NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|967507785|ref|XP_014983978|]
View 

protein FAM3A isoform X2 [Macaca mulatta]

Protein Classification

FAM3C domain-containing protein( domain architecture ID 10195373)

FAM3C (FAM3 Metabolism Regulating Signaling Molecule C) 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
ILEI_FAM3C cd13940
Interleukin-like EMT inducer; The secreted factor FAM3C or ILEI (InterLeukin-like Emt Inducer) ...
 55-207 5.86e-106

Interleukin-like EMT inducer; The secreted factor FAM3C or ILEI (InterLeukin-like Emt Inducer) has been identifed as a protein involved in the epithelial-mesenchymal transition (EMT) and in processes associated with metastasis formation and the progression of cancer. The protein had initially been predicted to be a member of the four-helical cytokine family, hence the FAM3C designation. ILEI has been found to be widely expressed, and to be involved in retinal development.


:

Pssm-ID: 260114  Cd Length: 171  Bit Score: 301.88  E-value: 5.86e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967507785  55 RRYKCGLPQPCPEEHLAFRVVSGAANVIGPKICLEDKMLMSSVKDNVGRGLNIALVN-----------------DVNDLL 117
Cdd:cd13940    2 PKYKCGLSKPCPEDHFAFRIISGAANVVGPKICFEGKIIMSSVLNNVGRGLNIALVNgetgevlktgffdmysgDVKPLL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967507785 118 KFIRPLHEGTLVFVASYDDPATKMNEETRKLFSELGSRNAKELAFRDSWVFVGAKGVQNKSPFEQHVKNSKHTNKYEGWP 197
Cdd:cd13940   82 EFLKSIKPGSIVLVASFDDPATKLNDEARKLFAELGSSSIKSLGFRDNWVFVGGKGIKTKSPFEKHIKNDKDTNKYEGWP 161

                        170
                 ....*....|
gi 967507785 198 EALEMEGCIP 207
Cdd:cd13940  162 EMIEMEGCIP 171
 
Name Accession Description Interval E-value
ILEI_FAM3C cd13940
Interleukin-like EMT inducer; The secreted factor FAM3C or ILEI (InterLeukin-like Emt Inducer) ...
 55-207 5.86e-106

Interleukin-like EMT inducer; The secreted factor FAM3C or ILEI (InterLeukin-like Emt Inducer) has been identifed as a protein involved in the epithelial-mesenchymal transition (EMT) and in processes associated with metastasis formation and the progression of cancer. The protein had initially been predicted to be a member of the four-helical cytokine family, hence the FAM3C designation. ILEI has been found to be widely expressed, and to be involved in retinal development.


Pssm-ID: 260114  Cd Length: 171  Bit Score: 301.88  E-value: 5.86e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967507785  55 RRYKCGLPQPCPEEHLAFRVVSGAANVIGPKICLEDKMLMSSVKDNVGRGLNIALVN-----------------DVNDLL 117
Cdd:cd13940    2 PKYKCGLSKPCPEDHFAFRIISGAANVVGPKICFEGKIIMSSVLNNVGRGLNIALVNgetgevlktgffdmysgDVKPLL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967507785 118 KFIRPLHEGTLVFVASYDDPATKMNEETRKLFSELGSRNAKELAFRDSWVFVGAKGVQNKSPFEQHVKNSKHTNKYEGWP 197
Cdd:cd13940   82 EFLKSIKPGSIVLVASFDDPATKLNDEARKLFAELGSSSIKSLGFRDNWVFVGGKGIKTKSPFEKHIKNDKDTNKYEGWP 161

                        170
                 ....*....|
gi 967507785 198 EALEMEGCIP 207
Cdd:cd13940  162 EMIEMEGCIP 171
ILEI pfam15711
Interleukin-like EMT inducer; ILEI is a family of proteins found in vertebrates. It is heavily ...
 103-173 6.07e-25

Interleukin-like EMT inducer; ILEI is a family of proteins found in vertebrates. It is heavily involved in the process of the transition from epithelial to mesenchymal tissue - EMT - during all of embryonic development, cancer progression, metastasis, and chronic inflammation/fibrosis. ILEI is upregulated exclusively at the level of translation, and abnormal ILEI expression, ie cytoplasmic over-expression instead of vesicular localization, is associated with EMT in human cancerous tissue. In order to induce and maintain the EMT of hepatocytes in a TGF-beta-independent fashion ILEI needs the cooperation of oncogenic Ras.


