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Conserved domains on  [gi|1890258305|ref|NP_001277059|]
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protein O-linked-mannose beta-1,2-N-acetylglucosaminyltransferase 1 isoform 4 [Homo sapiens]

Protein Classification

PANDER_like and GT13_GLCNAC-TI domain-containing protein( domain architecture ID 10363476)

PANDER_like and GT13_GLCNAC-TI domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GT13_GLCNAC-TI cd02514
GT13_GLCNAC-TI is involved in an essential step in the synthesis of complex or hybrid-type ...
 158-485 0e+00

GT13_GLCNAC-TI is involved in an essential step in the synthesis of complex or hybrid-type N-linked oligosaccharides; Alpha-1,3-mannosyl-glycoprotein beta-1,2-N-acetylglucosaminyltransferase (GLCNAC-T I , GNT-I) transfers N-acetyl-D-glucosamine from UDP to high-mannose glycoprotein N-oligosaccharide, an essential step in the synthesis of complex or hybrid-type N-linked oligosaccharides. The enzyme is an integral membrane protein localized to the Golgi apparatus. The catalytic domain is located at the C-terminus. These proteins are members of the glycosy transferase family 13.


:

Pssm-ID: 133007  Cd Length: 334  Bit Score: 523.43  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890258305 158 NVPVAVIAGNRPNYLYRMLRSLLSAQ-GVSPQMITVFIDGYYEEPMDVVALFG--LRGIQHTPISIKN----------AR 224
Cdd:cd02514     1 VIPVLVIACNRPDYLRRMLDSLLSYRpSAEKFPIIVSQDGGYEEVADVAKSFGdgVTHIQHPPISIKNvnpphkfqgyYR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890258305 225 VSQHYKASLTATFNLFpEAKFAVVLEEDLDIAVDFFSFLSQSIHLLEEDDSLYCISAWNDQGYEHTAED-PALLYRVETM 303
Cdd:cd02514    81 IARHYKWALTQTFNLF-GYSFVIILEDDLDIAPDFFSYFQATLPLLEEDPSLWCISAWNDNGKEHFVDDtPSLLYRTDFF 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890258305 304 PGLGWVLRRSLYKeELEPKWPTpeklWDWDMWMRMPEQRRGRECIIPDVSRSYHFGIVGLnMNGYFHEAYFKKHKFNTVP 383
Cdd:cd02514   160 PGLGWMLTRKLWK-ELEPKWPK----AFWDDWMRLPEQRKGRECIRPEISRTYHFGKKGV-SNGQFFDKYLKKIKLNTVF 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890258305 384 GVQL-RNVDSLKKEAYEVEVHRLLSEAEVLDHSKNPCEDSFLPDTEGHTYVAFIRmekDDDFTTWTQ-LAKCLHIWDLDV 461
Cdd:cd02514   234 VVFTkLDLSYLKKDNYDKEFHRLVYGAVVLDHEKNPCELSFVPDTEGKVRVVYTG---RDDFKTWAKaFGVMDDLKDGVP 310

                         330       340
                  ....*....|....*....|....
gi 1890258305 462 RGNHRGLWRLFRKKNHFLMVGVPA 485
Cdd:cd02514   311 RTAYKGIVRFFFKGNRVFLVPPPT 334
PANDER_like super family cl19122
Domains similar to the Pancreatic-derived factor; FAM3B or PANDER (PANcreatic DERived factor) ...
 1-103 5.87e-64

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.


The actual alignment was detected with superfamily member cd13937:

Pssm-ID: 473142  Cd Length: 148  Bit Score: 204.84  E-value: 5.87e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890258305   1 MAKRVFDTYSPHEDEAMVLFLNMVAPGRVLICTVKDEGSFHLKDTAKALLRSLGSQAGPALGWRDTWAFVGRKGGPVFGE 80
Cdd:cd13937    46 MAQRVFDTYSPGEDEAMILFLNMVSDGRILIFTIKDEGSFHLKDEARSLLKKLGSQKVSKLGWRDMWAMVTRKGGPVYGE 125

                          90       100
                  ....*....|....*....|...
gi 1890258305  81 KHSKSPALSSWGDPVLLKTDVPL 103
Cdd:cd13937   126 KHSKSPDLSSWGEPVLLKAEVPL 148
 
