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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot Q9HBA0: Variant p.Arg316Cys

Transient receptor potential cation channel subfamily V member 4
Gene: TRPV4
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Variant information Variant position: help 316 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 Arginine (R) to Cysteine (C) at position 316 (R316C, p.Arg316Cys). 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 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: 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 In CMT2C and SPSMA; decreased protein stability; decreased ATP-binding. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 316 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 871 The length of the canonical sequence.
Location on the sequence: help NQPHIVNYLTENPHKKADMR R QDSRGNTVLHALVAIADNTR 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                         NQPHIVNYLTENPHKKADMRRQDSRGNTVLHALVAIADNTR

Mouse                         NQPHIVNYLTENPHKKADMRRQDSRGNTVLHALVAIADNTR

Rat                           NQPHIVNYLTENPHKKADMRRQDSRGNTVLHALVAIADNTR

Chicken                       NQPHIVHYLTENGHKQADLRRQDSRGNTVLHALVAIADNTR
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 – 871 Transient receptor potential cation channel subfamily V member 4
Topological domain 1 – 469 Cytoplasmic
Mutagenesis 296 – 296 N -> D. Loss of interaction with membranes enriched in phosphatidylinositol-2,4-bisphosphate; when associated with P-299.
Mutagenesis 299 – 299 H -> P. Strongly decreased interaction with membranes enriched in phosphatidylinositol-2,4-bisphosphate. Loss of interaction with membranes enriched in phosphatidylinositol-2,4-bisphosphate; when associated with D-296.



Literature citations
Structural and biochemical consequences of disease-causing mutations in the ankyrin repeat domain of the human TRPV4 channel.
Inada H.; Procko E.; Sotomayor M.; Gaudet R.;
Biochemistry 51:6195-6206(2012)
Cited for: X-RAY CRYSTALLOGRAPHY (2.85 ANGSTROMS) OF 149-397 ALONE AND IN COMPLEX WITH ATP; MUTAGENESIS OF PHE-231; CHARACTERIZATION OF VARIANTS MTD ARG-197; PHE-199; ALA-295; PHE-331; THR-331 AND PHE-342; CHARACTERIZATION OF VARIANTS SMDK LYS-278 AND GLY-333; CHARACTERIZATION OF VARIANTS CMT2C CYS-232; HIS-269; TRP-315 AND CYS-316; CHARACTERIZATION OF VARIANT SPSMA CYS-316; CHARACTERIZATION OF VARIANT LYS-183; CHARACTERIZATION OF VARIANTS HMND8 CYS-232 AND HIS-269; Alterations in the ankyrin domain of TRPV4 cause congenital distal SMA, scapuloperoneal SMA and HMSN2C.
Auer-Grumbach M.; Olschewski A.; Papic L.; Kremer H.; McEntagart M.E.; Uhrig S.; Fischer C.; Frohlich E.; Balint Z.; Tang B.; Strohmaier H.; Lochmuller H.; Schlotter-Weigel B.; Senderek J.; Krebs A.; Dick K.J.; Petty R.; Longman C.; Anderson N.E.; Padberg G.W.; Schelhaas H.J.; van Ravenswaaij-Arts C.M.; Pieber T.R.; Crosby A.H.; Guelly C.;
Nat. Genet. 42:160-164(2010)
Cited for: VARIANTS CMT2C TRP-315 AND CYS-316; VARIANT HMND8 HIS-269; SUBCELLULAR LOCATION; Scapuloperoneal spinal muscular atrophy and CMT2C are allelic disorders caused by alterations in TRPV4.
Deng H.X.; Klein C.J.; Yan J.; Shi Y.; Wu Y.; Fecto F.; Yau H.J.; Yang Y.; Zhai H.; Siddique N.; Hedley-Whyte E.T.; Delong R.; Martina M.; Dyck P.J.; Siddique T.;
Nat. Genet. 42:165-169(2010)
Cited for: VARIANT CMT2C HIS-269; VARIANT SPSMA CYS-316; SUBCELLULAR LOCATION;
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.