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UniProtKB/Swiss-Prot Q15848: Variant p.Arg112Cys

Adiponectin
Gene: ADIPOQ
Variant information

Variant position:  112
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 Arginine (R) to Cysteine (C) at position 112 (R112C, p.Arg112Cys).
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 basic (R) to medium size and polar (C)
The physico-chemical property of the reference and variant residues and the change implicated.

BLOSUM score:  -3
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 ADPND; does not assemble into trimers resulting in impaired secretion from the cell.
Any additional useful information about the variant.

Other resources:  
Links to websites of interest for the variant.



Sequence information

Variant position:  112
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Protein sequence length:  244
The length of the canonical sequence.

Location on the sequence:   RGFPGIQGRKGEPGEGAYVY  R SAFSVGLETYVTIPNMPIRF
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                         RGFPGIQGRKGEPGEGAYVYRSAFSVGLETYVTIPNMPIRF

Mouse                         RGFPGTPGRKGEPGEAAYVYRSAFSVGLETRVTVPNVPIRF

Bovine                        RGFPGTPGRKGEPGESAYVYRSAFSVGLERQVTVPNVPIRF

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 19 – 244 Adiponectin
Domain 108 – 244 C1q
Site 104 – 104 Not hydroxylated
Modified residue 95 – 95 4-hydroxyproline; partial
Modified residue 101 – 101 5-hydroxylysine
Glycosylation 101 – 101 O-linked (Gal...) hydroxylysine; partial
Mutagenesis 101 – 101 K -> R. Impaired formation of HMW multimers; when associated with R-77.


Literature citations

Impaired multimerization of human adiponectin mutants associated with diabetes. Molecular structure and multimer formation of adiponectin.
Waki H.; Yamauchi T.; Kamon J.; Ito Y.; Uchida S.; Kita S.; Hara K.; Hada Y.; Vasseur F.; Froguel P.; Kimura S.; Nagai R.; Kadowaki T.;
J. Biol. Chem. 278:40352-40363(2003)
Cited for: SUBUNIT; DISULFIDE BOND; MUTAGENESIS OF CYS-36; CHARACTERIZATION OF VARIANTS ARG-84; SER-90; CYS-112 AND THR-164;

Genomic structure and mutations in adipose-specific gene, adiponectin.
Takahashi M.; Arita Y.; Yamagata K.; Matsukawa Y.; Okutomi K.; Horie M.; Shimomura I.; Hotta K.; Kuriyama H.; Kihara S.; Nakamura T.; Yamashita S.; Funahashi T.; Matsuzawa Y.;
Int. J. Obes. Relat. Metab. Disord. 24:861-868(2000)
Cited for: VARIANT ADPND CYS-112;

Association of adiponectin mutation with type 2 diabetes: a candidate gene for the insulin resistance syndrome.
Kondo H.; Shimomura I.; Matsukawa Y.; Kumada M.; Takahashi M.; Matsuda M.; Ouchi N.; Kihara S.; Kawamoto T.; Sumitsuji S.; Funahashi T.; Matsuzawa Y.;
Diabetes 51:2325-2328(2002)
Cited for: VARIANTS CYS-112; THR-164; SER-221 AND PRO-241; ASSOCIATION WITH LOW PLASMA ADIPONECTIN CONCENTRATION AND DIABETES MELLITUS TYPE 2;

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.