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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot Q96RD7: Variant p.Ile272Val

Pannexin-1
Gene: PANX1
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Variant information Variant position: help 272 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Type of variant: help LB/B 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 Isoleucine (I) to Valine (V) at position 272 (I272V, p.Ile272Val). 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 Similar physico-chemical property. Both residues are medium size and hydrophobic. The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help 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: help No change in glycosylation pattern. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 272 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 426 The length of the canonical sequence.
Location on the sequence: help ILRNDSTVPDQFQCKLIAVG I FQLLSVINLVVYVLLAPVVV 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                         ILRNDSTVPDQFQCKLIAVGIFQLLSVINLVVYVLLAPVVV

Mouse                         VLKNDSTIPDRFQCKLIAVGIFQLLSLINLIVYALLIPVVV

Rat                           VLRNDSTIPDSFQCKLIAVGIFQLLSLINLLVYALLVPVVI

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 1 – 426 Pannexin-1
Chain 1 – 379 Caspase-activated pannexin-1
Transmembrane 267 – 287 Helical
Glycosylation 255 – 255 N-linked (GlcNAc...) asparagine
Mutagenesis 255 – 255 N -> A. Impaired glycosylation. Forms gap junctions by 2 hemichannels.
Mutagenesis 255 – 255 N -> Q. Impaired glycosylation. Loss of GLY1 and GLY2 forms. No effect on oocyte survival. Located in the cytoplasm. Decreased levels of pro-IL1B upon LPS priming and ATP stimulation. Attenuated pyroptotic cell death induced by LPS and ATP.
Helix 270 – 295



Literature citations
A pannexin 1 channelopathy causes human oocyte death.
Sang Q.; Zhang Z.; Shi J.; Sun X.; Li B.; Yan Z.; Xue S.; Ai A.; Lyu Q.; Li W.; Zhang J.; Wu L.; Mao X.; Chen B.; Mu J.; Li Q.; Du J.; Sun Q.; Jin L.; He L.; Zhu S.; Kuang Y.; Wang L.;
Sci. Transl. Med. 11:0-0(2019)
Cited for: FUNCTION; SUBCELLULAR LOCATION; TISSUE SPECIFICITY; INVOLVEMENT IN OZEMA7; VARIANTS OZEMA7 21-THR--PRO-23 DEL; GLU-346; SER-347 AND 392-GLN--CYS-426 DEL; CHARACTERIZATION OF VARIANTS OZEMA7 21-THR--PRO-23 DEL; GLU-346; SER-347 AND 392-GLN--CYS-426 DEL; MUTAGENESIS OF ASN-255; ASN-338 AND ASN-394; VARIANTS HIS-217 AND VAL-272; CHARACTERIZATION OF VARIANTS HIS-217 AND VAL-272; GLYCOSYLATION;
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.