Q6E279 · RRT3_ARATH
- ProteinRhamnogalacturonan I rhamnosyltransferase 4
- GeneRRT3
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids481 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
Function
function
Glycosyltransferase involved in the formation of rhamnogalacturonan I (RG-I) oligosaccharides in the seed coat mucilage, which is a specialized cell wall with abundant RG-I (By similarity).
Transfers the rhamnose residue from UDP-beta-L-rhamnose to RG-I oligosaccharides (PubMed:30082766).
Transfers the rhamnose residue from UDP-beta-L-rhamnose to RG-I oligosaccharides (PubMed:30082766).
Catalytic activity
- alpha-D-galacturonosyl-[(1->2)-alpha-L-rhamnosyl-(1->4)-alpha-D-galacturonosyl](n) + UDP-beta-L-rhamnose = [(1->2)-alpha-L-rhamnosyl-(1->4)-alpha-D-galacturonosyl](n+1) + H+ + UDP
α-D-galacturonosyl-[(1→2)-α-L-rhamnosyl-(1→4)-α-D-galacturonosyl](n) RHEA-COMP:14274 + CHEBI:83836 = [(1→2)-α-L-rhamnosyl-(1→4)-α-D-galacturonosyl](n+1) RHEA-COMP:14276 + CHEBI:15378 + CHEBI:58223
Pathway
Glycan metabolism; pectin biosynthesis.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 258-260 | substrate | ||||
Sequence: HLR |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | chloroplast | |
Cellular Component | Golgi membrane | |
Molecular Function | glycosyltransferase activity | |
Biological Process | cell wall organization | |
Biological Process | fucose metabolic process | |
Biological Process | pectin biosynthetic process |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameRhamnogalacturonan I rhamnosyltransferase 4
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > malvids > Brassicales > Brassicaceae > Camelineae > Arabidopsis
Accessions
- Primary accessionQ6E279
- Secondary accessions
Proteomes
Organism-specific databases
Genome annotation databases
Subcellular Location
UniProt Annotation
GO Annotation
Golgi apparatus membrane ; Single-pass type II membrane protein
Features
Showing features for transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transmembrane | 33-55 | Helical; Signal-anchor for type II membrane protein | ||||
Sequence: VWFFRVCSCILVWTCLIQLFWHS |
Keywords
- Cellular component
PTM/Processing
Features
Showing features for chain, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000442080 | 1-481 | Rhamnogalacturonan I rhamnosyltransferase 4 | |||
Sequence: MSVVVGDRSESTLMRSDYKAPPSQAIPKARLQVWFFRVCSCILVWTCLIQLFWHSQIFTGLTNHISRFSLPVQSVPLPPPLPPRNYTSNGILLVSCNGGLNQMRAAICDMVTVARLLNLTLVVPELDKKSFWADTSDFEDIFDIKHFIDSLRDEVRIIRRLPKRYSKKYGFKLFEMPPVSWSNDKYYLQQVLPRFSKRKVIHFVRSDTRLANNGLSLDLQRLRCRVNFQGLRFTPRIEALGSKLVRILQQRGSFVALHLRYEMDMLAFSGCTHGCTDEEAEELKKMRYAYPWWREKEIVSEERRVQGLCPLTPEEAVLVLKALGFQKDTQIYIAAGEIFGGAKRLALLKESFPRIVKKEMLLDPTELQQFQNHSSQMAALDFIVSVASNTFIPTYYGNMAKVVEGHRRYLGFKKTILLDRKRLVELLDLHNNKTLSWDQFAVAVKDAHQGRRMGEPTHRKVISVRPKEEDYFYANPQECIS | ||||||
Glycosylation | 85 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 118 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 372 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 432 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Gene expression databases
Interaction
Protein-protein interaction databases
Structure
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
Q6E279-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- Length481
- Mass (Da)55,631
- Last updated2004-08-16 v1
- Checksum6C43190B50E75F16
Q6E279-2
- Name2
- Differences from canonical
- 135-135: T → TRYMFVSHVNDPTRFVCSLKHSFVSSFY
Sequence caution
Features
Showing features for sequence conflict, alternative sequence.
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
KY906056 EMBL· GenBank· DDBJ | ARJ31420.1 EMBL· GenBank· DDBJ | mRNA | ||
AC005313 EMBL· GenBank· DDBJ | AAM15036.1 EMBL· GenBank· DDBJ | Genomic DNA | Sequence problems. | |
AC006284 EMBL· GenBank· DDBJ | AAD17446.1 EMBL· GenBank· DDBJ | Genomic DNA | Sequence problems. | |
CP002685 EMBL· GenBank· DDBJ | AEC05682.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CP002685 EMBL· GenBank· DDBJ | AEC05683.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BT002839 EMBL· GenBank· DDBJ | AAO22658.1 EMBL· GenBank· DDBJ | mRNA | ||
AY600544 EMBL· GenBank· DDBJ | AAT68343.1 EMBL· GenBank· DDBJ | mRNA | ||
AY924736 EMBL· GenBank· DDBJ | AAX23811.1 EMBL· GenBank· DDBJ | mRNA | ||
AY600545 EMBL· GenBank· DDBJ | AAT68344.1 EMBL· GenBank· DDBJ | mRNA |