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Conserved domains on  [gi|3114608|gb|AAC39725|]
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gremlin [Homo sapiens]

Protein Classification

DAN domain-containing protein( domain architecture ID 10503509)

DAN domain-containing protein similar to neuroblastoma suppressor of tumorigenicity 1 that may play an important role in preventing cells from entering the final stage (G1/S) of the transformation process

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DAN pfam03045
DAN domain; This domain contains 9 conserved cysteines and is extracellular. Therefore the ...
 72-179 7.04e-56

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: 171.70  E-value: 7.04e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3114608     72 EVLESSQE-ALHVTERKYLKRDWCKTQPLKQTIHEEGCNSRTIINRFCYGQCNSFYIPRHIRKEEGSFQSCSFCKPKKFT 150
Cdd:pfam03045   1 NFLNRAKPgALLPTKRRELKRDWCRTQPFTQTITEEGCLSRTVQNRFCYGQCNSFYIPNSIGRGKWSFASCSRCKPSKFT 80

                          90       100
                  ....*....|....*....|....*....
gi 3114608    151 TMMVTLNCPElQPPTKKKRVTRVKQCRCI 179
Cdd:pfam03045  81 TVTVTLNCPG-GPPTRTKRVMRVKECKCK 108
 
Name Accession Description Interval E-value
DAN pfam03045
DAN domain; This domain contains 9 conserved cysteines and is extracellular. Therefore the ...
 72-179 7.04e-56

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: 171.70  E-value: 7.04e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3114608     72 EVLESSQE-ALHVTERKYLKRDWCKTQPLKQTIHEEGCNSRTIINRFCYGQCNSFYIPRHIRKEEGSFQSCSFCKPKKFT 150
Cdd:pfam03045   1 NFLNRAKPgALLPTKRRELKRDWCRTQPFTQTITEEGCLSRTVQNRFCYGQCNSFYIPNSIGRGKWSFASCSRCKPSKFT 80

                          90       100
                  ....*....|....*....|....*....
gi 3114608    151 TMMVTLNCPElQPPTKKKRVTRVKQCRCI 179
Cdd:pfam03045  81 TVTVTLNCPG-GPPTRTKRVMRVKECKCK 108
CT smart00041
C-terminal cystine knot-like domain (CTCK); The structures of transforming growth factor-beta ...
 96-181 2.16e-18

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: 75.52  E-value: 2.16e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3114608      96 TQPLKQTIHEEGCNSRTIINRFCYGQCNSFyiprHIRKEEGSFQSCSFCKPKKFTTMMVTLNCPELQppTKKKRVTRVKQ 175
Cdd:smart00041   1 KSPVRQTITYNGCTSVTVKNAFCEGKCGSA----SSYSIQDVQHSCSCCQPHKTKTRQVRLRCPDGS--TVKKTVMHIEE 74


                   ....*.
gi 3114608     176 CRCISI 181
Cdd:smart00041  75 CGCEPN 80
 
Name Accession Description Interval E-value
DAN pfam03045
DAN domain; This domain contains 9 conserved cysteines and is extracellular. Therefore the ...
 72-179 7.04e-56

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: 171.70  E-value: 7.04e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3114608     72 EVLESSQE-ALHVTERKYLKRDWCKTQPLKQTIHEEGCNSRTIINRFCYGQCNSFYIPRHIRKEEGSFQSCSFCKPKKFT 150
Cdd:pfam03045   1 NFLNRAKPgALLPTKRRELKRDWCRTQPFTQTITEEGCLSRTVQNRFCYGQCNSFYIPNSIGRGKWSFASCSRCKPSKFT 80

                          90       100
                  ....*....|....*....|....*....
gi 3114608    151 TMMVTLNCPElQPPTKKKRVTRVKQCRCI 179
Cdd:pfam03045  81 TVTVTLNCPG-GPPTRTKRVMRVKECKCK 108
CT smart00041
C-terminal cystine knot-like domain (CTCK); The structures of transforming growth factor-beta ...
 96-181 2.16e-18

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: 75.52  E-value: 2.16e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3114608      96 TQPLKQTIHEEGCNSRTIINRFCYGQCNSFyiprHIRKEEGSFQSCSFCKPKKFTTMMVTLNCPELQppTKKKRVTRVKQ 175
Cdd:smart00041   1 KSPVRQTITYNGCTSVTVKNAFCEGKCGSA----SSYSIQDVQHSCSCCQPHKTKTRQVRLRCPDGS--TVKKTVMHIEE 74


                   ....*.
gi 3114608     176 CRCISI 181
Cdd:smart00041  75 CGCEPN 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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