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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot Q9BWP8: Variant p.Gly204Ser

Collectin-11
Gene: COLEC11
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Variant information Variant position: help 204 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Type of variant: help 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: help From Glycine (G) to Serine (S) at position 204 (G204S, p.Gly204Ser). 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: help Change from glycine (G) to small size and polar (S) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help 0 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: help In 3MC2; no effect on homotrimerization; loss of calcium-binding; loss of carbohydrate-binding probably due to the inability to bind calcium; not secreted probably due to degradation early after biosynthesis. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 204 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 271 The length of the canonical sequence.
Location on the sequence: help AANGLMAAYLAQAGLARVFI G INDLEKEGAFVYSDHSPMRT 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: help The multiple alignment of the region surrounding the variant against various orthologous sequences. 
Human                         AANGLMAAYLAQAGLARVFIGINDLEKEGAFVYSDHSPMRT

Mouse                         AANGLMASYLAQAGLARVFIGINDLEKEGAFVYSDRSPMQT

Bovine                        AANALLAAYITQAGLARVFIGINDLEREGAFVYADRSPMQT

Chicken                       NANNLIASYINQAGLTRVFIGINDLEKEGNFVYSDRSPMQT

Xenopus laevis                ATNSLIASYINHAGLSRVFIGINDLEREGHFVYSDRSPMQT

Zebrafish                     AANRAIAGYVTDAGLSRVYIGINDLEREGHFVYVERSPMTT
Sequence annotation in neighborhood: help 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 26 – 271 Collectin-11
Domain 149 – 265 C-type lectin
Binding site 200 – 200
Binding site 207 – 207
Binding site 211 – 211
Binding site 211 – 211
Disulfide bond 170 – 264
Beta strand 199 – 206



Literature citations
Molecular basis of sugar recognition by collectin-K1 and the effects of mutations associated with 3MC syndrome.
Venkatraman Girija U.; Furze C.M.; Gingras A.R.; Yoshizaki T.; Ohtani K.; Marshall J.E.; Wallis A.K.; Schwaeble W.J.; El-Mezgueldi M.; Mitchell D.A.; Moody P.C.; Wakamiya N.; Wallis R.;
BMC Biol. 13:27-27(2015)
Cited for: X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS) OF 116-270 OF HOMOTRIMER IN COMPLEX WITH CALCIUM AND CARBOHYDRATE; FUNCTION; SUBUNIT; SUBCELLULAR LOCATION; DISULFIDE BONDS; CHARACTERIZATION OF VARIANTS 3MC2 PRO-169; SER-204 AND SER-217 DEL; Mutations in lectin complement pathway genes COLEC11 and MASP1 cause 3MC syndrome.
Rooryck C.; Diaz-Font A.; Osborn D.P.; Chabchoub E.; Hernandez-Hernandez V.; Shamseldin H.; Kenny J.; Waters A.; Jenkins D.; Kaissi A.A.; Leal G.F.; Dallapiccola B.; Carnevale F.; Bitner-Glindzicz M.; Lees M.; Hennekam R.; Stanier P.; Burns A.J.; Peeters H.; Alkuraya F.S.; Beales P.L.;
Nat. Genet. 43:197-203(2011)
Cited for: FUNCTION; VARIANTS 3MC2 PRO-169; SER-204 AND SER-217 DEL;
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.