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Conserved domains on  [gi|21358239|ref|NP_651824|]
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Niemann-Pick type C-2h, isoform A [Drosophila melanogaster]

Protein Classification

NPC2 family protein( domain architecture ID 10097044)

NPC2 (Niemann-Pick proteins type C2) family protein similar to Homo sapiens NPC intracellular cholesterol transporter 2 (NPC2) that acts as intracellular cholesterol transporter which acts in concert with NPC1 and plays an important role in the egress of cholesterol from the lysosomal compartment

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Npc2_like cd00916
Niemann-Pick type C2 (Npc2) is a lysosomal protein in which a mutation in the gene causes a ...
 26-153 2.50e-38

Niemann-Pick type C2 (Npc2) is a lysosomal protein in which a mutation in the gene causes a rare form of Niemann-Pick type C disease, an autosomal recessive lipid storage disorder characterized by accumulation of low-density lipoprotein-derived cholesterol in lysosomes. Although Npc2 is known to bind cholesterol, the function of this protein is unknown. These proteins belong to the ML domain family.


:

Pssm-ID: 238458  Cd Length: 123  Bit Score: 126.65  E-value: 2.50e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358239  26 FQTCEDSVdsCSISQVRVTPCPEAnanaACHIRRRHRFTMSFDFTPHFDADTLVASLGWAKSeNVELPLLTMDQEACKY- 104
Cdd:cd00916   1 FRDCGSSR--PTPSEVRISGCATL----PCKLKRGSTAKVSIDFTPNFDSTSLKTEVHAILL-GVPVPFPLPNPDACKNl 73

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 21358239 105 -TTCPVRSGVTQTYTNNMPADARFPLSPYTIRWALKDPVSQKRCCFTIDI 153
Cdd:cd00916  74 gTSCPLSAGEDVTYTLSLPVLAPYPGISVTVEWELTDDDGQVLTCFQIPA 123
 
Name Accession Description Interval E-value
Npc2_like cd00916
Niemann-Pick type C2 (Npc2) is a lysosomal protein in which a mutation in the gene causes a ...
 26-153 2.50e-38

Niemann-Pick type C2 (Npc2) is a lysosomal protein in which a mutation in the gene causes a rare form of Niemann-Pick type C disease, an autosomal recessive lipid storage disorder characterized by accumulation of low-density lipoprotein-derived cholesterol in lysosomes. Although Npc2 is known to bind cholesterol, the function of this protein is unknown. These proteins belong to the ML domain family.


Pssm-ID: 238458  Cd Length: 123  Bit Score: 126.65  E-value: 2.50e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358239  26 FQTCEDSVdsCSISQVRVTPCPEAnanaACHIRRRHRFTMSFDFTPHFDADTLVASLGWAKSeNVELPLLTMDQEACKY- 104
Cdd:cd00916   1 FRDCGSSR--PTPSEVRISGCATL----PCKLKRGSTAKVSIDFTPNFDSTSLKTEVHAILL-GVPVPFPLPNPDACKNl 73

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 21358239 105 -TTCPVRSGVTQTYTNNMPADARFPLSPYTIRWALKDPVSQKRCCFTIDI 153
Cdd:cd00916  74 gTSCPLSAGEDVTYTLSLPVLAPYPGISVTVEWELTDDDGQVLTCFQIPA 123
ML smart00737
Domain involved in innate immunity and lipid metabolism; ML (MD-2-related lipid-recognition) ...
 26-153 9.77e-29

Domain involved in innate immunity and lipid metabolism; ML (MD-2-related lipid-recognition) is a novel domain identified in MD-1, MD-2, GM2A, Npc2 and multiple proteins of unknown function in plants, animals and fungi. These single-domain proteins were predicted to form a beta-rich fold containing multiple strands, and to mediate diverse biological functions through interacting with specific lipids.


Pssm-ID: 214796  Cd Length: 119  Bit Score: 102.06  E-value: 9.77e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358239     26 FQTCeDSVDSCSISQVRVTPCPEAnanaachirRRHRFTMSFDFTPHFDADTLVASLGWaKSENVELPLLTMDQEACKYT 105
Cdd:smart00737   1 FKDC-GSNDPGQISSVSISPCPPV---------RGKTLTISISFTLNEDISKLKVVVHV-KIGGIEVPIPGETYDLCKLT 69

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 21358239    106 --TCPVRSGVTQTYTNNMPADARFPLSPYTIRWALKDPVSQKRCCFTIDI 153
Cdd:smart00737  70 gsKCPIEKGETVNYTNSLTVPGIFPPGKYTVKWELTDEDGEELACINFTV 119
E1_DerP2_DerF2 pfam02221
ML domain; ML domain - MD-2-related lipid recognition domain. This family consists of proteins ...
 24-155 2.23e-10

ML domain; ML domain - MD-2-related lipid recognition domain. This family consists of proteins from plants, animals and fungi, including dust mite allergen Der P 2. It has been implicate in lipid recognition, particularly in the recognition of pathogen related products. A mutation in Npc2 causes a rare form of Niemann-Pick type C2 disease. This domain has a similar topology to immunoglobulin domains.


