UniProtKB/Swiss-Prot Q9Y231: Variant p.Thr237Ala

4-galactosyl-N-acetylglucosaminide 3-alpha-L-fucosyltransferase 9
Gene: FUT9
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Variant information Variant position:

237 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Type of variant:

LB/B The variants are classified into three categories: LP/P, LB/B and US.

LP/P: likely pathogenic or pathogenic.
LB/B: likely benign or benign.
US: uncertain significance

Residue change:

From Threonine (T) to Alanine (A) at position 237 (T237A, p.Thr237Ala). Indicates the amino acid change of the variant. The one-letter and three-letter codes for amino acids used in UniProtKB/Swiss-Prot are those adopted by the commission on Biochemical Nomenclature of the IUPAC-IUB.
Physico-chemical properties:

Change from medium size and polar (T) to small size and hydrophobic (A) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score:

0 The score within a Blosum matrix for the corresponding wild-type to variant amino acid change. The log-odds score measures the logarithm for the ratio of the likelihood of two amino acids appearing by chance. The Blosum62 substitution matrix is used. This substitution matrix contains scores for all possible exchanges of one amino acid with another:

Lowest score: -4 (low probability of substitution).
Highest score: 11 (high probability of substitution).

More information can be found on the following page
Other resources:

Links to websites of interest for the variant.

Variant rs3811069 [ dbSNP | Ensembl ]

Sequence information Variant position:

237 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length:

359 The length of the canonical sequence.
Location on the sequence:

TYGQAFGEYVNDKNLIPTIS T CKFYLSFENSIHKDYITEKL The residue change on the sequence. Unless the variant is located at the beginning or at the end of the protein sequence, both residues upstream (20) and downstream (20) of the variant will be shown.
Residue conservation:

The multiple alignment of the region surrounding the variant against various orthologous sequences.

Human                         TYGQAFGEYVNDKNLIPTISTCKFYLSFENSIHKDYITEKL

                              TYGQAFGEYVNDKNLIPTISTCKFYLSFENSIHKDYITEKL

Chimpanzee                    TYGQAFGEYVNDKNLIPTISTCKFYLSFENSIHKDYITEKL

Mouse                         TYGQAFGEYVNDKNLIPTISTCKFYLSFENSIHKDYITEKL

Rat                           TYGQAFGEYVNDKNLIPTISTCKFYLSFENSIHKDYITEKL

Bovine                        TYGQAFGEYVTDKNLIPTISTCKFYLSFENSIHKDYITEKL

Sequence annotation in neighborhood:

The regions or sites of interest surrounding the variant. In general the features listed are posttranslational modifications, binding sites, enzyme active sites, local secondary structure or other characteristics reported in the cited references. The "Sequence annotation in neighborhood" lines have a fixed format:

Type: the type of sequence feature.
Positions: endpoints of the sequence feature.
Description: contains additional information about the feature.

Type	Positions	Description
Chain	1 – 359	4-galactosyl-N-acetylglucosaminide 3-alpha-L-fucosyltransferase 9
Topological domain	33 – 359	Lumenal
Region	169 – 326	Donor-binding
Binding site	226 – 226
Binding site	241 – 241
Binding site	246 – 246
Binding site	252 – 252
Binding site	255 – 255
Binding site	256 – 256
Disulfide bond	82 – 335
Disulfide bond	91 – 338
Disulfide bond	190 – 238
Mutagenesis	228 – 228	D -> A. Decreases catalytic efficiency toward GDP-beta-L-fucose, LNnT and H-type 2 LacNAc by 39-fold, 9-fold and 25-fold, respectively.
Mutagenesis	228 – 228	D -> K. Decreases catalytic efficiency toward GDP-beta-L-fucose, LNnT and H-type 2 LacNAc by 19-fold, 3-fold and 19-fold, respectively.
Mutagenesis	241 – 241	Y -> A. Decreases expression.
Mutagenesis	246 – 246	N -> A. Decreases catalytic efficiency toward GDP-beta-L-fucose, LNnT and H-type 2 LacNAc by 70-fold, 30-fold and 109-fold, respectively.
Mutagenesis	252 – 252	Y -> A. Decreases expression.
Mutagenesis	254 – 254	T -> A. Decreases catalytic efficiency toward LNnT and H-type 2 LacNAc by 270-fold and 394-fold, respectively.
Mutagenesis	255 – 255	E -> A. Decreases catalytic efficiency toward GDP-beta-L-fucose, LNnT and H-type 2 LacNAc by 288-fold, 112-fold and 367-fold, respectively.
Mutagenesis	256 – 256	K -> A. Complete loss of alpha 1,3-fucosyltransferase activity toward LNnT and H-type 2 LacNAc.

Literature citations
Alpha-1,3-fucosyltransferase IX (Fuc-TIX) is very highly conserved between human and mouse; molecular cloning, characterization and tissue distribution of human Fuc-TIX.
Kaneko M.; Kudo T.; Iwasaki H.; Ikehara Y.; Nishihara S.; Nakagawa S.; Sasaki K.; Shiina T.; Inoko H.; Saitou N.; Narimatsu H.;
FEBS Lett. 452:237-242(1999)
Cited for: NUCLEOTIDE SEQUENCE [MRNA]; FUNCTION; TISSUE SPECIFICITY; VARIANT ALA-237; FUT4 and FUT9 genes are expressed early in human embryogenesis.
Cailleau-Thomas A.; Coullin P.; Candelier J.J.; Balanzino L.; Oriol R.; Mollicone R.; Mennesson B.;
Glycobiology 10:789-802(2000)
Cited for: NUCLEOTIDE SEQUENCE [MRNA]; VARIANT ALA-237; The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).
The MGC Project Team;
Genome Res. 14:2121-2127(2004)
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]; VARIANT ALA-237;

Disclaimer: Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. They are not in any way intended to be used as a substitute for professional medical advice, diagnostic, treatment or care.