Home  |  Contact

UniProtKB/Swiss-Prot P27918: Variant p.Cys32Tyr

Properdin
Gene: CFP
Variant information

Variant position:  32
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Type of variant:  LP/P [Disclaimer]
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 Cysteine (C) to Tyrosine (Y) at position 32 (C32Y, p.Cys32Tyr).
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 (C) to large size and aromatic (Y)
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:  In PFD; type II; inhibits secretion and oligomerization.
Any additional useful information about the variant.



Sequence information

Variant position:  32
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Protein sequence length:  469
The length of the canonical sequence.

Location on the sequence:   LLPPLLLLLTLPATGSDPVL  C FTQYEESSGKCKGLLGGGVS
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                         LLPPLLLLLTLPATGSDPVLCFTQYEESSGKCKGLLGGGVS

Mouse                         L---LLLLVILPATGSDPVLCFTQYEESSGRCKGLLGRDIR

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 28 – 469 Properdin
Domain 28 – 76 TSP type-1 0
Disulfide bond 32 – 56
Mutagenesis 47 – 47 L -> A. Inhibits oligomerization; when associated with A-58 and A-275.
Beta strand 30 – 37


Literature citations

Structural Basis for Properdin Oligomerization and Convertase Stimulation in the Human Complement System.
Pedersen D.V.; Gadeberg T.A.F.; Thomas C.; Wang Y.; Joram N.; Jensen R.K.; Mazarakis S.M.M.; Revel M.; El Sissy C.; Petersen S.V.; Lindorff-Larsen K.; Thiel S.; Laursen N.S.; Fremeaux-Bacchi V.; Andersen G.R.;
Front. Immunol. 10:2007-2007(2019)
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 28-191 AND 256-469 IN COMPLEX WITH COMPLEMENT C3 BETA CHAIN; COMPLEMENT FACTOR B BB FRAGMENT AND STAPHYLOCOCCUS AUREUS PROTEIN SCN; IDENTIFICATION BY MASS SPECTROMETRY; FUNCTION; SUBUNIT; INTERACTION WITH COMPLEMENT C3 BETA CHAIN AND COMPLEMENT FACTOR B BB FRAGMENT; SUBCELLULAR LOCATION; DOMAIN; GLYCOSYLATION AT TRP-83; TRP-86; THR-92; TRP-139; TRP-142; TRP-145; THR-151; TRP-196; TRP-199; TRP-202; SER-208; TRP-260; TRP-263; THR-272; TRP-321; TRP-324; TRP-382; TRP-385 AND TRP-388; DISULFIDE BOND; VARIANT PFD TYR-32; CHARACTERIZATION OF VARIANTS PFD TYR-32; ARG-343 AND ASP-414; MUTAGENESIS OF LEU-47; LEU-58; GLU-244; LEU-275; ARG-329; ARG-330; ARG-351; ARG-353; ARG-359; 364-GLN-GLN-365 AND LEU-456;

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.