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:
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 LLPPLLLLLTLPATGSDPVL CFTQYEESSGKCKGLLGGGVS
Mouse L---LLLLVILPATGSDPVL CFTQYEESSGRCKGLLGRDIR
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
28 – 469 Properdin
28 – 76 TSP type-1 0
32 – 56
47 – 47 L -> A. Inhibits oligomerization; when associated with A-58 and A-275.
30 – 37
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;
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