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Conserved domains on  [gi|1958668026|ref|XP_038945071|]
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mucolipin-1 isoform X4 [Rattus norvegicus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ELD_TRPML super family cl41763
extracytosolic/lumenal domain (ELD) found in transient receptor potential channel mucolipins ...
 127-274 1.90e-82

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).


The actual alignment was detected with superfamily member cd21070:

Pssm-ID: 425394  Cd Length: 171  Bit Score: 254.34  E-value: 1.90e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668026 127 GSDDTFAAYTREQLYQAIFYAVDQYLTLPEISLGRYAYVRGGggpWANGSALALCQRYYHRGHVDPANDTFDIDPRVVTD 206
Cdd:cd21070     1 GADDTFAVYTQEDLYQAIFYAVDQYLALPNVTLGRYAYVRGG---WTNGSALALCQQYYHKGHIDPANDTFNIDPLVVTD 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958668026 207 CIQVDPPDRPPdipsedlDFLDGSTSYKNITLKFHKLINVTIHFQLKTINLQSLINNEIPDCYTFSIL 274
Cdd:cd21070    78 CIGVDPPERPP-------PPLESSRSYKNFTLKFHKLINVTIQFQLKAINLQTIINNEIPDCYTFSIT 138
PLN03223 super family cl33665
Polycystin cation channel protein; Provisional
 388-496 1.11e-04

Polycystin cation channel protein; Provisional


The actual alignment was detected with superfamily member PLN03223:

Pssm-ID: 215637 [Multi-domain]  Cd Length: 1634  Bit Score: 45.32  E-value: 1.11e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668026  388 TLRVALPSVMRFCCCVAVIYLGYCFCGWIVLGPYHVKFRSLSMVSECLFSLINGDDMFVtfaaMQAQQGRSSLVWLFSQL 467
Cdd:PLN03223  1322 TLWLAGADLMHFFVIFGMVFVGYAFIGHVIFGNASVHFSDMTDSINSLFENLLGDITYF----NEDLKNLTGLQFVVGMI 1397

                           90       100       110
                   ....*....|....*....|....*....|
gi 1958668026  468 YLYSFiSLFIYMVLSLF-IALITGAYDTIK 496
Cdd:PLN03223  1398 YFYSY-NIFVFMILFNFlLAIICDAFGEVK 1426
 
Name Accession Description Interval E-value
ELD_TRPML1 cd21070
extracytosolic/lumenal domain (ELD) found in transient receptor potential channel mucolipin 1 ...
 127-274 1.90e-82

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: 254.34  E-value: 1.90e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668026 127 GSDDTFAAYTREQLYQAIFYAVDQYLTLPEISLGRYAYVRGGggpWANGSALALCQRYYHRGHVDPANDTFDIDPRVVTD 206
Cdd:cd21070     1 GADDTFAVYTQEDLYQAIFYAVDQYLALPNVTLGRYAYVRGG---WTNGSALALCQQYYHKGHIDPANDTFNIDPLVVTD 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958668026 207 CIQVDPPDRPPdipsedlDFLDGSTSYKNITLKFHKLINVTIHFQLKTINLQSLINNEIPDCYTFSIL 274
Cdd:cd21070    78 CIGVDPPERPP-------PPLESSRSYKNFTLKFHKLINVTIQFQLKAINLQTIINNEIPDCYTFSIT 138
PLN03223 PLN03223
Polycystin cation channel protein; Provisional
 388-496 1.11e-04

Polycystin cation channel protein; Provisional


Pssm-ID: 215637 [Multi-domain]  Cd Length: 1634  Bit Score: 45.32  E-value: 1.11e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668026  388 TLRVALPSVMRFCCCVAVIYLGYCFCGWIVLGPYHVKFRSLSMVSECLFSLINGDDMFVtfaaMQAQQGRSSLVWLFSQL 467
Cdd:PLN03223  1322 TLWLAGADLMHFFVIFGMVFVGYAFIGHVIFGNASVHFSDMTDSINSLFENLLGDITYF----NEDLKNLTGLQFVVGMI 1397

