Q9XT98 · CLD16_BOVIN
- ProteinClaudin-16
- GeneCLDN16
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids254 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score5/5
Function
function
Forms paracellular channels: coassembles with CLDN19 into tight junction strands with cation-selective channels through the strands, conveying epithelial permeability in a process known as paracellular tight junction permeability (By similarity).
Involved in the maintenance of ion gradients along the nephron. In the thick ascending limb (TAL) of Henle's loop, facilitates sodium paracellular permeability from the interstitial compartment to the lumen, contributing to the lumen-positive transepithelial potential that drives paracellular magnesium and calcium reabsorption (By similarity).
Involved in the maintenance of ion gradients along the nephron. In the thick ascending limb (TAL) of Henle's loop, facilitates sodium paracellular permeability from the interstitial compartment to the lumen, contributing to the lumen-positive transepithelial potential that drives paracellular magnesium and calcium reabsorption (By similarity).
Catalytic activity
- Mg2+(in) = Mg2+(out)
- Ca2+(in) = Ca2+(out)
- Na+(in) = Na+(out)
- K+(in) = K+(out)
- Rb+(in) = Rb+(out)
- Cs+(in) = Cs+(out)
- Li+(in) = Li+(out)
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | bicellular tight junction | |
Cellular Component | plasma membrane | |
Cellular Component | tight junction | |
Molecular Function | identical protein binding | |
Molecular Function | paracellular tight junction channel activity | |
Molecular Function | PDZ domain binding | |
Molecular Function | structural molecule activity | |
Biological Process | bicellular tight junction assembly | |
Biological Process | calcium-independent cell-cell adhesion via plasma membrane cell-adhesion molecules | |
Biological Process | cell adhesion | |
Biological Process | monoatomic ion transport | |
Biological Process | paracellular transport | |
Biological Process | renal absorption |
Keywords
- Biological process
- Ligand
Names & Taxonomy
Protein names
- Recommended nameClaudin-16
- Short namesCL-16
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Laurasiatheria > Artiodactyla > Ruminantia > Pecora > Bovidae > Bovinae > Bos
Accessions
- Primary accessionQ9XT98
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Multi-pass membrane protein
Note: Cotrafficks with CLDN19 from ER to tight junctions.
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-22 | Cytoplasmic | ||||
Sequence: MGPGLAASHVSFPDSLLAKMRD | ||||||
Transmembrane | 23-43 | Helical | ||||
Sequence: LLQYVACFFAFFSAGFLVVAT | ||||||
Topological domain | 44-98 | Extracellular | ||||
Sequence: WTDCWMVNADDSLEVSTKCRGLWWECVTNAFDGIRTCDEYDSILAEHSLKLVVTR | ||||||
Transmembrane | 99-119 | Helical | ||||
Sequence: ALMITADILAGFGFITLLLGL | ||||||
Topological domain | 120-134 | Cytoplasmic | ||||
Sequence: DCVKFLPDEPYIKVR | ||||||
Transmembrane | 135-155 | Helical | ||||
Sequence: ISFVAGTTLLIAGAPGIIGSV | ||||||
Topological domain | 156-188 | Extracellular | ||||
Sequence: WYAVDVYVERSSLVLHNIFLGIQYKFGWSCWLG | ||||||
Transmembrane | 189-209 | Helical | ||||
Sequence: MAGSLGCFLAGAILTCCLYLF | ||||||
Topological domain | 210-254 | Cytoplasmic | ||||
Sequence: KDVGPERSYPYSTRKAYSTTAVSMPRSHAIPRTQTAKMYAVDTRV |
Keywords
- Cellular component
Phenotypes & Variants
Involvement in disease
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 17 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000144773 | 1-254 | Claudin-16 | |||
Sequence: MGPGLAASHVSFPDSLLAKMRDLLQYVACFFAFFSAGFLVVATWTDCWMVNADDSLEVSTKCRGLWWECVTNAFDGIRTCDEYDSILAEHSLKLVVTRALMITADILAGFGFITLLLGLDCVKFLPDEPYIKVRISFVAGTTLLIAGAPGIIGSVWYAVDVYVERSSLVLHNIFLGIQYKFGWSCWLGMAGSLGCFLAGAILTCCLYLFKDVGPERSYPYSTRKAYSTTAVSMPRSHAIPRTQTAKMYAVDTRV |
Proteomic databases
Expression
Interaction
Subunit
Can form heteropolymeric tight junction strands with other claudins. Interacts with CLDN19 (By similarity).
Interacts (via PDZ-binding motif TRV) with TJP1 (via PDZ domain) (By similarity).
Cannot form tight junction strands on its own (By similarity).
Interacts (via PDZ-binding motif TRV) with TJP1 (via PDZ domain) (By similarity).
Cannot form tight junction strands on its own (By similarity).
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Motif | 252-254 | Interaction with TJP1 | ||||
Sequence: TRV |
Domain
The first extracellular loop contains negatively charged amino acids that affect cation selectivity.
Sequence similarities
Belongs to the claudin family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length254
- Mass (Da)27,992
- Last updated1999-11-01 v1
- Checksum38B00835FF894ECC
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AB030082 EMBL· GenBank· DDBJ | BAA82553.1 EMBL· GenBank· DDBJ | mRNA |