ID MUC6_MOUSE Reviewed; 2850 AA. AC Q80T03; Q80Z22; DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2003, sequence version 1. DT 08-NOV-2023, entry version 98. DE RecName: Full=Mucin-6; DE Short=MUC-6; DE AltName: Full=Gastric mucin-6; DE AltName: Full=Secreted gel-forming mucin-6; DE Flags: Precursor; GN Name=Muc6; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY. RC STRAIN=C57BL/6J; RX PubMed=12676567; DOI=10.1016/s0888-7543(03)00036-3; RA Desseyn J.-L., Laine A.; RT "Characterization of mouse muc6 and evidence of conservation of the gel- RT forming mucin gene cluster between human and mouse."; RL Genomics 81:433-436(2003). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1436-2850, AND TISSUE SPECIFICITY. RC STRAIN=C57BL/6J; RX PubMed=14984930; DOI=10.1016/j.bbaexp.2004.01.001; RA Escande F., Porchet N., Bernigaud A., Petitprez D., Aubert J.-P., RA Buisine M.-P.; RT "The mouse secreted gel-forming mucin gene cluster."; RL Biochim. Biophys. Acta 1676:240-250(2004). CC -!- FUNCTION: May provide a mechanism for modulation of the composition of CC the protective mucus layer related to acid secretion or the presence of CC bacteria and noxious agents in the lumen. Plays an important role in CC the cytoprotection of epithelial surfaces and are used as tumor markers CC in a variety of cancers. May play a role in epithelial organogenesis. CC -!- SUBUNIT: Multimer; disulfide-linked. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Secreted. CC -!- TISSUE SPECIFICITY: Expressed in stomach, duodenum and small intestine. CC {ECO:0000269|PubMed:12676567, ECO:0000269|PubMed:14984930}. CC -!- PTM: O-glycosylated. {ECO:0000250}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AY184388; AAO47735.1; -; Genomic_DNA. DR EMBL; AY184385; AAO47735.1; JOINED; Genomic_DNA. DR EMBL; AY184387; AAO47735.1; JOINED; Genomic_DNA. DR EMBL; AY184386; AAO47735.1; JOINED; Genomic_DNA. DR EMBL; AJ511869; CAD54411.1; -; Genomic_DNA. DR SMR; Q80T03; -. DR STRING; 10090.ENSMUSP00000140483; -. DR MEROPS; I08.952; -. DR GlyCosmos; Q80T03; 6 sites, No reported glycans. DR GlyGen; Q80T03; 6 sites. DR iPTMnet; Q80T03; -. DR PhosphoSitePlus; Q80T03; -. DR MaxQB; Q80T03; -. DR PaxDb; 10090-ENSMUSP00000140483; -. DR ProteomicsDB; 287330; -. DR UCSC; uc009klu.2; mouse. DR AGR; MGI:2663233; -. DR MGI; MGI:2663233; Muc6. DR eggNOG; KOG1216; Eukaryota. DR InParanoid; Q80T03; -. DR PhylomeDB; Q80T03; -. DR Reactome; R-MMU-913709; O-linked glycosylation of mucins. DR Reactome; R-MMU-977068; Termination of O-glycan biosynthesis. DR PRO; PR:Q80T03; -. DR Proteomes; UP000000589; Unplaced. DR RNAct; Q80T03; Protein. DR GO; GO:0031012; C:extracellular matrix; IBA:GO_Central. DR GO; GO:0005615; C:extracellular space; IBA:GO_Central. DR CDD; cd19941; TIL; 3. DR Gene3D; 2.10.25.10; Laminin; 3. DR InterPro; IPR006207; Cys_knot_C. DR InterPro; IPR036084; Ser_inhib-like_sf. DR InterPro; IPR002919; TIL_dom. DR InterPro; IPR014853; VWF/SSPO/ZAN-like_Cys-rich_dom. DR InterPro; IPR001007; VWF_dom. DR InterPro; IPR001846; VWF_type-D. DR PANTHER; PTHR11339; EXTRACELLULAR MATRIX GLYCOPROTEIN RELATED; 1. DR PANTHER; PTHR11339:SF264; MUCIN-6; 1. DR Pfam; PF08742; C8; 3. DR Pfam; PF01826; TIL; 2. DR Pfam; PF00094; VWD; 4. DR SMART; SM00832; C8; 3. DR SMART; SM00215; VWC_out; 2. DR SMART; SM00216; VWD; 3. DR SUPFAM; SSF57567; Serine protease inhibitors; 3. DR PROSITE; PS01225; CTCK_2; 1. DR PROSITE; PS51233; VWFD; 3. PE 2: Evidence at