NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|225543554|ref|NP_084062|]
View 

protein O-linked-mannose beta-1,2-N-acetylglucosaminyltransferase 1 isoform 2 [Mus musculus]

Protein Classification

glycosyltransferase family 13 protein; glycosyltransferase family 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 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
GT13_GLCNAC-TI cd02514
GT13_GLCNAC-TI is involved in an essential step in the synthesis of complex or hybrid-type ...
 268-595 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: 521.89  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543554 268 NVPVAVIAGNRPNYLYRMLRSLLSAQ-GVSPQMITVFIDGYYEEPMDVVALFG--LRGIQHTPISIKN----------AR 334
Cdd:cd02514    1 VIPVLVIACNRPDYLRRMLDSLLSYRpSAEKFPIIVSQDGGYEEVADVAKSFGdgVTHIQHPPISIKNvnpphkfqgyYR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543554 335 VSQHYKASLTATFNLFpEAKFAVVLEEDLDIAVDFFSFLSQSIHLLEEDDSLYCISAWNDQGYEHTAED-PALLYRVETM 413
Cdd:cd02514   81 IARHYKWALTQTFNLF-GYSFVIILEDDLDIAPDFFSYFQATLPLLEEDPSLWCISAWNDNGKEHFVDDtPSLLYRTDFF 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543554 414 PGLGWVLRKSLYKeELEPKWPTpeklWDWDMWMRMPEQRRGRECIIPDVSRSYHFGIVGLnMNGYFHEAYFKKHKFNTVP 493
Cdd:cd02514  160 PGLGWMLTRKLWK-ELEPKWPK----AFWDDWMRLPEQRKGRECIRPEISRTYHFGKKGV-SNGQFFDKYLKKIKLNTVF 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543554 494 GVQL-RNVDSLKKEAYEVEIHRLLSEAEVLDHSKDPCEDSFLPDTEGHTYVAFIRmetDDDFATWTQ-LAKCLHIWDLDV 571
Cdd:cd02514  234 VVFTkLDLSYLKKDNYDKEFHRLVYGAVVLDHEKNPCELSFVPDTEGKVRVVYTG---RDDFKTWAKaFGVMDDLKDGVP 310

                        330       340
                 ....*....|....*....|....
gi 225543554 572 RGNHRGLWRLFRKKNHFLVVGVPA 595
Cdd:cd02514  311 RTAYKGIVRFFFKGNRVFLVPPPT 334
PANDER_GnT-1_2_like cd13937
PANDER-like domain of N-acetylglucosaminyltransferases; O-linked-mannose beta-1, ...
 99-229 4.40e-78

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: 244.52  E-value: 4.40e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543554  99 LDVEVYSSRSKVYVAVDGTTVLEDEAREQGRGIHVIVLNQATGHVMAKRVFDTYSPHEDEAMVLFLNMVAPGRVLICTVK 178
Cdd:cd13937    1 LDIEVYSSKSKVSVSVDGTTVLEDEEAEAGRGIHVVVLNQATGSVMAQRVFDTYSPGEDEAMILFLNMVSDGRILIFTIK 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 225543554 179 DEGSFHLKDTAKALLRSLGSQAGPALGWRDTWAFVGRKG---EAECHWADTELN 229
Cdd:cd13937   81 DEGSFHLKDEARSLLKKLGSQKVSKLGWRDMWAMVTRKGgpvYGEKHSKSPDLS 134
 
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 ...
 268-595 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: 521.89  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543554 268 NVPVAVIAGNRPNYLYRMLRSLLSAQ-GVSPQMITVFIDGYYEEPMDVVALFG--LRGIQHTPISIKN----------AR 334
Cdd:cd02514    1 VIPVLVIACNRPDYLRRMLDSLLSYRpSAEKFPIIVSQDGGYEEVADVAKSFGdgVTHIQHPPISIKNvnpphkfqgyYR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543554 335 VSQHYKASLTATFNLFpEAKFAVVLEEDLDIAVDFFSFLSQSIHLLEEDDSLYCISAWNDQGYEHTAED-PALLYRVETM 413
Cdd:cd02514   81 IARHYKWALTQTFNLF-GYSFVIILEDDLDIAPDFFSYFQATLPLLEEDPSLWCISAWNDNGKEHFVDDtPSLLYRTDFF 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543554 414 PGLGWVLRKSLYKeELEPKWPTpeklWDWDMWMRMPEQRRGRECIIPDVSRSYHFGIVGLnMNGYFHEAYFKKHKFNTVP 493
Cdd:cd02514  160 PGLGWMLTRKLWK-ELEPKWPK----AFWDDWMRLPEQRKGRECIRPEISRTYHFGKKGV-SNGQFFDKYLKKIKLNTVF 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543554 494 GVQL-RNVDSLKKEAYEVEIHRLLSEAEVLDHSKDPCEDSFLPDTEGHTYVAFIRmetDDDFATWTQ-LAKCLHIWDLDV 571
Cdd:cd02514  234 VVFTkLDLSYLKKDNYDKEFHRLVYGAVVLDHEKNPCELSFVPDTEGKVRVVYTG---RDDFKTWAKaFGVMDDLKDGVP 310

