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Conserved domains on  [gi|568921969|ref|XP_006501148|]
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mucolipin-3 isoform X2 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ELD_TRPML3 cd21072
extracytosolic/lumenal domain (ELD) found in transient receptor potential channel mucolipin 3 ...
 109-277 3.79e-117

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: 340.91  E-value: 3.79e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921969 109 RMDDTYAVYTQSEVYDQIIFAVTQYLQLQNISVGNHAYENKGTKQSAMAICQHFYRQGTICPGNDTFDIDPEVETECFLV 188
Cdd:cd21072    1 RMDDTYAVYTQSDVYDHIDFIINQYLQLQNISVGNHAYERKGTKQTPLSICQDFYKRGSIFPGNETFDIDPEIETECFNI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921969 189 EPDEASHLGTPGENKLNLSLDFHRLLTVELQFKLKAINLQTVRHQELPDCYDFTLTITFDNKAHSGRIKISLDNDISIKE 268
Cdd:cd21072   81 YPLQPFHNGTAAENKLNFTLDFHRLLSVEVHFKLKAINLQTVRHHELPDCYDFTVTITFDNKAHSGRIKISLDNDVDIRE 160


                 ....*....
gi 568921969 269 CKDWHVSGS 277
Cdd:cd21072  161 CKDWHVSGS 169
 
Name Accession Description Interval E-value
ELD_TRPML3 cd21072
extracytosolic/lumenal domain (ELD) found in transient receptor potential channel mucolipin 3 ...
 109-277 3.79e-117

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: 340.91  E-value: 3.79e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921969 109 RMDDTYAVYTQSEVYDQIIFAVTQYLQLQNISVGNHAYENKGTKQSAMAICQHFYRQGTICPGNDTFDIDPEVETECFLV 188
Cdd:cd21072    1 RMDDTYAVYTQSDVYDHIDFIINQYLQLQNISVGNHAYERKGTKQTPLSICQDFYKRGSIFPGNETFDIDPEIETECFNI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921969 189 EPDEASHLGTPGENKLNLSLDFHRLLTVELQFKLKAINLQTVRHQELPDCYDFTLTITFDNKAHSGRIKISLDNDISIKE 268
Cdd:cd21072   81 YPLQPFHNGTAAENKLNFTLDFHRLLSVEVHFKLKAINLQTVRHHELPDCYDFTVTITFDNKAHSGRIKISLDNDVDIRE 160


                 ....*....
gi 568921969 269 CKDWHVSGS 277
Cdd:cd21072  161 CKDWHVSGS 169
 
Name Accession Description Interval E-value
ELD_TRPML3 cd21072
extracytosolic/lumenal domain (ELD) found in transient receptor potential channel mucolipin 3 ...
 109-277 3.79e-117

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: 340.91  E-value: 3.79e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921969 109 RMDDTYAVYTQSEVYDQIIFAVTQYLQLQNISVGNHAYENKGTKQSAMAICQHFYRQGTICPGNDTFDIDPEVETECFLV 188
Cdd:cd21072    1 RMDDTYAVYTQSDVYDHIDFIINQYLQLQNISVGNHAYERKGTKQTPLSICQDFYKRGSIFPGNETFDIDPEIETECFNI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921969 189 EPDEASHLGTPGENKLNLSLDFHRLLTVELQFKLKAINLQTVRHQELPDCYDFTLTITFDNKAHSGRIKISLDNDISIKE 268
Cdd:cd21072   81 YPLQPFHNGTAAENKLNFTLDFHRLLSVEVHFKLKAINLQTVRHHELPDCYDFTVTITFDNKAHSGRIKISLDNDVDIRE 160


                 ....*....
gi 568921969 269 CKDWHVSGS 277
Cdd:cd21072  161 CKDWHVSGS 169
ELD_TRPML1 cd21070
extracytosolic/lumenal domain (ELD) found in transient receptor potential channel mucolipin 1 ...
 111-276 3.57e-73

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: 228.53  E-value: 3.57e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921969 111 DDTYAVYTQSEVYDQIIFAVTQYLQLQNISVGNHAY-ENKGTKQSAMAICQHFYRQGTICPGNDTFDIDPEVETECFLVE 189
Cdd:cd21070    3 DDTFAVYTQEDLYQAIFYAVDQYLALPNVTLGRYAYvRGGWTNGSALALCQQYYHKGHIDPANDTFNIDPLVVTDCIGVD 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921969 190 PDEASHLG-TPGENKLNLSLDFHRLLTVELQFKLKAINLQTVRHQELPDCYDFTLTITFDNKAHSGRIKISLDNDISIKE 268
Cdd:cd21070   83 PPERPPPPlESSRSYKNFTLKFHKLINVTIQFQLKAINLQTIINNEIPDCYTFSITITFDNKAHSGRIKISLENQAHIKE 162


                 ....*...
gi 568921969 269 CKDWHVSG 276
Cdd:cd21070  163 CKDPSVFG 170
ELD_TRPML cd21050
extracytosolic/lumenal domain (ELD) found in transient receptor potential channel mucolipins ...
 114-270 5.49e-59

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: 191.69  E-value: 5.49e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921969 114 YAVYTQSEVYDQIIFAVTQYLQLQNISVGNHAYENKGTKQSAMAICQHFYRQGTICPGNDTFDIDPEVETECFLVEPDEA 193
Cdd:cd21050    6 YAVYTKDDFYEHLDFAVNQYYNLENIAIGSYGYDSNNGTPPPITLCVTQYKNGEVDPFNNTYVFDPTVITDCLSIPPTYP 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921969 194 SHLGTPGENK-----LNLSLDFHRLLTVELQFKLKAINLQTVRHQELPDCYDFTLTITFDNKAHSGRIKISLDNDISIKE 268
Cdd:cd21050   86 ENDNLWDSIKdflksKNFTLNFDRLIKIELKFSLKTIHLKSLKPLDSPECYKFNVTILFDNSAHDGQMPVSLDTNISELE 165


                 ..
gi 568921969 269 CK 270
Cdd:cd21050  166 CN 167
ELD_TRPML2 cd21071
extracytosolic/lumenal domain (ELD) found in transient receptor potential channel mucolipin 2 ...
 108-272 6.07e-59

extracytosolic/lumenal domain (ELD) found in transient receptor potential channel mucolipin 2 (TRPML2); TRPML2, also called mucolipin-2 (ML2), acts as Ca(2+)-permeable cation channel with inwardly rectifying activity. It may activate ARF6 and be involved in the trafficking of GPI-anchored cargo proteins to the cell surface via the ARF6-regulated recycling pathway. The model corresponds to extracytosolic/lumenal domain (ELD), a linker located between the first two transmembrane segments (S1 and S2) of TRPML2. It forms a tight tetramer that is crucial for full-length TRPML2 assembly and localization.


Pssm-ID: 410967  Cd Length: 167  Bit Score: 191.46  E-value: 6.07e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921969 108 DRMDDTYAVYTQSEVYDQIIFAVTQYLQLQNISVGNHAYENKGTKQSAMAICQHFYRQGTICPGNDTFDIDPEVETECFL 187
Cdd:cd21071    3 DEDDYSIAVYTQQDVYDSLFYAIDQYAQLKNLSVGPLSYAEDEDELLPLKICKQLYKKGSVKPSEEVYDIDAQLETVCLT 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568921969 188 VEPDEASHLGTPGENKLNLSLDFHRLLTVELQFKLKAINLQTVRHQELPDCYDFTLTITFDNKAHSGRIKISLDNDISIK 267
Cdd:cd21071   83 IDPKTLNDKKWKMSNSSFFELDFYRLVQIEITFRLKGINLQTIRSRELPDCYTFFVTITFDNQCHSGKIKIYFDSDAVSS 162


                 ....*
gi 568921969 268 ECKDW 272
Cdd:cd21071  163 ACKDW 167
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options: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.
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