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Mucin-2 (MUC-2) (Colonic mucin) (MCM) (Secreted gel-forming mucin) (Fragments)

 MUC2_MOUSE              Reviewed;        2680 AA.
Q80Z19; Q0P637; Q80Z17; Q8K0Q1; Q9CVG8; Q9Z2U5;
16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
16-JUN-2009, sequence version 2.
18-JUL-2018, entry version 106.
RecName: Full=Mucin-2 {ECO:0000303|PubMed:9886986};
Short=MUC-2 {ECO:0000303|PubMed:9886986};
AltName: Full=Colonic mucin {ECO:0000303|PubMed:9886986};
Short=MCM {ECO:0000303|PubMed:9886986};
AltName: Full=Secreted gel-forming mucin {ECO:0000312|EMBL:CAD54414.1};
Flags: Precursor; Fragments;
Name=Muc2 {ECO:0000312|MGI:MGI:1339364};
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1] {ECO:0000305, ECO:0000312|EMBL:CAD54414.1}
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-1442 AND 1759-2680, AND TISSUE
SPECIFICITY.
STRAIN=C57BL/6J {ECO:0000312|EMBL:CAD54414.1};
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).
[2] {ECO:0000305, ECO:0000312|EMBL:AAD01593.1}
NUCLEOTIDE SEQUENCE [MRNA] OF 1-301, TISSUE SPECIFICITY, AND
GLYCOSYLATION.
STRAIN=129 {ECO:0000312|EMBL:AAD01593.1};
TISSUE=Colon {ECO:0000312|EMBL:AAD01593.1};
PubMed=9886986;
van Klinken B.J.-W., Einerhand A.W.C., Duits L.A., Makkink M.K.,
Tytgat K.M.A.J., Renes I.B., Verburg M., Bueller H.A., Dekker J.;
"Gastrointestinal expression and partial cDNA cloning of murine
Muc2.";
Am. J. Physiol. 276:G115-G124(1999).
[3] {ECO:0000305, ECO:0000312|EMBL:AAH30862.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1443-1758 AND 1795-2680.
STRAIN=FVB/N {ECO:0000312|EMBL:AAH30862.1};
TISSUE=Colon {ECO:0000312|EMBL:AAH30862.1};
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4] {ECO:0000305, ECO:0000312|EMBL:BAB25557.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2199-2680.
STRAIN=C57BL/6J {ECO:0000312|EMBL:BAB25557.1};
TISSUE=Small intestine {ECO:0000312|EMBL:BAB25557.1};
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[5] {ECO:0000305}
DISRUPTION PHENOTYPE.
PubMed=11872843; DOI=10.1126/science.1069094;
Velcich A., Yang W., Heyer J., Fragale A., Nicholas C., Viani S.,
Kucherlapati R., Lipkin M., Yang K., Augenlicht L.;
"Colorectal cancer in mice genetically deficient in the mucin Muc2.";
Science 295:1726-1729(2002).
[6] {ECO:0000305}
FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
PubMed=18806221; DOI=10.1073/pnas.0803124105;
Johansson M.E.V., Phillipson M., Petersson J., Velcich A., Holm L.,
Hansson G.C.;
"The inner of the two Muc2 mucin-dependent mucus layers in colon is
devoid of bacteria.";
Proc. Natl. Acad. Sci. U.S.A. 105:15064-15069(2008).
[7] {ECO:0000305}
IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, INTERACTION WITH FCGBP,
AND SUBCELLULAR LOCATION.
PubMed=19432394; DOI=10.1021/pr9002504;
Johansson M.E.V., Thomsson K.A., Hansson G.C.;
"Proteomic analyses of the two mucus layers of the colon barrier
reveal that their main component, the Muc2 mucin, is strongly bound to
the Fcgbp protein.";
J. Proteome Res. 8:3549-3557(2009).
-!- FUNCTION: Coats the epithelia of the intestines, airways, and
other mucus membrane-containing organs. Thought to provide a
protective, lubricating barrier against particles and infectious
agents at mucosal surfaces. Major constituent of both the inner
and outer mucus layers of the colon and may play a role in
excluding bacteria from the inner mucus layer.
{ECO:0000250|UniProtKB:Q02817, ECO:0000269|PubMed:18806221,
ECO:0000269|PubMed:19432394}.
-!- SUBUNIT: Homotrimer; disulfide-linked. Dimerizes in the
endoplasmic reticulum via its C-terminal region and polymerizes
via its N-terminal region by disulfide-linked trimerization (By
similarity). Interacts with FCGBP. Interacts with AGR2; disulfide-
linked (By similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18806221,
ECO:0000269|PubMed:19432394}. Note=In the intestine, secreted into
the inner and outer mucus layers.