Pssm-ID: 464817  Cd Length: 89  Bit Score: 93.48  E-value: 6.07e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967507785  103 RGLNIALVN------------------DVNDLLKFIRPLHEGTLVFVASYDDPATKMNEETRKLFSELGSRNAKELAFRD 164
Cdd:pfam15711   1 RGINVVVVDactgkvldsksfdtysysDSSRLANFLKSIPDGSIVLIATKDEASSKLSDEARKALESLGSSKIDNLGFRD 80


                  ....*....
gi 967507785  165 SWVFVGAKG 173
Cdd:pfam15711  81 SWAFIGFKG 89
 
Name Accession Description Interval E-value
ILEI_FAM3C cd13940
Interleukin-like EMT inducer; The secreted factor FAM3C or ILEI (InterLeukin-like Emt Inducer) ...
 55-207 5.86e-106

Interleukin-like EMT inducer; The secreted factor FAM3C or ILEI (InterLeukin-like Emt Inducer) has been identifed as a protein involved in the epithelial-mesenchymal transition (EMT) and in processes associated with metastasis formation and the progression of cancer. The protein had initially been predicted to be a member of the four-helical cytokine family, hence the FAM3C designation. ILEI has been found to be widely expressed, and to be involved in retinal development.


Pssm-ID: 260114  Cd Length: 171  Bit Score: 301.88  E-value: 5.86e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967507785  55 RRYKCGLPQPCPEEHLAFRVVSGAANVIGPKICLEDKMLMSSVKDNVGRGLNIALVN-----------------DVNDLL 117
Cdd:cd13940    2 PKYKCGLSKPCPEDHFAFRIISGAANVVGPKICFEGKIIMSSVLNNVGRGLNIALVNgetgevlktgffdmysgDVKPLL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967507785 118 KFIRPLHEGTLVFVASYDDPATKMNEETRKLFSELGSRNAKELAFRDSWVFVGAKGVQNKSPFEQHVKNSKHTNKYEGWP 197
Cdd:cd13940   82 EFLKSIKPGSIVLVASFDDPATKLNDEARKLFAELGSSSIKSLGFRDNWVFVGGKGIKTKSPFEKHIKNDKDTNKYEGWP 161

                        170
                 ....*....|
gi 967507785 198 EALEMEGCIP 207
Cdd:cd13940  162 EMIEMEGCIP 171
PANDER_FAM3B cd13939
Pancreatic derived factor; FAM3B or PANDER (PANcreatic DERived factor) has been identifed as a ...
 55-208 8.94e-47

Pancreatic derived factor; FAM3B or PANDER (PANcreatic DERived factor) has been identifed as a regulator of glucose homeostasis and beta cell function. The protein is expressed in the endocrine pancreas and co-secreted with insulin in response to glucose, particularly under conditions of insulin resistance. The protein had initially been predicted to be a member of the four-helical cytokine family, hence the FAM3B designation. PANDER induces apoptosis of insulin-secreting beta-cells when over-expressed in vitro. It has been associated with the progression of type 2 diabetes by downregulating beta cell function as well as insulin sensitivity in the liver.


Pssm-ID: 260113  Cd Length: 175  Bit Score: 152.00  E-value: 8.94e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967507785  55 RRYKCGLPQPCPEEHLAFRVVSGAANVIGPKICLEDKMLMSSVKDNVGRGLNIALVN------------DVND------L 116
Cdd:cd13939    1 KRQKCDHWSPCAPNQYAYRIRSGGGKDIMPEICFEDNMLITGKEGNSNRGINIAVVSyetgkvvatkyfDMYEgdfsgpM 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967507785 117 LKFIRPLHEGTLVFVASYDDPATKMNEETRKLFSELGSRNAKELAFRDSWVFVGAKGVQNKSPFEQ----HVKNSKhtNK 192
Cdd:cd13939   81 IEFINKIPKKSLVFVVTHDDGSTKLKDPAKKAIEDLGSKEIRNLKFRSAWVFIAAKGFQLPDNIEKekinHSDGSK--NR 158

                        170
                 ....*....|....*.
gi 967507785 193 YEGWPEALEMEGCIPR 208
Cdd:cd13939  159 YSGWPAEIQIEGCIPK 174
PANDER_like cd13936
Domains similar to the Pancreatic-derived factor; FAM3B or PANDER (PANcreatic DERived factor) ...
 70-206 5.05e-30

Domains similar to the Pancreatic-derived factor; FAM3B or PANDER (PANcreatic DERived factor) has been identifed as a regulator of glucose homeostasis and beta cell function. The protein is expressed in the endocrine pancreas and co-secreted with insulin in response to glucose, particularly under conditions of insulin resistance. The protein had initially been predicted to be a member of the four-helical cytokine family, hence the FAM3B designation. This wider family contains FAM3B and FAM4C, N-terminal domains of N-acetylglucosaminyltransferases, and domains in poorly characterized proteins that have been associated with deafness and the progression of cancer.


