Q86SR1 · GLT10_HUMAN
- ProteinPolypeptide N-acetylgalactosaminyltransferase 10
- GeneGALNT10
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids603 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. Has activity toward Muc5Ac and EA2 peptide substrates.
Catalytic activity
- L-seryl-[protein] + UDP-N-acetyl-alpha-D-galactosamine = 3-O-[N-acetyl-alpha-D-galactosaminyl]-L-seryl-[protein] + H+ + UDP
Cofactor
Pathway
Protein modification; protein glycosylation.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 154 | substrate | ||||
Sequence: H | ||||||
Binding site | 156 | substrate | ||||
Sequence: E | ||||||
Binding site | 185 | substrate | ||||
Sequence: D | ||||||
Binding site | 214 | substrate | ||||
Sequence: R | ||||||
Binding site | 237 | Mn2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 238 | substrate | ||||
Sequence: S | ||||||
Binding site | 239 | Mn2+ (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 342 | substrate | ||||
Sequence: W | ||||||
Binding site | 370 | Mn2+ (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 373 | substrate | ||||
Sequence: R | ||||||
Binding site | 378 | substrate | ||||
Sequence: Y |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | Golgi apparatus | |
Cellular Component | Golgi membrane | |
Molecular Function | carbohydrate binding | |
Molecular Function | metal ion binding | |
Molecular Function | polypeptide N-acetylgalactosaminyltransferase activity | |
Biological Process | O-glycan processing | |
Biological Process | protein O-linked glycosylation |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended namePolypeptide N-acetylgalactosaminyltransferase 10
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ86SR1
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Golgi apparatus membrane ; Single-pass type II membrane protein
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-11 | Cytoplasmic | ||||
Sequence: MRRKEKRLLQA | ||||||
Transmembrane | 12-31 | Helical; Signal-anchor for type II membrane protein | ||||
Sequence: VALVLAALVLLPNVGLWALY | ||||||
Topological domain | 32-603 | Lumenal | ||||
Sequence: RERQPDGTPGGSGAAVAPAAGQGSHSRQKKTFFLGDGQKLKDWHDKEAIRRDAQRVGNGEQGRPYPMTDAERVDQAYRENGFNIYVSDKISLNRSLPDIRHPNCNSKRYLETLPNTSIIIPFHNEGWSSLLRTVHSVLNRSPPELVAEIVLVDDFSDREHLKKPLEDYMALFPSVRILRTKKREGLIRTRMLGASVATGDVITFLDSHCEANVNWLPPLLDRIARNRKTIVCPMIDVIDHDDFRYETQAGDAMRGAFDWEMYYKRIPIPPELQKADPSDPFESPVMAGGLFAVDRKWFWELGGYDPGLEIWGGEQYEISFKVWMCGGRMEDIPCSRVGHIYRKYVPYKVPAGVSLARNLKRVAEVWMDEYAEYIYQRRPEYRHLSAGDVAVQKKLRSSLNCKSFKWFMTKIAWDLPKFYPPVEPPAAAWGEIRNVGTGLCADTKHGALGSPLRLEGCVRGRGEAAWNNMQVFTFTWREDIRPGDPQHTKKFCFDAISHTSPVTLYDCHSMKGNQLWKYRKDKTLYHPVSGSCMDCSESDHRIFMNTCNPSSLTQQWLFEHTNSTVLEKFNRN |
Keywords
- Cellular component
Disease & Variants
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 634 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for chain, glycosylation, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000059122 | 1-603 | Polypeptide N-acetylgalactosaminyltransferase 10 | |||
Sequence: MRRKEKRLLQAVALVLAALVLLPNVGLWALYRERQPDGTPGGSGAAVAPAAGQGSHSRQKKTFFLGDGQKLKDWHDKEAIRRDAQRVGNGEQGRPYPMTDAERVDQAYRENGFNIYVSDKISLNRSLPDIRHPNCNSKRYLETLPNTSIIIPFHNEGWSSLLRTVHSVLNRSPPELVAEIVLVDDFSDREHLKKPLEDYMALFPSVRILRTKKREGLIRTRMLGASVATGDVITFLDSHCEANVNWLPPLLDRIARNRKTIVCPMIDVIDHDDFRYETQAGDAMRGAFDWEMYYKRIPIPPELQKADPSDPFESPVMAGGLFAVDRKWFWELGGYDPGLEIWGGEQYEISFKVWMCGGRMEDIPCSRVGHIYRKYVPYKVPAGVSLARNLKRVAEVWMDEYAEYIYQRRPEYRHLSAGDVAVQKKLRSSLNCKSFKWFMTKIAWDLPKFYPPVEPPAAAWGEIRNVGTGLCADTKHGALGSPLRLEGCVRGRGEAAWNNMQVFTFTWREDIRPGDPQHTKKFCFDAISHTSPVTLYDCHSMKGNQLWKYRKDKTLYHPVSGSCMDCSESDHRIFMNTCNPSSLTQQWLFEHTNSTVLEKFNRN | ||||||
Glycosylation | 124 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 135↔365 | |||||
Sequence: CNSKRYLETLPNTSIIIPFHNEGWSSLLRTVHSVLNRSPPELVAEIVLVDDFSDREHLKKPLEDYMALFPSVRILRTKKREGLIRTRMLGASVATGDVITFLDSHCEANVNWLPPLLDRIARNRKTIVCPMIDVIDHDDFRYETQAGDAMRGAFDWEMYYKRIPIPPELQKADPSDPFESPVMAGGLFAVDRKWFWELGGYDPGLEIWGGEQYEISFKVWMCGGRMEDIPC | ||||||
Glycosylation | 146 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 356↔432 | |||||
Sequence: CGGRMEDIPCSRVGHIYRKYVPYKVPAGVSLARNLKRVAEVWMDEYAEYIYQRRPEYRHLSAGDVAVQKKLRSSLNC | ||||||
Disulfide bond | 471↔488 | |||||
Sequence: CADTKHGALGSPLRLEGC | ||||||
Disulfide bond | 523↔538 | |||||
Sequence: CFDAISHTSPVTLYDC | ||||||
Disulfide bond | 563↔578 | |||||
Sequence: CMDCSESDHRIFMNTC | ||||||
Glycosylation | 593 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Widely expressed. Expressed at high level in small intestine, and at intermediate levels in stomach, pancreas, ovary, thyroid gland and spleen. Weakly expressed in other tissues.