Name Accession Description Interval E-value
GT13_GLCNAC-TI cd02514
GT13_GLCNAC-TI is involved in an essential step in the synthesis of complex or hybrid-type ...
 158-485 0e+00

GT13_GLCNAC-TI is involved in an essential step in the synthesis of complex or hybrid-type N-linked oligosaccharides; Alpha-1,3-mannosyl-glycoprotein beta-1,2-N-acetylglucosaminyltransferase (GLCNAC-T I , GNT-I) transfers N-acetyl-D-glucosamine from UDP to high-mannose glycoprotein N-oligosaccharide, an essential step in the synthesis of complex or hybrid-type N-linked oligosaccharides. The enzyme is an integral membrane protein localized to the Golgi apparatus. The catalytic domain is located at the C-terminus. These proteins are members of the glycosy transferase family 13.


Pssm-ID: 133007  Cd Length: 334  Bit Score: 523.43  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890258305 158 NVPVAVIAGNRPNYLYRMLRSLLSAQ-GVSPQMITVFIDGYYEEPMDVVALFG--LRGIQHTPISIKN----------AR 224
Cdd:cd02514     1 VIPVLVIACNRPDYLRRMLDSLLSYRpSAEKFPIIVSQDGGYEEVADVAKSFGdgVTHIQHPPISIKNvnpphkfqgyYR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890258305 225 VSQHYKASLTATFNLFpEAKFAVVLEEDLDIAVDFFSFLSQSIHLLEEDDSLYCISAWNDQGYEHTAED-PALLYRVETM 303
Cdd:cd02514    81 IARHYKWALTQTFNLF-GYSFVIILEDDLDIAPDFFSYFQATLPLLEEDPSLWCISAWNDNGKEHFVDDtPSLLYRTDFF 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890258305 304 PGLGWVLRRSLYKeELEPKWPTpeklWDWDMWMRMPEQRRGRECIIPDVSRSYHFGIVGLnMNGYFHEAYFKKHKFNTVP 383
Cdd:cd02514   160 PGLGWMLTRKLWK-ELEPKWPK----AFWDDWMRLPEQRKGRECIRPEISRTYHFGKKGV-SNGQFFDKYLKKIKLNTVF 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890258305 384 GVQL-RNVDSLKKEAYEVEVHRLLSEAEVLDHSKNPCEDSFLPDTEGHTYVAFIRmekDDDFTTWTQ-LAKCLHIWDLDV 461
Cdd:cd02514   234 VVFTkLDLSYLKKDNYDKEFHRLVYGAVVLDHEKNPCELSFVPDTEGKVRVVYTG---RDDFKTWAKaFGVMDDLKDGVP 310

                         330       340
                  ....*....|....*....|....
gi 1890258305 462 RGNHRGLWRLFRKKNHFLMVGVPA 485
Cdd:cd02514   311 RTAYKGIVRFFFKGNRVFLVPPPT 334
PANDER_GnT-1_2_like cd13937
PANDER-like domain of N-acetylglucosaminyltransferases; O-linked-mannose beta-1, ...
 1-103 5.87e-64

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: 204.84  E-value: 5.87e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890258305   1 MAKRVFDTYSPHEDEAMVLFLNMVAPGRVLICTVKDEGSFHLKDTAKALLRSLGSQAGPALGWRDTWAFVGRKGGPVFGE 80
Cdd:cd13937    46 MAQRVFDTYSPGEDEAMILFLNMVSDGRILIFTIKDEGSFHLKDEARSLLKKLGSQKVSKLGWRDMWAMVTRKGGPVYGE 125

                          90       100
                  ....*....|....*....|...
gi 1890258305  81 KHSKSPALSSWGDPVLLKTDVPL 103
Cdd:cd13937   126 KHSKSPDLSSWGEPVLLKAEVPL 148
GNT-I pfam03071
GNT-I family; Alpha-1,3-mannosyl-glycoprotein beta-1,2-N-acetylglucosaminyltransferase (GNT-I, ...
 159-458 6.53e-48

GNT-I family; Alpha-1,3-mannosyl-glycoprotein beta-1,2-N-acetylglucosaminyltransferase (GNT-I, GLCNAC-T I) EC:2.4.1.101 transfers N-acetyl-D-glucosamine from UDP to high-mannose glycoprotein N-oligosaccharide. This is an essential step in the synthesis of complex or hybrid-type N-linked oligosaccharides. The enzyme is an integral membrane protein localized to the Golgi apparatus, and is probably distributed in all tissues. The catalytic domain is located at the C-terminus.