Pssm-ID: 460498  Cd Length: 133  Bit Score: 55.07  E-value: 2.23e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358239    24 VNFQTC-EDSVDSCSISQVRVTPcpeananaACHIRRRHRFTMSFDF-TPHFDADTLVA----SLGWaksenVELPL-LT 96
Cdd:pfam02221   2 VPFRDCgRNKDDAPTPKSVDISP--------PCPLVRGQNLTISASGtTSDEISQGLKVdvevRLGG-----ITLPFpLP 68

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21358239    97 MDQEACKYT------TCPVRSGVTQTYTNNMPADARFPLSPYTIRWALKDPVSQKRCCFTIDIKV 155
Cdd:pfam02221  69 ETRDLCDELevgsglSCPIKAGEYVTYTLTLPLPSEYPPGKYTVEAELYDQDGKPLTCFKIDVSI 133
 
Name Accession Description Interval E-value
Npc2_like cd00916
Niemann-Pick type C2 (Npc2) is a lysosomal protein in which a mutation in the gene causes a ...
 26-153 2.50e-38

Niemann-Pick type C2 (Npc2) is a lysosomal protein in which a mutation in the gene causes a rare form of Niemann-Pick type C disease, an autosomal recessive lipid storage disorder characterized by accumulation of low-density lipoprotein-derived cholesterol in lysosomes. Although Npc2 is known to bind cholesterol, the function of this protein is unknown. These proteins belong to the ML domain family.


Pssm-ID: 238458  Cd Length: 123  Bit Score: 126.65  E-value: 2.50e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358239  26 FQTCEDSVdsCSISQVRVTPCPEAnanaACHIRRRHRFTMSFDFTPHFDADTLVASLGWAKSeNVELPLLTMDQEACKY- 104
Cdd:cd00916   1 FRDCGSSR--PTPSEVRISGCATL----PCKLKRGSTAKVSIDFTPNFDSTSLKTEVHAILL-GVPVPFPLPNPDACKNl 73

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 21358239 105 -TTCPVRSGVTQTYTNNMPADARFPLSPYTIRWALKDPVSQKRCCFTIDI 153
Cdd:cd00916  74 gTSCPLSAGEDVTYTLSLPVLAPYPGISVTVEWELTDDDGQVLTCFQIPA 123
ML smart00737
Domain involved in innate immunity and lipid metabolism; ML (MD-2-related lipid-recognition) ...
 26-153 9.77e-29

Domain involved in innate immunity and lipid metabolism; ML (MD-2-related lipid-recognition) is a novel domain identified in MD-1, MD-2, GM2A, Npc2 and multiple proteins of unknown function in plants, animals and fungi. These single-domain proteins were predicted to form a beta-rich fold containing multiple strands, and to mediate diverse biological functions through interacting with specific lipids.


Pssm-ID: 214796  Cd Length: 119  Bit Score: 102.06  E-value: 9.77e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358239     26 FQTCeDSVDSCSISQVRVTPCPEAnanaachirRRHRFTMSFDFTPHFDADTLVASLGWaKSENVELPLLTMDQEACKYT 105
Cdd:smart00737   1 FKDC-GSNDPGQISSVSISPCPPV---------RGKTLTISISFTLNEDISKLKVVVHV-KIGGIEVPIPGETYDLCKLT 69

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 21358239    106 --TCPVRSGVTQTYTNNMPADARFPLSPYTIRWALKDPVSQKRCCFTIDI 153
Cdd:smart00737  70 gsKCPIEKGETVNYTNSLTVPGIFPPGKYTVKWELTDEDGEELACINFTV 119
E1_DerP2_DerF2 pfam02221
ML domain; ML domain - MD-2-related lipid recognition domain. This family consists of proteins ...
 24-155 2.23e-10

ML domain; ML domain - MD-2-related lipid recognition domain. This family consists of proteins from plants, animals and fungi, including dust mite allergen Der P 2. It has been implicate in lipid recognition, particularly in the recognition of pathogen related products. A mutation in Npc2 causes a rare form of Niemann-Pick type C2 disease. This domain has a similar topology to immunoglobulin domains.


Pssm-ID: 460498  Cd Length: 133  Bit Score: 55.07  E-value: 2.23e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358239    24 VNFQTC-EDSVDSCSISQVRVTPcpeananaACHIRRRHRFTMSFDF-TPHFDADTLVA----SLGWaksenVELPL-LT 96
Cdd:pfam02221   2 VPFRDCgRNKDDAPTPKSVDISP--------PCPLVRGQNLTISASGtTSDEISQGLKVdvevRLGG-----ITLPFpLP 68

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21358239    97 MDQEACKYT------TCPVRSGVTQTYTNNMPADARFPLSPYTIRWALKDPVSQKRCCFTIDIKV 155
Cdd:pfam02221  69 ETRDLCDELevgsglSCPIKAGEYVTYTLTLPLPSEYPPGKYTVEAELYDQDGKPLTCFKIDVSI 133
Der-p2_like cd00918
Several group 2 allergen proteins belong to the ML domain family. They include ...
 38-123 1.51e-03

Several group 2 allergen proteins belong to the ML domain family. They include Dermatophagoides pteronyssinus, group 2 (Der p 2) and D. farinae, group 2 (Der f 2) allergens. These house dust mites cause heavy atopic diseases such as asthma and dermatitis. Although the allergenic properties of these proteins have been well characterized, their biological function in mites is unknown.


Pssm-ID: 238460  Cd Length: 120  Bit Score: 36.63  E-value: 1.51e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21358239  38 ISQVRVTPCpeanANAACHIRRRHRFTMSFDFTPHFDADTLVASLGwAKSENVELPLLTMDQEACKYTTCPVRSGVTQT- 116
Cdd:cd00918   9 IKSLEVDGC----SGDYCVIHRGKPLTLEAKFTANQDTAKAKIKIT-ASIDGLEIDVPGIETDGCKYVKCPIKKGQHYDi 83


                ....*...
gi 21358239 117 -YTNNMPA 123
Cdd:cd00918  84 kYTWNVPA 91
 
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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