Q5HZL5
Gene name |
b3gnt5-a |
Protein name |
Lactosylceramide 1,3-N-acetyl-beta-D-glucosaminyltransferase A |
Names |
Lactotriaosylceramide synthase A, Lc(3)Cer synthase A, Lc3 synthase A, UDP-GlcNAc:beta-Gal beta-1,3-N-acetylglucosaminyltransferase 5A, BGnT-5A, Beta-1,3-Gn-T5A, Beta-1,3-N-acetylglucosaminyltransferase 5A, Beta3Gn-T5A |
Species |
Xenopus laevis (African clawed frog) |
KEGG Pathway |
xla:496364 |
EC number |
2.4.1.206: Hexosyltransferases |
Protein Class |
|
Descriptions
The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.
Autoinhibitory domains (AIDs)
Target domain |
|
Relief mechanism |
|
Assay |
cis-regPred |
Accessory elements
No accessory elements
Autoinhibited structure
Activated structure
1 structures for Q5HZL5
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q5HZL5-F1 | Predicted | AlphaFoldDB |
No variants for Q5HZL5
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q5HZL5 | |||||
No associated diseases with Q5HZL5
No regional properties for Q5HZL5
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| No domain, repeats, and functional sites for Q5HZL5 | |||
Functions
| Description | ||
|---|---|---|
| EC Number | 2.4.1.206 | Hexosyltransferases |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
2 GO annotations of cellular component
| Name | Definition |
|---|---|
| Golgi membrane | The lipid bilayer surrounding any of the compartments of the Golgi apparatus. |
| integral component of membrane | The component of a membrane consisting of the gene products and protein complexes having at least some part of their peptide sequence embedded in the hydrophobic region of the membrane. |
2 GO annotations of molecular function
| Name | Definition |
|---|---|
| beta-galactosyl-N-acetylglucosaminylgalactosylglucosyl-ceramide beta-1,3-acetylglucosaminyltransferase activity | Catalysis of the reaction: UDP-N-acetyl-D-glucosamine + beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosaminyl-1,3-beta-D-galactosyl-1,4-beta-D-glucosylceramide = UDP + N-acetyl-D-glucosaminyl-1,3-beta-D-galactosyl-1,4-N-acetyl-beta-D-glucosaminyl-1,3-beta-D-galactosyl-1,4-beta-D-glucosylceramide. |
| lactosylceramide 1,3-N-acetyl-beta-D-glucosaminyltransferase activity | Catalysis of the reaction: cytolipin-H + UDP-N-acetyl-D-glucosamine = N-acetyl-D-glucosaminyl-1,3-beta-D-galactosyl-1,4-beta-D-glucosylceramide + UDP. |
1 GO annotations of biological process
| Name | Definition |
|---|---|
| protein glycosylation | A protein modification process that results in the addition of a carbohydrate or carbohydrate derivative unit to a protein amino acid, e.g. the addition of glycan chains to proteins. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MLISARRLRR | CQFLQLLASC | FVLSLMALLV | QEDNSLISHV | KSYSYRYLIN | SYDFVNVSLS |
| 70 | 80 | 90 | 100 | 110 | 120 |
| IPRDRLDGAA | SYRYLLNNRH | ICLNEDVLLL | LFVKTAPENR | RRRDAIRNTW | GNEDFIRSQY |
| 130 | 140 | 150 | 160 | 170 | 180 |
| DANIKVVFAL | GAEGDPVKSR | EIQQDLVNEN | KRFKDLIQQD | FSDTFHNLTL | KLLLQFGWVN |
| 190 | 200 | 210 | 220 | 230 | 240 |
| SFCPSAKFIM | SADDDIFVHT | PNLVSYLKSL | PIETQDFWIG | RVHRGSPPIR | RKTSKYYVPY |
| 250 | 260 | 270 | 280 | 290 | 300 |
| EMYPWSSYPD | YTAGAAYVVS | RDVAAKVYEA | SQTLNTSLYI | DDVFMGICAN | KMGLVPQYHV |
| 310 | 320 | 330 | 340 | 350 | 360 |
| FFSGEGKSPY | HPCIYNKMMT | SHGHLDDLDY | LWRQAIDPNV | KSISSGFWGN | LYCRFVNIML |
| 370 | |||||
| LCRISYVDTY | PCSAAWS |