Pssm-ID: 397273  Cd Length: 434  Bit Score: 171.63  E-value: 6.53e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890258305 159 VPVAVIAGNRPNYLYRMLRSLLSAQGVSPQM-ITVFIDGYYEEPMDVVALFG--LRGIQH---TPISIKNA--------R 224
Cdd:pfam03071  95 IPVLVMACSRADYVRRTVKKLLTYRPSAEKFpIIVSQDCSDEAVKSKSLSYGnqVTYIQHldfEPIVTPPGhrqltayyK 174

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890258305 225 VSQHYKASLTatfNLFPEAKF--AVVLEEDLDIAVDFFSFLSQSIHLLEEDDSLYCISAWNDQGYEHTAED--PALLYRV 300
Cdd:pfam03071 175 IARHYKWALD---QVFYKHKFsrVIILEDDLEIAPDFFDYFEATASLLDRDKTLWCVSAWNDNGKKQFVDDtaPYALYRS 251

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890258305 301 ETMPGLGWVLRRSLYkEELEPKWPTPEklwdWDMWMRMPEQRRGRECIIPDVSRSYHFGIVGLNMnGYFHEAYFKKHKFN 380
Cdd:pfam03071 252 DFFPGLGWMLKRSTW-DELEPKWPKAF----WDDWMRLPENRKGRQCIRPEISRTMNFGEHGSSL-GQFFSQHLEPIKLN 325

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890258305 381 --TVPGVQLrNVDSLKKEAYEVEVHRLLSEAevldhsknpcedsflPDTEGHTYVAFIRMEKDD------DFTTWTQLAK 452
Cdd:pfam03071 326 dvTVDFKAK-DLGYLTEGNYTKYFSGLVRQA---------------RPLQGSDVVLKAQNIKGDvrvrykGQVEFERIAG 389


                  ....*.
gi 1890258305 453 CLHIWD 458
Cdd:pfam03071 390 ELGIME 395
ILEI pfam15711
Interleukin-like EMT inducer; ILEI is a family of proteins found in vertebrates. It is heavily ...
 1-74 1.94e-23

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: 94.25  E-value: 1.94e-23
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1890258305   1 MAKRVFDTYSPHEDEAMVLFLNMVAPGRVLICTVKDEGSFHLKDTAKALLRSLGSQAGPALGWRDTWAFVGRKG 74
Cdd:pfam15711  16 LDSKSFDTYSYSDSSRLANFLKSIPDGSIVLIATKDEASSKLSDEARKALESLGSSKIDNLGFRDSWAFIGFKG 89
 
Name Accession Description Interval E-value
GT13_GLCNAC-TI cd02514
GT13_GLCNAC-TI is involved in an essential step in the synthesis of complex or hybrid-type ...
 158-485 0e+00

GT13_GLCNAC-TI is involved in an essential step in the synthesis of complex or hybrid-type N-linked oligosaccharides; Alpha-1,3-mannosyl-glycoprotein beta-1,2-N-acetylglucosaminyltransferase (GLCNAC-T I , GNT-I) transfers N-acetyl-D-glucosamine from UDP to high-mannose glycoprotein N-oligosaccharide, an essential step in the synthesis of complex or hybrid-type N-linked oligosaccharides. The enzyme is an integral membrane protein localized to the Golgi apparatus. The catalytic domain is located at the C-terminus. These proteins are members of the glycosy transferase family 13.


