Lypd8
entrez
70163
canonical
uniprot
Q9D7S0
canonical
ensembl
ENSMUSG00000013643
resolver
ensp
ENSMUSP00000013787
resolver
ensp
ENSMUSP00000104454
resolver
ensp
ENSMUSP00000348384
resolver
enst
ENSMUST00000013787
resolver
enst
ENSMUST00000108826
resolver
genesymbol
Lypd8
resolver
uniprot_entry
LYPD8_MOUSE
resolver
amino_acid_sequence
MRGVFIAGVIAAFAITVVDSLNCTQCYTYNSTCDGQATECNEQSFSCVESSINSTLGGFLHVYQNKFCSASNCTENSTEVAFTVHLFDDQRYHFASQCCQGESCNATHSESGTQNVTDMQCMSCYGHNKTLCEEKPQKCYEGEQCVFIIAEMVNGSGRVELKGCSDISNSTCQFLSPGNTTVGEFVFKSVECTQPTEYTNSTTTIPPITNTSLTSVTRPGIKTSPASVTPQASMGTKASFTSSIFGSLLLLKLLF
uniprot
proteins
function
FUNCTION: Secreted protein specifically required to prevent invasion of Gram-negative bacteria in the inner mucus layer of the colon epithelium, a portion of the large intestine which is free of commensal microbiota. Prevents invasion of flagellated microbiota by binding to the flagellum of bacteria, such as P.mirabilis, thereby inhibiting bacterial motility in the intestinal lumen. Segregation of intestinal bacteria and epithelial cells in the colon is required to preserve intestinal homeostasis. {ECO:0000269|PubMed:27027293}.
uniprot
proteins
mass_dalton
27524
uniprot
proteins
mutagenesis
MUTAGEN 22; /note="N->D: In mutant N-D: Abolished N-glycosylation; when associated with D-30; D-53; D-72; D-76; D-105; D-115; D-128; D-154; D-169; D-179; D-200 and D-210."; /evidence="ECO:0000269|PubMed:27027293"; MUTAGEN 30; /note="N->D: In mutant N-D: Abolished N-glycosylation; when associated with D-22; D-53; D-72; D-76; D-105; D-115; D-128; D-154; D-169; D-179; D-200 and D-210."; /evidence="ECO:0000269|PubMed:27027293"; MUTAGEN 53; /note="N->D: In mutant N-D: Abolished N-glycosylation; when associated with D-22; D-30; D-72; D-76; D-105; D-115; D-128; D-154; D-169; D-179; D-200 and D-210."; /evidence="ECO:0000269|PubMed:27027293"; MUTAGEN 72; /note="N->D: In mutant N-D: Abolished N-glycosylation; when associated with D-22; D-30; D-53; D-76; D-105; D-115; D-128; D-154; D-169; D-179; D-200 and D-210."; /evidence="ECO:0000269|PubMed:27027293"; MUTAGEN 76; /note="N->D: In mutant N-D: Abolished N-glycosylation; when associated with D-22; D-30; D-53; D-72; D-105; D-115; D-128; D-154; D-169; D-179; D-200 and D-210."; /evidence="ECO:0000269|PubMed:27027293"; MUTAGEN 105; /note="N->D: In mutant N-D: Abolished N-glycosylation; when associated with D-22; D-30; D-53; D-72; D-76; D-115; D-128; D-154; D-169; D-179; D-200 and D-210."; /evidence="ECO:0000269|PubMed:27027293"; MUTAGEN 115; /note="N->D: In mutant N-D: Abolished N-glycosylation; when associated with D-22; D-30; D-53; D-72; D-76; D-105; D-128; D-154; D-169; D-179; D-200 and D-210."; /evidence="ECO:0000269|PubMed:27027293"; MUTAGEN 128; /note="N->D: In mutant N-D: Abolished N-glycosylation; when associated with D-22; D-30; D-53; D-72; D-76; D-105; D-115; D-154; D-169; D-179; D-200 and D-210."; /evidence="ECO:0000269|PubMed:27027293"; MUTAGEN 154; /note="N->D: In mutant N-D: Abolished N-glycosylation; when associated with D-22; D-30; D-53; D-72; D-76; D-105; D-115; D-128; D-169; D-179; D-200 and D-210."; /evidence="ECO:0000269|PubMed:27027293"; MUTAGEN 169; /note="N->D: In mutant N-D: Abolished N-glycosylation; when associated with D-22; D-30; D-53; D-72; D-76; D-105; D-115; D-128; D-154; D-179; D-200 and D-210."; /evidence="ECO:0000269|PubMed:27027293"; MUTAGEN 179; /note="N->D: In mutant N-D: Abolished N-glycosylation; when associated with D-22; D-30; D-53; D-72; D-76; D-105; D-115; D-128; D-154; D-169; D-200 and D-210."; /evidence="ECO:0000269|PubMed:27027293"; MUTAGEN 200; /note="N->D: In mutant N-D: Abolished N-glycosylation; when associated with D-22; D-30; D-53; D-72; D-76; D-105; D-115; D-128; D-154; D-169; D-179 and D-210."; /evidence="ECO:0000269|PubMed:27027293"; MUTAGEN 210; /note="N->D: In mutant N-D: Abolished N-glycosylation; when associated with D-22; D-30; D-53; D-72; D-76; D-105; D-115; D-128; D-154; D-169; D-179 and D-200."; /evidence="ECO:0000269|PubMed:27027293
uniprot
proteins
post_translational_modification
PTM: Highly N-glycosylated. Not O-glycosylated. {ECO:0000269|PubMed:27027293}.; PTM: GPI-anchored. The GPI-anchor is cleaved, leading to secretion into the colonic lumen. {ECO:0000269|PubMed:27027293}.
uniprot
proteins
protein_family
CNF-like-inhibitor family
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
19468303
uniprot
proteins
pubmed
27027293
uniprot
proteins
sequence_length
255
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:27027293}. Secreted {ECO:0000269|PubMed:27027293}. Note=Secreted into the lumen of the colon following cleavage of the GPI-anchor. {ECO:0000269|PubMed:27027293}.
uniprot
proteins