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Conserved domains on  [gi|1824615236|ref|NP_001366110|]
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protein FAM3A isoform 2 [Mus musculus]

Protein Classification

FAM3C domain-containing protein( domain architecture ID 10195373)

FAM3C (FAM3 Metabolism Regulating Signaling Molecule C) domain-containing protein

Graphical summary

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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) ...
 55-249 7.92e-114

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: 323.84  E-value: 7.92e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824615236  55 RKYKCGLPQPCPEEHLSFRIVSGAANVIGPKICLEDKMLMSSVKDNVGRGLNIALVNGVSGELLEARAFDMWAGeeyclv 134
Cdd:cd13940     2 PKYKCGLSKPCPEDHFAFRIISGAANVVGPKICFEGKIIMSSVLNNVGRGLNIALVNGETGEVLKTGFFDMYSG------ 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824615236 135 gkgclveseapysvgpsppDVNDLLKFIRPLHEGTLVFVASYDDPATKMNEETRKLFSELGSRNAKDLAFRDSWVFVGAK 214
Cdd:cd13940    76 -------------------DVKPLLEFLKSIKPGSIVLVASFDDPATKLNDEARKLFAELGSSSIKSLGFRDNWVFVGGK 136

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1824615236 215 GVQNKSPFEQHMKNSKHTNKYEGWPEALEMEGCIP 249
Cdd:cd13940   137 GIKTKSPFEKHIKNDKDTNKYEGWPEMIEMEGCIP 171
 
Name Accession Description Interval E-value
ILEI_FAM3C cd13940
Interleukin-like EMT inducer; The secreted factor FAM3C or ILEI (InterLeukin-like Emt Inducer) ...
 55-249 7.92e-114

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: 323.84  E-value: 7.92e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824615236  55 RKYKCGLPQPCPEEHLSFRIVSGAANVIGPKICLEDKMLMSSVKDNVGRGLNIALVNGVSGELLEARAFDMWAGeeyclv 134
Cdd:cd13940     2 PKYKCGLSKPCPEDHFAFRIISGAANVVGPKICFEGKIIMSSVLNNVGRGLNIALVNGETGEVLKTGFFDMYSG------ 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824615236 135 gkgclveseapysvgpsppDVNDLLKFIRPLHEGTLVFVASYDDPATKMNEETRKLFSELGSRNAKDLAFRDSWVFVGAK 214
Cdd:cd13940    76 -------------------DVKPLLEFLKSIKPGSIVLVASFDDPATKLNDEARKLFAELGSSSIKSLGFRDNWVFVGGK 136

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1824615236 215 GVQNKSPFEQHMKNSKHTNKYEGWPEALEMEGCIP 249
Cdd:cd13940   137 GIKTKSPFEKHIKNDKDTNKYEGWPEMIEMEGCIP 171
ILEI pfam15711
Interleukin-like EMT inducer; ILEI is a family of proteins found in vertebrates. It is heavily ...
 103-215 4.98e-31

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: 110.43  E-value: 4.98e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824615236 103 RGLNIALVNGVSGELLEARAFDMWageeyclvgkgclveseapysvgpSPPDVNDLLKFIRPLHEGTLVFVASYDDPATK 182
Cdd:pfam15711   1 RGINVVVVDACTGKVLDSKSFDTY------------------------SYSDSSRLANFLKSIPDGSIVLIATKDEASSK 56

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1824615236 183 MNEETRKLFSELGSRNAKDLAFRDSWVFVGAKG 215
Cdd:pfam15711  57 LSDEARKALESLGSSKIDNLGFRDSWAFIGFKG 89
 
Name Accession Description Interval E-value
ILEI_FAM3C cd13940
Interleukin-like EMT inducer; The secreted factor FAM3C or ILEI (InterLeukin-like Emt Inducer) ...
 55-249 7.92e-114

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: 323.84  E-value: 7.92e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824615236  55 RKYKCGLPQPCPEEHLSFRIVSGAANVIGPKICLEDKMLMSSVKDNVGRGLNIALVNGVSGELLEARAFDMWAGeeyclv 134
Cdd:cd13940     2 PKYKCGLSKPCPEDHFAFRIISGAANVVGPKICFEGKIIMSSVLNNVGRGLNIALVNGETGEVLKTGFFDMYSG------ 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824615236 135 gkgclveseapysvgpsppDVNDLLKFIRPLHEGTLVFVASYDDPATKMNEETRKLFSELGSRNAKDLAFRDSWVFVGAK 214
Cdd:cd13940    76 -------------------DVKPLLEFLKSIKPGSIVLVASFDDPATKLNDEARKLFAELGSSSIKSLGFRDNWVFVGGK 136

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1824615236 215 GVQNKSPFEQHMKNSKHTNKYEGWPEALEMEGCIP 249
Cdd:cd13940   137 GIKTKSPFEKHIKNDKDTNKYEGWPEMIEMEGCIP 171
PANDER_FAM3B cd13939
Pancreatic derived factor; FAM3B or PANDER (PANcreatic DERived factor) has been identifed as a ...
 55-250 9.25e-53

