MUC2_RAT
ID MUC2_RAT Reviewed; 1513 AA.
AC Q62635;
DT 17-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Mucin-2;
DE Short=MUC-2;
DE AltName: Full=Intestinal mucin-2;
DE Flags: Precursor; Fragment;
GN Name=Muc2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Intestine;
RX PubMed=8027037; DOI=10.1016/s0021-9258(17)32384-0;
RA Ohmori H., Dohrman A.F., Gallup M., Tsuda T., Kai H., Gum J.R. Jr.,
RA Kim Y.S., Basbaum C.B.;
RT "Molecular cloning of the amino-terminal region of a rat MUC 2 mucin gene
RT homologue. Evidence for expression in both intestine and airway.";
RL J. Biol. Chem. 269:17833-17840(1994).
RN [2]
RP PROTEIN SEQUENCE OF 21-36.
RC TISSUE=Intestinal epithelium;
RX PubMed=9512496; DOI=10.1042/bj3310323;
RA Khatri I.A., Forstner G.G., Forstner J.F.;
RT "Susceptibility of the cysteine-rich N-terminal and C-terminal ends of rat
RT intestinal mucin Muc 2 to proteolytic cleavage.";
RL Biochem. J. 331:323-330(1998).
CC -!- FUNCTION: Coats the epithelia of the intestines, airways, and other
CC mucus membrane-containing organs. Thought to provide a protective,
CC lubricating barrier against particles and infectious agents at mucosal
CC surfaces. Major constituent of both the inner and outer mucus layers of
CC the colon and may play a role in excluding bacteria from the inner
CC mucus layer (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homotrimer; disulfide-linked. Dimerizes in the endoplasmic
CC reticulum via its C-terminal region and polymerizes via its N-terminal
CC region by disulfide-linked trimerization. Interacts with FCGBP (By
CC similarity). Interacts with AGR2; disulfide-linked (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted. Note=In the intestine, secreted into
CC the inner and outer mucus layers. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in intestine and airway.
CC -!- PTM: O-glycosylated. {ECO:0000250}.
CC -!- PTM: May undergo proteolytic cleavage in the outer mucus layer of the
CC colon, contributing to the expanded volume and loose nature of this
CC layer which allows for bacterial colonization in contrast to the inner
CC mucus layer which is dense and devoid of bacteria. {ECO:0000250}.
CC -!- PTM: May undergo autocatalytic cleavage in vivo triggered by the low pH
CC of the late secretory pathway. {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; U07615; AAA21655.2; -; mRNA.
DR PIR; A54895; A54895.
DR AlphaFoldDB; Q62635; -.
DR SMR; Q62635; -.
DR MEROPS; I08.954; -.
DR GlyConnect; 380; 63 O-Linked glycans.
DR GlyConnect; 381; 28 O-Linked glycans.
DR GlyGen; Q62635; 13 sites, 72 O-linked glycans (1 site).
DR PRIDE; Q62635; -.
DR RGD; 3123; Muc2.
DR InParanoid; Q62635; -.
DR PhylomeDB; Q62635; -.
DR Reactome; R-RNO-913709; O-linked glycosylation of mucins.
DR Reactome; R-RNO-977068; Termination of O-glycan biosynthesis.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0031012; C:extracellular matrix; ISO:RGD.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0070702; C:inner mucus layer; ISS:UniProtKB.
DR GO; GO:0070701; C:mucus layer; IDA:RGD.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0070703; C:outer mucus layer; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IMP:RGD.
DR GO; GO:0006915; P:apoptotic process; ISO:RGD.
DR GO; GO:0071356; P:cellular response to tumor necrosis factor; IEP:RGD.
DR GO; GO:0002064; P:epithelial cell development; ISO:RGD.
DR GO; GO:0030277; P:maintenance of gastrointestinal epithelium; ISO:RGD.
DR GO; GO:0030336; P:negative regulation of cell migration; ISO:RGD.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISO:RGD.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISO:RGD.
DR GO; GO:0140459; P:response to Gram-positive bacterium; IEP:RGD.
DR GO; GO:0009725; P:response to hormone; IEP:RGD.
DR GO; GO:0032496; P:response to lipopolysaccharide; IEP:RGD.
DR GO; GO:0071559; P:response to transforming growth factor beta; IEP:RGD.
DR GO; GO:0033189; P:response to vitamin A; IEP:RGD.
DR InterPro; IPR028580; MUC2.
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 InterPro; IPR025155; WxxW_domain.
DR PANTHER; PTHR11339:SF261; PTHR11339:SF261; 1.
DR Pfam; PF08742; C8; 3.
DR Pfam; PF13330; Mucin2_WxxW; 1.
DR Pfam; PF01826; TIL; 1.
DR Pfam; PF00094; VWD; 3.
DR SMART; SM00832; C8; 3.
DR SMART; SM00215; VWC_out; 2.
DR SMART; SM00216; VWD; 3.
DR SUPFAM; SSF57567; SSF57567; 3.
DR PROSITE; PS51233; VWFD; 3.
PE 1: Evidence at protein level;
KW Autocatalytic cleavage; Direct protein sequencing; Disulfide bond;
KW Glycoprotein; Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..>1513
FT /note="Mucin-2"
FT /id="PRO_0000019282"
FT DOMAIN 32..204
FT /note="VWFD 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DOMAIN 292..348
FT /note="TIL"
FT DOMAIN 350..410
FT /note="VWFC"
FT DOMAIN 386..561
FT /note="VWFD 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DOMAIN 856..1025
FT /note="VWFD 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT REPEAT 1392..1407
FT /note="1"
FT REPEAT 1408..1423
FT /note="2"
FT REPEAT 1424..1434
FT /note="3"
FT REPEAT 1435..1445
FT /note="4"
FT REPEAT 1446..1456
FT /note="5"
FT REPEAT 1457..1467
FT /note="6"
FT REPEAT 1468..1478
FT /note="7"
FT REPEAT 1479..1489
FT /note="8"
FT REPEAT 1490..1500
FT /note="9"
FT REPEAT 1501..1511
FT /note="10"
FT REPEAT 1512..>1513
FT /note="11"
FT REGION 1392..>1513
FT /note="Approximate repeats"
FT REGION 1392..1513
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 160
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 420
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 667
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 767
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 837
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 892
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1136
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1151
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1212
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1227
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1243
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1350
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 34..166
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 56..203
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 388..525
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 410..560
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 432..440
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 858..989
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 880..1024
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 889..986
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT DISULFID 906..913
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00580"
FT NON_TER 1513
SQ 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
