Q02734 (SIAT6_RAT) Reviewed, UniProtKB/Swiss-Prot
Last modified
November 16, 2011.
Version 88.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: CMP-N-acetylneuraminate-beta-1,4-galactoside alpha-2,3-sialyltransferase EC=2.4.99.6 Alternative name(s): Beta-galactoside alpha-2,3-sialyltransferase 3 Short name=Alpha 2,3-ST 3 Gal beta-1,3(4) GlcNAc alpha-2,3 sialyltransferase N-acetyllactosaminide alpha-2,3-sialyltransferase ST3Gal III Short name=ST3GalIII ST3N Sialyltransferase 6 Cleaved into the following chain: | ||||
| Gene names |
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| Organism | Rattus norvegicus (Rat) | ||||
| Taxonomic identifier | 10116 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus |
Protein attributes
| Sequence length | 374 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Catalyzes the formation of the NeuAc-alpha-2,3-Gal-beta-1,4-GlcNAc-, NeuAc-alpha-2,3-Gal-beta-1,3-GlcNAc- or NeuAc-alpha-2,3-Gal-beta-1,3-GalNAc- sequences found in terminal carbohydrate groups of glycoproteins and glycolipids. The highest activity is toward Gal-beta-1,3-GlcNAc and the lowest toward Gal-beta-1,3-GalNAc By similarity. |
| Catalytic activity | CMP-N-acetylneuraminate + beta-D-galactosyl-(1->4)-N-acetyl-D-glucosaminyl-glycoprotein = CMP + alpha-N-acetylneuraminyl-(2->3)-beta-D-galactosyl-(1->4)-N-acetyl-D-glucosaminyl-glycoprotein. |
| Pathway | |
| Subcellular location | Golgi apparatus › Golgi stack membrane; Single-pass type II membrane protein. Secreted. Note: Membrane-bound form in trans cisternae of Golgi. Secreted into the body fluid. |
| Tissue specificity | Found in all tissues tested. High expression found in brain, liver, kidney, colon, heart and lung. |
| Post-translational modification | The soluble form derives from the membrane form by proteolytic processing. |
| Sequence similarities | Belongs to the glycosyltransferase 29 family. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Golgi apparatus Membrane Secreted |
| Domain | Signal-anchor Transmembrane Transmembrane helix |
| Molecular function | Glycosyltransferase Transferase |
| PTM | Disulfide bond Glycoprotein |
| Technical term | Complete proteome Direct protein sequencing Reference proteome |
| Gene Ontology (GO) | |
| Cellular component | Golgi cisterna membrane Inferred from electronic annotation. Source: UniProtKB-SubCell extracellular regionInferred from electronic annotation. Source: UniProtKB-SubCell integral to Golgi membraneInferred from electronic annotation. Source: InterPro |
| Molecular function | N-acetyllactosaminide alpha-2,3-sialyltransferase activity Traceable author statement Ref.1. Source: RGD |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||
Molecule processing | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 374 | 374 | CMP-N-acetylneuraminate-beta-1,4-galactoside alpha-2,3-sialyltransferase | PRO_0000012143 | |||||||
| Chain | 48 – 374 | 327 | CMP-N-acetylneuraminate-beta-1,4-galactoside alpha-2,3-sialyltransferase soluble form | PRO_0000012144 | |||||||
Regions | |||||||||||
| Topological domain | 1 – 8 | 8 | Cytoplasmic Potential | ||||||||
| Transmembrane | 9 – 28 | 20 | Helical; Signal-anchor for type II membrane protein; Potential | ||||||||
| Topological domain | 29 – 374 | 346 | Lumenal Potential | ||||||||
Sites | |||||||||||
| Site | 46 – 47 | 2 | Cleavage; partial | ||||||||
Amino acid modifications | |||||||||||
| Glycosylation | 79 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 170 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Disulfide bond | 159 ↔ 313 | By similarity | |||||||||
Sequences
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References
| [1] | "Primary structure of Gal beta 1,3(4)GlcNAc alpha 2,3-sialyltransferase determined by mass spectrometry sequence analysis and molecular cloning. Evidence for a protein motif in the sialyltransferase gene family." Wen D.X., Livingston B.D., Medzihradszky K.F., Kelm S., Burlingame A.L., Paulson J.C. J. Biol. Chem. 267:21011-21019(1992) [PubMed: 1400416] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE. Tissue: Liver. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | M97754 mRNA. Translation: AAA42146.1. |
| IPI | IPI00210122. |
| PIR | A45074. |
| RefSeq | NP_113885.1. NM_031697.1. |
| UniGene | Rn.44390. |
3D structure databases | |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | Q02734. |
Protein family/group databases | |
| CAZy | GT29. Glycosyltransferase Family 29. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 64445. |
| KEGG | rno:64445. |
Organism-specific databases | |
| CTD | 6487. |
| RGD | 68414. St3gal3. |
Phylogenomic databases | |
| eggNOG | roNOG05023. |
| GeneTree | ENSGT00550000074199. |
| HOVERGEN | HBG056676. |
| InParanoid | Q02734. |
Enzyme and pathway databases | |
| BRENDA | 2.4.99.6. 5301. |
Gene expression databases | |
| ArrayExpress | Q02734. |
| Genevestigator | Q02734. |
| GermOnline | ENSRNOG00000019843. Rattus norvegicus. |
Family and domain databases | |
| InterPro | IPR001675. Glyco_trans_29. IPR012163. Sialyl_trans. [Graphical view] |
| KO | K00781. |
| Pfam | PF00777. Glyco_transf_29. 1 hit. [Graphical view] |
| PIRSF | PIRSF005557. Sialyl_trans. 1 hit. |
| ProtoNet | Search... |
Other | |
| NextBio | 613178. |
Entry information
| Entry name | SIAT6_RAT | ||||||||
| Accession | Primary (citable) accession number: Q02734 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with