                        330       340
                 ....*....|....*....|....
gi 225543554 572 RGNHRGLWRLFRKKNHFLVVGVPA 595
Cdd:cd02514  311 RTAYKGIVRFFFKGNRVFLVPPPT 334
PANDER_GnT-1_2_like cd13937
PANDER-like domain of N-acetylglucosaminyltransferases; O-linked-mannose beta-1, ...
 99-229 4.40e-78

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: 244.52  E-value: 4.40e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543554  99 LDVEVYSSRSKVYVAVDGTTVLEDEAREQGRGIHVIVLNQATGHVMAKRVFDTYSPHEDEAMVLFLNMVAPGRVLICTVK 178
Cdd:cd13937    1 LDIEVYSSKSKVSVSVDGTTVLEDEEAEAGRGIHVVVLNQATGSVMAQRVFDTYSPGEDEAMILFLNMVSDGRILIFTIK 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 225543554 179 DEGSFHLKDTAKALLRSLGSQAGPALGWRDTWAFVGRKG---EAECHWADTELN 229
Cdd:cd13937   81 DEGSFHLKDEARSLLKKLGSQKVSKLGWRDMWAMVTRKGgpvYGEKHSKSPDLS 134
GNT-I pfam03071
GNT-I family; Alpha-1,3-mannosyl-glycoprotein beta-1,2-N-acetylglucosaminyltransferase (GNT-I, ...
 269-526 6.70e-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: 168.16  E-value: 6.70e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543554  269 VPVAVIAGNRPNYLYRMLRSLLSAQGVSPQM-ITVFIDGYYEEPMDVVALFG--LRGIQH---TPISIKNA--------R 334
Cdd:pfam03071  95 IPVLVMACSRADYVRRTVKKLLTYRPSAEKFpIIVSQDCSDEAVKSKSLSYGnqVTYIQHldfEPIVTPPGhrqltayyK 174

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543554  335 VSQHYKASLTatfNLFPEAKF--AVVLEEDLDIAVDFFSFLSQSIHLLEEDDSLYCISAWNDQGYEHTAED--PALLYRV 410
Cdd:pfam03071 175 IARHYKWALD---QVFYKHKFsrVIILEDDLEIAPDFFDYFEATASLLDRDKTLWCVSAWNDNGKKQFVDDtaPYALYRS 251

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543554  411 ETMPGLGWVLRKSLYkEELEPKWPTPEklwdWDMWMRMPEQRRGRECIIPDVSRSYHFGIVGLNMnGYFHEAYFKKHKFN 490
Cdd:pfam03071 252 DFFPGLGWMLKRSTW-DELEPKWPKAF----WDDWMRLPENRKGRQCIRPEISRTMNFGEHGSSL-GQFFSQHLEPIKLN 325

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 225543554  491 --TVPGVQLrNVDSLKKEAYEVEIHRLLSEAEVLDHSK 526
Cdd:pfam03071 326 dvTVDFKAK-DLGYLTEGNYTKYFSGLVRQARPLQGSD 362
ILEI pfam15711
Interleukin-like EMT inducer; ILEI is a family of proteins found in vertebrates. It is heavily ...
 129-217 1.66e-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: 1.66e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543554  129 RGIHVIVLNQATGHVMAKRVFDTYSPHEDEAMVLFLNMVAPGRVLICTVKDEGSFHLKDTAKALLRSLGSQAGPALGWRD 208
Cdd:pfam15711   1 RGINVVVVDACTGKVLDSKSFDTYSYSDSSRLANFLKSIPDGSIVLIATKDEASSKLSDEARKALESLGSSKIDNLGFRD 80


