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UniProtKB/Swiss-Prot Q15125: Variant p.Arg110Gln

3-beta-hydroxysteroid-Delta(8),Delta(7)-isomerase
Gene: EBP
Variant information

Variant position:  110
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Type of variant:  Disease [Disclaimer]
The variants are classified into three categories: Disease, Polymorphism and Unclassified.
  • Disease: Variants implicated in disease according to literature reports.
  • Polymorphism: Variants not reported to be implicated in disease.
  • Unclassified: Variants with uncertain implication in disease according to literature reports. Evidence against or in favor of a pathogenic role is limited and/or conflicting.

Residue change:  From Arginine (R) to Glutamine (Q) at position 110 (R110Q, p.Arg110Gln).
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 (Q)
The physico-chemical property of the reference and variant residues and the change implicated.

BLOSUM score:  1
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

Involvement in disease:  Chondrodysplasia punctata 2, X-linked dominant (CDPX2) [MIM:302960]: A clinically and genetically heterogeneous disorder characterized by punctiform calcification of the bones. The key clinical features of CDPX2 are chondrodysplasia punctata, linear ichthyosis, cataracts and short stature. CDPX2 is a rare disorder of defective cholesterol biosynthesis, biochemically characterized by an increased amount of 8-dehydrocholesterol and cholest-8(9)-en-3-beta-ol in the plasma and tissues. {ECO:0000269|PubMed:10391218, ECO:0000269|PubMed:10391219, ECO:0000269|PubMed:10942423, ECO:0000269|PubMed:11493318, ECO:0000269|PubMed:18176751, ECO:0000269|PubMed:25814754}. Note=The disease is caused by mutations affecting the gene represented in this entry.
The name and a short description of the disease associated with the variant. For more information about the disease, the user can refer to OMIM, following the link provided after the disease acronym.

Variant description:  In CDPX2.
Any additional useful information about the variant.



Sequence information

Variant position:  110
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Protein sequence length:  230
The length of the canonical sequence.

Location on the sequence:   LLGDQAFLSQLWKEYAKGDS  R YILGDNFTVCMETITACLWG
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                         LLG--------DQAFLSQLWKEYAKGDSRYILGDNFTV--CMETITACLWG

Mouse                         LLE--------DQAFLSQLWKEYSKGDSRYILSDSFVV--C

Rat                           LLE--------DQAFLSQLWKEYSKGDSRYILSDGFIV--C

Slime mold                    MLELVPLENAWNPHWYAQLYSQYAKYDLRYAIQDPMVVFFC

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 2 – 230 3-beta-hydroxysteroid-Delta(8),Delta(7)-isomerase
Domain 61 – 204 EXPERA
Mutagenesis 111 – 111 Y -> W. Reduces catalytic activity to less than 2% of wild-type.
Mutagenesis 121 – 121 M -> A. Reduces catalytic activity to less than 35% of wild-type.
Mutagenesis 121 – 121 M -> V. No effect on catalytic activity.
Mutagenesis 122 – 122 E -> A. Reduces catalytic activity to less than 10% of wild-type.
Mutagenesis 125 – 125 T -> A. Reduces catalytic activity to less than 10% of wild-type.


Literature citations

Mutations in a delta(8)-delta(7) sterol isomerase in the tattered mouse and X-linked dominant chondrodysplasia punctata.
Derry J.M.J.; Gormally E.; Means G.D.; Zhao W.; Meindl A.; Kelley R.I.; Boyd Y.; Herman G.E.;
Nat. Genet. 22:286-290(1999)
Cited for: VARIANT CDPX2 GLN-110;

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.