Pssm-ID: 133007  Cd Length: 334  Bit Score: 523.43  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890258305 158 NVPVAVIAGNRPNYLYRMLRSLLSAQ-GVSPQMITVFIDGYYEEPMDVVALFG--LRGIQHTPISIKN----------AR 224
Cdd:cd02514     1 VIPVLVIACNRPDYLRRMLDSLLSYRpSAEKFPIIVSQDGGYEEVADVAKSFGdgVTHIQHPPISIKNvnpphkfqgyYR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890258305 225 VSQHYKASLTATFNLFpEAKFAVVLEEDLDIAVDFFSFLSQSIHLLEEDDSLYCISAWNDQGYEHTAED-PALLYRVETM 303
Cdd:cd02514    81 IARHYKWALTQTFNLF-GYSFVIILEDDLDIAPDFFSYFQATLPLLEEDPSLWCISAWNDNGKEHFVDDtPSLLYRTDFF 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890258305 304 PGLGWVLRRSLYKeELEPKWPTpeklWDWDMWMRMPEQRRGRECIIPDVSRSYHFGIVGLnMNGYFHEAYFKKHKFNTVP 383
Cdd:cd02514   160 PGLGWMLTRKLWK-ELEPKWPK----AFWDDWMRLPEQRKGRECIRPEISRTYHFGKKGV-SNGQFFDKYLKKIKLNTVF 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890258305 384 GVQL-RNVDSLKKEAYEVEVHRLLSEAEVLDHSKNPCEDSFLPDTEGHTYVAFIRmekDDDFTTWTQ-LAKCLHIWDLDV 461
Cdd:cd02514   234 VVFTkLDLSYLKKDNYDKEFHRLVYGAVVLDHEKNPCELSFVPDTEGKVRVVYTG---RDDFKTWAKaFGVMDDLKDGVP 310

                         330       340
                  ....*....|....*....|....
gi 1890258305 462 RGNHRGLWRLFRKKNHFLMVGVPA 485
Cdd:cd02514   311 RTAYKGIVRFFFKGNRVFLVPPPT 334
PANDER_GnT-1_2_like cd13937
PANDER-like domain of N-acetylglucosaminyltransferases; O-linked-mannose beta-1, ...
 1-103 5.87e-64

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: 204.84  E-value: 5.87e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890258305   1 MAKRVFDTYSPHEDEAMVLFLNMVAPGRVLICTVKDEGSFHLKDTAKALLRSLGSQAGPALGWRDTWAFVGRKGGPVFGE 80
Cdd:cd13937    46 MAQRVFDTYSPGEDEAMILFLNMVSDGRILIFTIKDEGSFHLKDEARSLLKKLGSQKVSKLGWRDMWAMVTRKGGPVYGE 125

                          90       100
                  ....*....|....*....|...
gi 1890258305  81 KHSKSPALSSWGDPVLLKTDVPL 103
Cdd:cd13937   126 KHSKSPDLSSWGEPVLLKAEVPL 148
GNT-I pfam03071
GNT-I family; Alpha-1,3-mannosyl-glycoprotein beta-1,2-N-acetylglucosaminyltransferase (GNT-I, ...
 159-458 6.53e-48

GNT-I family; Alpha-1,3-mannosyl-glycoprotein beta-1,2-N-acetylglucosaminyltransferase (GNT-I, GLCNAC-T I) EC:2.4.1.101 transfers N-acetyl-D-glucosamine from UDP to high-mannose glycoprotein N-oligosaccharide. This is an essential step in the synthesis of complex or hybrid-type N-linked oligosaccharides. The enzyme is an integral membrane protein localized to the Golgi apparatus, and is probably distributed in all tissues. The catalytic domain is located at the C-terminus.


Pssm-ID: 397273  Cd Length: 434  Bit Score: 171.63  E-value: 6.53e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890258305 159 VPVAVIAGNRPNYLYRMLRSLLSAQGVSPQM-ITVFIDGYYEEPMDVVALFG--LRGIQH---TPISIKNA--------R 224
Cdd:pfam03071  95 IPVLVMACSRADYVRRTVKKLLTYRPSAEKFpIIVSQDCSDEAVKSKSLSYGnqVTYIQHldfEPIVTPPGhrqltayyK 174

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890258305 225 VSQHYKASLTatfNLFPEAKF--AVVLEEDLDIAVDFFSFLSQSIHLLEEDDSLYCISAWNDQGYEHTAED--PALLYRV 300
Cdd:pfam03071 175 IARHYKWALD---QVFYKHKFsrVIILEDDLEIAPDFFDYFEATASLLDRDKTLWCVSAWNDNGKKQFVDDtaPYALYRS 251

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890258305 301 ETMPGLGWVLRRSLYkEELEPKWPTPEklwdWDMWMRMPEQRRGRECIIPDVSRSYHFGIVGLNMnGYFHEAYFKKHKFN 380
Cdd:pfam03071 252 DFFPGLGWMLKRSTW-DELEPKWPKAF----WDDWMRLPENRKGRQCIRPEISRTMNFGEHGSSL-GQFFSQHLEPIKLN 325

