extracytosolic/lumenal domain (ELD) found in transient receptor potential channel mucolipins ...
128-311
1.66e-37
extracytosolic/lumenal domain (ELD) found in transient receptor potential channel mucolipins (TRPMLs); TRPML family proteins contain a linker between the first two transmembrane helices (S1 and S2), which is called TRPML I-II linker. It forms a tight tetramer that is crucial for full-length TRPMLs assembly and localization. In lysosomes and endosomes, this linker faces the lumen (it is therefore also referred to as the 'luminal linker'); on the plasma membrane, it faces the extracellular solution. TRPML I-II linker has been named as extracytosolic/lumenal domain (ELD).
:
Pssm-ID: 410965 Cd Length: 167 Bit Score: 137.38 E-value: 1.66e-37
Polycystin cation channel; This family contains the cation channel region from group II of ...
382-556
1.02e-12
Polycystin cation channel; This family contains the cation channel region from group II of Transient receptor potential (TRP) channels, the TRPP subfamily, including PKD1, PKD2, PKD2L and mucolipin proteins.
The actual alignment was detected with superfamily member pfam08016:
Pssm-ID: 462341 [Multi-domain] Cd Length: 225 Bit Score: 68.07 E-value: 1.02e-12
extracytosolic/lumenal domain (ELD) found in transient receptor potential channel mucolipins ...
128-311
1.66e-37
extracytosolic/lumenal domain (ELD) found in transient receptor potential channel mucolipins (TRPMLs); TRPML family proteins contain a linker between the first two transmembrane helices (S1 and S2), which is called TRPML I-II linker. It forms a tight tetramer that is crucial for full-length TRPMLs assembly and localization. In lysosomes and endosomes, this linker faces the lumen (it is therefore also referred to as the 'luminal linker'); on the plasma membrane, it faces the extracellular solution. TRPML I-II linker has been named as extracytosolic/lumenal domain (ELD).
Pssm-ID: 410965 Cd Length: 167 Bit Score: 137.38 E-value: 1.66e-37
Polycystin cation channel; This family contains the cation channel region from group II of ...
382-556
1.02e-12
Polycystin cation channel; This family contains the cation channel region from group II of Transient receptor potential (TRP) channels, the TRPP subfamily, including PKD1, PKD2, PKD2L and mucolipin proteins.
Pssm-ID: 462341 [Multi-domain] Cd Length: 225 Bit Score: 68.07 E-value: 1.02e-12
extracytosolic/lumenal domain (ELD) found in transient receptor potential channel mucolipins ...
128-311
1.66e-37
extracytosolic/lumenal domain (ELD) found in transient receptor potential channel mucolipins (TRPMLs); TRPML family proteins contain a linker between the first two transmembrane helices (S1 and S2), which is called TRPML I-II linker. It forms a tight tetramer that is crucial for full-length TRPMLs assembly and localization. In lysosomes and endosomes, this linker faces the lumen (it is therefore also referred to as the 'luminal linker'); on the plasma membrane, it faces the extracellular solution. TRPML I-II linker has been named as extracytosolic/lumenal domain (ELD).
Pssm-ID: 410965 Cd Length: 167 Bit Score: 137.38 E-value: 1.66e-37
Polycystin cation channel; This family contains the cation channel region from group II of ...
382-556
1.02e-12
Polycystin cation channel; This family contains the cation channel region from group II of Transient receptor potential (TRP) channels, the TRPP subfamily, including PKD1, PKD2, PKD2L and mucolipin proteins.
Pssm-ID: 462341 [Multi-domain] Cd Length: 225 Bit Score: 68.07 E-value: 1.02e-12
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ...
383-559
8.64e-09
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This family is 6 transmembrane helices in which the last two helices flank a loop which determines ion selectivity. In some sub-families (e.g. Na channels) the domain is repeated four times, whereas in others (e.g. K channels) the protein forms as a tetramer in the membrane.
Pssm-ID: 459842 [Multi-domain] Cd Length: 238 Bit Score: 56.51 E-value: 8.64e-09
extracytosolic/lumenal domain (ELD) found in transient receptor potential channel mucolipin 3 ...
133-321
8.86e-07
extracytosolic/lumenal domain (ELD) found in transient receptor potential channel mucolipin 3 (TRPML3); TRPML3, also called mucolipin-3 (ML3), acts as Ca(2+)-permeable cation channel with inwardly rectifying activity. It mediates release of Ca(2+) from endosomes to the cytoplasm, contributes to endosomal acidification and is involved in the regulation of membrane trafficking and fusion in the endosomal pathway. The model corresponds to extracytosolic/lumenal domain (ELD), a linker located between the first two transmembrane segments (S1 and S2) of TRPML3. It forms a tight tetramer that is crucial for full-length TRPML3 assembly and localization.
Pssm-ID: 410968 Cd Length: 169 Bit Score: 49.32 E-value: 8.86e-07
extracytosolic/lumenal domain (ELD) found in transient receptor potential channel mucolipin 1 ...
252-302
1.25e-04
extracytosolic/lumenal domain (ELD) found in transient receptor potential channel mucolipin 1 (TRPML1); TRPML1, also called mucolipin-1 (ML1), or MG-2, or Mucolipidin, may play a major role in Ca(2+) release from late endosome and lysosome vesicles to the cytoplasm, which is important for many lysosome-dependent cellular events, including the fusion and trafficking of these organelles, exocytosis and autophagy. The model corresponds to extracytosolic/lumenal domain (ELD), a linker located between the first two transmembrane segments (S1 and S2) of TRPML1. It forms a tight tetramer that is crucial for full-length TRPML1 assembly and localization.
Pssm-ID: 410966 Cd Length: 171 Bit Score: 43.25 E-value: 1.25e-04
Database: CDSEARCH/cdd Low complexity filter: no Composition Based Adjustment: yes E-value threshold: 0.01
References:
Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
of the residues that compose this conserved feature have been mapped to the query sequence.
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