NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1907130436|ref|XP_036017093|]
View 

protein APCDD1 isoform X1 [Mus musculus]

Protein Classification

APCDDC domain-containing protein( domain architecture ID 10633044)

APCDDC domain-containing protein

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
APCDDC pfam14921
Adenomatosis polyposis coli down-regulated 1; The domain is duplicated in most members of this ...
1-192 5.61e-110

Adenomatosis polyposis coli down-regulated 1; The domain is duplicated in most members of this family. APCDD is directly regulated by the beta-catenin/Tcf complex, and its elevated expression promotes proliferation of colonic epithelial cells in vitro and in vivo. APCDD1 has an N-terminal signal-peptide and a C-terminal transmembrane region. The domain is rich in cysteines, there being up to 12 such residues, a structural motif important for interaction between Wnt ligands and their receptors. APCDD1 is expressed in a broad repertoire of cell types, indicating that it may regulate a diverse range of biological processes controlled by Wnt signalling.


:

Pssm-ID: 464377  Cd Length: 235  Bit Score: 323.14  E-value: 5.61e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130436   1 MTRSYRFYNNNTFKAYQFYYGSNRCTNPTYTLIIRGKIRLRQASWIIRGGTEADYQLHGVQVICHTEAVAEQLSRLVNRT 80
Cdd:pfam14921  41 LTRSYTFFSNRTFKALQHYYADESCTIPTYTLVIRGKIRLRQASWIVRGATEADYHLHKVHIVPHSQAVAHKLAQRLNQS 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130436  81 CPGFLAPGGPWVQDVAYDLWQEES----NHECTKAVNFAMHELQLIRVEKQYPHHSlDHLVEELFLGDIHTDATQRVFYR 156
Cdd:pfam14921 121 CPGPLPPWRPWVPGTLYELLRQHNakfnSRDCLEAFGFSMHELSLLRVEKQYHLHG-QQPVEELFLGDIHTDWSQRRHYR 199
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1907130436 157 PSSYQPPLQNAKNHNHACIACRIIFRSDEHHPPILP 192
Cdd:pfam14921 200 PTSYQPPLQNAMNHTHPCPICGLISRSTEHSPPILP 235
APCDDC super family cl20807
Adenomatosis polyposis coli down-regulated 1; The domain is duplicated in most members of this ...
177-373 5.21e-19

Adenomatosis polyposis coli down-regulated 1; The domain is duplicated in most members of this family. APCDD is directly regulated by the beta-catenin/Tcf complex, and its elevated expression promotes proliferation of colonic epithelial cells in vitro and in vivo. APCDD1 has an N-terminal signal-peptide and a C-terminal transmembrane region. The domain is rich in cysteines, there being up to 12 such residues, a structural motif important for interaction between Wnt ligands and their receptors. APCDD1 is expressed in a broad repertoire of cell types, indicating that it may regulate a diverse range of biological processes controlled by Wnt signalling.


The actual alignment was detected with superfamily member pfam14921:

Pssm-ID: 464377  Cd Length: 235  Bit Score: 85.47  E-value: 5.21e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130436 177 CRIIFRSDEHHPPI---LPPKadltigLHGEWVSQRCEVRPEVLFLTRHFIFHdNNNTWEGHYYHYSDPVCKHPTFTIYA 253
Cdd:pfam14921   2 CRQALRHIQNGARItadIPPR------LEGHWVSQRCEVRPGPEFLTRSYTFF-SNRTFKALQHYYADESCTIPTYTLVI 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130436 254 RGRYSRGVLSSKVMGGTEFVFKVNHMKVTPMDAA----TASLLNVFSGNECGAEGSWQVGIQQDVTHTNG-------C-V 321
Cdd:pfam14921  75 RGKIRLRQASWIVRGATEADYHLHKVHIVPHSQAvahkLAQRLNQSCPGPLPPWRPWVPGTLYELLRQHNakfnsrdClE 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1907130436 322 ALGI---KLPHTEYEIFKMEQDTRGRYLLFNGQRPSDGSSpdRPEKRATSYQMPL 373
Cdd:pfam14921 155 AFGFsmhELSLLRVEKQYHLHGQQPVEELFLGDIHTDWSQ--RRHYRPTSYQPPL 207
 