-!- 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). {ECO:0000269|PubMed:14984930,
ECO:0000269|PubMed:9886986}.
-!- PTM: O-glycosylated. {ECO:0000269|PubMed:9886986}.
-!- PTM: 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.
{ECO:0000269|PubMed:18806221}.
-!- PTM: May undergo autocatalytic cleavage in vivo triggered by the
low pH of the late secretory pathway.
{ECO:0000250|UniProtKB:Q02817}.
-!- DISRUPTION PHENOTYPE: Aberrant intestinal crypt morphology and
altered cell maturation and migration. Frequent development of
adenomas in the small intestine which progress to invasive
adenocarcinomas, as well as rectal tumors. 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. {ECO:0000269|PubMed:11872843,
ECO:0000269|PubMed:18806221}.
-!- SEQUENCE CAUTION:
Sequence=AAH30862.1; Type=Erroneous initiation; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Mucin database;
URL="http://www.medkem.gu.se/mucinbiology/databases/";
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EMBL; AJ511872; CAD54414.1; -; Genomic_DNA.
EMBL; AJ511873; CAD54416.1; -; Genomic_DNA.
EMBL; AJ511874; CAD54416.1; JOINED; Genomic_DNA.
EMBL; AF016695; AAD01593.1; -; mRNA.
EMBL; BC024540; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; BC030862; AAH30862.1; ALT_INIT; mRNA.
EMBL; BC036168; AAH36168.1; -; mRNA.
EMBL; AK008250; BAB25557.1; -; mRNA.
UniGene; Mm.2041; -.
UniGene; Mm.461296; -.
ProteinModelPortal; Q80Z19; -.
SMR; Q80Z19; -.
STRING; 10090.ENSMUSP00000026590; -.
MEROPS; I08.954; -.
SwissPalm; Q80Z19; -.
MaxQB; Q80Z19; -.
PaxDb; Q80Z19; -.
PeptideAtlas; Q80Z19; -.
PRIDE; Q80Z19; -.
UCSC; uc029wpp.2; mouse.
MGI; MGI:1339364; Muc2.
HOGENOM; HOG000203111; -.
InParanoid; Q80Z19; -.
TreeFam; TF337106; -.
ChiTaRS; Muc2; mouse.
Proteomes; UP000000589; Unplaced.
GO; GO:0031012; C:extracellular matrix; IDA:MGI.
GO; GO:0070702; C:inner mucus layer; IDA:UniProtKB.
GO; GO:0070703; C:outer mucus layer; IDA:UniProtKB.
GO; GO:0006915; P:apoptotic process; IMP:MGI.
GO; GO:0002064; P:epithelial cell development; IMP:MGI.
GO; GO:0030277; P:maintenance of gastrointestinal epithelium; ISO:MGI.
GO; GO:0030336; P:negative regulation of cell migration; IMP:MGI.
GO; GO:0008285; P:negative regulation of cell proliferation; IMP:MGI.
GO; GO:0043065; P:positive regulation of apoptotic process; IMP:MGI.
InterPro; IPR006207; Cys_knot_C.
InterPro; IPR028580; MUC2.
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.
InterPro; IPR025155; WxxW_domain.
PANTHER; PTHR11339:SF261; PTHR11339:SF261; 3.
Pfam; PF08742; C8; 4.
Pfam; PF13330; Mucin2_WxxW; 2.
Pfam; PF01826; TIL; 2.
Pfam; PF00094; VWD; 4.
SMART; SM00832; C8; 4.
SMART; SM00041; CT; 1.
SMART; SM00214; VWC; 4.
SMART; SM00215; VWC_out; 2.
SMART; SM00216; VWD; 4.
SUPFAM; SSF57567; SSF57567; 4.
PROSITE; PS01185; CTCK_1; 1.
PROSITE; PS01225; CTCK_2; 1.
PROSITE; PS01208; VWFC_1; 2.
PROSITE; PS50184; VWFC_2; 2.
PROSITE; PS51233; VWFD; 4.
1: Evidence at protein level;
Autocatalytic cleavage; Complete proteome; Disulfide bond;
Glycoprotein; Phosphoprotein; Reference proteome; Repeat; Secreted;
Signal.
SIGNAL 1 20 {ECO:0000255}.
CHAIN 21 2680 Mucin-2. {ECO:0000255}.
/FTId=PRO_0000378062.
DOMAIN 33 238 VWFD 1. {ECO:0000255|PROSITE-
ProRule:PRU00580}.
DOMAIN 295 351 TIL. {ECO:0000255}.
DOMAIN 388 601 VWFD 2. {ECO:0000255|PROSITE-
ProRule:PRU00580}.
