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Conserved domains on  [gi|2462507482|ref|XP_054191759|]
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mucolipin-2 isoform X4 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ELD_TRPML2 cd21071
extracytosolic/lumenal domain (ELD) found in transient receptor potential channel mucolipin 2 ...
 111-277 4.69e-104

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: 302.39  E-value: 4.69e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507482 111 GTDEDDYSCSVYTQEDAYESIFFAINQYHQLKDITLGTLGYGENEDNRIGLKVCKQHYKKGTMFPSNETLNIDNDVELDC 190
Cdd:cd21071     1 GVDEDDYSIAVYTQQDVYDSLFYAIDQYAQLKNLSVGPLSYAEDEDELLPLKICKQLYKKGSVKPSEEVYDIDAQLETVC 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507482 191 VQLDLQDLSKKPPDWKNSSFFRLEFYRLLQVEISFHLKGIDLQTIHSRELPDCYVFQNTIIFDNKAHSGKIKIYFDSDAK 270
Cdd:cd21071    81 LTIDPKTLNDKKWKMSNSSFFELDFYRLVQIEITFRLKGINLQTIRSRELPDCYTFFVTITFDNQCHSGKIKIYFDSDAV 160


                  ....*..
gi 2462507482 271 IEECKDL 277
Cdd:cd21071   161 SSACKDW 167
 
Name Accession Description Interval E-value
ELD_TRPML2 cd21071
extracytosolic/lumenal domain (ELD) found in transient receptor potential channel mucolipin 2 ...
 111-277 4.69e-104

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: 302.39  E-value: 4.69e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507482 111 GTDEDDYSCSVYTQEDAYESIFFAINQYHQLKDITLGTLGYGENEDNRIGLKVCKQHYKKGTMFPSNETLNIDNDVELDC 190
Cdd:cd21071     1 GVDEDDYSIAVYTQQDVYDSLFYAIDQYAQLKNLSVGPLSYAEDEDELLPLKICKQLYKKGSVKPSEEVYDIDAQLETVC 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507482 191 VQLDLQDLSKKPPDWKNSSFFRLEFYRLLQVEISFHLKGIDLQTIHSRELPDCYVFQNTIIFDNKAHSGKIKIYFDSDAK 270
Cdd:cd21071    81 LTIDPKTLNDKKWKMSNSSFFELDFYRLVQIEITFRLKGINLQTIRSRELPDCYTFFVTITFDNQCHSGKIKIYFDSDAV 160


                  ....*..
gi 2462507482 271 IEECKDL 277
Cdd:cd21071   161 SSACKDW 167
 
Name Accession Description Interval E-value
ELD_TRPML2 cd21071
extracytosolic/lumenal domain (ELD) found in transient receptor potential channel mucolipin 2 ...
 111-277 4.69e-104

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: 302.39  E-value: 4.69e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507482 111 GTDEDDYSCSVYTQEDAYESIFFAINQYHQLKDITLGTLGYGENEDNRIGLKVCKQHYKKGTMFPSNETLNIDNDVELDC 190
Cdd:cd21071     1 GVDEDDYSIAVYTQQDVYDSLFYAIDQYAQLKNLSVGPLSYAEDEDELLPLKICKQLYKKGSVKPSEEVYDIDAQLETVC 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507482 191 VQLDLQDLSKKPPDWKNSSFFRLEFYRLLQVEISFHLKGIDLQTIHSRELPDCYVFQNTIIFDNKAHSGKIKIYFDSDAK 270
Cdd:cd21071    81 LTIDPKTLNDKKWKMSNSSFFELDFYRLVQIEITFRLKGINLQTIRSRELPDCYTFFVTITFDNQCHSGKIKIYFDSDAV 160


                  ....*..
gi 2462507482 271 IEECKDL 277
Cdd:cd21071   161 SSACKDW 167
ELD_TRPML3 cd21072
extracytosolic/lumenal domain (ELD) found in transient receptor potential channel mucolipin 3 ...
 116-282 4.63e-59

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: 187.99  E-value: 4.63e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507482 116 DYSCSVYTQEDAYESIFFAINQYHQLKDITLGTLGYGENEDNRIGLKVCKQHYKKGTMFPSNETLNIDNDVELDCVQLDL 195
Cdd:cd21072     3 DDTYAVYTQSDVYDHIDFIINQYLQLQNISVGNHAYERKGTKQTPLSICQDFYKRGSIFPGNETFDIDPEIETECFNIYP 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507482 196 QDLSKKPPDWKNSSFFRLEFYRLLQVEISFHLKGIDLQTIHSRELPDCYVFQNTIIFDNKAHSGKIKIYFDSDAKIEECK 275
Cdd:cd21072    83 LQPFHNGTAAENKLNFTLDFHRLLSVEVHFKLKAINLQTVRHHELPDCYDFTVTITFDNKAHSGRIKISLDNDVDIRECK 162


                  ....*..
gi 2462507482 276 DLNIFGS 282
Cdd:cd21072   163 DWHVSGS 169
ELD_TRPML1 cd21070
extracytosolic/lumenal domain (ELD) found in transient receptor potential channel mucolipin 1 ...
 116-281 1.79e-54

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: 176.14  E-value: 1.79e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507482 116 DYSCSVYTQEDAYESIFFAINQYHQLKDITLGTLGY-GENEDNRIGLKVCKQHYKKGTMFPSNETLNIDNDVELDCVQLD 194
Cdd:cd21070     3 DDTFAVYTQEDLYQAIFYAVDQYLALPNVTLGRYAYvRGGWTNGSALALCQQYYHKGHIDPANDTFNIDPLVVTDCIGVD 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507482 195 LQDLSKKPPD----WKNssfFRLEFYRLLQVEISFHLKGIDLQTIHSRELPDCYVFQNTIIFDNKAHSGKIKIYFDSDAK 270
Cdd:cd21070    83 PPERPPPPLEssrsYKN---FTLKFHKLINVTIQFQLKAINLQTIINNEIPDCYTFSITITFDNKAHSGRIKISLENQAH 159

                         170
                  ....*....|.
gi 2462507482 271 IEECKDLNIFG 281
Cdd:cd21070   160 IKECKDPSVFG 170
ELD_TRPML cd21050
extracytosolic/lumenal domain (ELD) found in transient receptor potential channel mucolipins ...
 119-275 2.32e-53

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: 173.20  E-value: 2.32e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507482 119 CSVYTQEDAYESIFFAINQYHQLKDITLGTLGYGENEDNRIGLKVCKQHYKKGTMFPSNETLNIDNDVELDCVQLDLQD- 197
Cdd:cd21050     6 YAVYTKDDFYEHLDFAVNQYYNLENIAIGSYGYDSNNGTPPPITLCVTQYKNGEVDPFNNTYVFDPTVITDCLSIPPTYp 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462507482 198 ----LSKKPPDWKNSSFFRLEFYRLLQVEISFHLKGIDLQTIHSRELPDCYVFQNTIIFDNKAHSGKIKIYFDSDAKIEE 273
Cdd:cd21050    86 endnLWDSIKDFLKSKNFTLNFDRLIKIELKFSLKTIHLKSLKPLDSPECYKFNVTILFDNSAHDGQMPVSLDTNISELE 165


                  ..
gi 2462507482 274 CK 275
Cdd:cd21050   166 CN 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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