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Conserved domains on  [gi|594591617|ref|NP_001277587|]
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protein O-linked-mannose beta-1,2-N-acetylglucosaminyltransferase 1 isoform 3 [Mus musculus]

Protein Classification

glycosyltransferase family 13 protein; glycosyltransferase family 8 protein( domain architecture ID 10195368)

glycosyltransferase family 13 protein catalyzes the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds| glycosyltransferase family 8 protein containing a class I SAM-dependent methyltransferase domain, catalyzes the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds, and possibly the methylation of one or more specific substrates using S-adenosyl-L-methionine (SAM or AdoMet) as the methyl donor

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 ...
 279-606 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: 526.13  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591617 279 NVPVAVIAGNRPNYLYRMLRSLLSAQ-GVSPQMITVFIDGYYEEPMDVVALFG--LRGIQHTPISIKN----------AR 345
Cdd:cd02514    1 VIPVLVIACNRPDYLRRMLDSLLSYRpSAEKFPIIVSQDGGYEEVADVAKSFGdgVTHIQHPPISIKNvnpphkfqgyYR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591617 346 VSQHYKASLTATFNLFpEAKFAVVLEEDLDIAVDFFSFLSQSIHLLEEDDSLYCISAWNDQGYEHTAED-PALLYRVETM 424
Cdd:cd02514   81 IARHYKWALTQTFNLF-GYSFVIILEDDLDIAPDFFSYFQATLPLLEEDPSLWCISAWNDNGKEHFVDDtPSLLYRTDFF 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591617 425 PGLGWVLRKSLYKeELEPKWPTpeklWDWDMWMRMPEQRRGRECIIPDVSRSYHFGIVGLnMNGYFHEAYFKKHKFNTVP 504
Cdd:cd02514  160 PGLGWMLTRKLWK-ELEPKWPK----AFWDDWMRLPEQRKGRECIRPEISRTYHFGKKGV-SNGQFFDKYLKKIKLNTVF 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591617 505 GVQL-RNVDSLKKEAYEVEIHRLLSEAEVLDHSKDPCEDSFLPDTEGHTYVAFIRmetDDDFATWTQ-LAKCLHIWDLDV 582
Cdd:cd02514  234 VVFTkLDLSYLKKDNYDKEFHRLVYGAVVLDHEKNPCELSFVPDTEGKVRVVYTG---RDDFKTWAKaFGVMDDLKDGVP 310

                        330       340
                 ....*....|....*....|....
gi 594591617 583 RGNHRGLWRLFRKKNHFLVVGVPA 606
Cdd:cd02514  311 RTAYKGIVRFFFKGNRVFLVPPPT 334
PANDER_GnT-1_2_like cd13937
PANDER-like domain of N-acetylglucosaminyltransferases; O-linked-mannose beta-1, ...
 77-224 1.94e-96

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: 292.28  E-value: 1.94e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591617  77 LDVEVYSSRSKVYVAVDGTTVLEDEAREQGRGIHVIVLNQATGHVMAKRVFDTYSPHEDEAMVLFLNMVAPGRVLICTVK 156
Cdd:cd13937    1 LDIEVYSSKSKVSVSVDGTTVLEDEEAEAGRGIHVVVLNQATGSVMAQRVFDTYSPGEDEAMILFLNMVSDGRILIFTIK 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 594591617 157 DEGSFHLKDTAKALLRSLGSQAGPALGWRDTWAFVGRKGGPVLGEKHSKSPALSSWGDPVLLKTDVPL 224
Cdd:cd13937   81 DEGSFHLKDEARSLLKKLGSQKVSKLGWRDMWAMVTRKGGPVYGEKHSKSPDLSSWGEPVLLKAEVPL 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 ...
 279-606 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: 526.13  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591617 279 NVPVAVIAGNRPNYLYRMLRSLLSAQ-GVSPQMITVFIDGYYEEPMDVVALFG--LRGIQHTPISIKN----------AR 345
Cdd:cd02514    1 VIPVLVIACNRPDYLRRMLDSLLSYRpSAEKFPIIVSQDGGYEEVADVAKSFGdgVTHIQHPPISIKNvnpphkfqgyYR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591617 346 VSQHYKASLTATFNLFpEAKFAVVLEEDLDIAVDFFSFLSQSIHLLEEDDSLYCISAWNDQGYEHTAED-PALLYRVETM 424
Cdd:cd02514   81 IARHYKWALTQTFNLF-GYSFVIILEDDLDIAPDFFSYFQATLPLLEEDPSLWCISAWNDNGKEHFVDDtPSLLYRTDFF 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591617 425 PGLGWVLRKSLYKeELEPKWPTpeklWDWDMWMRMPEQRRGRECIIPDVSRSYHFGIVGLnMNGYFHEAYFKKHKFNTVP 504
Cdd:cd02514  160 PGLGWMLTRKLWK-ELEPKWPK----AFWDDWMRLPEQRKGRECIRPEISRTYHFGKKGV-SNGQFFDKYLKKIKLNTVF 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591617 505 GVQL-RNVDSLKKEAYEVEIHRLLSEAEVLDHSKDPCEDSFLPDTEGHTYVAFIRmetDDDFATWTQ-LAKCLHIWDLDV 582
Cdd:cd02514  234 VVFTkLDLSYLKKDNYDKEFHRLVYGAVVLDHEKNPCELSFVPDTEGKVRVVYTG---RDDFKTWAKaFGVMDDLKDGVP 310

