Q6AYA5 · T106B_RAT
- ProteinTransmembrane protein 106B
- GeneTmem106b
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids275 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Involved in dendrite morphogenesis and maintenance by regulating lysosomal trafficking. May act as a molecular brake for retrograde transport of late endosomes/lysosomes, possibly via its interaction with MAP6 (PubMed:24357581).
In neurons, may also play a role in the regulation of lysosomal size and responsiveness to stress (By similarity).
Required for proper lysosomal acidification (By similarity).
In neurons, may also play a role in the regulation of lysosomal size and responsiveness to stress (By similarity).
Required for proper lysosomal acidification (By similarity).
In neurons, involved in the transport of late endosomes/lysosomes (PubMed:24357581).
May be involved in dendrite morphogenesis and maintenance by regulating lysosomal trafficking (PubMed:24357581).
May act as a molecular brake for retrograde transport of late endosomes/lysosomes, possibly via its interaction with MAP6 (PubMed:24357581).
In motoneurons, may mediate the axonal transport of lysosomes and axonal sorting at the initial segment (By similarity).
It remains unclear whether TMEM106B affects the transport of moving lysosomes in the anterograde or retrograde direction in neurites and whether it is particularly important in the sorting of lysosomes in axons or in dendrites (By similarity).
In neurons, may also play a role in the regulation of lysosomal size and responsiveness to stress (By similarity).
Required for proper lysosomal acidification (By similarity).
May be involved in dendrite morphogenesis and maintenance by regulating lysosomal trafficking (PubMed:24357581).
May act as a molecular brake for retrograde transport of late endosomes/lysosomes, possibly via its interaction with MAP6 (PubMed:24357581).
In motoneurons, may mediate the axonal transport of lysosomes and axonal sorting at the initial segment (By similarity).
It remains unclear whether TMEM106B affects the transport of moving lysosomes in the anterograde or retrograde direction in neurites and whether it is particularly important in the sorting of lysosomes in axons or in dendrites (By similarity).
In neurons, may also play a role in the regulation of lysosomal size and responsiveness to stress (By similarity).
Required for proper lysosomal acidification (By similarity).
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | late endosome membrane | |
Cellular Component | lysosomal membrane | |
Cellular Component | lysosome | |
Cellular Component | plasma membrane | |
Molecular Function | ATPase binding | |
Biological Process | dendrite morphogenesis | |
Biological Process | lysosomal lumen acidification | |
Biological Process | lysosomal protein catabolic process | |
Biological Process | lysosomal transport | |
Biological Process | lysosome localization | |
Biological Process | lysosome organization | |
Biological Process | neuron cellular homeostasis | |
Biological Process | positive regulation of dendrite development | |
Biological Process | regulation of lysosome organization |
Keywords
- Biological process
Names & Taxonomy
Protein names
- Recommended nameTransmembrane protein 106B
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Rattus
Accessions
- Primary accessionQ6AYA5
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Late endosome membrane ; Single-pass type II membrane protein
Lysosome membrane ; Single-pass type II membrane protein
Cell membrane ; Single-pass type II membrane protein
Note: Colocalizes with LAMP1 (PubMed:24357581).
A small fraction resides on the cell surface (By similarity).
A small fraction resides on the cell surface (By similarity).
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 2-97 | Cytoplasmic | ||||
Sequence: GKSLSHLPLHSNKEDGYDGVTSTDNMRNGLVSSEVRNEDGRSGDVSQFPYVEFTGRDSVTCPTCQGTGRIPRGQENQLVALIPYSDQRLRPRRTKL | ||||||
Transmembrane | 98-118 | Helical | ||||
Sequence: YVMASVFVCLLLSGLAVFFLF | ||||||
Topological domain | 119-275 | Lumenal | ||||
Sequence: PRSIDVKYIGVKSAYVSYDSQKRMIYLNITNTLNITNNNYYSVEVENITAQVQFSKTVIGKARLSNITNIGPLDMKQIDYTVPTVIAEEMSYMYDFCTLPSIKVHNIVLMMQVTVTTAYFGHSEQISQERYQYVDCGRNTTYQLAQSEYLNVLQPQQ |
Keywords
- Cellular component
PTM/Processing
Features
Showing features for initiator methionine, lipidation, chain, modified residue, glycosylation, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Initiator methionine | 1 | Removed | ||||
Sequence: M | ||||||
Lipidation | 2 | N-myristoyl glycine | ||||
Sequence: G | ||||||
Chain | PRO_0000242652 | 2-275 | Transmembrane protein 106B | |||
Sequence: GKSLSHLPLHSNKEDGYDGVTSTDNMRNGLVSSEVRNEDGRSGDVSQFPYVEFTGRDSVTCPTCQGTGRIPRGQENQLVALIPYSDQRLRPRRTKLYVMASVFVCLLLSGLAVFFLFPRSIDVKYIGVKSAYVSYDSQKRMIYLNITNTLNITNNNYYSVEVENITAQVQFSKTVIGKARLSNITNIGPLDMKQIDYTVPTVIAEEMSYMYDFCTLPSIKVHNIVLMMQVTVTTAYFGHSEQISQERYQYVDCGRNTTYQLAQSEYLNVLQPQQ | ||||||
Modified residue | 34 | Phosphoserine | ||||
Sequence: S | ||||||
Glycosylation | 146 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 152 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 165 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 184 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 215↔254 | |||||
Sequence: CTLPSIKVHNIVLMMQVTVTTAYFGHSEQISQERYQYVDC | ||||||
Glycosylation | 257 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Expressed in cortical neurons (at protein level).
Gene expression databases
Interaction
Subunit
Can form homomers (By similarity).
Interacts (via N-terminus) with MAP6 (via C-terminus) (PubMed:24357581).
Interacts (via C-terminus) with the vacuolar-type ATPase subunit ATP6AP1 (By similarity).
Interacts (via N-terminus) with AP2M1 and CLTC (By similarity).
Interacts with TMEM106C (By similarity).
Interacts (via N-terminus) with MAP6 (via C-terminus) (PubMed:24357581).
Interacts (via C-terminus) with the vacuolar-type ATPase subunit ATP6AP1 (By similarity).
Interacts (via N-terminus) with AP2M1 and CLTC (By similarity).
Interacts with TMEM106C (By similarity).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q6AYA5 | Map6 Q63560 | 6 | EBI-9316198, EBI-1638469 |
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-24 | Disordered | ||||
Sequence: MGKSLSHLPLHSNKEDGYDGVTST |
Sequence similarities
Belongs to the TMEM106 family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length275
- Mass (Da)31,152
- Last updated2004-09-13 v1
- Checksum327903F97AE30141
Computationally mapped potential isoform sequences
There are 2 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A8I6AL12 | A0A8I6AL12_RAT | Tmem106b | 268 | ||
Q6TUE3 | Q6TUE3_RAT | Tmem106b | 348 |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
BC079127 EMBL· GenBank· DDBJ | AAH79127.1 EMBL· GenBank· DDBJ | mRNA |