Gene expression databases
Organism-specific databases
Structure
Family & Domains
Features
Showing features for region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 38-59 | Disordered | ||||
Sequence: GTPGGSGAAVAPAAGQGSHSRQ | ||||||
Region | 144-253 | Catalytic subdomain A | ||||
Sequence: LPNTSIIIPFHNEGWSSLLRTVHSVLNRSPPELVAEIVLVDDFSDREHLKKPLEDYMALFPSVRILRTKKREGLIRTRMLGASVATGDVITFLDSHCEANVNWLPPLLDR | ||||||
Region | 311-373 | Catalytic subdomain B | ||||
Sequence: PFESPVMAGGLFAVDRKWFWELGGYDPGLEIWGGEQYEISFKVWMCGGRMEDIPCSRVGHIYR | ||||||
Region | 373-384 | Flexible loop | ||||
Sequence: RKYVPYKVPAGV | ||||||
Domain | 458-590 | Ricin B-type lectin | ||||
Sequence: AAWGEIRNVGTGLCADTKHGALGSPLRLEGCVRGRGEAAWNNMQVFTFTWREDIRPGDPQHTKKFCFDAISHTSPVTLYDCHSMKGNQLWKYRKDKTLYHPVSGSCMDCSESDHRIFMNTCNPSSLTQQWLFE |
Domain
There are two conserved domains in the glycosyltransferase region: the N-terminal domain (domain A, also called GT1 motif), which is probably involved in manganese coordination and substrate binding and the C-terminal domain (domain B, also called Gal/GalNAc-T motif), which is probably involved in catalytic reaction and UDP-Gal binding.
The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity.
Sequence similarities
Belongs to the glycosyltransferase 2 family. GalNAc-T subfamily.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 4 isoforms produced by Alternative splicing.
Q86SR1-1
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
- Length603
- Mass (Da)68,992
- Last updated2004-08-16 v2
- ChecksumEE176F6139B92573
Q86SR1-2
- Name2
- Differences from canonical
- 190-251: Missing
Q86SR1-3
- Name3
Q86SR1-4
- Name4
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
F2Z2M7 | F2Z2M7_HUMAN | GALNT10 | 202 |
Sequence caution
Features
Showing features for alternative sequence, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_011207 | 1-329 | in isoform 4 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_011209 | 190-251 | in isoform 2 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_011208 | 330-352 | in isoform 4 | |||
Sequence: WELGGYDPGLEIWGGEQYEISFK → MLAWRDGELEAETSSSLFLLAMQ | ||||||
Alternative sequence | VSP_011212 | 354-366 | in isoform 3 | |||
Sequence: WMCGGRMEDIPCS → SQLSRRPVLGTAS | ||||||
Alternative sequence | VSP_011213 | 367-603 | in isoform 3 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_011214 | 389 | in isoform 4 | |||
Sequence: N → VRT | ||||||
Sequence conflict | 518 | in Ref. 1; BAC56890 and 3; BAB14676 | ||||
Sequence: H → Y |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AB078145 EMBL· GenBank· DDBJ | BAC56890.1 EMBL· GenBank· DDBJ | mRNA | ||
AJ505950 EMBL· GenBank· DDBJ | CAD44532.1 EMBL· GenBank· DDBJ | mRNA | ||
AK023782 EMBL· GenBank· DDBJ | BAB14676.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AK127135 EMBL· GenBank· DDBJ | BAG54441.1 EMBL· GenBank· DDBJ | mRNA | ||
AL096739 EMBL· GenBank· DDBJ | CAB46378.1 EMBL· GenBank· DDBJ | mRNA | ||
AK074132 EMBL· GenBank· DDBJ | BAB84958.1 EMBL· GenBank· DDBJ | mRNA | ||
BC007224 EMBL· GenBank· DDBJ | AAH07224.2 EMBL· GenBank· DDBJ | mRNA | ||
BC072450 EMBL· GenBank· DDBJ | AAH72450.1 EMBL· GenBank· DDBJ | mRNA |