MUC15_BOVIN
ID MUC15_BOVIN Reviewed; 330 AA.
AC Q8MI01; Q8MI16;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 25-MAY-2022, entry version 81.
DE RecName: Full=Mucin-15;
DE Short=MUC-15;
DE AltName: Full=Component II;
DE AltName: Full=Glycoprotein 4;
DE AltName: Full=Glycoprotein C;
DE AltName: Full=PAS3;
DE AltName: Full=PASIII;
DE Flags: Precursor;
GN Name=MUC15;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), PROTEIN SEQUENCE OF 24-53;
RP 64-183; 186-193; 197-227; 250-254; 260-268 AND 270-308, TISSUE SPECIFICITY,
RP AND GLYCOSYLATION.
RC STRAIN=Holstein; TISSUE=Lactating mammary gland;
RX PubMed=12047385; DOI=10.1046/j.1432-1033.2002.02949.x;
RA Pallesen L.T., Berglund L., Rasmussen L.K., Petersen T.E., Rasmussen J.T.;
RT "Isolation and characterization of MUC15, a novel cell membrane associated
RT mucin.";
RL Eur. J. Biochem. 269:2755-2763(2002).
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane {ECO:0000305}; Single-
CC pass type I membrane protein {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Secreted {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=MUC15;
CC IsoId=Q8MI01-1; Sequence=Displayed;
CC Name=2; Synonyms=MUC15/S;
CC IsoId=Q8MI01-2; Sequence=VSP_010824;
CC -!- TISSUE SPECIFICITY: Mainly expressed on apical surfaces of the mammary
CC epithelial cells. {ECO:0000269|PubMed:12047385}.
CC -!- PTM: Highly glycosylated (N- and O-linked carbohydrates).
CC {ECO:0000269|PubMed:12047385}.
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DR EMBL; AJ417816; CAD10622.1; -; mRNA.
DR EMBL; AJ417817; CAD10623.1; -; mRNA.
DR RefSeq; NP_788804.1; NM_176631.1. [Q8MI01-1]
DR AlphaFoldDB; Q8MI01; -.
DR STRING; 9913.ENSBTAP00000038673; -.
DR iPTMnet; Q8MI01; -.
DR PaxDb; Q8MI01; -.
DR PRIDE; Q8MI01; -.
DR GeneID; 337919; -.
DR KEGG; bta:337919; -.
DR CTD; 143662; -.
DR eggNOG; ENOG502S7P0; Eukaryota.
DR InParanoid; Q8MI01; -.
DR OrthoDB; 1169762at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR InterPro; IPR031371; Mucin-15.
DR PANTHER; PTHR45427; PTHR45427; 1.
DR Pfam; PF15672; Mucin15; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Direct protein sequencing;
KW Glycoprotein; Membrane; Reference proteome; Secreted; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..23
FT /evidence="ECO:0000269|PubMed:12047385"
FT CHAIN 24..330
FT /note="Mucin-15"
FT /id="PRO_0000019287"
FT TOPO_DOM 24..232
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 233..253
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 254..330
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 23..115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 164..185
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 279..330
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..54
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 66..115
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 289..313
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 30
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12047385"
FT CARBOHYD 44
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 54
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 71
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12047385"
FT CARBOHYD 79
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12047385"
FT CARBOHYD 89
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 94
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12047385"
FT CARBOHYD 122
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12047385"
FT CARBOHYD 138
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12047385"
FT CARBOHYD 147
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12047385"
FT CARBOHYD 154
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12047385"
FT CARBOHYD 162
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12047385"
FT CARBOHYD 175
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12047385"
FT CARBOHYD 214
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12047385"
FT CARBOHYD 221
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 228..277
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12047385"
FT /id="VSP_010824"
SQ SEQUENCE 330 AA; 35715 MW; E790C9F520154414 CRC64;
MLTSAKILLI SILSSLLLFG SHGEEGQKTN TTESTAEDLK TMENQSVPLE SKANLTSDKE
NRETSNPKAS NFSFEDPSNK THETGFYSNL STDNSSRSPS LMPTLSPRSP STHSFVSKLP
WNSSIADNSL LPASAPPNTT VPVSSENFTL SSINDTMKAP DNSSITVSNL PSGPNTTSVT
PMVTEGWPTT TRESMEGFTV YQETTLHPTL KFTNNSKIFP NTSDPQEENR NTGVVFGAIL
GAILGASLLS LVGYLLCGKR KTDSFSHRRL YDDRNEPVLR LDNAPEPYDM SFGNSSYYNP
TANDSSTSAG GENAHDSIPM DDIPPLRTSV
