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UniProtKB/Swiss-Prot P08637: Variant p.Phe203Ser

Low affinity immunoglobulin gamma Fc region receptor III-A
Gene: FCGR3A
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.



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.

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.

TypePositionsDescription
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.