                        330       340
                 ....*....|....*....|....
gi 594591617 583 RGNHRGLWRLFRKKNHFLVVGVPA 606
Cdd:cd02514  311 RTAYKGIVRFFFKGNRVFLVPPPT 334
PANDER_GnT-1_2_like cd13937
PANDER-like domain of N-acetylglucosaminyltransferases; O-linked-mannose beta-1, ...
 77-224 1.94e-96

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: 292.28  E-value: 1.94e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591617  77 LDVEVYSSRSKVYVAVDGTTVLEDEAREQGRGIHVIVLNQATGHVMAKRVFDTYSPHEDEAMVLFLNMVAPGRVLICTVK 156
Cdd:cd13937    1 LDIEVYSSKSKVSVSVDGTTVLEDEEAEAGRGIHVVVLNQATGSVMAQRVFDTYSPGEDEAMILFLNMVSDGRILIFTIK 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 594591617 157 DEGSFHLKDTAKALLRSLGSQAGPALGWRDTWAFVGRKGGPVLGEKHSKSPALSSWGDPVLLKTDVPL 224
Cdd:cd13937   81 DEGSFHLKDEARSLLKKLGSQKVSKLGWRDMWAMVTRKGGPVYGEKHSKSPDLSSWGEPVLLKAEVPL 148
GNT-I pfam03071
GNT-I family; Alpha-1,3-mannosyl-glycoprotein beta-1,2-N-acetylglucosaminyltransferase (GNT-I, ...
 280-537 1.33e-46

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: 170.47  E-value: 1.33e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591617  280 VPVAVIAGNRPNYLYRMLRSLLSAQGVSPQM-ITVFIDGYYEEPMDVVALFG--LRGIQH---TPISIKNA--------R 345
Cdd:pfam03071  95 IPVLVMACSRADYVRRTVKKLLTYRPSAEKFpIIVSQDCSDEAVKSKSLSYGnqVTYIQHldfEPIVTPPGhrqltayyK 174

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591617  346 VSQHYKASLTatfNLFPEAKF--AVVLEEDLDIAVDFFSFLSQSIHLLEEDDSLYCISAWNDQGYEHTAED--PALLYRV 421
Cdd:pfam03071 175 IARHYKWALD---QVFYKHKFsrVIILEDDLEIAPDFFDYFEATASLLDRDKTLWCVSAWNDNGKKQFVDDtaPYALYRS 251

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591617  422 ETMPGLGWVLRKSLYkEELEPKWPTPEklwdWDMWMRMPEQRRGRECIIPDVSRSYHFGIVGLNMnGYFHEAYFKKHKFN 501
Cdd:pfam03071 252 DFFPGLGWMLKRSTW-DELEPKWPKAF----WDDWMRLPENRKGRQCIRPEISRTMNFGEHGSSL-GQFFSQHLEPIKLN 325

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 594591617  502 --TVPGVQLrNVDSLKKEAYEVEIHRLLSEAEVLDHSK 537
Cdd:pfam03071 326 dvTVDFKAK-DLGYLTEGNYTKYFSGLVRQARPLQGSD 362
ILEI pfam15711
Interleukin-like EMT inducer; ILEI is a family of proteins found in vertebrates. It is heavily ...
 107-195 1.74e-32

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: 120.06  E-value: 1.74e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591617  107 RGIHVIVLNQATGHVMAKRVFDTYSPHEDEAMVLFLNMVAPGRVLICTVKDEGSFHLKDTAKALLRSLGSQAGPALGWRD 186
Cdd:pfam15711   1 RGINVVVVDACTGKVLDSKSFDTYSYSDSSRLANFLKSIPDGSIVLIATKDEASSKLSDEARKALESLGSSKIDNLGFRD 80


