Domains within Mus musculus protein LBP_MOUSE (Q61805)

Lipopolysaccharide-binding protein

Alternative representations: 1 /

Protein length481 aa
Source databaseUniProt
Identifiers LBP_MOUSE, Q61805, ENSMUSP00000016168.2, ENSMUSP00000016168, A2AC66, Q99KA0, A2AC65_MOUSE, A2AC65
Source gene ENSMUSG00000016024
Alternative splicing ENSMUSP00000105117.1, LBP_MOUSE, F6XKX9_MOUSE

Domain architecture analysis

Display all proteins with similar:

Domain organisationProteins having all the domains as the query in the same order. Additional domains are allowed.
Domain compositionProteins with the same domain composition have at least one copy of each of the domains of the query.

This domain architecture was probably invented with the emergence of Eukaryota

Predicted functional partners

LBP_MOUSE is shown as Lbp in the network

Click and drag to pan the network, and zoom by using your mouse wheel. Click the protein nodes for additional options.

The network on the left comes from STRING, a database of known and predicted protein interactions. Displayed here is the evidence view, where different line colors represent the types of evidence for the association.

Open the STRING annotation page for Lbp

Protein LBP_MOUSE is possibly involved in these pathways, based on its similarity to the listed KEGG orthologous groups:

KEGG pathways

PathwayDescription
map04936Alcoholic liver disease

KEGG orthologous groups

KONameDescription
K25376BPIFB, LPLUNCBPI fold-containing family B
K25374BPIbactericidal permeability-increasing protein
K05399LBPlipopolysaccharide-binding protein

Post-translational modifications

PTM annotation is taken from PTMcode, a resource of known and predicted functional associations between protein post-translational modifications (PTMs). There are 11 PTMs annotated in this protein:

PTMCount
N-linked glycosylation6
Acetylation3
Phosphorylation2

To see the full details, including possible functional associations between the PTMs, please visit the PTMcode annotation page for protein Lbp.

Orthologous groups

Orthology information is taken from eggNOG, a database of orthologous groups of genes. Orthologous groups containing this protein are listed below. This protein is named 10090.ENSMUSP00000016168 in eggNOG.

OGTaxonomic classDescription
LKOG4160All organisms (root)BPI fold-containing family B,lipopolysaccharide-binding protein,bactericidal permeability-increasing protein
KOG4160Eukaryota (superkingdom)BPI fold-containing family B,lipopolysaccharide-binding protein,bactericidal permeability-increasing protein
HTY7NMetazoa (kingdom)lipopolysaccharide-binding protein,BPI fold-containing family C,bactericidal permeability-increasing protein
94R9VChordata (phylum)lipopolysaccharide-binding protein,BPI fold-containing family C,bactericidal permeability-increasing protein
5R8ZWSarcopterygii (superclass)lipopolysaccharide-binding protein,bactericidal permeability-increasing protein
8Z7U4Mammalia (class)lipopolysaccharide-binding protein,bactericidal permeability-increasing protein
4RFRUEuarchontoglires (superorder)lipopolysaccharide-binding protein,bactericidal permeability-increasing protein
AI3XBRodentia (order)lipopolysaccharide-binding protein,bactericidal permeability-increasing protein
8DAG1Myomorpha (suborder)lipopolysaccharide-binding protein,bactericidal permeability-increasing protein
9G6Z5Vertebrata (clade)lipopolysaccharide-binding protein,BPI fold-containing family C,bactericidal permeability-increasing protein
7H3S6Opisthokonta (clade)lipopolysaccharide-binding protein,BPI fold-containing family C,bactericidal permeability-increasing protein
H3XIPBilateria (clade)lipopolysaccharide-binding protein,BPI fold-containing family C,bactericidal permeability-increasing protein
CQ0YQMuridae (family)lipopolysaccharide-binding protein
AE0N6Murinae (subfamily)lipopolysaccharide-binding protein
5PJZJMus (genus)lipopolysaccharide-binding protein
HE390Mus (subgenus)lipopolysaccharide-binding protein

The SMART diagram above represents a summary of the results shown below. Domains with scores less significant than established cutoffs are not shown in the diagram. Features are also not shown when two or more occupy the same piece of sequence; the priority for display is given by SMART > PFAM > PROSPERO repeats > Signal peptide > Transmembrane > Coiled coil > Low complexity. In either case, features not shown in the above diagram are listed in the right side table below, and the reason for their omission is shown in the 'Reason' column.

Confidently predicted domains, repeats, motifs and features:

Outlier homologues and homologues of known structure:

Features NOT shown in the diagram: