glycosyltransferase family 13 protein catalyzes the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds; glycosyltransferase family protein
GT13_GLCNAC-TI is involved in an essential step in the synthesis of complex or hybrid-type ...
296-623
1.52e-180
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: 514.96 E-value: 1.52e-180
PANDER-like domain of N-acetylglucosaminyltransferases; O-linked-mannose beta-1, ...
94-241
7.29e-93
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: 283.42 E-value: 7.29e-93
GT13_GLCNAC-TI is involved in an essential step in the synthesis of complex or hybrid-type ...
296-623
1.52e-180
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: 514.96 E-value: 1.52e-180
PANDER-like domain of N-acetylglucosaminyltransferases; O-linked-mannose beta-1, ...
94-241
7.29e-93
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: 283.42 E-value: 7.29e-93
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: 170.86 E-value: 9.44e-47
Interleukin-like EMT inducer; ILEI is a family of proteins found in vertebrates. It is heavily ...
124-212
2.30e-26
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: 103.11 E-value: 2.30e-26
GT13_GLCNAC-TI is involved in an essential step in the synthesis of complex or hybrid-type ...
296-623
1.52e-180
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: 514.96 E-value: 1.52e-180
PANDER-like domain of N-acetylglucosaminyltransferases; O-linked-mannose beta-1, ...
94-241
7.29e-93
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: 283.42 E-value: 7.29e-93
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: 170.86 E-value: 9.44e-47
Domains similar to the Pancreatic-derived factor; FAM3B or PANDER (PANcreatic DERived factor) ...
94-241
4.61e-37
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: 135.16 E-value: 4.61e-37
Interleukin-like EMT inducer; ILEI is a family of proteins found in vertebrates. It is heavily ...
124-212
2.30e-26
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: 103.11 E-value: 2.30e-26
PANDER-like domain of the transmembrane protein TMEM2; TMEM2 has been characterized as a ...
117-220
1.10e-14
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: 72.36 E-value: 1.10e-14
Interleukin-like EMT inducer; The secreted factor FAM3C or ILEI (InterLeukin-like Emt Inducer) ...
107-223
6.33e-14
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: 69.99 E-value: 6.33e-14
Pancreatic derived factor; FAM3B or PANDER (PANcreatic DERived factor) has been identifed as a ...
115-215
5.59e-13
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: 67.64 E-value: 5.59e-13
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.
of the residues that compose this conserved feature have been mapped to the query sequence.
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Functional characterization of the conserved domain architecture found on the query.
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This image shows a graphical summary of conserved domains identified on the query sequence.
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if a domain or superfamily has been annotated with functional sites (conserved features),
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click on the bars or triangles to view your query sequence embedded in a multiple sequence alignment of the proteins used to develop the corresponding domain model.
The table lists conserved domains identified on the query sequence. Click on the plus sign (+) on the left to display full descriptions, alignments, and scores.
Click on the domain model's accession number to view the multiple sequence alignment of the proteins used to develop the corresponding domain model.
To view your query sequence embedded in that multiple sequence alignment, click on the colored bars in the Graphical Summary portion of the search results page,
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Concise Display shows only the best scoring domain model, in each hit category listed below except non-specific hits, for each region on the query sequence.
(labeled illustration) Standard Display shows only the best scoring domain model from each source, in each hit category listed below for each region on the query sequence.
(labeled illustration) Full Display shows all domain models, in each hit category below, that meet or exceed the RPS-BLAST threshold for statistical significance.
(labeled illustration) Four types of hits can be shown, as available,
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specific hits meet or exceed a domain-specific e-value threshold
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and represent a very high confidence that the query sequence belongs to the same protein family as the sequences use to create the domain model
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the domain superfamily to which the specific and non-specific hits belong
multi-domain models that were computationally detected and are likely to contain multiple single domains
Retrieve proteins that contain one or more of the domains present in the query sequence, using the Conserved Domain Architecture Retrieval Tool
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