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890258305 381 --TVPGVQLrNVDSLKKEAYEVEVHRLLSEAevldhsknpcedsflPDTEGHTYVAFIRMEKDD------DFTTWTQLAK 452
Cdd:pfam03071 326 dvTVDFKAK-DLGYLTEGNYTKYFSGLVRQA---------------RPLQGSDVVLKAQNIKGDvrvrykGQVEFERIAG 389


                  ....*.
gi 1890258305 453 CLHIWD 458
Cdd:pfam03071 390 ELGIME 395
PANDER_like cd13936
Domains similar to the Pancreatic-derived factor; FAM3B or PANDER (PANcreatic DERived factor) ...
 1-103 6.27e-38

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: 136.31  E-value: 6.27e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890258305   1 MAKRVFDTYSPHEDEAMVLFLNMVAPGRVLICTVKDEGSFHLKDTAKALLRSLGSQAGPALGWRDTWAFVGRKGGPVF-G 79
Cdd:cd13936    46 IATKTFDTYGAGASNDMIDFLNSVPPGSIVLIATKDDASKSLKDEARRALESLGSSLIQNLGFRDSWAFVGQKGIKRPsT 125

                          90       100
                  ....*....|....*....|....
gi 1890258305  80 EKHSKSPALSSWGDPVLLKTDVPL 103
Cdd:cd13936   126 EQHEISPKNSSWGGPALIQTCFPL 149
ILEI pfam15711
Interleukin-like EMT inducer; ILEI is a family of proteins found in vertebrates. It is heavily ...
 1-74 1.94e-23

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: 94.25  E-value: 1.94e-23
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1890258305   1 MAKRVFDTYSPHEDEAMVLFLNMVAPGRVLICTVKDEGSFHLKDTAKALLRSLGSQAGPALGWRDTWAFVGRKG 74
Cdd:pfam15711  16 LDSKSFDTYSYSDSSRLANFLKSIPDGSIVLIATKDEASSKLSDEARKALESLGSSKIDNLGFRDSWAFIGFKG 89
PANDER_like_TMEM2 cd13938
PANDER-like domain of the transmembrane protein TMEM2; TMEM2 has been characterized as a ...
 6-76 1.23e-15

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: 74.67  E-value: 1.23e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1890258305   6 FDTYSpHEDEAMVL--FLNMVAPGRVLICTVKDEGSFHLKDTAKALLRSLGSQAGPALGWRDTWAFVGRKGGP 76
Cdd:cd13938    68 FDTYE-SEDESKRLaeFLDQIPPGRIVALAVGDEASKNLEDSARKKIRELGSKEIDHLGYRQPWAFVGVKGGP 139
ILEI_FAM3C cd13940
Interleukin-like EMT inducer; The secreted factor FAM3C or ILEI (InterLeukin-like Emt Inducer) ...
 6-85 1.63e-10

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: 59.97  E-value: 1.63e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1890258305   6 FDTYSpHEDEAMVLFLNMVAPGRVLICTVKDEGSFHLKDTAKALLRSLGSQAGPALGWRDTWAFVGRKGGPVFG--EKHS 83
Cdd:cd13940    70 FDMYS-GDVKPLLEFLKSIKPGSIVLVASFDDPATKLNDEARKLFAELGSSSIKSLGFRDNWVFVGGKGIKTKSpfEKHI 148


                  ..
gi 1890258305  84 KS 85
Cdd:cd13940   149 KN 150
PANDER_FAM3B cd13939
Pancreatic derived factor; FAM3B or PANDER (PANcreatic DERived factor) has been identifed as a ...
 1-74 1.96e-06

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: 47.99  E-value: 1.96e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1890258305   1 MAKRVFDTYSPHEDEAMVLFLNMVAPGRVLICTVKDEGSFHLKDTAKALLRSLGSQAGPALGWRDTWAFVGRKG 74
Cdd:cd13939    64 VATKYFDMYEGDFSGPMIEFINKIPKKSLVFVVTHDDGSTKLKDPAKKAIEDLGSKEIRNLKFRSAWVFIAAKG 137
 
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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