Pssm-ID: 260110  Cd Length: 149  Bit Score: 108.19  E-value: 5.05e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967507785  70 LAFRVVSGAANViGPKICLEDKMLMSsvKDNVGRGLNIALVN------------------DVNDLLKFIRPLHEGTLVFV 131
Cdd:cd13936    1 LEVKIASGGGGN-YAKICVNGGVLFD--GDKSGRGINVVVINgdtgkviatktfdtygagASNDMIDFLNSVPPGSIVLI 77

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 967507785 132 ASYDDPATKMNEETRKLFSELGSRNAKELAFRDSWVFVGAKGvqNKSP-FEQHVKNSKHTNkyEGWPEALEMEGCI 206
Cdd:cd13936   78 ATKDDASKSLKDEARRALESLGSSLIQNLGFRDSWAFVGQKG--IKRPsTEQHEISPKNSS--WGGPALIQTCFPL 149
ILEI pfam15711
Interleukin-like EMT inducer; ILEI is a family of proteins found in vertebrates. It is heavily ...
 103-173 6.07e-25

Interleukin-like EMT inducer; ILEI is a family of proteins found in vertebrates. It is heavily involved in the process of the transition from epithelial to mesenchymal tissue - EMT - during all of embryonic development, cancer progression, metastasis, and chronic inflammation/fibrosis. ILEI is upregulated exclusively at the level of translation, and abnormal ILEI expression, ie cytoplasmic over-expression instead of vesicular localization, is associated with EMT in human cancerous tissue. In order to induce and maintain the EMT of hepatocytes in a TGF-beta-independent fashion ILEI needs the cooperation of oncogenic Ras.


Pssm-ID: 464817  Cd Length: 89  Bit Score: 93.48  E-value: 6.07e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967507785  103 RGLNIALVN------------------DVNDLLKFIRPLHEGTLVFVASYDDPATKMNEETRKLFSELGSRNAKELAFRD 164
Cdd:pfam15711   1 RGINVVVVDactgkvldsksfdtysysDSSRLANFLKSIPDGSIVLIATKDEASSKLSDEARKALESLGSSKIDNLGFRD 80


                  ....*....
gi 967507785  165 SWVFVGAKG 173
Cdd:pfam15711  81 SWAFIGFKG 89
PANDER_GnT-1_2_like cd13937
PANDER-like domain of N-acetylglucosaminyltransferases; O-linked-mannose beta-1, ...
 70-208 3.46e-11

PANDER-like domain of N-acetylglucosaminyltransferases; O-linked-mannose beta-1,2-N-acetylglucosaminyltransferase 1 participates in O-mannosyl glycosylation and may be responsible for creating GlcNAc(beta1-2)Man(alpha1-)O-Ser/Thr moieties on alpha dystroglycan and other O-mannosylated proteins. The domain characterized by this model lies N-terminal to the catalytic domain. Its function has not been determined.


Pssm-ID: 260111  Cd Length: 148  Bit Score: 58.85  E-value: 3.46e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 967507785  70 LAFRVVSGAANVigpKICLEDKMLMSSVKDNVGRGLNIALVNDVN---------D---------LLKFIRPLHEGTLVFV 131
Cdd:cd13937    1 LDIEVYSSKSKV---SVSVDGTTVLEDEEAEAGRGIHVVVLNQATgsvmaqrvfDtyspgedeaMILFLNMVSDGRILIF 77

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 967507785 132 ASYDDPATKMNEETRKLFSELGSRNAKELAFRDSWVFVGAKGVQNKSpfEQHVKNSkhtnKYEGWPEALEMEGCIPR 208
Cdd:cd13937   78 TIKDEGSFHLKDEARSLLKKLGSQKVSKLGWRDMWAMVTRKGGPVYG--EKHSKSP----DLSSWGEPVLLKAEVPL 148
PANDER_like_TMEM2 cd13938
PANDER-like domain of the transmembrane protein TMEM2; TMEM2 has been characterized as a ...
 116-183 4.90e-09

PANDER-like domain of the transmembrane protein TMEM2; TMEM2 has been characterized as a transmembrane protein that maps to the DFNB7-DFNB11 deafness locus on human chromosome 9. It contains a domain similar to the Pancreatic-derived factor PANDER, C-terminal to a glycine rich G8-domain. The function of the PANDER-like domain in TMEM2 has not been characterized.


Pssm-ID: 260112  Cd Length: 168  Bit Score: 53.48  E-value: 4.90e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 967507785 116 LLKFIRPLHEGTLVFVASYDDPATKMNEETRKLFSELGSRNAKELAFRDSWVFVGAKG-----VQNKSPFEQH 183
Cdd:cd13938   80 LAEFLDQIPPGRIVALAVGDEASKNLEDSARKKIRELGSKEIDHLGYRQPWAFVGVKGgpssaVEDRREYEGH 152
 
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