UniProtKB/Swiss-Prot P08637: Variant p.Phe203Ser

Low affinity immunoglobulin gamma Fc region receptor III-A
Gene: FCGR3A
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Variant information Variant position:

203 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 Phenylalanine (F) to Serine (S) at position 203 (F203S, p.Phe203Ser). 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 large size and aromatic (F) to small size and polar (S) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score:

-2 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
Variant description:

Enables membrane anchoring via glycosylphosphatidylinositol; disrupts transmembrane anchoring. Any additional useful information about the variant.
Other resources:

Links to websites of interest for the variant.

Variant rs1042206 [ dbSNP | Ensembl ]

Sequence information Variant position:

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

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

SETVNITITQGLAVSTISSF F PPGYQVSFCLVMVLLFAVDT 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                         SETVNITITQGLAVSTISSFFPPGYQVSFCLVMVLLFAVDT

Rhesus macaque                SETVNITITQDLAVSSISSFFPPGYQVSFCLVMVLLFAVDT

Mouse                         SASFRISL----GDPGSPSMFPPWHQITFCLLIGLLFAIDT

Rat                           SASLQISI----GDPTSPSSFLPWHQITFCLLIGLLFAIDT

Pig                           SEPVKVTVQGSKSPSPILSFFLPWHQIIFCLVMGFLFAVDT

Bovine                        SESVQITVQAPETLQTVSSFFLPWHQITFCLVMGVLFAVDT

Rabbit                        SETVTITV-QGPANPVISSSVLPWHQIAFCLVMGLLLAADT

Cat                           SEAVNITV-QGPPVPSTSTFLPHWYQIAFFLVTALLFVVDT

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	17 – 254	Low affinity immunoglobulin gamma Fc region receptor III-A
Topological domain	17 – 208	Extracellular
Site	222 – 222	Important for receptor turnover
Glycosylation	187 – 187	N-linked (GlcNAc...) asparagine
Mutagenesis	197 – 197	S -> P. Impairs receptor shedding. Impairs the detachment of NK cells from opsonized target cells upon sequential activation.
Mutagenesis	203 – 203	F -> P. Disrupts transmembrane anchoring.
Mutagenesis	203 – 203	F -> TYNEADK. Enables membrane anchoring via glycosylphosphatidylinositol. Disrupts transmembrane anchoring.
Mutagenesis	203 – 203	F -> VIL. Enables only transmembrane anchoring.
Mutagenesis	208 – 208	Q -> A. Decreases the association with either CD247 or FCER1G.
Mutagenesis	210 – 210	S -> A. Has no effect on complex association with CD247 or FCER1G. Decreases cell surface expression; when associated with A-211 and A-212.
Mutagenesis	211 – 211	F -> A. Decreases the association with either CD247 or FCER1G. Decreases cell surface expression; when associated with A-210 and A-212.
Mutagenesis	212 – 212	C -> A. Has no effect on complex formation with CD247 or FCER1G. Decreases cell surface expression; when associated with A-210 and A-211.
Mutagenesis	219 – 219	F -> A. Decreases the association with either CD247 or FCER1G. Decreases cell surface expression.
Mutagenesis	222 – 222	D -> A. Decreases the association with either CD247 or FCER1G. Strongly increases cell surface expression.
Mutagenesis	222 – 222	D -> EK. Strongly decreases complex formation with CD247 or FCER1G.
Mutagenesis	222 – 222	D -> N. Has little effect on complex formation with CD247 or FCER1G.
Mutagenesis	223 – 223	T -> A. Decreases the association with either CD247 or FCER1G. Decreases cell surface expression.

Literature citations
Analysis of Fc gamma RIII (CD16) membrane expression and association with CD3 zeta and Fc epsilon RI-gamma by site-directed mutation.
Lanier L.L.; Yu G.; Phillips J.H.;
J. Immunol. 146:1571-1576(1991)
Cited for: FUNCTION; SUBUNIT; INTERACTION WITH CD247 AND FCER1G; SUBCELLULAR LOCATION; MUTAGENESIS OF PHE-203; VARIANT SER-203;

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.