DOMAIN 857 1062 VWFD 3. {ECO:0000255|PROSITE-
ProRule:PRU00580}.
DOMAIN 1985 2197 VWFD 4. {ECO:0000255|PROSITE-
ProRule:PRU00580}.
DOMAIN 2315 2386 VWFC 1. {ECO:0000255|PROSITE-
ProRule:PRU00220}.
DOMAIN 2424 2491 VWFC 2. {ECO:0000255|PROSITE-
ProRule:PRU00220}.
DOMAIN 2575 2660 CTCK. {ECO:0000255|PROSITE-
ProRule:PRU00039}.
COMPBIAS 1257 1913 Thr-rich. {ECO:0000255}.
MOD_RES 21 21 Phosphoserine.
{ECO:0000250|UniProtKB:Q02817}.
CARBOHYD 667 667 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1227 1227 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1849 1849 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 56 64 {ECO:0000255}.
DISULFID 2575 2622 {ECO:0000255}.
DISULFID 2589 2636 {ECO:0000255}.
DISULFID 2598 2652 {ECO:0000255}.
DISULFID 2602 2654 {ECO:0000255}.
DISULFID ? 2659 {ECO:0000255}.
CONFLICT 301 301 E -> G (in Ref. 2; AAD01593).
{ECO:0000305}.
CONFLICT 2120 2120 V -> G (in Ref. 3; AAH30862/AAH36168).
{ECO:0000305}.
CONFLICT 2398 2398 T -> P (in Ref. 3; AAH36168).
{ECO:0000305}.
NON_CONS 1442 1443 {ECO:0000305}.
NON_CONS 1758 1759 {ECO:0000305}.
SEQUENCE 2680 AA; 293436 MW; D67D8664AAB15933 CRC64;
MGLPLARLVA ACLVLALAKG SELQKEARSR NHVCSTWGDF HYKTFDGDVY RFPGLCDYNF
ASDCRDSYKE FAVHLKRGLG EAGGHSQIES ILITIKDDTI YLTHKLAVVN GAMVSTPHYS
SGLLIEKNDA YTKVYSRAGL SLMWNREDAL MVELDSRFQN HTCGLCGDFN GMQTNYEFLS
EEGIQFSAIE FGNMQKINKP EVQCEDPEAV QEPESCSEHR AECERLLTSA AFEDCQTRVP
VESYVRACMH DRCQCPKGGA CECSTLAEFS RQCSHAGGRP ENWRTASLCP KKCPNNMVYL
ESSSPCVDTC SHLEVSSLCE EHYMDGCFCP EGTVYDDITG SGCIPVSQCH CKLHGHLYMP
GQEFTNDCEQ CVCNAGRWVC KDLPCPETCA LEGGSHITTF DGKKFTFHGD CYYVLTKSEH
NDSYALLGEL ASCGSTDKQT CLKTVVLLTD DKKNVVAFKS GGSVLLNEME VTLPHVAASF
SIFQPSSYHI VVNTKFGLRL QIQLLPVMQL FVTLDQAAQG QVQGLCGNFN GLESDDFMTS
GGMVEATGAG FANTWKAQSS CHDKLDWLDD PCSLNIETNY AEHWCSLLKR SETPFARCHL
AVDPTEYYKR CKYDTCNCQN NEDCMCAALS SYARACAAKG VMLWGWRERV CNKDVHACPS
SQIFMYNLTT CQQTCRSLSE GDSHCLKGFA PVEGCGCPDH TFMDEKGRCV PLAKCSCYHH
GLYLEAGDVI LRQEERCICR NGRLQCTQVK LIGHTCQYPK ILVDCNNLTA LAVRKPRPTS
CQTLVAGYYH TECISGCVCP DGLLDDGRGG CVEEDKCPCI HNKDLYSSGE SIKLDCNNTC
TCQKGRWECT RYACHSTCSI YGSGHYITFD GKHYDFDGHC SYVAVQDYCG QNSTGSFSII
TENVPCGTTG VTCSKAIKIF IGGTELKLVD KHRVVKQLEE GHHVPYITRE VGQYLVVEAS
SGIIVIWDKK TTIFIKLDPS YKGTVCGLCG NFDDQTKNDF TTRDHMVVTS ELDFGNSWKE
ASTCPDVSHN PDPCSLNPHR RSWAEKQCSI IKSRVFKVCH SKVDPTVFYE ACVHDSCSCD
TGGDCDCFCS AVASYAQECT KAEACVFWRT PDLCPIFCDY YNPPDECEWH YEPCGNRSFE
TCRTLNGIHS NISVSYLEGC YPRCPEDRPI YDEDLKKCVT GDKCGCYIED TRYPPGGSVP
