Dmbt1
entrez
12945
canonical
uniprot
Q60997
canonical
ensembl
ENSMUSG00000047517
resolver
ensp
ENSMUSP00000081556
resolver
ensp
ENSMUSP00000146685
resolver
ensp
ENSMUSP00000148657
resolver
enst
ENSMUST00000084509
resolver
enst
ENSMUST00000208311
resolver
genesymbol
Dmbt1
resolver
genesymbol_syn
Crpd
resolver
uniprot
A0A140LI59
resolver
uniprot
E9QPG8
resolver
uniprot
Q80YC6
resolver
uniprot
Q9JMJ9
resolver
uniprot_entry
A0A140LI59_MOUSE
resolver
uniprot_entry
DMBT1_MOUSE
resolver
uniprot_entry
E9QPG8_MOUSE
resolver
uniprot_sec
Q80YC6
resolver
uniprot_sec
Q9JMJ9
resolver
amino_acid_sequence
MGISTVIFEICLLWGQILSTASQTAVPTDGTDSGLAVRLVNGGDRCQGRVEILYQGSWGTVCDDSWDLNDANVVCRQLGCGLAVSAPGNARFGQGSGPIVMDDVACGGYEDYLWRCSHRGWLSHNCGHQEDAGVICSDSQTSSPTPGWWNPGGTNNDVFYPTEQTTAEQTTIPDYTPIGTDSGLAVRLVNGGDRCQGRVEILYQGSWGTVCDDSWDVSDANVVCRQLGCGWAVSAPGNAYFGQGQGPIVLDDVACGGYENYLWSCSHQGWLSHNCGHQEDAGVICSASQSSSPTPGWWNPGGTNNDVFYPTEQTTAGTDSGLAVRLVNGGDRCQGRVEILYQGSWGTVCDDSWDTNDANVVCRQLGCGWAVSAPGNAYFGPGSGSIVLDDVACTGHEDYLWRCSHRGWLSHNCGHHEDAGVICSASQSSSPTPDVFYPTDQTTAEQTTVPDYTPIGTDSGLAVRLVNGGDRCQGRVEILYQGSWGTVCDDSWDLNDANVVCRQLGCGLAVSAPGSARFGQGTGPIVMDDVACGGYEDYLWRCSHRGWLSHNCGHHEDAGVICSASQSSSPTPDVFYPTDQTTAEQTTVPDYTPIGTDSGLAVRLVNGGDRCQGRVEILYQGSWGTVCDDSWDLNDANVVCRQLGCGLAVSAPGSARFGQGTGPIVMDDVACGGYEDYLWRCSHRGWLSHNCGHHEDAGVICSASQSSSPTPDVFYPTDQTTAEQTTVPDYTTIGTENSLAVRLENGGDRCQGRVEILYQGSWGTVCDDSWDLNDANVVCRQLGCGLAVSAPGSARFGQGTGPIVMDDVACGGYEDYLWRCSHRGWLSHNCGHHEDAGVICSASQSSSPTPDVFYPTDQTTVEQTTVPDYTPIGTENSLAVRLENGGDRCQGRVEILYQGSWGTVCDDSWDTKDANVVCRQLGCGWAVSAPGNAYFGPGSGSIVLDDVACTGHEDYLWSCSHRGWLSHNCGHHEDAGVICSDAQIQSTTRPDLWPTTTTPETTTELLTTTPYFDWWTTTSDYSCGGLLTQPSGQFSSPYYPSNYPNNARCSWKIVLPNMNRVTVVFTDVQLEGGCNYDYILVYDGPEYNSSLIARVCDGSNGSFTSTGNFMSVVFITDGSVTRRGFQAHYYSTVSTNYSCGGLLTQPSGQFSSPYYPSNYPNNARCSWEILVPNMNRVTVVFTDVQLEGGCNYDYILVYDGPQYNSSLIARVCDGSNGSFTSTGNFMSVVFITDGSVTRRGFQAHYYSTVSTTPPVPIPTTDDYSCGGLLTLPSGQFSSPHYPSNYPNNARCSWEILVPNMNRVTVAFTDVQLEGGCNYDYILVYDGPEYNSSLIARVCDGSNGSFTSTGNFMSVVFITDGSVTRRGFQAHYYSTVSTNYSCGGLLTQPSGQFSSPHYPSNYPNNVRCSWEILVPSMNRVTVAFTDVQLEGGCSFDYILVYDGPEYNSSLIAPVCDGFNGSFTSTGNFMSVVFITDGSVTRRGFQAYYYSTVSTPPSFHPNITGNDSSLALRLVNGSNRCEGRVEILYRGSWGTVCDDSWGISDANVVCRQLGCGSALSAPGNAWFGQGSGLIVLDDVSCSGYESHLWNCHHPGWLVHNCRHSEDAGVICALPEVTSPSPGWWTTSPSYVNYTCGGFLTQPSGQFSSPFYPGNYPNNARCLWNIEVPNNYRVTVVFRDLQLERGCSYDYIEIFDGPHHSSPLIARVCDGSLGSFTSTSNFMSIRFITDHSITARGFQAHYYSDFDNNTTNLLCQSNHMQASVSRSYLQSMGYSARDLVIPGWNSSYHCQPQITQREVIFTIPYTGCGTIKQADNETINYSNFLRAVVSNGIIKRRKDLNIHVSCKMLQNTWVNTMYITNNTVEIQEVQYGNFDVNISFYTSSSFLFPVTSSPYYVDLDQNLYLQAEILHSDASLALFVDTCVASPHPNDFSSLTYDLIRSGCVRDDTYQSYSSPSPRVSRFKFSSFHFLNRFPSVYLQCKLVVCRAYDTSSRCYRGCVVRSKRDVGSYQEKVDVVLGPIQLQSPSKEKRSLDLAVEDVKKPASSQAVYPTAAIFGGVFLAMVLAVAAFTLGRRTHIDRGQPPSTKL
uniprot
proteins
function
