Domains within Mus musculus protein CHIA_MOUSE (Q91XA9)

Acidic mammalian chitinase

Alternative representations: 1 /

Protein length473 aa
Source databaseUniProt
Identifiers CHIA_MOUSE, Q91XA9, ENSMUSP00000078134.5, ENSMUSP00000078134, A0T468, B8K282, Q3TVE7, Q99PH2, Q9D803, Q9JLN1, D3Z1S6_MOUSE, D3Z1S6
Source gene ENSMUSG00000062778
Alternative splicing CHIA_MOUSE, ENSMUSP00000121967.1

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 Bilateria

Predicted functional partners

CHIA_MOUSE is shown as Chia1 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 Chia1

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

KEGG pathways

PathwayDescription
map00520Amino sugar and nucleotide sugar metabolism iPath3
Some of these pathways are included in the interactive Pathways Explorer overview maps. Select an overview map and click the button below to highlight them in iPath.

KEGG orthologous groups

KONameDescription
K01183E3.2.1.14chitinase [EC:3.2.1.14] iPath3
Some of these orthologous groups are included in the interactive Pathways Explorer overview maps. Select an overview map and click the button below to highlight them in iPath.

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 5 PTMs annotated in this protein:

PTMCount
Phosphorylation4
N-linked glycosylation1

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

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.ENSMUSP00000078134 in eggNOG.

OGTaxonomic classDescription
LCOG3325All organisms (root)chitinase [EC:3.2.1.14],Di-N-acetylchitobiase [EC:3.2.1.-],chitinase-3-like protein 1/2
KOG2806Eukaryota (superkingdom)chitinase [EC:3.2.1.14],Di-N-acetylchitobiase [EC:3.2.1.-],chitinase-3-like protein 1/2
HVG3ZMetazoa (kingdom)chitinase [EC:3.2.1.14],Di-N-acetylchitobiase [EC:3.2.1.-],chitinase-3-like protein 1/2
94B8UChordata (phylum)chitinase [EC:3.2.1.14],chitinase-3-like protein 1/2,oviduct-specific glycoprotein
5R6WRSarcopterygii (superclass)chitinase [EC:3.2.1.14],chitinase-3-like protein 1/2,oviduct-specific glycoprotein
8ZME8Mammalia (class)chitinase [EC:3.2.1.14],oviduct-specific glycoprotein,chitinase 3-like 3/4
4R7ZGEuarchontoglires (superorder)chitinase [EC:3.2.1.14],chitinase 3-like 3/4
AI0I3Rodentia (order)chitinase [EC:3.2.1.14],chitinase 3-like 3/4
8DFX0Myomorpha (suborder)chitinase [EC:3.2.1.14]
9G0P7Vertebrata (clade)chitinase [EC:3.2.1.14],chitinase-3-like protein 1/2,oviduct-specific glycoprotein
H4RRKBilateria (clade)chitinase [EC:3.2.1.14],Di-N-acetylchitobiase [EC:3.2.1.-],chitinase-3-like protein 1/2
7GGSCOpisthokonta (clade)chitinase [EC:3.2.1.14],Di-N-acetylchitobiase [EC:3.2.1.-],chitinase-3-like protein 1/2
CPZQFMuridae (family)chitinase [EC:3.2.1.14]
AE1JPMurinae (subfamily)chitinase [EC:3.2.1.14]
5PXD2Mus (genus)chitinase [EC:3.2.1.14]
HE1FNMus (subgenus)chitinase [EC:3.2.1.14]

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: