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Mucin-2 (MUC-2) (Intestinal mucin-2) (Fragment)

 MUC2_RAT                Reviewed;        1513 AA.
Q62635;
17-JAN-2003, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
23-MAY-2018, entry version 100.
RecName: Full=Mucin-2;
Short=MUC-2;
AltName: Full=Intestinal mucin-2;
Flags: Precursor; Fragment;
Name=Muc2;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Intestine;
PubMed=8027037;
Ohmori H., Dohrman A.F., Gallup M., Tsuda T., Kai H., Gum J.R. Jr.,
Kim Y.S., Basbaum C.B.;
"Molecular cloning of the amino-terminal region of a rat MUC 2 mucin
gene homologue. Evidence for expression in both intestine and
airway.";
J. Biol. Chem. 269:17833-17840(1994).
[2]
PROTEIN SEQUENCE OF 21-36.
TISSUE=Intestinal epithelium;
PubMed=9512496; DOI=10.1042/bj3310323;
Khatri I.A., Forstner G.G., Forstner J.F.;
"Susceptibility of the cysteine-rich N-terminal and C-terminal ends of
rat intestinal mucin Muc 2 to proteolytic cleavage.";
Biochem. J. 331:323-330(1998).
-!- 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 (By similarity).
{ECO:0000250}.
-!- 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.
Interacts with FCGBP (By similarity). Interacts with AGR2;
disulfide-linked (By similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Secreted. Note=In the intestine, secreted
into the inner and outer mucus layers. {ECO:0000250}.
-!- TISSUE SPECIFICITY: Expressed in intestine and airway.
-!- PTM: O-glycosylated. {ECO:0000250}.
-!- 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:0000250}.
-!- PTM: May undergo autocatalytic cleavage in vivo triggered by the
low pH of the late secretory pathway. {ECO:0000250}.
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EMBL; U07615; AAA21655.2; -; mRNA.
PIR; A54895; A54895.
UniGene; Rn.217174; -.
ProteinModelPortal; Q62635; -.
SMR; Q62635; -.
MEROPS; I08.954; -.
PRIDE; Q62635; -.
RGD; 3123; Muc2.
HOVERGEN; HBG004380; -.
InParanoid; Q62635; -.
PhylomeDB; Q62635; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0005737; C:cytoplasm; IDA:RGD.
GO; GO:0070702; C:inner mucus layer; ISS:UniProtKB.
GO; GO:0070701; C:mucus layer; IDA:RGD.
GO; GO:0005634; C:nucleus; IDA:RGD.
GO; GO:0070703; C:outer mucus layer; ISS:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; IMP:RGD.
GO; GO:0071356; P:cellular response to tumor necrosis factor; IEP:RGD.
GO; GO:0009725; P:response to hormone; IEP:RGD.
GO; GO:0032496; P:response to lipopolysaccharide; IEP:RGD.
GO; GO:0071559; P:response to transforming growth factor beta; IEP:RGD.
GO; GO:0033189; P:response to vitamin A; IEP:RGD.
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; 1.
Pfam; PF08742; C8; 3.
Pfam; PF13330; Mucin2_WxxW; 1.
Pfam; PF01826; TIL; 2.
Pfam; PF00094; VWD; 3.
SMART; SM00832; C8; 3.
SMART; SM00215; VWC_out; 2.
SMART; SM00216; VWD; 3.
SUPFAM; SSF57567; SSF57567; 3.
PROSITE; PS51233; VWFD; 3.
1: Evidence at protein level;
Autocatalytic cleavage; Complete proteome; Direct protein sequencing;
Disulfide bond; Glycoprotein; Reference proteome; Repeat; Secreted;
Signal.
SIGNAL 1 20 {ECO:0000255}.
CHAIN 21 >1513 Mucin-2.
/FTId=PRO_0000019282.
DOMAIN 33 237 VWFD 1. {ECO:0000255|PROSITE-
ProRule:PRU00580}.
DOMAIN 292 348 TIL.
DOMAIN 350 410 VWFC.
DOMAIN 387 601 VWFD 2. {ECO:0000255|PROSITE-
ProRule:PRU00580}.
DOMAIN 857 1062 VWFD 3. {ECO:0000255|PROSITE-
ProRule:PRU00580}.
REPEAT 1392 1407 1.
REPEAT 1408 1423 2.
REPEAT 1424 1434 3.
REPEAT 1435 1445 4.
REPEAT 1446 1456 5.
REPEAT 1457 1467 6.
REPEAT 1468 1478 7.
REPEAT 1479 1489 8.
REPEAT 1490 1500 9.
REPEAT 1501 1511 10.
REPEAT 1512 >1513 11.
REGION 1392 >1513 Approximate repeats.
COMPBIAS 1257 1292 Thr-rich.
COMPBIAS 1389 1512 Ser-rich.
CARBOHYD 160 160 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 420 420 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 667 667 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 767 767 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 837 837 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 892 892 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1136 1136 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1151 1151 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1212 1212 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1227 1227 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1243 1243 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1350 1350 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
NON_TER 1513 1513
SEQUENCE 1513 AA; 166038 MW; 26109DCA1BE7D008 CRC64;
MGLPLARLVA VCLVLALAKG LELQKEARSR NHVCSTWGDF HYKTFDGDVF RFPGLCDYNF
ASDCRDSYKE FAVHLKRGLD KAGGHSSIES VLITIKDDTI YLTHKLAVVN GAMVSTPHYS
SGLLIEKNDA YTKVYSRAGL SLMWNREDAL MVELDGRFQN HTCGLCGDFN GMQANNEFLS
DGIRFSAIEF GNMQKINKPE VVCEDPEEVQ EPESCSEHRA ECERLLTSTA FEDCQARVPV
ELYVLACMHD RCQCPQGGAC ECSTLAEFSR QCSHAGGRPE NWRTASLCPK KCPGNMVYLE
SGSPWLDTCS HLEVSSLCEE HYMDGCFCPE GTVYDDITGS GCIPVSQCHC KLHGHLYMPG
QEITNDCEQC VCNAGRWMCK DLPCPETCAL EGGSHITTFD GKKFTFHGDC YYVLTKTKYN
DSYALLGELA SCGSTDKQTC LKTVVLLTDN KKNVVAFKSG GSVLLNEMEV SLPHVAASFS
IFKPSSYHIV VNTMFGLRLQ IQLVPVMQLF VTLDQSAQGQ VQGLCGNFNG LESDDFMTSG
GMVEATGAGF ANTWKAQSSC HDKLDWLDDP CPLNIESANY AEHWCSLLKR SETPFARCHL
AVDPTEYYKR CKYDTCNCQN NEDCMCAALS SYARACAAKG VMLWGWRESV CNKDVHACPS
SQIFMYNLTT CQQTCRSISE GDTHCLKGFA PVEGCGCPDH TFMDEKGRCV PLSKCSCYHH
GLYLEAGDVI LRQEERCICR NGRLQCTQVK LIGHTCLSPQ ILVDCNNLTA LAIREPRPTS
CQTLVARYYH TECISGCVCP DGLLDNGRGG CVVEDECPCI HNKQFYDSGK SIKLDCNNTC
TCQKGRWECT RYACHSTCSI YGSGHYITFD GKHYDFDGHC SYVAVQDYCG QNSTGSFSII
TENVPCGTTG VTCSKAIKIF IGGTELKLVD KHRVVKQLEE GHHVPFITRE VGLYLVVEVS
SGIIVIWDKK TTIFIKLDPS YKGNVCGLCG NFDDQTKNDF TTRDHMVVAS ELDFGNSWKE
ASTCPDVSHN PDPCSLNPHR RSWAEKQCSI IKSDVFLACH GKVDPTVFYD ACVHDSCSCD
TGGDCECFCS AVASYAQECT KAEACVFWRT PDLCPVFCDY YNPPDECEWH YEPCGNRSFE
TCRTLNGIHS NISVSYLEGC YPRCPEDRPI YDEDLKKCVS GDKCGCYIED TRYPPGGSVP
TDEICMSCTC TNTSEIICRP DEGKIINQTQ DGIFCYWETC GSNGTVEKHF EICVSSTLSP
TSMTSFTTTS TPISTTPIST TITTTSATAT TTVPCCFWSD WINNNHPTSG NGGDRENFEH
VCSAPENIEC RAATDPKLDW TELGQKVQCN VSEGLICNNE DQYGTGQFEL CYDYEIRVNC
CFPMEYCLST VSPTTSTPIS STPQPTSSPT TLPTTSPLTS SATSPTTSHI TSTVSPTTSP
TTSTTSPTTS PTTSTTSPTT STTSPTPSPT TSTTSPTPSP TTSTTSPTPS PTTSTTSPTT
SPITSPTTST TSP


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