                  ....*....
gi 225543554  209 TWAFVGRKG 217
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 ...
 268-595 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: 521.89  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543554 268 NVPVAVIAGNRPNYLYRMLRSLLSAQ-GVSPQMITVFIDGYYEEPMDVVALFG--LRGIQHTPISIKN----------AR 334
Cdd:cd02514    1 VIPVLVIACNRPDYLRRMLDSLLSYRpSAEKFPIIVSQDGGYEEVADVAKSFGdgVTHIQHPPISIKNvnpphkfqgyYR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543554 335 VSQHYKASLTATFNLFpEAKFAVVLEEDLDIAVDFFSFLSQSIHLLEEDDSLYCISAWNDQGYEHTAED-PALLYRVETM 413
Cdd:cd02514   81 IARHYKWALTQTFNLF-GYSFVIILEDDLDIAPDFFSYFQATLPLLEEDPSLWCISAWNDNGKEHFVDDtPSLLYRTDFF 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543554 414 PGLGWVLRKSLYKeELEPKWPTpeklWDWDMWMRMPEQRRGRECIIPDVSRSYHFGIVGLnMNGYFHEAYFKKHKFNTVP 493
Cdd:cd02514  160 PGLGWMLTRKLWK-ELEPKWPK----AFWDDWMRLPEQRKGRECIRPEISRTYHFGKKGV-SNGQFFDKYLKKIKLNTVF 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543554 494 GVQL-RNVDSLKKEAYEVEIHRLLSEAEVLDHSKDPCEDSFLPDTEGHTYVAFIRmetDDDFATWTQ-LAKCLHIWDLDV 571
Cdd:cd02514  234 VVFTkLDLSYLKKDNYDKEFHRLVYGAVVLDHEKNPCELSFVPDTEGKVRVVYTG---RDDFKTWAKaFGVMDDLKDGVP 310

                        330       340
                 ....*....|....*....|....
gi 225543554 572 RGNHRGLWRLFRKKNHFLVVGVPA 595
Cdd:cd02514  311 RTAYKGIVRFFFKGNRVFLVPPPT 334
PANDER_GnT-1_2_like cd13937
PANDER-like domain of N-acetylglucosaminyltransferases; O-linked-mannose beta-1, ...
 99-229 4.40e-78

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: 244.52  E-value: 4.40e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543554  99 LDVEVYSSRSKVYVAVDGTTVLEDEAREQGRGIHVIVLNQATGHVMAKRVFDTYSPHEDEAMVLFLNMVAPGRVLICTVK 178
Cdd:cd13937    1 LDIEVYSSKSKVSVSVDGTTVLEDEEAEAGRGIHVVVLNQATGSVMAQRVFDTYSPGEDEAMILFLNMVSDGRILIFTIK 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 225543554 179 DEGSFHLKDTAKALLRSLGSQAGPALGWRDTWAFVGRKG---EAECHWADTELN 229
Cdd:cd13937   81 DEGSFHLKDEARSLLKKLGSQKVSKLGWRDMWAMVTRKGgpvYGEKHSKSPDLS 134
GNT-I pfam03071
GNT-I family; Alpha-1,3-mannosyl-glycoprotein beta-1,2-N-acetylglucosaminyltransferase (GNT-I, ...
 269-526 6.70e-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: 168.16  E-value: 6.70e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543554  269 VPVAVIAGNRPNYLYRMLRSLLSAQGVSPQM-ITVFIDGYYEEPMDVVALFG--LRGIQH---TPISIKNA--------R 334
Cdd:pfam03071  95 IPVLVMACSRADYVRRTVKKLLTYRPSAEKFpIIVSQDCSDEAVKSKSLSYGnqVTYIQHldfEPIVTPPGhrqltayyK 174

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543554  335 VSQHYKASLTatfNLFPEAKF--AVVLEEDLDIAVDFFSFLSQSIHLLEEDDSLYCISAWNDQGYEHTAED--PALLYRV 410
Cdd:pfam03071 175 IARHYKWALD---QVFYKHKFsrVIILEDDLEIAPDFFDYFEATASLLDRDKTLWCVSAWNDNGKKQFVDDtaPYALYRS 251

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543554  411 ETMPGLGWVLRKSLYkEELEPKWPTPEklwdWDMWMRMPEQRRGRECIIPDVSRSYHFGIVGLNMnGYFHEAYFKKHKFN 490
Cdd:pfam03071 252 DFFPGLGWMLKRSTW-DELEPKWPKAF----WDDWMRLPENRKGRQCIRPEISRTMNFGEHGSSL-GQFFSQHLEPIKLN 325