                           90       100       110
                   ....*....|....*....|....*....|
gi 1958668026  468 YLYSFiSLFIYMVLSLF-IALITGAYDTIK 496
Cdd:PLN03223  1398 YFYSY-NIFVFMILFNFlLAIICDAFGEVK 1426
Ion_trans pfam00520
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ...
 384-496 1.36e-04

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: 43.41  E-value: 1.36e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668026 384 ILIATLRVALPSVMRF---CCCVAVIY-------LGYCFCGWIVLGPYHVKFRSLSMVSECLFSLINGDDMFVTFAAMQA 453
Cdd:pfam00520 117 TLVNSLIRSLKSLGNLlllLLLFLFIFaiigyqlFGGKLKTWENPDNGRTNFDNFPNAFLWLFQTMTTEGWGDIMYDTID 196

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1958668026 454 QQGRSslvwlFSQLYLYSFISLFIYMVLSLFIALITGAYDTIK 496
Cdd:pfam00520 197 GKGEF-----WAYIYFVSFIILGGFLLLNLFIAVIIDNFQELT 234
 
Name Accession Description Interval E-value
ELD_TRPML1 cd21070
extracytosolic/lumenal domain (ELD) found in transient receptor potential channel mucolipin 1 ...
 127-274 1.90e-82

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: 254.34  E-value: 1.90e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668026 127 GSDDTFAAYTREQLYQAIFYAVDQYLTLPEISLGRYAYVRGGggpWANGSALALCQRYYHRGHVDPANDTFDIDPRVVTD 206
Cdd:cd21070     1 GADDTFAVYTQEDLYQAIFYAVDQYLALPNVTLGRYAYVRGG---WTNGSALALCQQYYHKGHIDPANDTFNIDPLVVTD 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958668026 207 CIQVDPPDRPPdipsedlDFLDGSTSYKNITLKFHKLINVTIHFQLKTINLQSLINNEIPDCYTFSIL 274
Cdd:cd21070    78 CIGVDPPERPP-------PPLESSRSYKNFTLKFHKLINVTIQFQLKAINLQTIINNEIPDCYTFSIT 138
ELD_TRPML3 cd21072
extracytosolic/lumenal domain (ELD) found in transient receptor potential channel mucolipin 3 ...
 127-279 2.91e-42

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: 149.08  E-value: 2.91e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668026 127 GSDDTFAAYTREQLYQAIFYAVDQYLTLPEISLGRYAYVRGGGGPwangSALALCQRYYHRGHVDPANDTFDIDPRVVTD 206
Cdd:cd21072     1 RMDDTYAVYTQSDVYDHIDFIINQYLQLQNISVGNHAYERKGTKQ----TPLSICQDFYKRGSIFPGNETFDIDPEIETE 76

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958668026 207 CIQVDPPDRppdipsedldFLDGSTSYK--NITLKFHKLINVTIHFQLKTINLQSLINNEIPDCYTFSILefVVF 279
Cdd:cd21072    77 CFNIYPLQP----------FHNGTAAENklNFTLDFHRLLSVEVHFKLKAINLQTVRHHELPDCYDFTVT--ITF 139
ELD_TRPML cd21050
extracytosolic/lumenal domain (ELD) found in transient receptor potential channel mucolipins ...
 128-273 1.76e-40

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: 144.31  E-value: 1.76e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668026 128 SDDTFAAYTREQLYQAIFYAVDQYLTLPEISLGRYAYVRGGGGPwangSALALCQRYYHRGHVDPANDTFDIDPRVVTDC 207
Cdd:cd21050     2 ATGPYAVYTKDDFYEHLDFAVNQYYNLENIAIGSYGYDSNNGTP----PPITLCVTQYKNGEVDPFNNTYVFDPTVITDC 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958668026 208 IQVDPPDRPPDIPSED-LDFLdgstSYKNITLKFHKLINVTIHFQLKTINLQSLINNEIPDCYTFSI 273
Cdd:cd21050    78 LSIPPTYPENDNLWDSiKDFL----KSKNFTLNFDRLIKIELKFSLKTIHLKSLKPLDSPECYKFNV 140
ELD_TRPML2 cd21071
extracytosolic/lumenal domain (ELD) found in transient receptor potential channel mucolipin 2 ...
 126-273 1.15e-30