FUNCTION: May play roles in mucosal defense system and cellular immune defense. May play a role in liver regeneration. May be an important factor in fate decision and differentiation of transit-amplifying ductular (oval) cells within the hepatic lineage. May function as a binding protein in saliva for the regulation of taste sensation. May play a role as an opsonin receptor for SFTPD and SPAR in macrophage tissues throughout the body, including epithelial cells lining the gastrointestinal tract (By similarity). Required for terminal differentiation of columnar epithelial cells during early embryogenesis. Displays a broad calcium-dependent binding spectrum against both Gram-positive and Gram-negative bacteria, suggesting a role in defense against bacterial pathogens. Binds to a range of poly-sulfated and poly-phosphorylated ligands which may explain its broad bacterial-binding specificity. Inhibits cytoinvasion of S.enterica. Associates with the actin cytoskeleton and is involved in its remodeling during regulated exocytosis. Interacts with pancreatic zymogens in a pH-dependent manner and may act as a Golgi cargo receptor in the regulated secretory pathway of the pancreatic acinar cell. {ECO:0000250, ECO:0000269|PubMed:11152281, ECO:0000269|PubMed:12082154, ECO:0000269|PubMed:12884308, ECO:0000269|PubMed:15146979, ECO:0000269|PubMed:15292166, ECO:0000269|PubMed:15452149, ECO:0000269|PubMed:15987769, ECO:0000269|PubMed:8742698}.
uniprot
proteins
mass_dalton
226815
uniprot
proteins
mutagenesis
MUTAGEN 2073; /note="T->A: Abolishes phosphorylation."; /evidence="ECO:0000269|PubMed:15146979"; MUTAGEN 2082; /note="S->A: Abolishes phosphorylation."; /evidence="ECO:0000269|PubMed:15146979
uniprot
proteins
post_translational_modification
PTM: Highly N- and O-glycosylated. The O-glycans are heavily sulfated. O-glycosylation and sulfation in pancreatic acinar cells are required for zymogen granule maturation. Glycoconjugate composition changes during development with fucose only acquired post-natally during weaning. {ECO:0000269|PubMed:7876332, ECO:0000269|PubMed:8543783}.
uniprot
proteins
protein_family
DMBT1 family
uniprot
proteins
pubmed
10679193
uniprot
proteins
pubmed
11152281
uniprot
proteins
pubmed
12082154
uniprot
proteins
pubmed
12884308
uniprot
proteins
pubmed
15146979
uniprot
proteins
pubmed
15292166
uniprot
proteins
pubmed
15452149
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15987769
uniprot
proteins
pubmed
17983803
uniprot
proteins
pubmed
18202109
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
7537458
uniprot
proteins
pubmed
7876332
uniprot
proteins
pubmed
8543783
uniprot
proteins
pubmed
8742698
uniprot
proteins
pubmed
9247472
uniprot
proteins
pubmed
9688648
uniprot
proteins
sequence_length
2085
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Secreted. Cytoplasmic vesicle, secretory vesicle membrane; Single-pass membrane protein; Lumenal side. Note=Localized to the lumenal aspect of crypt cells in the small intestine. In the colon, seen in the lumenal aspect of surface epithelial cells. Formed in the ducts of von Ebner gland and released into the fluid bathing the taste buds contained in the taste papillae. In the CFTR knockout mouse, enhanced on the acinar luminar surface.
uniprot
proteins
transmembrane_region
TRANSMEM 2050..2070; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins