Q8NBJ5 · GT251_HUMAN
- ProteinProcollagen galactosyltransferase 1
- GeneCOLGALT1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids622 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Beta-galactosyltransferase that transfers beta-galactose to hydroxylysine residues of type I collagen (PubMed:19075007, PubMed:22216269, PubMed:27402836).
By acting on collagen glycosylation, facilitates the formation of collagen triple helix (PubMed:27402836).
Also involved in the biosynthesis of collagen type IV (PubMed:30412317).
By acting on collagen glycosylation, facilitates the formation of collagen triple helix (PubMed:27402836).
Also involved in the biosynthesis of collagen type IV (PubMed:30412317).
Catalytic activity
- (5R)-5-hydroxy-L-lysyl-[collagen] + UDP-alpha-D-galactose = (5R)-5-O-(beta-D-galactosyl)-5-hydroxy-L-lysyl-[collagen] + H+ + UDP
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
18.7 μM | UDP-galactose | 7.4 | 37 | |||
29.9 μM | UDP-galactose | 7.4 | 37 |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | endoplasmic reticulum lumen | |
Cellular Component | membrane | |
Molecular Function | procollagen galactosyltransferase activity | |
Biological Process | collagen fibril organization | |
Biological Process | positive regulation of collagen fibril organization |
Keywords
- Molecular function
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameProcollagen galactosyltransferase 1
- 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 accessionQ8NBJ5
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Colocalized with PLOD3 and mannose binding lectin/MBL2.
Keywords
- Cellular component
Disease & Variants
Involvement in disease
Brain small vessel disease 3 (BSVD3)
- Note
- DescriptionAn autosomal recessive form of brain small vessel disease, a cerebrovascular disorder with variable manifestations reflecting the location and severity of the vascular defect. BSVD3 patients may have disease onset in utero or early infancy with subsequent global developmental delay, spasticity, and porencephaly on brain imaging. Other patients may have normal or mildly delayed development with sudden onset of intracranial hemorrhage causing acute neurologic deterioration.
- See alsoMIM:618360
Natural variants in BSVD3
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_081752 | 151 | L>R | in BSVD3; loss of galactosyltransferase activity; dbSNP:rs1478523191 | |
VAR_081753 | 154 | A>P | in BSVD3; dbSNP:rs181844791 | |
VAR_081754 | 377 | G>R | in BSVD3; dbSNP:rs1568481244 |
Features
Showing features for natural variant, mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_081752 | 151 | in BSVD3; loss of galactosyltransferase activity; dbSNP:rs1478523191 | |||
Sequence: L → R | ||||||
Natural variant | VAR_081753 | 154 | in BSVD3; dbSNP:rs181844791 | |||
Sequence: A → P | ||||||
Mutagenesis | 166 | Loss of galactosyltransferase activity; when associated with A-168. | ||||
Sequence: D → A | ||||||
Mutagenesis | 168 | Loss of galactosyltransferase activity; when associated with A-166. | ||||
Sequence: D → A | ||||||
Mutagenesis | 292 | Small decrease of galactosyltransferase activity. | ||||
Sequence: P → N | ||||||
Mutagenesis | 336 | Small decrease of galactosyltransferase activity. | ||||
Sequence: D → S | ||||||
Natural variant | VAR_081754 | 377 | in BSVD3; dbSNP:rs1568481244 | |||
Sequence: G → R | ||||||
Mutagenesis | 461 | Loss of galactosyltransferase activity; when associated with A-463. | ||||
Sequence: D → A | ||||||
Mutagenesis | 463 | Loss of galactosyltransferase activity; when associated with A-461. | ||||
Sequence: D → A | ||||||
Mutagenesis | 585 | No effect on galactosyltransferase activity; when associated with A-587. | ||||
Sequence: D → A | ||||||
Mutagenesis | 587 | No effect on galactosyltransferase activity; when associated with A-585. | ||||
Sequence: D → A |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 789 variants from UniProt as well as other sources including ClinVar and dbSNP.
Keywords
- Disease
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for signal, chain, glycosylation, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Signal | 1-29 | UniProt | |||||
Sequence: MAAAPRAGRRRGQPLLALLLLLLAPLPPG | |||||||
Chain | PRO_0000309536 | 30-622 | UniProt | Procollagen galactosyltransferase 1 | |||
Sequence: APPGADAYFPEERWSPESPLQAPRVLIALLARNAAHALPTTLGALERLRHPRERTALWVATDHNMDNTSTVLREWLVAVKSLYHSVEWRPAEEPRSYPDEEGPKHWSDSRYEHVMKLRQAALKSARDMWADYILFVDADNLILNPDTLSLLIAENKTVVAPMLDSRAAYSNFWCGMTSQGYYKRTPAYIPIRKRDRRGCFAVPMVHSTFLIDLRKAASRNLAFYPPHPDYTWSFDDIIVFAFSCKQAEVQMYVCNKEEYGFLPVPLRAHSTLQDEAESFMHVQLEVMVKHPPAEPSRFISAPTKTPDKMGFDEVFMINLRRRQDRRERMLRALQAQEIECRLVEAVDGKAMNTSQVEALGIQMLPGYRDPYHGRPLTKGELGCFLSHYNIWKEVVDRGLQKSLVFEDDLRFEIFFKRRLMNLMRDVEREGLDWDLIYVGRKRMQVEHPEKAVPRVRNLVEADYSYWTLAYVISLQGARKLLAAEPLSKMLPVDEFLPVMFDKHPVSEYKAHFSLRNLHAFSVEPLLIYPTHYTGDDGYVSDTETSVVWNNEHVKTDWDRAKSQKMREQQALSREAKNSDVLQSPLDSAARDEL | |||||||
Glycosylation | 96 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Glycosylation | 184 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Glycosylation | 381 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Modified residue (large scale data) | 612 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 616 | PRIDE | Phosphoserine | ||||
Sequence: S |
Post-translational modification
N-glycosylated.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Ubiquitous with higher levels in placenta, heart, lung and spleen.
Gene expression databases
Organism-specific databases
Structure
Family & Domains
Features
Showing features for compositional bias, region, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 588-602 | Basic and acidic residues | ||||
Sequence: RAKSQKMREQQALSR | ||||||
Region | 588-622 | Disordered | ||||
Sequence: RAKSQKMREQQALSREAKNSDVLQSPLDSAARDEL | ||||||
Motif | 619-622 | Endoplasmic reticulum retention motif | ||||
Sequence: RDEL |
Sequence similarities
Belongs to the glycosyltransferase 25 family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length622
- Mass (Da)71,636
- Last updated2002-10-01 v1
- ChecksumC430974CB1CF5280
Computationally mapped potential isoform sequences
There are 3 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A8I5QL08 | A0A8I5QL08_HUMAN | COLGALT1 | 315 | ||
A0A8I5QKL8 | A0A8I5QKL8_HUMAN | COLGALT1 | 282 | ||
M0QX72 | M0QX72_HUMAN | COLGALT1 | 460 |
Features
Showing features for sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 100 | in Ref. 1; BAC11307 | ||||
Sequence: V → E | ||||||
Sequence conflict | 220 | in Ref. 1; BAC11307 | ||||
Sequence: I → T | ||||||
Compositional bias | 588-602 | Basic and acidic residues | ||||
Sequence: RAKSQKMREQQALSR |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AK074941 EMBL· GenBank· DDBJ | BAC11307.1 EMBL· GenBank· DDBJ | mRNA | ||
AK075541 EMBL· GenBank· DDBJ | BAC11684.1 EMBL· GenBank· DDBJ | mRNA | ||
AC010618 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471106 EMBL· GenBank· DDBJ | EAW84622.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC108308 EMBL· GenBank· DDBJ | AAI08309.1 EMBL· GenBank· DDBJ | mRNA |