESGINIVVNISRLEAKISYNGLSFSIRLPYKLFGNNTKGQCGTCTNNTADDCILPSGKIISDCEIAADEWLVNDPSKPHCP | ||||||
Domain | 4213-4282 | VWFC 1 | ||||
Sequence: CVGPDNVPREFGEHFEFDCKDCVCREGGSGIVCQPKKCSGGNQTTCEEDGTYLVVETNPDDKCCNITSCK | ||||||
Domain | 4320-4387 | VWFC 2 | ||||
Sequence: GVCVHQNAEYQPGSPVYSNKCQDCVCTNILDNSTQLNVISCTHVPCNISCSSGFELVDVPGECCKKCQ | ||||||
Domain | 4471-4556 | CTCK | ||||
Sequence: CSAVSVMKEISYNGCTKNISMNYCFGSCGTFAMYSAQVQGLDHRCSCCKEEKTSVRSVTLECPDGSELSHTYTHIESCLCQDTVCG |
Domain
The CTCK domain mediates interchain disulfide bonds with another molecule of MUC2.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length4,576
- Mass (Da)479,290
- Last updated2023-02-22 v3
- ChecksumA7FF1C6456439021
Sequence caution
Features
Showing features for sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 301 | in Ref. 2; AAD01593 | ||||
Sequence: E → G | ||||||
Compositional bias | 3776-3806 | Polar residues | ||||
Sequence: SQTTTPSTTSSKSTPSTPQSTSPKSTLSTPT | ||||||
Sequence conflict | 4294 | in Ref. 3; AAH36168 | ||||
Sequence: T → P |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AJ511872 EMBL· GenBank· DDBJ | CAD54414.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AJ511873 EMBL· GenBank· DDBJ | CAD54416.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AJ511874 EMBL· GenBank· DDBJ | CAD54416.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF016695 EMBL· GenBank· DDBJ | AAD01593.1 EMBL· GenBank· DDBJ | mRNA | ||
BC024540 EMBL· GenBank· DDBJ | - | mRNA | No translation available. | |
BC030862 EMBL· GenBank· DDBJ | AAH30862.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
BC036168 EMBL· GenBank· DDBJ | AAH36168.1 EMBL· GenBank· DDBJ | mRNA | ||
AK008250 EMBL· GenBank· DDBJ | BAB25557.1 EMBL· GenBank· DDBJ | mRNA |