1.H.1.1.12 Claudin-15 of 227 aas and 4 TMSs, Cldn15. Suzuki et al. 2013 reported the crystal structure of mouse claudin-15
at a resolution of 2.4 angstroms. The structure revealed a
characteristic β-sheet fold consisting of two extracellular segments anchored to a transmembrane four-helix bundle by a consensus motif. Potential paracellular pathways with distinctive
charges on the extracellular surface provided insight into the
molecular basis of ion homeostasis across tight junctions. Site-specific distributions of claudin-2- and claudin-15-based
paracellular channels drive their organ-specific functions in the liver,
kidney, and intestine (Tanaka et al. 2017). A model of the claudin-15-based paracellular channel has been presented (Alberini et al. 2017).
|
Accession Number: | Q9Z0S5 |
Protein Name: | Claudin-15 |
Length: | 227 |
Molecular Weight: | 24280.00 |
Species: | Mus musculus (Mouse) [10090] |
Number of TMSs: | 4 |
Location1 / Topology2 / Orientation3: |
Cell junction1 |
Substrate |
ion |
---|
1: MSVAVETFGF FMSALGLLML GLTLSNSYWR VSTVHGNVIT TNTIFENLWY SCATDSLGVS
61: NCWDFPSMLA LSGYVQGCRA LMITAILLGF LGLFLGMVGL RCTNVGNMDL SKKAKLLAIA
121: GTLHILAGAC GMVAISWYAV NITTDFFNPL YAGTKYELGP ALYLGWSASL LSILGGICVF
181: STCCCSSKEE PATRAGLPYK PSTVVIPRAT SDESDISFGK YGKNAYV