MUC13_RAT
ID MUC13_RAT Reviewed; 547 AA.
AC P97881;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Mucin-13;
DE Short=MUC-13;
DE Flags: Precursor;
GN Name=Muc13;
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;
RA Hajdu A., Flanagan P.R.;
RL Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Epithelial and hemopoietic transmembrane mucin that may play
CC a role in cell signaling.
CC -!- SUBUNIT: Homodimer of beta subunits. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}. Secreted {ECO:0000250}. Note=Also
CC exists as a soluble form. {ECO:0000250}.
CC -!- PTM: Cleaved into two subunits, alpha and beta, probably between the
CC first EGF domain and the SEA domain. Beta subunit contains the
CC cytoplasmic tail and alpha subunit the extracellular tail. The
CC homooligomerization into dimers is dependent on intrachain disulfide
CC bonds (By similarity). {ECO:0000250}.
CC -!- PTM: Highly glycosylated. {ECO:0000250}.
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DR EMBL; U89744; AAB49894.1; -; mRNA.
DR STRING; 10116.ENSRNOP00000067923; -.
DR GlyGen; P97881; 3 sites.
DR PRIDE; P97881; -.
DR UCSC; RGD:708547; rat.
DR RGD; 708547; Muc13.
DR InParanoid; P97881; -.
DR PhylomeDB; P97881; -.
DR Reactome; R-RNO-913709; O-linked glycosylation of mucins.
DR Reactome; R-RNO-9696264; RND3 GTPase cycle.
DR Reactome; R-RNO-9696270; RND2 GTPase cycle.
DR Reactome; R-RNO-9696273; RND1 GTPase cycle.
DR Reactome; R-RNO-977068; Termination of O-glycan biosynthesis.
DR PRO; PR:P97881; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0016324; C:apical plasma membrane; IDA:RGD.
DR GO; GO:0005829; C:cytosol; ISO:RGD.
DR GO; GO:0005615; C:extracellular space; ISO:RGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:RGD.
DR GO; GO:0030277; P:maintenance of gastrointestinal epithelium; ISO:RGD.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000082; SEA_dom.
DR SMART; SM00181; EGF; 3.
DR SMART; SM00200; SEA; 1.
DR PROSITE; PS01186; EGF_2; 2.
DR PROSITE; PS50026; EGF_3; 1.
DR PROSITE; PS50024; SEA; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Disulfide bond; EGF-like domain; Glycoprotein; Membrane;
KW Reference proteome; Repeat; Secreted; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..?
FT CHAIN ?..547
FT /note="Mucin-13"
FT /id="PRO_0000019286"
FT TOPO_DOM ?..458
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 459..479
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 480..547
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 210..249
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 250..366
FT /note="SEA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00188"
FT DOMAIN 361..401
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 401..441
FT /note="EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REGION 1..214
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 525..547
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 525..539
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 243
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 244
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 263
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 214..225
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 219..234
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 236..248
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 365..378
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 370..384
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 386..400
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 409..427
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 429..440
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 547 AA; 57652 MW; EA86608C704080CF CRC64;
MSQSSGGTST PTTTATQPTS TSTQTPGTTQ LLSTTSTPTT TATQPTSTST QTPGTTQLPS
TTSTPTTTAT QPTXTSTQTP GTTQLPGTTS TPTTTATQPT STSFQTPGTT QLPSSTSTPT
TTATQPTSTA SQTPGTTQPP GGASSPTTTV TQPTGSSSQT PGTTQPPGGA STPTTTVTQP
TGSSSQTSGT TQPPGGASSS TVTSSSSTGS NDPCNSNPCK SPASCVKLYD SYFCLCLEGY
YYNNSSSCVK GTTFPGEIGM SVNETTDLED KNSVNYQTLH SSVVKFFENT FKKTDYGQTV
ILKVSKDSLM SSRSVMRAAT QTVYVSVVNM FGENTKEDEE SVASVIKEAV KTDNNVERYF
QQDRCDYYGC VKSGSNVCRN GLQCTCKPGL ERLNPQVPFC VAPTCSEPCS AEKKQLCLKK
DNGAMECGCM AGYRKANGKC EECPFGYSGM DCKDQFQLIL TIVGTIAGAF ILILLIVFIV
SMRSKNKKKS GEEQNLIEDD FHNLRMRPTG FSNFGADTSI FPKVKTGVPS QTSNPYANHR
SMPRPDY
