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Conserved domains on  [gi|110625864|ref|NP_573500|]
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protein APCDD1 precursor [Mus musculus]

Protein Classification

APCDDC domain-containing protein( domain architecture ID 10633044)

APCDDC domain-containing protein

Graphical summary

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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 ...
 51-282 7.82e-140

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: 402.49  E-value: 7.82e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625864   51 QCHHMLKHLHNGARITVQMPPTIEGHWVSTGCEVRSGPEFMTRSYRFYNNNTFKAYQFYYGSNRCTNPTYTLIIRGKIRL 130
Cdd:pfam14921   1 QCRQALRHIQNGARITADIPPRLEGHWVSQRCEVRPGPEFLTRSYTFFSNRTFKALQHYYADESCTIPTYTLVIRGKIRL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625864  131 RQASWIIRGGTEADYQLHGVQVICHTEAVAEQLSRLVNRTCPGFLAPGGPWVQDVAYDLWQEES----NHECTKAVNFAM 206
Cdd:pfam14921  81 RQASWIVRGATEADYHLHKVHIVPHSQAVAHKLAQRLNQSCPGPLPPWRPWVPGTLYELLRQHNakfnSRDCLEAFGFSM 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 110625864  207 HELQLIRVEKQYPHHSlDHLVEELFLGDIHTDATQRVFYRPSSYQPPLQNAKNHNHACIACRIIFRSDEHHPPILP 282
Cdd:pfam14921 161 HELSLLRVEKQYHLHG-QQPVEELFLGDIHTDWSQRRHYRPTSYQPPLQNAMNHTHPCPICGLISRSTEHSPPILP 235
APCDDC super family cl20807
Adenomatosis polyposis coli down-regulated 1; The domain is duplicated in most members of this ...
 267-463 1.73e-18

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: 84.70  E-value: 1.73e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625864  267 CRIIFRSDEHHPPI---LPPKadltigLHGEWVSQRCEVRPEVLFLTRHFIFHdNNNTWEGHYYHYSDPVCKHPTFTIYA 343
Cdd:pfam14921   2 CRQALRHIQNGARItadIPPR------LEGHWVSQRCEVRPGPEFLTRSYTFF-SNRTFKALQHYYADESCTIPTYTLVI 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625864  344 RGRYSRGVLSSKVMGGTEFVFKVNHMKVTPMDAA----TASLLNVFSGNECGAEGSWQVGIQQDVTHTNG-------C-V 411
Cdd:pfam14921  75 RGKIRLRQASWIVRGATEADYHLHKVHIVPHSQAvahkLAQRLNQSCPGPLPPWRPWVPGTLYELLRQHNakfnsrdClE 154

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 110625864  412 ALGI---KLPHTEYEIFKMEQDTRGRYLLFNGQRPSDGSSpdRPEKRATSYQMPL 463
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 ...
 51-282 7.82e-140

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: 402.49  E-value: 7.82e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625864   51 QCHHMLKHLHNGARITVQMPPTIEGHWVSTGCEVRSGPEFMTRSYRFYNNNTFKAYQFYYGSNRCTNPTYTLIIRGKIRL 130
Cdd:pfam14921   1 QCRQALRHIQNGARITADIPPRLEGHWVSQRCEVRPGPEFLTRSYTFFSNRTFKALQHYYADESCTIPTYTLVIRGKIRL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625864  131 RQASWIIRGGTEADYQLHGVQVICHTEAVAEQLSRLVNRTCPGFLAPGGPWVQDVAYDLWQEES----NHECTKAVNFAM 206
Cdd:pfam14921  81 RQASWIVRGATEADYHLHKVHIVPHSQAVAHKLAQRLNQSCPGPLPPWRPWVPGTLYELLRQHNakfnSRDCLEAFGFSM 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 110625864  207 HELQLIRVEKQYPHHSlDHLVEELFLGDIHTDATQRVFYRPSSYQPPLQNAKNHNHACIACRIIFRSDEHHPPILP 282
Cdd:pfam14921 161 HELSLLRVEKQYHLHG-QQPVEELFLGDIHTDWSQRRHYRPTSYQPPLQNAMNHTHPCPICGLISRSTEHSPPILP 235
APCDDC pfam14921
Adenomatosis polyposis coli down-regulated 1; The domain is duplicated in most members of this ...
 267-463 1.73e-18

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: 84.70  E-value: 1.73e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625864  267 CRIIFRSDEHHPPI---LPPKadltigLHGEWVSQRCEVRPEVLFLTRHFIFHdNNNTWEGHYYHYSDPVCKHPTFTIYA 343
Cdd:pfam14921   2 CRQALRHIQNGARItadIPPR------LEGHWVSQRCEVRPGPEFLTRSYTFF-SNRTFKALQHYYADESCTIPTYTLVI 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625864  344 RGRYSRGVLSSKVMGGTEFVFKVNHMKVTPMDAA----TASLLNVFSGNECGAEGSWQVGIQQDVTHTNG-------C-V 411
Cdd:pfam14921  75 RGKIRLRQASWIVRGATEADYHLHKVHIVPHSQAvahkLAQRLNQSCPGPLPPWRPWVPGTLYELLRQHNakfnsrdClE 154

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 110625864  412 ALGI---KLPHTEYEIFKMEQDTRGRYLLFNGQRPSDGSSpdRPEKRATSYQMPL 463
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 ...
 51-282 7.82e-140

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: 402.49  E-value: 7.82e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625864   51 QCHHMLKHLHNGARITVQMPPTIEGHWVSTGCEVRSGPEFMTRSYRFYNNNTFKAYQFYYGSNRCTNPTYTLIIRGKIRL 130
Cdd:pfam14921   1 QCRQALRHIQNGARITADIPPRLEGHWVSQRCEVRPGPEFLTRSYTFFSNRTFKALQHYYADESCTIPTYTLVIRGKIRL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625864  131 RQASWIIRGGTEADYQLHGVQVICHTEAVAEQLSRLVNRTCPGFLAPGGPWVQDVAYDLWQEES----NHECTKAVNFAM 206
Cdd:pfam14921  81 RQASWIVRGATEADYHLHKVHIVPHSQAVAHKLAQRLNQSCPGPLPPWRPWVPGTLYELLRQHNakfnSRDCLEAFGFSM 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 110625864  207 HELQLIRVEKQYPHHSlDHLVEELFLGDIHTDATQRVFYRPSSYQPPLQNAKNHNHACIACRIIFRSDEHHPPILP 282
Cdd:pfam14921 161 HELSLLRVEKQYHLHG-QQPVEELFLGDIHTDWSQRRHYRPTSYQPPLQNAMNHTHPCPICGLISRSTEHSPPILP 235
APCDDC pfam14921
Adenomatosis polyposis coli down-regulated 1; The domain is duplicated in most members of this ...
 267-463 1.73e-18

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: 84.70  E-value: 1.73e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625864  267 CRIIFRSDEHHPPI---LPPKadltigLHGEWVSQRCEVRPEVLFLTRHFIFHdNNNTWEGHYYHYSDPVCKHPTFTIYA 343
Cdd:pfam14921   2 CRQALRHIQNGARItadIPPR------LEGHWVSQRCEVRPGPEFLTRSYTFF-SNRTFKALQHYYADESCTIPTYTLVI 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625864  344 RGRYSRGVLSSKVMGGTEFVFKVNHMKVTPMDAA----TASLLNVFSGNECGAEGSWQVGIQQDVTHTNG-------C-V 411
Cdd:pfam14921  75 RGKIRLRQASWIVRGATEADYHLHKVHIVPHSQAvahkLAQRLNQSCPGPLPPWRPWVPGTLYELLRQHNakfnsrdClE 154

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 110625864  412 ALGI---KLPHTEYEIFKMEQDTRGRYLLFNGQRPSDGSSpdRPEKRATSYQMPL 463
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.
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