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Conserved domains on  [gi|1720432212|ref|XP_030100335|]
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secretory carrier-associated membrane protein 5 isoform X1 [Mus musculus]

Protein Classification

secretory carrier-associated membrane protein( domain architecture ID 10514244)

secretory carrier-associated membrane protein (SCAMP) probably functions in endocytosis by recruiting EH-domain proteins to the N-terminal NPF repeats but may also have additional functions mediated by their other sequences

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SCAMP pfam04144
SCAMP family; In vertebrates, secretory carrier membrane proteins (SCAMPs) 1-3 constitute a ...
 107-240 4.31e-43

SCAMP family; In vertebrates, secretory carrier membrane proteins (SCAMPs) 1-3 constitute a family of putative membrane-trafficking proteins composed of cytoplasmic N-terminal sequences with NPF repeats, four central transmembrane regions (TMRs), and a cytoplasmic tail. SCAMPs probably function in endocytosis by recruiting EH-domain proteins to the N-terminal NPF repeats but may have additional functions mediated by their other sequences.


:

Pssm-ID: 461193  Cd Length: 172  Bit Score: 145.37  E-value: 4.31e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432212 107 VNSVTLAVNLVGCLAWLIGGG--GATNFGLAFLWLILFTPCSYVCWFRPIYKAFKTDSSFSFMAFFFTFMAQLVISIIQA 184
Cdd:pfam04144  36 LLTLTLFLNFIACLALFIGGGsgGGAFLGLSILYLLLFTPLSFVLWYRPLYKAFRKDSSFNFFVFFFVFFFHLAFCIIQA 115

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1720432212 185 VGIPGWGVCGWIATISFF-GTNIGSAVVMLIPTVMFTVVAVFSFIALSMVHKFYRGS 240
Cdd:pfam04144 116 IGIPGWGSCGWITAISLFaSGNIAVGILMLISAILFTLEAVLSLWLLKKVHRYYRGT 172
 
Name Accession Description Interval E-value
SCAMP pfam04144
SCAMP family; In vertebrates, secretory carrier membrane proteins (SCAMPs) 1-3 constitute a ...
 107-240 4.31e-43

SCAMP family; In vertebrates, secretory carrier membrane proteins (SCAMPs) 1-3 constitute a family of putative membrane-trafficking proteins composed of cytoplasmic N-terminal sequences with NPF repeats, four central transmembrane regions (TMRs), and a cytoplasmic tail. SCAMPs probably function in endocytosis by recruiting EH-domain proteins to the N-terminal NPF repeats but may have additional functions mediated by their other sequences.


Pssm-ID: 461193  Cd Length: 172  Bit Score: 145.37  E-value: 4.31e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432212 107 VNSVTLAVNLVGCLAWLIGGG--GATNFGLAFLWLILFTPCSYVCWFRPIYKAFKTDSSFSFMAFFFTFMAQLVISIIQA 184
Cdd:pfam04144  36 LLTLTLFLNFIACLALFIGGGsgGGAFLGLSILYLLLFTPLSFVLWYRPLYKAFRKDSSFNFFVFFFVFFFHLAFCIIQA 115

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1720432212 185 VGIPGWGVCGWIATISFF-GTNIGSAVVMLIPTVMFTVVAVFSFIALSMVHKFYRGS 240
Cdd:pfam04144 116 IGIPGWGSCGWITAISLFaSGNIAVGILMLISAILFTLEAVLSLWLLKKVHRYYRGT 172
 
Name Accession Description Interval E-value
SCAMP pfam04144
SCAMP family; In vertebrates, secretory carrier membrane proteins (SCAMPs) 1-3 constitute a ...
 107-240 4.31e-43

SCAMP family; In vertebrates, secretory carrier membrane proteins (SCAMPs) 1-3 constitute a family of putative membrane-trafficking proteins composed of cytoplasmic N-terminal sequences with NPF repeats, four central transmembrane regions (TMRs), and a cytoplasmic tail. SCAMPs probably function in endocytosis by recruiting EH-domain proteins to the N-terminal NPF repeats but may have additional functions mediated by their other sequences.


Pssm-ID: 461193  Cd Length: 172  Bit Score: 145.37  E-value: 4.31e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720432212 107 VNSVTLAVNLVGCLAWLIGGG--GATNFGLAFLWLILFTPCSYVCWFRPIYKAFKTDSSFSFMAFFFTFMAQLVISIIQA 184
Cdd:pfam04144  36 LLTLTLFLNFIACLALFIGGGsgGGAFLGLSILYLLLFTPLSFVLWYRPLYKAFRKDSSFNFFVFFFVFFFHLAFCIIQA 115

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1720432212 185 VGIPGWGVCGWIATISFF-GTNIGSAVVMLIPTVMFTVVAVFSFIALSMVHKFYRGS 240
Cdd:pfam04144 116 IGIPGWGSCGWITAISLFaSGNIAVGILMLISAILFTLEAVLSLWLLKKVHRYYRGT 172
 
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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