TDEICKSCTC TNTSKIECHP DEGKILNMTQ DGIFCYWEFC GPNGTVGQHF NICGSSTAIP
STTTSFTTIS TPISTTPIST TITTTTVTMT TEQVPCCFWS DWINKYHPTK ENGGDRETFT
HVCSAPEDIE CRAATDPKLS WEELGQKVQC NVSTGLICNN EDQYGIGEFE LCYDYEIRVN
CCYPMEYCTP STISPTTSTT TLSTTPPTSS PTTLPTSSPV TSSATLPTTS SITSTISPTT
SPSTATQTIS VTTSQTSSSA TPPNSSPTSS ATTSPTTSSG TSTATSPSTS PTTSSTFTTP
PSTTCIDDCK WTGWLDSGKP TYDIKSGDFE LIKGVCEPHW EVQNISCRAV MHSNIPLDQL
GQIVVCNKEV GLVCKNEDQE IGGIIPMRMC LNYEINVYCC NPICFTSTPS STTTETPTTT
STTKTSILTS TTTQTPSPSP TTTVTPTPAP TTTQIPTSTS TTTQTTTPTP ITETSTPTST
ISQTPSPAST TTVTPATTST TTETSTSTST TTQTTSPTPT VTETSTPRST TTQTPSPVPT
TTVTSTPTPT IGETTTPKRP PSTSTPTSFT VPTETTTQTR PLSTTPTTLE TTRTSSWGTF
SSTSPITSPS TVWTHTETQV TCCVLNEMFY GPGELVYNST HGGTCFYVNC SLDCHLQFFN
WSCPSTPSTP TPSTPTPTPS QTTTPSTTSS KSTPSTPQST SPKSTLSTPT KTTPYGCPDF
DPPRQVNETW WLCNCTMAIC NHDNVVEIVP LKCDPPPMPT CANGLKPVRV PDADNCCWHW
ECDCYCTGWG DPHFVTFDGL YYSYQGNCTY VLVEEITPTV DNFGVYIDNY HCDANDKVSC
PRTLIVRHET QEVQIKTVRM MPIEVEVQVN KQLVALPYKK YGLEVYESGI NIVVNISRLE
AKISYNGLSF SIRLPYKLFV NNTKGQCGTC TNNTADDCIL PSGKIISDCE IAADEWLVND
PSKPHCPHKG LTTKRPATTT PGLSLNNCTV SPVCHLIMDS LFSQCHAFVP PKHYYEACLF
DSCYVPGSNM ECASVQAYAT LCAKEGVCID WRNHTQGVCS VKCPPHKQYQ ACGPEEEPTC
QPSSSQNSTL LVEGCFCPEG TTKFAPGYDV CVKTCGCVGP DNVPREFGEH FEFDCKDCVC
REGGSGIVCQ PKKCSGGNQT TCEEDGTYLV VETNPDDKCC NITSCKCDTK RCKAERPTCL
LGFEVKTEIV PGKCCPVYSC VPKGVCVHQN AEYQPGSPVY SNKCQDCVCT NILDNSTQLN
VISCTHVPCN ISCSSGFELV DVPGECCKKC QQTHCIIEGP KQQYIILKPG EIHKNPSNKC
TFFSCMKINN QLISSVSNIT CPDFNPSDCV SGSITYMPNG CCKTCIPQNQ TRVPCSAVSV
MKEISYNGCT KNISMNYCFG SCGTFAMYSA QVQGLDHRCS CCKEEKTSVR SVTLECPDGS
ELSHTYTHIE SCLCQDTVCG LPQAQQVRTR RSSPRFLGRK


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U1034m CLIA Ascites sialoglycoprotein,ASGP,Mouse,Muc4,MUC-4,Mucin-4,Mus musculus,Pancreatic adenocarcinoma mucin,Testis mucin 96T
E1034m ELISA Ascites sialoglycoprotein,ASGP,Mouse,Muc4,MUC-4,Mucin-4,Mus musculus,Pancreatic adenocarcinoma mucin,Testis mucin 96T
E1034m ELISA kit Ascites sialoglycoprotein,ASGP,Mouse,Muc4,MUC-4,Mucin-4,Mus musculus,Pancreatic adenocarcinoma mucin,Testis mucin 96T
gen10408 MUC2_MOUSE Secreted gel-forming mucin ELISA tesk kit 1
20-272-191614 Mucin 5AC. prediluted - Mouse monoclonal [SPM297] to Mucin 5AC. prediluted; Mucin-5 subtype AC. tracheobronchial; Tracheobronchial mucin; TBM; Major airway glycoprotein Monoclonal 7 ml


 

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