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: 117.50  E-value: 1.15e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668026 126 DGSDDTFAAYTREQLYQAIFYAVDQYLTLPEISLGRYAYVRGGGGPWAngsaLALCQRYYHRGHVDPANDTFDIDPRVVT 205
Cdd:cd21071     3 DEDDYSIAVYTQQDVYDSLFYAIDQYAQLKNLSVGPLSYAEDEDELLP----LKICKQLYKKGSVKPSEEVYDIDAQLET 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958668026 206 DCIQVDPPDrppdipSEDLDFLDGSTSYKNitLKFHKLINVTIHFQLKTINLQSLINNEIPDCYTFSI 273
Cdd:cd21071    79 VCLTIDPKT------LNDKKWKMSNSSFFE--LDFYRLVQIEITFRLKGINLQTIRSRELPDCYTFFV 138
PLN03223 PLN03223
Polycystin cation channel protein; Provisional
 388-496 1.11e-04

Polycystin cation channel protein; Provisional


Pssm-ID: 215637 [Multi-domain]  Cd Length: 1634  Bit Score: 45.32  E-value: 1.11e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668026  388 TLRVALPSVMRFCCCVAVIYLGYCFCGWIVLGPYHVKFRSLSMVSECLFSLINGDDMFVtfaaMQAQQGRSSLVWLFSQL 467
Cdd:PLN03223  1322 TLWLAGADLMHFFVIFGMVFVGYAFIGHVIFGNASVHFSDMTDSINSLFENLLGDITYF----NEDLKNLTGLQFVVGMI 1397

                           90       100       110
                   ....*....|....*....|....*....|
gi 1958668026  468 YLYSFiSLFIYMVLSLF-IALITGAYDTIK 496
Cdd:PLN03223  1398 YFYSY-NIFVFMILFNFlLAIICDAFGEVK 1426
Ion_trans pfam00520
Ion transport protein; This family contains sodium, potassium and calcium ion channels. This ...
 384-496 1.36e-04

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: 43.41  E-value: 1.36e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668026 384 ILIATLRVALPSVMRF---CCCVAVIY-------LGYCFCGWIVLGPYHVKFRSLSMVSECLFSLINGDDMFVTFAAMQA 453
Cdd:pfam00520 117 TLVNSLIRSLKSLGNLlllLLLFLFIFaiigyqlFGGKLKTWENPDNGRTNFDNFPNAFLWLFQTMTTEGWGDIMYDTID 196

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1958668026 454 QQGRSslvwlFSQLYLYSFISLFIYMVLSLFIALITGAYDTIK 496
Cdd:pfam00520 197 GKGEF-----WAYIYFVSFIILGGFLLLNLFIAVIIDNFQELT 234
PKD_channel pfam08016
Polycystin cation channel; This family contains the cation channel region from group II of ...
 388-495 1.56e-03

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: 40.34  E-value: 1.56e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958668026 388 TLRVALPSVMRFCCCVAVIYLGYCFCGWIVLGPYHVKFRSLSMVSECLFSLINGDDMFVTFaamqAQQGRsslvwLFSQL 467
Cdd:pfam08016 127 TLSRAWKDLAGFALMFVIFFFAYAQFGYLLFGTQAPNFSNFVKSILTLFRTILGDFGYNEI----FSGNR-----VLGPL 197

                          90       100
                  ....*....|....*....|....*...
gi 1958668026 468 YLYSFISLFIYMVLSLFIALITGAYDTI 495
Cdd:pfam08016 198 LFLTFVFLVIFILLNLFLAIINDSYVEV 225
 
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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