transcript level; KW Disulfide bond; Glycoprotein; Reference proteome; Repeat; Secreted; Signal. FT SIGNAL 1..22 FT /evidence="ECO:0000255" FT CHAIN 23..2850 FT /note="Mucin-6" FT /id="PRO_0000259497" FT DOMAIN 43..256 FT /note="VWFD 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580" FT DOMAIN 344..399 FT /note="TIL 1" FT DOMAIN 437..621 FT /note="VWFD 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580" FT DOMAIN 806..869 FT /note="TIL 2" FT DOMAIN 908..1080 FT /note="VWFD 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580" FT REPEAT 1440..1555 FT /note="1" FT REPEAT 1556..1712 FT /note="2" FT REPEAT 1713..1885 FT /note="3" FT REPEAT 1886..2054 FT /note="4" FT REPEAT 2055..2227 FT /note="5" FT REPEAT 2228..2396 FT /note="6" FT REPEAT 2397..2563 FT /note="7" FT REPEAT 2564..2671 FT /note="8" FT DOMAIN 2760..2849 FT /note="CTCK" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00039" FT REGION 160..183 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1263..1363 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1377..1400 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1440..2671 FT /note="Approximate repeats" FT /evidence="ECO:0000250" FT REGION 1466..1504 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1580..1600 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1626..1650 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1705..1813 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1877..1942 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1968..1992 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 2049..2119 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 2219..2254 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 2276..2295 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 2306..2338 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 2370..2473 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 2511..2621 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 2634..2674 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 2692..2761 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1291..1319 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1320..1334 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1335..1363 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT CARBOHYD 94 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 310 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 528 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 701 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 1017 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 1221 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 45..218 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580" FT DISULFID 67..255 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580" FT DISULFID 439..575 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580" FT DISULFID 461..620 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580" FT DISULFID 910..1044 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580" FT DISULFID 932..1079 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580" FT DISULFID 941..1041 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580" FT DISULFID 959..966 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580" FT DISULFID 2760..2807 FT /evidence="ECO:0000250" FT DISULFID 2774..2821 FT /evidence="ECO:0000250" FT DISULFID 2783..2841 FT /evidence="ECO:0000250" FT DISULFID 2787..2843 FT /evidence="ECO:0000250" FT DISULFID ?..2848 FT /evidence="ECO:0000250" FT CONFLICT 1436..1446 FT /note="DITKTQNLFST -> ILHRRTSTSTS (in Ref. 2; CAD54411)" FT /evidence="ECO:0000305" FT CONFLICT 2793 FT /note="Missing (in Ref. 2; CAD54411)" FT /evidence="ECO:0000305" SQ SEQUENCE 2850 AA; 300401 MW; 9CD95F0845C79C9D CRC64; MLRVRQLLLL LLFRGPLIDA GAWTGDVTDS DTEDNLQSSP EKGWCSTWGA GHFSTFDGHE YNFQGMCNYI FTATCGDDVP ATFSIQLRRD MEGNISRIIM ELGASVVTVN KETISVRDIG VVSLPYTSNG LQITPYGQSV QLVAKQLELE LVITWGPDAH LTEGQGGDEV GTPGTLKQES KGSPAWAGSS LCIPTETNST TPQVQVETKY MGKLCGLCGN FDGKIDNEFL SEDGKLLEAH KYATLQKLDD PNEICAHEAI PSTIILKTRY AQICNQLLTL VSPGCDVPKE TLMLSCQADM AACARPGQPN CSCATLSEYS RRCSMTGQPV RNWRTPALCP MSQCPANQVY QECGEVCIKT CSNPQHSCSS PCTFGCFCPH GTLLDDISGN QSCVPVNQCP CMLNGMVYGP GEITKTACQT CQCTMGRWTC TKQPCPGHCS LEGGSFVTTF DARPYRFHGT CTYTLLQSPQ LPNEGTLMAV YDKSGYSHSE TSLVAIMYLS KKDKIVISED EVITNNGDTK LLPYKTHNIT IFRQTSTHLQ MATTFGLELV FQMQPVFQVY ITVGPQFKGQ TRGLCGNFNG DTTDDFTTSM GIDEGTASLF VDSWRAGNCP AALEREMDPC SMSQLNKVCA ETHCSMLLKK GSVFEKCHSV VNPQPFYKRC VYQACNYEET FPHICSALGA YAHACSARGI LLWGWRNSVD NCTVPCTGNR TFSYDSQACD RTCLSLSDRE TECHVSPVPV DGCNCPEGTY LNHKAECVHK AQCPCLLDDY KFVQADQSTM INGVICHCIN GRLSCPRQAE MFFASCPEPK TFQSCSQSSE DKFGAACAPT CQMLATGIDC VPTKCESGCV CPKGLYENSD GQCVPAEECP CDYAGVSYPG GFELHTDCKT CTCSQGRWTC QLSTQCPSTC VLYGEGHIIT FDGQRFVFDG DCEYMLATDD CGANSSQPTF KVLTENVICG KSGVTCSRAI KISLGGLFIT MADSNYTVSG EEPLVHLKVK PSPLNLVLDI DIPGRLNLTL VWNKHMSVSI KIRRATQDAL CGLCGNANGN MKDDFETRSK YVASNELEFV NSWKESPLCG DASYAVDPCS LNTFRRSWAE RKCNIINSQT FAACHSKVYH LPYYEACVRD ACGCDTGGDC ECLCDAVAAY AKACLDKGVC VDWRTPDFCP IYCDFYNTHT LVGENEYQYA QESNCTWHYQ PCLCPGSLGS FPDTNTEGCY NCSQNEYFDH SEGTCVPCAP PTTTLPPTTT GSQPTTETTI STEFHSSTSA NTPVAPSYLP GLPTPPPSAP SSTEELTVWT TPKESTVSSG EYPQTTMAAT PPTSPWPPTS IPKSTPTELP VTQATSKPTA SSLSSSTKTT AELTESTTVT LLTLMPGMST SQEGTPTSKI PVTQTTTHRV PSRCITNQST TMFQTTTVQE AEITQTLAPS TYTTNDITKT QNLFSTAPHL SETSAVTAHQ STPTAVSANS IKPTMSSTGT PVVHTTSGTS SSPQTPRTTH PSTTVAVSGT VHTTGLPSGT SVHTTTNFPT HSGPQSSLST HLPLFSTLSV TPTTEGLNTQ STPIPAITNS LMTTGGLTGT PPVHTTSGTT SSPQTPRTTH PFSTVAVSNT KHTTGVSLET SVQTTIASPT PSAPQTSLAT HLPFSSTSSV TPTSEVIITP TPQHTLSSAS TSTTTGNILP TTIGKTGSPH TSVPVIYTTS AITQTKTSFS TDRTSTSTSA PHLSETSAVT AHQSTPTAVS ANSIKPTMSS TGTPVVHTTS GTTSSPQTPR TTHPSTTVAV SGTVHTTGLP SGTSVHTTTN FPTHSGPQSS LSTHLPLFST LSVTPTTEGL NTPTSPHSLS VASTSMPLMT VLPTTLEGTR PPHTSVPVTY TTTAATQTKS SFSTDRTSAP HLSQPSTVTP TQSTPIPATT NSLMTTGGLT GTPPVHTTSG TTSSPQTPRT THPFSTVAVS NTKHTTGVSL ETSVQTTIAS PTPSAPQTSL ATHLPFSSTS SVTPTSEVII TPTPQHTLSS ASTSTTTGNI LPTTIGQTGS PHTSVPVIYT TSAITQTKTS FSTDRTSTST SAPHLSETSA VTAHQSTPTA VSANSIKPTM SSTGTPVVHT TSGTTSSPQT PRTTHPSTTV AVSGTVHTTG LPSGTSVHTT TNFPTHSGPQ SSLSTHLPLF STLSVTPTTE GLNTPTSPHS LSAASTSMPL MTVLPTTLEG TRPPHTSVPV TYTTTAATQT KSSFSTDRTS TPHLSQSSTV TPTQPTPIPA TTNSPMTTVG LTGTPVVHTP SGTSSIAHTP HTTHSLPTAA SSSTTLSTAP QFRTSEQSTT TFPTPSAPQT SLVTSLPPFS TSSVSPTDEI HITSTNPHTV SSVSMSRPVS TILQTTIEVT TPPNTSTPVT HSTSATTEAQ GSFSTERTST SYLSHPSSTT VHQSTAGPVI TSIKSTMGVT GTPPVHTTSG TTSSPQTPHS THPISTAAIS RTTGISGTPF RTPMKTTITF PTPSSLQTSM ATLFPPFSTS VMSSTEIFNT PTNPHSVSSA STSRPLSTSL PTTIKGTGTP QTPVSDINTT SATTQAHSSF PTTRTSTSHL SLPSSMTSTL TPASRSASTL QYTPTPSSVS HSPLLTTPTA SPPSSAPTFV SPTAASTVIS SALPTIHMTP TPSSRPTSST GLLSTSKTTS HVPTFSSFSS KSTTAHLTSL TTQAATSGLL SSTMGMTNLP SSGSPDINHT TRPPGSSPLP TSAFLSRSTS PTGSSSPSTP VSSSNPDSSV SSPPSHPGTC SLQEEEHQIT YQGCVANVTL TRCQGFCASS VSFNKDTLQL ESSCGCCQPL STYKKQLSLP CPDPDAPGQQ LTLTLQVFSS CVCSPLQCKN //