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: 168.95  E-value: 9.25e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824615236  55 RKYKCGLPQPCPEEHLSFRIVSGAANVIGPKICLEDKMLMSSVKDNVGRGLNIALVNGVSGELLEARAFDMWAGEeyclv 134
Cdd:cd13939     1 KRQKCDHWSPCAPNQYAYRIRSGGGKDIMPEICFEDNMLITGKEGNSNRGINIAVVSYETGKVVATKYFDMYEGD----- 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824615236 135 gkgclveseapySVGPsppdvndLLKFIRPLHEGTLVFVASYDDPATKMNEETRKLFSELGSRNAKDLAFRDSWVFVGAK 214
Cdd:cd13939    76 ------------FSGP-------MIEFINKIPKKSLVFVVTHDDGSTKLKDPAKKAIEDLGSKEIRNLKFRSAWVFIAAK 136

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1824615236 215 GVQNKSPFEQ----HMKNSKhtNKYEGWPEALEMEGCIPR 250
Cdd:cd13939   137 GFQLPDNIEKekinHSDGSK--NRYSGWPAEIQIEGCIPK 174
PANDER_like cd13936
Domains similar to the Pancreatic-derived factor; FAM3B or PANDER (PANcreatic DERived factor) ...
 72-248 3.71e-33

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: 117.82  E-value: 3.71e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824615236  72 FRIVSGAANViGPKICLEDKMLMSsvKDNVGRGLNIALVNGVSGELLEARAFDMWAGEeyclvgkgclveseapysvgps 151
Cdd:cd13936     3 VKIASGGGGN-YAKICVNGGVLFD--GDKSGRGINVVVINGDTGKVIATKTFDTYGAG---------------------- 57

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824615236 152 ppDVNDLLKFIRPLHEGTLVFVASYDDPATKMNEETRKLFSELGSRNAKDLAFRDSWVFVGAKGvqNKSP-FEQHMKNSK 230
Cdd:cd13936    58 --ASNDMIDFLNSVPPGSIVLIATKDDASKSLKDEARRALESLGSSLIQNLGFRDSWAFVGQKG--IKRPsTEQHEISPK 133

                         170
                  ....*....|....*...
gi 1824615236 231 HTNkyEGWPEALEMEGCI 248
Cdd:cd13936   134 NSS--WGGPALIQTCFPL 149
ILEI pfam15711
Interleukin-like EMT inducer; ILEI is a family of proteins found in vertebrates. It is heavily ...
 103-215 4.98e-31

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: 110.43  E-value: 4.98e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824615236 103 RGLNIALVNGVSGELLEARAFDMWageeyclvgkgclveseapysvgpSPPDVNDLLKFIRPLHEGTLVFVASYDDPATK 182
Cdd:pfam15711   1 RGINVVVVDACTGKVLDSKSFDTY------------------------SYSDSSRLANFLKSIPDGSIVLIATKDEASSK 56

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1824615236 183 MNEETRKLFSELGSRNAKDLAFRDSWVFVGAKG 215
Cdd:pfam15711  57 LSDEARKALESLGSSKIDNLGFRDSWAFIGFKG 89
PANDER_GnT-1_2_like cd13937
PANDER-like domain of N-acetylglucosaminyltransferases; O-linked-mannose beta-1, ...
 70-250 4.34e-15

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: 70.41  E-value: 4.34e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824615236  70 LSFRIVSGAANVigpKICLEDKMLMSSVKDNVGRGLNIALVNGVSGELLEARAFDMWA-GEEyclvgkgclvesEApysv 148
Cdd:cd13937     1 LDIEVYSSKSKV---SVSVDGTTVLEDEEAEAGRGIHVVVLNQATGSVMAQRVFDTYSpGED------------EA---- 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824615236 149 gpsppdvndLLKFIRPLHEGTLVFVASYDDPATKMNEETRKLFSELGSRNAKDLAFRDSWVFVGAKGVQNKSpfEQHMKN 228
Cdd:cd13937    62 ---------MILFLNMVSDGRILIFTIKDEGSFHLKDEARSLLKKLGSQKVSKLGWRDMWAMVTRKGGPVYG--EKHSKS 130

                         170       180
                  ....*....|....*....|..
gi 1824615236 229 SkhtnKYEGWPEALEMEGCIPR 250
Cdd:cd13937   131 P----DLSSWGEPVLLKAEVPL 148
PANDER_like_TMEM2 cd13938
PANDER-like domain of the transmembrane protein TMEM2; TMEM2 has been characterized as a ...
 95-225 1.62e-12

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: 63.88  E-value: 1.62e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1824615236  95 SSVKDNVGRGLNIALVNGVSGELLEARAFDMWAGEEyclvgkgclvESEApysvgpsppdvndLLKFIRPLHEGTLVFVA 174
Cdd:cd13938    40 SFERSWGSRGINVRVIDEDTGEVLESDRFDTYESED----------ESKR-------------LAEFLDQIPPGRIVALA 96

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1824615236 175 SYDDPATKMNEETRKLFSELGSRNAKDLAFRDSWVFVGAKG-----VQNKSPFEQH 225
Cdd:cd13938    97 VGDEASKNLEDSARKKIRELGSKEIDHLGYRQPWAFVGVKGgpssaVEDRREYEGH 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.
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