                  ....*....
gi 594591617  187 TWAFVGRKG 195
Cdd:pfam15711  81 SWAFIGFKG 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 ...
 279-606 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: 526.13  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591617 279 NVPVAVIAGNRPNYLYRMLRSLLSAQ-GVSPQMITVFIDGYYEEPMDVVALFG--LRGIQHTPISIKN----------AR 345
Cdd:cd02514    1 VIPVLVIACNRPDYLRRMLDSLLSYRpSAEKFPIIVSQDGGYEEVADVAKSFGdgVTHIQHPPISIKNvnpphkfqgyYR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591617 346 VSQHYKASLTATFNLFpEAKFAVVLEEDLDIAVDFFSFLSQSIHLLEEDDSLYCISAWNDQGYEHTAED-PALLYRVETM 424
Cdd:cd02514   81 IARHYKWALTQTFNLF-GYSFVIILEDDLDIAPDFFSYFQATLPLLEEDPSLWCISAWNDNGKEHFVDDtPSLLYRTDFF 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591617 425 PGLGWVLRKSLYKeELEPKWPTpeklWDWDMWMRMPEQRRGRECIIPDVSRSYHFGIVGLnMNGYFHEAYFKKHKFNTVP 504
Cdd:cd02514  160 PGLGWMLTRKLWK-ELEPKWPK----AFWDDWMRLPEQRKGRECIRPEISRTYHFGKKGV-SNGQFFDKYLKKIKLNTVF 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591617 505 GVQL-RNVDSLKKEAYEVEIHRLLSEAEVLDHSKDPCEDSFLPDTEGHTYVAFIRmetDDDFATWTQ-LAKCLHIWDLDV 582
Cdd:cd02514  234 VVFTkLDLSYLKKDNYDKEFHRLVYGAVVLDHEKNPCELSFVPDTEGKVRVVYTG---RDDFKTWAKaFGVMDDLKDGVP 310

                        330       340
                 ....*....|....*....|....
gi 594591617 583 RGNHRGLWRLFRKKNHFLVVGVPA 606
Cdd:cd02514  311 RTAYKGIVRFFFKGNRVFLVPPPT 334
PANDER_GnT-1_2_like cd13937
PANDER-like domain of N-acetylglucosaminyltransferases; O-linked-mannose beta-1, ...
 77-224 1.94e-96

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: 292.28  E-value: 1.94e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591617  77 LDVEVYSSRSKVYVAVDGTTVLEDEAREQGRGIHVIVLNQATGHVMAKRVFDTYSPHEDEAMVLFLNMVAPGRVLICTVK 156
Cdd:cd13937    1 LDIEVYSSKSKVSVSVDGTTVLEDEEAEAGRGIHVVVLNQATGSVMAQRVFDTYSPGEDEAMILFLNMVSDGRILIFTIK 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 594591617 157 DEGSFHLKDTAKALLRSLGSQAGPALGWRDTWAFVGRKGGPVLGEKHSKSPALSSWGDPVLLKTDVPL 224
Cdd:cd13937   81 DEGSFHLKDEARSLLKKLGSQKVSKLGWRDMWAMVTRKGGPVYGEKHSKSPDLSSWGEPVLLKAEVPL 148
PANDER_like cd13936
Domains similar to the Pancreatic-derived factor; FAM3B or PANDER (PANcreatic DERived factor) ...
 77-224 2.85e-50

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: 171.37  E-value: 2.85e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591617  77 LDVEVYSSR--SKVYVAVDGTtVLEDEAReQGRGIHVIVLNQATGHVMAKRVFDTYSPHEDEAMVLFLNMVAPGRVLICT 154
Cdd:cd13936    1 LEVKIASGGggNYAKICVNGG-VLFDGDK-SGRGINVVVINGDTGKVIATKTFDTYGAGASNDMIDFLNSVPPGSIVLIA 78

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 594591617 155 VKDEGSFHLKDTAKALLRSLGSQAGPALGWRDTWAFVGRKGGPVL-GEKHSKSPALSSWGDPVLLKTDVPL 224
Cdd:cd13936   79 TKDDASKSLKDEARRALESLGSSLIQNLGFRDSWAFVGQKGIKRPsTEQHEISPKNSSWGGPALIQTCFPL 149
GNT-I pfam03071
GNT-I family; Alpha-1,3-mannosyl-glycoprotein beta-1,2-N-acetylglucosaminyltransferase (GNT-I, ...
 280-537 1.33e-46

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: 170.47  E-value: 1.33e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591617  280 VPVAVIAGNRPNYLYRMLRSLLSAQGVSPQM-ITVFIDGYYEEPMDVVALFG--LRGIQH---TPISIKNA--------R 345
Cdd:pfam03071  95 IPVLVMACSRADYVRRTVKKLLTYRPSAEKFpIIVSQDCSDEAVKSKSLSYGnqVTYIQHldfEPIVTPPGhrqltayyK 174

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591617  346 VSQHYKASLTatfNLFPEAKF--AVVLEEDLDIAVDFFSFLSQSIHLLEEDDSLYCISAWNDQGYEHTAED--PALLYRV 421
Cdd:pfam03071 175 IARHYKWALD---QVFYKHKFsrVIILEDDLEIAPDFFDYFEATASLLDRDKTLWCVSAWNDNGKKQFVDDtaPYALYRS 251

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591617  422 ETMPGLGWVLRKSLYkEELEPKWPTPEklwdWDMWMRMPEQRRGRECIIPDVSRSYHFGIVGLNMnGYFHEAYFKKHKFN 501
Cdd:pfam03071 252 DFFPGLGWMLKRSTW-DELEPKWPKAF----WDDWMRLPENRKGRQCIRPEISRTMNFGEHGSSL-GQFFSQHLEPIKLN 325

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 594591617  502 --TVPGVQLrNVDSLKKEAYEVEIHRLLSEAEVLDHSK 537
Cdd:pfam03071 326 dvTVDFKAK-DLGYLTEGNYTKYFSGLVRQARPLQGSD 362
ILEI pfam15711
Interleukin-like EMT inducer; ILEI is a family of proteins found in vertebrates. It is heavily ...
 107-195 1.74e-32

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: 120.06  E-value: 1.74e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591617  107 RGIHVIVLNQATGHVMAKRVFDTYSPHEDEAMVLFLNMVAPGRVLICTVKDEGSFHLKDTAKALLRSLGSQAGPALGWRD 186
Cdd:pfam15711   1 RGINVVVVDACTGKVLDSKSFDTYSYSDSSRLANFLKSIPDGSIVLIATKDEASSKLSDEARKALESLGSSKIDNLGFRD 80


                  ....*....
gi 594591617  187 TWAFVGRKG 195
Cdd:pfam15711  81 SWAFIGFKG 89
PANDER_like_TMEM2 cd13938
PANDER-like domain of the transmembrane protein TMEM2; TMEM2 has been characterized as a ...
 100-197 2.14e-22

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: 94.31  E-value: 2.14e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591617 100 DEAREQGRGIHVIVLNQATGHVMAKRVFDTYSpHEDEAMVL--FLNMVAPGRVLICTVKDEGSFHLKDTAKALLRSLGSQ 177
Cdd:cd13938   41 FERSWGSRGINVRVIDEDTGEVLESDRFDTYE-SEDESKRLaeFLDQIPPGRIVALAVGDEASKNLEDSARKKIRELGSK 119

                         90       100
                 ....*....|....*....|
gi 594591617 178 AGPALGWRDTWAFVGRKGGP 197
Cdd:cd13938  120 EIDHLGYRQPWAFVGVKGGP 139
ILEI_FAM3C cd13940
Interleukin-like EMT inducer; The secreted factor FAM3C or ILEI (InterLeukin-like Emt Inducer) ...
 90-206 3.24e-16

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: 76.54  E-value: 3.24e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591617  90 VAVDGTTVLEDEAREQGRGIHVIVLNQATGHVMAKRVFDTYSpHEDEAMVLFLNMVAPGRVLICTVKDEGSFHLKDTAKA 169
Cdd:cd13940   33 ICFEGKIIMSSVLNNVGRGLNIALVNGETGEVLKTGFFDMYS-GDVKPLLEFLKSIKPGSIVLVASFDDPATKLNDEARK 111

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 594591617 170 LLRSLGSQAGPALGWRDTWAFVGRKGGPV--LGEKHSKS 206
Cdd:cd13940  112 LFAELGSSSIKSLGFRDNWVFVGGKGIKTksPFEKHIKN 150
PANDER_FAM3B cd13939
Pancreatic derived factor; FAM3B or PANDER (PANcreatic DERived factor) has been identifed as a ...
 90-195 2.64e-12

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: 65.71  E-value: 2.64e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 594591617  90 VAVDGTTVLEDEAREQGRGIHVIVLNQATGHVMAKRVFDTYSPHEDEAMVLFLNMVAPGRVLICTVKDEGSFHLKDTAKA 169
Cdd:cd13939   32 ICFEDNMLITGKEGNSNRGINIAVVSYETGKVVATKYFDMYEGDFSGPMIEFINKIPKKSLVFVVTHDDGSTKLKDPAKK 111

                         90       100
                 ....*....|....*....|....*.
gi 594591617 170 LLRSLGSQAGPALGWRDTWAFVGRKG 195
Cdd:cd13939  112 AIEDLGSKEIRNLKFRSAWVFIAAKG 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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