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Mucin-6 (MUC-6) (Gastric mucin-6) (Secreted gel-forming mucin-6)

 MUC6_MOUSE              Reviewed;        2850 AA.
Q80T03; Q80Z22;
31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
01-JUN-2003, sequence version 1.
25-OCT-2017, entry version 81.
RecName: Full=Mucin-6;
Short=MUC-6;
AltName: Full=Gastric mucin-6;
AltName: Full=Secreted gel-forming mucin-6;
Flags: Precursor;
Name=Muc6;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
STRAIN=C57BL/6J;
PubMed=12676567; DOI=10.1016/S0888-7543(03)00036-3;
Desseyn J.-L., Laine A.;
"Characterization of mouse muc6 and evidence of conservation of the
gel-forming mucin gene cluster between human and mouse.";
Genomics 81:433-436(2003).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1436-2850, AND TISSUE
SPECIFICITY.
STRAIN=C57BL/6J;
PubMed=14984930; DOI=10.1016/j.bbaexp.2004.01.001;
Escande F., Porchet N., Bernigaud A., Petitprez D., Aubert J.-P.,
Buisine M.-P.;
"The mouse secreted gel-forming mucin gene cluster.";
Biochim. Biophys. Acta 1676:240-250(2004).
-!- FUNCTION: May provide a mechanism for modulation of the
composition of the protective mucus layer related to acid
secretion or the presence of bacteria and noxious agents in the
lumen. Plays an important role in the cytoprotection of epithelial
surfaces and are used as tumor markers in a variety of cancers.
May play a role in epithelial organogenesis.
-!- SUBUNIT: Multimer; disulfide-linked. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Secreted.
-!- TISSUE SPECIFICITY: Expressed in stomach, duodenum and small
intestine. {ECO:0000269|PubMed:12676567,
ECO:0000269|PubMed:14984930}.
-!- PTM: O-glycosylated. {ECO:0000250}.
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EMBL; AY184388; AAO47735.1; -; Genomic_DNA.
EMBL; AY184385; AAO47735.1; JOINED; Genomic_DNA.
EMBL; AY184387; AAO47735.1; JOINED; Genomic_DNA.
EMBL; AY184386; AAO47735.1; JOINED; Genomic_DNA.
EMBL; AJ511869; CAD54411.1; -; Genomic_DNA.
UniGene; Mm.246621; -.
ProteinModelPortal; Q80T03; -.
SMR; Q80T03; -.
STRING; 10090.ENSMUSP00000049941; -.
MEROPS; I08.952; -.
iPTMnet; Q80T03; -.
PhosphoSitePlus; Q80T03; -.
MaxQB; Q80T03; -.
PaxDb; Q80T03; -.
PRIDE; Q80T03; -.
UCSC; uc009klu.2; mouse.
MGI; MGI:2663233; Muc6.
eggNOG; KOG1216; Eukaryota.
eggNOG; ENOG410XNSK; LUCA.
HOGENOM; HOG000170714; -.
HOVERGEN; HBG081998; -.
InParanoid; Q80T03; -.
PhylomeDB; Q80T03; -.
PRO; PR:Q80T03; -.
Proteomes; UP000000589; Unplaced.
CleanEx; MM_MUC6; -.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0030277; P:maintenance of gastrointestinal epithelium; IEA:InterPro.
InterPro; IPR006207; Cys_knot_C.
InterPro; IPR030124; MUC6.
InterPro; IPR036084; Ser_inhib-like_sf.
InterPro; IPR002919; TIL_dom.
InterPro; IPR014853; Unchr_dom_Cys-rich.
InterPro; IPR001007; VWF_dom.
InterPro; IPR001846; VWF_type-D.
PANTHER; PTHR11339:SF264; PTHR11339:SF264; 6.
Pfam; PF08742; C8; 3.
Pfam; PF01826; TIL; 2.
Pfam; PF00094; VWD; 4.
SMART; SM00832; C8; 3.
SMART; SM00215; VWC_out; 2.
SMART; SM00216; VWD; 3.
SUPFAM; SSF57567; SSF57567; 3.
PROSITE; PS01225; CTCK_2; 1.
PROSITE; PS51233; VWFD; 3.
2: Evidence at transcript level;
Complete proteome; Disulfide bond; Glycoprotein; Reference proteome;
Repeat; Secreted; Signal.
SIGNAL 1 22 {ECO:0000255}.
CHAIN 23 2850 Mucin-6.
/FTId=PRO_0000259497.
DOMAIN 44 288 VWFD 1. {ECO:0000255|PROSITE-
ProRule:PRU00580}.
DOMAIN 344 399 TIL 1.
DOMAIN 438 650 VWFD 2. {ECO:0000255|PROSITE-
ProRule:PRU00580}.
DOMAIN 806 869 TIL 2.
DOMAIN 909 1117 VWFD 3. {ECO:0000255|PROSITE-
ProRule:PRU00580}.
REPEAT 1440 1555 1.
REPEAT 1556 1712 2.
REPEAT 1713 1885 3.
REPEAT 1886 2054 4.
REPEAT 2055 2227 5.
REPEAT 2228 2396 6.
REPEAT 2397 2563 7.
REPEAT 2564 2671 8.
DOMAIN 2760 2849 CTCK. {ECO:0000255|PROSITE-
ProRule:PRU00039}.
REGION 1440 2671 Approximate repeats. {ECO:0000250}.
COMPBIAS 2291 2755 Ser-rich.
CARBOHYD 94 94 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 310 310 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 528 528 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 701 701 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1017 1017 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1221 1221 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 67 75 {ECO:0000250}.
DISULFID 2760 2807 {ECO:0000250}.
DISULFID 2774 2821 {ECO:0000250}.
DISULFID 2783 2841 {ECO:0000250}.
DISULFID 2787 2843 {ECO:0000250}.
DISULFID ? 2848 {ECO:0000250}.
CONFLICT 1436 1446 DITKTQNLFST -> ILHRRTSTSTS (in Ref. 2;
CAD54411). {ECO:0000305}.
CONFLICT 2793 2793 Missing (in Ref. 2; CAD54411).
{ECO:0000305}.
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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