Variant position: 1158 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 1663 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 EKDMALTAFVLISLQEAKDI CEEQVNSLPGSITKAGDFLEA
Mouse EADVSLTAFVLIALQEARDI CEGQVNSLPGSINKAGEYIEA
Rat EADVSLTAFVLIALQEARDI CEGQVNSLPGSINKAGEYLEA
Pig EKDVSLTAFVLIALQEAKDI CEPQVNSLLRSINKARDFLAD
Bovine EKDVSLTAFVLIALHEAKDI CEAQVNSLGRSIAKAGDFLEN
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
23 – 1663 Complement C3
672 – 1663 Complement C3 alpha chain
749 – 1663 Complement C3b alpha' chain
955 – 1303 Complement C3dg fragment
1002 – 1303 Complement C3d fragment
873 – 1513
1101 – 1158
1140 – 1140 D -> A. No effect on binding of C3d to CR2.
1153 – 1153 E -> A. Impaired binding of C3d to CR2.
1156 – 1156 D -> A. Impaired binding of C3d to CR2.
1159 – 1159 E -> A. Impaired binding of C3d to CR2.
1160 – 1160 E -> A. Minor effect on binding of C3d to CR2.
1163 – 1163 N -> A. No effect on binding of C3d to CR2. Impaired binding of C3d to CR2; when associated with 1108-R-R-1109.
1163 – 1163 N -> R. Impaired binding of C3d to CR2.
1139 – 1158
Mutations in complement C3 predispose to development of atypical hemolytic uremic syndrome.
Fremeaux-Bacchi V.; Miller E.C.; Liszewski M.K.; Strain L.; Blouin J.; Brown A.L.; Moghal N.; Kaplan B.S.; Weiss R.A.; Lhotta K.; Kapur G.; Mattoo T.; Nivet H.; Wong W.; Gie S.; Hurault de Ligny B.; Fischbach M.; Gupta R.; Hauhart R.; Meunier V.; Loirat C.; Dragon-Durey M.A.; Fridman W.H.; Janssen B.J.; Goodship T.H.; Atkinson J.P.;
Cited for: VARIANTS AHUS5 GLN-592; TRP-592; TRP-735; VAL-1094; ASN-1115; TRP-1158; LYS-1161 AND ASP-1464; CHARACTERIZATION OF VARIANTS AHUS5 GLN-592; TRP-592; VAL-1094; ASN-1115 AND LYS-1161;
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.