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Conserved domains on  [gi|74729571|sp|Q8N907|]
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RecName: Full=DAN domain family member 5; AltName: Full=Cerberus-like protein 2; Short=Cerl-2; AltName: Full=Cysteine knot superfamily 1, BMP antagonist 3; AltName: Full=Gremlin-3; Flags: Precursor

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DAN super family cl47789
DAN domain; This domain contains 9 conserved cysteines and is extracellular. Therefore the ...
 77-185 7.42e-18

DAN domain; This domain contains 9 conserved cysteines and is extracellular. Therefore the cysteines may form disulphide bridges. This family of proteins has been termed the DAN family after the first member to be reported. This family includes DAN, Cerberus and Gremlin. The gremlin protein is an antagonist of bone morphogenetic protein signaling. It is postulated that all members of this family antagonize different TGF beta pfam00019 ligands. Recent work shows that the DAN protein is not an efficient antagonist of BMP-2/4 class signals, we found that DAN was able to interact with GDF-5 in a frog embryo assay, suggesting that DAN may regulate signaling by the GDF-5/6/7 class of BMPs in vivo.


The actual alignment was detected with superfamily member pfam03045:

Pssm-ID: 460786  Cd Length: 108  Bit Score: 75.01  E-value: 7.42e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74729571    77 LQRGQdevAAVTLPLNPQEVIQGMCKAVPFVQVFSRPGCSAIRLRNHLCFGHCSSLYIPGS---DPTPLVLCNSCMPARK 153
Cdd:pfam03045   3 LNRAK---PGALLPTKRRELKRDWCRTQPFTQTITEEGCLSRTVQNRFCYGQCNSFYIPNSigrGKWSFASCSRCKPSKF 79

                          90       100       110
                  ....*....|....*....|....*....|..
gi 74729571   154 RWAPVVLWCLTGSSASRRRVkistMLIEGCHC 185
Cdd:pfam03045  80 TTVTVTLNCPGGPPTRTKRV----MRVKECKC 107
 
Name Accession Description Interval E-value
DAN pfam03045
DAN domain; This domain contains 9 conserved cysteines and is extracellular. Therefore the ...
 77-185 7.42e-18

DAN domain; This domain contains 9 conserved cysteines and is extracellular. Therefore the cysteines may form disulphide bridges. This family of proteins has been termed the DAN family after the first member to be reported. This family includes DAN, Cerberus and Gremlin. The gremlin protein is an antagonist of bone morphogenetic protein signaling. It is postulated that all members of this family antagonize different TGF beta pfam00019 ligands. Recent work shows that the DAN protein is not an efficient antagonist of BMP-2/4 class signals, we found that DAN was able to interact with GDF-5 in a frog embryo assay, suggesting that DAN may regulate signaling by the GDF-5/6/7 class of BMPs in vivo.


Pssm-ID: 460786  Cd Length: 108  Bit Score: 75.01  E-value: 7.42e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74729571    77 LQRGQdevAAVTLPLNPQEVIQGMCKAVPFVQVFSRPGCSAIRLRNHLCFGHCSSLYIPGS---DPTPLVLCNSCMPARK 153
Cdd:pfam03045   3 LNRAK---PGALLPTKRRELKRDWCRTQPFTQTITEEGCLSRTVQNRFCYGQCNSFYIPNSigrGKWSFASCSRCKPSKF 79

                          90       100       110
                  ....*....|....*....|....*....|..
gi 74729571   154 RWAPVVLWCLTGSSASRRRVkistMLIEGCHC 185
Cdd:pfam03045  80 TTVTVTLNCPGGPPTRTKRV----MRVKECKC 107
CT smart00041
C-terminal cystine knot-like domain (CTCK); The structures of transforming growth factor-beta ...
 104-188 6.50e-06

C-terminal cystine knot-like domain (CTCK); The structures of transforming growth factor-beta (TGFbeta), nerve growth factor (NGF), platelet-derived growth factor (PDGF) and gonadotropin all form 2 highly twisted antiparallel pairs of beta-strands and contain three disulphide bonds. The domain is non-globular and little is conserved among these presumed homologues except for their cysteine residues. CT domains are predicted to form homodimers.


Pssm-ID: 214482  Cd Length: 82  Bit Score: 42.78  E-value: 6.50e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74729571    104 VPFVQVFSRPGCSAIRLRNHLCFGHCSSLYIPgSDPTPLVLCNSCMPARKRWAPVVLWCLTGSSasrrrVKISTMLIEGC 183
Cdd:smart00041   2 SPVRQTITYNGCTSVTVKNAFCEGKCGSASSY-SIQDVQHSCSCCQPHKTKTRQVRLRCPDGST-----VKKTVMHIEEC 75


                   ....*
gi 74729571    184 HCSPK 188
Cdd:smart00041  76 GCEPN 80
 
Name Accession Description Interval E-value
DAN pfam03045
DAN domain; This domain contains 9 conserved cysteines and is extracellular. Therefore the ...
 77-185 7.42e-18

DAN domain; This domain contains 9 conserved cysteines and is extracellular. Therefore the cysteines may form disulphide bridges. This family of proteins has been termed the DAN family after the first member to be reported. This family includes DAN, Cerberus and Gremlin. The gremlin protein is an antagonist of bone morphogenetic protein signaling. It is postulated that all members of this family antagonize different TGF beta pfam00019 ligands. Recent work shows that the DAN protein is not an efficient antagonist of BMP-2/4 class signals, we found that DAN was able to interact with GDF-5 in a frog embryo assay, suggesting that DAN may regulate signaling by the GDF-5/6/7 class of BMPs in vivo.


Pssm-ID: 460786  Cd Length: 108  Bit Score: 75.01  E-value: 7.42e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74729571    77 LQRGQdevAAVTLPLNPQEVIQGMCKAVPFVQVFSRPGCSAIRLRNHLCFGHCSSLYIPGS---DPTPLVLCNSCMPARK 153
Cdd:pfam03045   3 LNRAK---PGALLPTKRRELKRDWCRTQPFTQTITEEGCLSRTVQNRFCYGQCNSFYIPNSigrGKWSFASCSRCKPSKF 79

                          90       100       110
                  ....*....|....*....|....*....|..
gi 74729571   154 RWAPVVLWCLTGSSASRRRVkistMLIEGCHC 185
Cdd:pfam03045  80 TTVTVTLNCPGGPPTRTKRV----MRVKECKC 107
CT smart00041
C-terminal cystine knot-like domain (CTCK); The structures of transforming growth factor-beta ...
 104-188 6.50e-06

C-terminal cystine knot-like domain (CTCK); The structures of transforming growth factor-beta (TGFbeta), nerve growth factor (NGF), platelet-derived growth factor (PDGF) and gonadotropin all form 2 highly twisted antiparallel pairs of beta-strands and contain three disulphide bonds. The domain is non-globular and little is conserved among these presumed homologues except for their cysteine residues. CT domains are predicted to form homodimers.


Pssm-ID: 214482  Cd Length: 82  Bit Score: 42.78  E-value: 6.50e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74729571    104 VPFVQVFSRPGCSAIRLRNHLCFGHCSSLYIPgSDPTPLVLCNSCMPARKRWAPVVLWCLTGSSasrrrVKISTMLIEGC 183
Cdd:smart00041   2 SPVRQTITYNGCTSVTVKNAFCEGKCGSASSY-SIQDVQHSCSCCQPHKTKTRQVRLRCPDGST-----VKKTVMHIEEC 75


                   ....*
gi 74729571    184 HCSPK 188
Cdd:smart00041  76 GCEPN 80
 
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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