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 225543554  491 --TVPGVQLrNVDSLKKEAYEVEIHRLLSEAEVLDHSK 526
Cdd:pfam03071 326 dvTVDFKAK-DLGYLTEGNYTKYFSGLVRQARPLQGSD 362
PANDER_like cd13936
Domains similar to the Pancreatic-derived factor; FAM3B or PANDER (PANcreatic DERived factor) ...
 99-257 3.62e-42

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: 149.02  E-value: 3.62e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543554  99 LDVEVYSSR--SKVYVAVDGTtVLEDEAReQGRGIHVIVLNQATGHVMAKRVFDTYSPHEDEAMVLFLNMVAPGRVLICT 176
Cdd:cd13936    1 LEVKIASGGggNYAKICVNGG-VLFDGDK-SGRGINVVVINGDTGKVIATKTFDTYGAGASNDMIDFLNSVPPGSIVLIA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543554 177 VKDEGSFHLKDTAKALLRSLGSQAGPALGWRDTWAFVGRKGEaecHWADTElnrrrrrFCSKVEGYGSVcscKDPTPIEF 256
Cdd:cd13936   79 TKDDASKSLKDEARRALESLGSSLIQNLGFRDSWAFVGQKGI---KRPSTE-------QHEISPKNSSW---GGPALIQT 145


                 .
gi 225543554 257 S 257
Cdd:cd13936  146 C 146
ILEI pfam15711
Interleukin-like EMT inducer; ILEI is a family of proteins found in vertebrates. It is heavily ...
 129-217 1.66e-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: 1.66e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543554  129 RGIHVIVLNQATGHVMAKRVFDTYSPHEDEAMVLFLNMVAPGRVLICTVKDEGSFHLKDTAKALLRSLGSQAGPALGWRD 208
Cdd:pfam15711   1 RGINVVVVDACTGKVLDSKSFDTYSYSDSSRLANFLKSIPDGSIVLIATKDEASSKLSDEARKALESLGSSKIDNLGFRD 80


                  ....*....
gi 225543554  209 TWAFVGRKG 217
Cdd:pfam15711  81 SWAFIGFKG 89
PANDER_like_TMEM2 cd13938
PANDER-like domain of the transmembrane protein TMEM2; TMEM2 has been characterized as a ...
 122-218 3.76e-21

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: 90.85  E-value: 3.76e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543554 122 DEAREQGRGIHVIVLNQATGHVMAKRVFDTYSpHEDEAMVL--FLNMVAPGRVLICTVKDEGSFHLKDTAKALLRSLGSQ 199
Cdd:cd13938   41 FERSWGSRGINVRVIDEDTGEVLESDRFDTYE-SEDESKRLaeFLDQIPPGRIVALAVGDEASKNLEDSARKKIRELGSK 119

                         90
                 ....*....|....*....
gi 225543554 200 AGPALGWRDTWAFVGRKGE 218
Cdd:cd13938  120 EIDHLGYRQPWAFVGVKGG 138
ILEI_FAM3C cd13940
Interleukin-like EMT inducer; The secreted factor FAM3C or ILEI (InterLeukin-like Emt Inducer) ...
 112-217 5.41e-15

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: 73.07  E-value: 5.41e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543554 112 VAVDGTTVLEDEAREQGRGIHVIVLNQATGHVMAKRVFDTYSpHEDEAMVLFLNMVAPGRVLICTVKDEGSFHLKDTAKA 191
Cdd:cd13940   33 ICFEGKIIMSSVLNNVGRGLNIALVNGETGEVLKTGFFDMYS-GDVKPLLEFLKSIKPGSIVLVASFDDPATKLNDEARK 111

                         90       100
                 ....*....|....*....|....*.
gi 225543554 192 LLRSLGSQAGPALGWRDTWAFVGRKG 217
Cdd:cd13940  112 LFAELGSSSIKSLGFRDNWVFVGGKG 137
PANDER_FAM3B cd13939
Pancreatic derived factor; FAM3B or PANDER (PANcreatic DERived factor) has been identifed as a ...
 112-217 2.59e-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: 2.59e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 225543554 112 VAVDGTTVLEDEAREQGRGIHVIVLNQATGHVMAKRVFDTYSPHEDEAMVLFLNMVAPGRVLICTVKDEGSFHLKDTAKA 191
Cdd:cd13939   32 ICFEDNMLITGKEGNSNRGINIAVVSYETGKVVATKYFDMYEGDFSGPMIEFINKIPKKSLVFVVTHDDGSTKLKDPAKK 111

                         90       100
                 ....*....|....*....|....*.
gi 225543554 192 LLRSLGSQAGPALGWRDTWAFVGRKG 217
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH