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MUC6_MOUSE
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   29-SEP-2021, entry version 93.
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}.
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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   GlyGen; Q80T03; 6 sites.
DR   iPTMnet; Q80T03; -.
DR   PhosphoSitePlus; Q80T03; -.
DR   MaxQB; Q80T03; -.
DR   PaxDb; Q80T03; -.
DR   PRIDE; Q80T03; -.
DR   ProteomicsDB; 287330; -.
DR   UCSC; uc009klu.2; mouse.
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   GO; GO:0030277; P:maintenance of gastrointestinal epithelium; IEA:InterPro.
DR   InterPro; IPR006207; Cys_knot_C.
DR   InterPro; IPR030124; MUC6.
DR   InterPro; IPR036084; Ser_inhib-like_sf.
DR   InterPro; IPR002919; TIL_dom.
DR   InterPro; IPR014853; Unchr_dom_Cys-rich.
DR   InterPro; IPR001007; VWF_dom.
DR   InterPro; IPR001846; VWF_type-D.
DR   PANTHER; PTHR11339:SF264; PTHR11339:SF264; 6.
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; SSF57567; 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
 
 
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