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Protein

Ly6/PLAUR domain-containing protein 8

Gene

Lypd8

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

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.1 Publication

GO - Biological processi

  • defense response to Gram-negative bacterium Source: UniProtKB

Enzyme and pathway databases

ReactomeiR-MMU-163125 Post-translational modification: synthesis of GPI-anchored proteins

Names & Taxonomyi

Protein namesi
Recommended name:
Ly6/PLAUR domain-containing protein 8Curated
Gene namesi
Name:Lypd8Imported
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 11

Organism-specific databases

MGIiMGI:1917413 Lypd8

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell membrane, Membrane, Secreted

Pathology & Biotechi

Disruption phenotypei

Mice are highly sensitive to intestinal inflammation induced by dextran sulfate sodium (DSS), due to the presence of bacteria in the inner mucus layer. Mice are healthy when raised in a specific-pathogen-free environment, in which bacterial contamination was strictly controlled.1 Publication

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi22N → 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. 1 Publication1
Mutagenesisi30N → 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. 1 Publication1
Mutagenesisi53N → 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. 1 Publication1
Mutagenesisi72N → 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. 1 Publication1
Mutagenesisi76N → 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. 1 Publication1
Mutagenesisi105N → 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. 1 Publication1
Mutagenesisi115N → 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. 1 Publication1
Mutagenesisi128N → 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. 1 Publication1
Mutagenesisi154N → 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. 1 Publication1
Mutagenesisi169N → 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. 1 Publication1
Mutagenesisi179N → 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. 1 Publication1
Mutagenesisi200N → 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. 1 Publication1
Mutagenesisi210N → 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. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 20Sequence analysisAdd BLAST20
ChainiPRO_000031774121 – 233Ly6/PLAUR domain-containing protein 8Add BLAST213
PropeptideiPRO_0000317742234 – 255Removed in mature formSequence analysisAdd BLAST22

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi22N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi30N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi53N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi72N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi76N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi105N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi115N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi128N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi154N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi169N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi179N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi200N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi210N-linked (GlcNAc...) asparagineSequence analysis1
Lipidationi233GPI-anchor amidated serineSequence analysis1

Post-translational modificationi

Highly N-glycosylated. Not O-glycosylated.1 Publication
GPI-anchored. The GPI-anchor is cleaved, leading to secretion into the colonic lumen.1 Publication

Keywords - PTMi

Glycoprotein, GPI-anchor, Lipoprotein

Proteomic databases

PaxDbiQ9D7S0
PRIDEiQ9D7S0

PTM databases

PhosphoSitePlusiQ9D7S0

Expressioni

Tissue specificityi

Specifically present in enterocytes located at the uppermost epithelial layer of the colon (at protein level). Exclusively expressed in the large intestine: specifically expressed on the apical surface of epithelial cells located at the uppermost layer of the colonic gland.1 Publication

Gene expression databases

BgeeiENSMUSG00000013643 Expressed in 53 organ(s), highest expression level in large intestine
CleanExiMM_2210415F13RIK
GenevisibleiQ9D7S0 MM

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000013787

Structurei

3D structure databases

ProteinModelPortaliQ9D7S0
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini121 – 170UPAR/Ly6Add BLAST50

Sequence similaritiesi

Belongs to the CNF-like-inhibitor family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG410JBTM Eukaryota
ENOG4111A5Z LUCA
GeneTreeiENSGT00570000079564
HOVERGENiHBG073147
InParanoidiQ9D7S0
OMAiFRKFECA
OrthoDBiEOG091G0R4I
PhylomeDBiQ9D7S0
TreeFamiTF339495

Family and domain databases

InterProiView protein in InterPro
IPR016054 LY6_UPA_recep-like
PfamiView protein in Pfam
PF00021 UPAR_LY6, 2 hits

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9D7S0-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MRGVFIAGVI AAFAITVVDS LNCTQCYTYN STCDGQATEC NEQSFSCVES
60 70 80 90 100
SINSTLGGFL HVYQNKFCSA SNCTENSTEV AFTVHLFDDQ RYHFASQCCQ
110 120 130 140 150
GESCNATHSE SGTQNVTDMQ CMSCYGHNKT LCEEKPQKCY EGEQCVFIIA
160 170 180 190 200
EMVNGSGRVE LKGCSDISNS TCQFLSPGNT TVGEFVFKSV ECTQPTEYTN
210 220 230 240 250
STTTIPPITN TSLTSVTRPG IKTSPASVTP QASMGTKASF TSSIFGSLLL

LKLLF
Length:255
Mass (Da):27,524
Last modified:June 1, 2001 - v1
Checksum:i6D699A3BF5DAE5DD
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK008940 mRNA Translation: BAB25981.1
AL663107 Genomic DNA No translation available.
CCDSiCCDS36163.1
RefSeqiNP_001077353.1, NM_001083884.1
NP_001317126.1, NM_001330197.1
NP_081615.2, NM_027339.2
UniGeneiMm.24119

Genome annotation databases

EnsembliENSMUST00000013787; ENSMUSP00000013787; ENSMUSG00000013643
ENSMUST00000108826; ENSMUSP00000104454; ENSMUSG00000013643
GeneIDi70163
KEGGimmu:70163
UCSCiuc007jbj.1 mouse

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK008940 mRNA Translation: BAB25981.1
AL663107 Genomic DNA No translation available.
CCDSiCCDS36163.1
RefSeqiNP_001077353.1, NM_001083884.1
NP_001317126.1, NM_001330197.1
NP_081615.2, NM_027339.2
UniGeneiMm.24119

3D structure databases

ProteinModelPortaliQ9D7S0
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000013787

PTM databases

PhosphoSitePlusiQ9D7S0

Proteomic databases

PaxDbiQ9D7S0
PRIDEiQ9D7S0

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000013787; ENSMUSP00000013787; ENSMUSG00000013643
ENSMUST00000108826; ENSMUSP00000104454; ENSMUSG00000013643
GeneIDi70163
KEGGimmu:70163
UCSCiuc007jbj.1 mouse

Organism-specific databases

CTDi646627
MGIiMGI:1917413 Lypd8

Phylogenomic databases

eggNOGiENOG410JBTM Eukaryota
ENOG4111A5Z LUCA
GeneTreeiENSGT00570000079564
HOVERGENiHBG073147
InParanoidiQ9D7S0
OMAiFRKFECA
OrthoDBiEOG091G0R4I
PhylomeDBiQ9D7S0
TreeFamiTF339495

Enzyme and pathway databases

ReactomeiR-MMU-163125 Post-translational modification: synthesis of GPI-anchored proteins

Miscellaneous databases

PROiPR:Q9D7S0
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000013643 Expressed in 53 organ(s), highest expression level in large intestine
CleanExiMM_2210415F13RIK
GenevisibleiQ9D7S0 MM

Family and domain databases

InterProiView protein in InterPro
IPR016054 LY6_UPA_recep-like
PfamiView protein in Pfam
PF00021 UPAR_LY6, 2 hits
ProtoNetiSearch...

Entry informationi

Entry nameiLYPD8_MOUSE
AccessioniPrimary (citable) accession number: Q9D7S0
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: June 1, 2001
Last modified: September 12, 2018
This is version 93 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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