Name Accession Description Interval E-value
APCDDC pfam14921
Adenomatosis polyposis coli down-regulated 1; The domain is duplicated in most members of this ...
1-192 5.61e-110

Adenomatosis polyposis coli down-regulated 1; The domain is duplicated in most members of this family. APCDD is directly regulated by the beta-catenin/Tcf complex, and its elevated expression promotes proliferation of colonic epithelial cells in vitro and in vivo. APCDD1 has an N-terminal signal-peptide and a C-terminal transmembrane region. The domain is rich in cysteines, there being up to 12 such residues, a structural motif important for interaction between Wnt ligands and their receptors. APCDD1 is expressed in a broad repertoire of cell types, indicating that it may regulate a diverse range of biological processes controlled by Wnt signalling.


Pssm-ID: 464377  Cd Length: 235  Bit Score: 323.14  E-value: 5.61e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130436   1 MTRSYRFYNNNTFKAYQFYYGSNRCTNPTYTLIIRGKIRLRQASWIIRGGTEADYQLHGVQVICHTEAVAEQLSRLVNRT 80
Cdd:pfam14921  41 LTRSYTFFSNRTFKALQHYYADESCTIPTYTLVIRGKIRLRQASWIVRGATEADYHLHKVHIVPHSQAVAHKLAQRLNQS 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130436  81 CPGFLAPGGPWVQDVAYDLWQEES----NHECTKAVNFAMHELQLIRVEKQYPHHSlDHLVEELFLGDIHTDATQRVFYR 156
Cdd:pfam14921 121 CPGPLPPWRPWVPGTLYELLRQHNakfnSRDCLEAFGFSMHELSLLRVEKQYHLHG-QQPVEELFLGDIHTDWSQRRHYR 199
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1907130436 157 PSSYQPPLQNAKNHNHACIACRIIFRSDEHHPPILP 192
Cdd:pfam14921 200 PTSYQPPLQNAMNHTHPCPICGLISRSTEHSPPILP 235
APCDDC pfam14921
Adenomatosis polyposis coli down-regulated 1; The domain is duplicated in most members of this ...
177-373 5.21e-19

Adenomatosis polyposis coli down-regulated 1; The domain is duplicated in most members of this family. APCDD is directly regulated by the beta-catenin/Tcf complex, and its elevated expression promotes proliferation of colonic epithelial cells in vitro and in vivo. APCDD1 has an N-terminal signal-peptide and a C-terminal transmembrane region. The domain is rich in cysteines, there being up to 12 such residues, a structural motif important for interaction between Wnt ligands and their receptors. APCDD1 is expressed in a broad repertoire of cell types, indicating that it may regulate a diverse range of biological processes controlled by Wnt signalling.


Pssm-ID: 464377  Cd Length: 235  Bit Score: 85.47  E-value: 5.21e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130436 177 CRIIFRSDEHHPPI---LPPKadltigLHGEWVSQRCEVRPEVLFLTRHFIFHdNNNTWEGHYYHYSDPVCKHPTFTIYA 253
Cdd:pfam14921   2 CRQALRHIQNGARItadIPPR------LEGHWVSQRCEVRPGPEFLTRSYTFF-SNRTFKALQHYYADESCTIPTYTLVI 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130436 254 RGRYSRGVLSSKVMGGTEFVFKVNHMKVTPMDAA----TASLLNVFSGNECGAEGSWQVGIQQDVTHTNG-------C-V 321
Cdd:pfam14921  75 RGKIRLRQASWIVRGATEADYHLHKVHIVPHSQAvahkLAQRLNQSCPGPLPPWRPWVPGTLYELLRQHNakfnsrdClE 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1907130436 322 ALGI---KLPHTEYEIFKMEQDTRGRYLLFNGQRPSDGSSpdRPEKRATSYQMPL 373
Cdd:pfam14921 155 AFGFsmhELSLLRVEKQYHLHGQQPVEELFLGDIHTDWSQ--RRHYRPTSYQPPL 207
 
Name Accession Description Interval E-value
APCDDC pfam14921
Adenomatosis polyposis coli down-regulated 1; The domain is duplicated in most members of this ...
1-192 5.61e-110

Adenomatosis polyposis coli down-regulated 1; The domain is duplicated in most members of this family. APCDD is directly regulated by the beta-catenin/Tcf complex, and its elevated expression promotes proliferation of colonic epithelial cells in vitro and in vivo. APCDD1 has an N-terminal signal-peptide and a C-terminal transmembrane region. The domain is rich in cysteines, there being up to 12 such residues, a structural motif important for interaction between Wnt ligands and their receptors. APCDD1 is expressed in a broad repertoire of cell types, indicating that it may regulate a diverse range of biological processes controlled by Wnt signalling.


Pssm-ID: 464377  Cd Length: 235  Bit Score: 323.14  E-value: 5.61e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130436   1 MTRSYRFYNNNTFKAYQFYYGSNRCTNPTYTLIIRGKIRLRQASWIIRGGTEADYQLHGVQVICHTEAVAEQLSRLVNRT 80
Cdd:pfam14921  41 LTRSYTFFSNRTFKALQHYYADESCTIPTYTLVIRGKIRLRQASWIVRGATEADYHLHKVHIVPHSQAVAHKLAQRLNQS 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130436  81 CPGFLAPGGPWVQDVAYDLWQEES----NHECTKAVNFAMHELQLIRVEKQYPHHSlDHLVEELFLGDIHTDATQRVFYR 156
Cdd:pfam14921 121 CPGPLPPWRPWVPGTLYELLRQHNakfnSRDCLEAFGFSMHELSLLRVEKQYHLHG-QQPVEELFLGDIHTDWSQRRHYR 199
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1907130436 157 PSSYQPPLQNAKNHNHACIACRIIFRSDEHHPPILP 192
Cdd:pfam14921 200 PTSYQPPLQNAMNHTHPCPICGLISRSTEHSPPILP 235
APCDDC pfam14921
Adenomatosis polyposis coli down-regulated 1; The domain is duplicated in most members of this ...
177-373 5.21e-19

Adenomatosis polyposis coli down-regulated 1; The domain is duplicated in most members of this family. APCDD is directly regulated by the beta-catenin/Tcf complex, and its elevated expression promotes proliferation of colonic epithelial cells in vitro and in vivo. APCDD1 has an N-terminal signal-peptide and a C-terminal transmembrane region. The domain is rich in cysteines, there being up to 12 such residues, a structural motif important for interaction between Wnt ligands and their receptors. APCDD1 is expressed in a broad repertoire of cell types, indicating that it may regulate a diverse range of biological processes controlled by Wnt signalling.


Pssm-ID: 464377  Cd Length: 235  Bit Score: 85.47  E-value: 5.21e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130436 177 CRIIFRSDEHHPPI---LPPKadltigLHGEWVSQRCEVRPEVLFLTRHFIFHdNNNTWEGHYYHYSDPVCKHPTFTIYA 253
Cdd:pfam14921   2 CRQALRHIQNGARItadIPPR------LEGHWVSQRCEVRPGPEFLTRSYTFF-SNRTFKALQHYYADESCTIPTYTLVI 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907130436 254 RGRYSRGVLSSKVMGGTEFVFKVNHMKVTPMDAA----TASLLNVFSGNECGAEGSWQVGIQQDVTHTNG-------C-V 321
Cdd:pfam14921  75 RGKIRLRQASWIVRGATEADYHLHKVHIVPHSQAvahkLAQRLNQSCPGPLPPWRPWVPGTLYELLRQHNakfnsrdClE 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1907130436 322 ALGI---KLPHTEYEIFKMEQDTRGRYLLFNGQRPSDGSSpdRPEKRATSYQMPL 373
Cdd:pfam14921 155 AFGFsmhELSLLRVEKQYHLHGQQPVEELFLGDIHTDWSQ--RRHYRPTSYQPPL 207
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH