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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P41181: Variant p.Ser216Pro

Aquaporin-2
Gene: AQP2
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Variant information Variant position: help 216 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 Serine (S) to Proline (P) at position 216 (S216P, p.Ser216Pro). 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 small size and polar (S) to medium size and hydrophobic (P) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help -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
Variant description: help In NDI2; loss of water channel activity. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 216 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 GKFDDHWVFWIGPLVGAILG S LLYNYVLFPPAKSLSERLAV 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                         GKFDDHWVFWIGPLVGAILGSLLYNYVLFPPAKSLSERLAV

Mouse                         GKFDDHWVFWIGPLVGAVIGSLLYNYLLFPSTKSLQERLAV

Rat                           GKFDDHWVFWIGPLVGAIIGSLLYNYLLFPSAKSLQERLAV

Bovine                        GKFDDHWVFWIGPLVGAIVASLLYNYVLFPPAKSLSERLAV

Sheep                         GKFDDHWVFWIGPLVGAIVASLLYNYVLFPPAKSLSERLAV
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 – 271 Aquaporin-2
Transmembrane 202 – 222 Helical
Mutagenesis 217 – 217 L -> A. Abolishes interaction with MIAC; when associated with A-221.
Mutagenesis 221 – 221 Y -> A. Abolishes interaction with MIAC; when associated with A-217.
Mutagenesis 229 – 229 S -> A. No effect on sorting from the ER to the vesicles, redistribution to apical membrane, or endocytosis.
Mutagenesis 229 – 229 S -> D. No effect on sorting from the ER to the vesicles, redistribution to apical membrane, or endocytosis.
Mutagenesis 231 – 231 S -> A. No effect on sorting from the ER to the vesicles, redistribution to apical membrane, or endocytosis.
Mutagenesis 231 – 231 S -> D. No effect on sorting from the ER to the vesicles, redistribution to apical membrane, or endocytosis.
Mutagenesis 232 – 232 E -> A. Reduces interaction with MIAC.
Helix 203 – 221



Literature citations
Requirement of human renal water channel aquaporin-2 for vasopressin-dependent concentration of urine.
Deen P.M.T.; Verdijk M.A.J.; Knoers V.V.A.M.; Wieringa B.; Monnens L.A.H.; van Os C.H.; van Oost B.A.;
Science 264:92-94(1994)
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]; FUNCTION; SUBCELLULAR LOCATION; VARIANTS NDI2 CYS-187 AND PRO-216; CHARACTERIZATION OF VARIANTS NDI2 CYS-187 AND PRO-216; Patients with autosomal nephrogenic diabetes insipidus homozygous for mutations in the aquaporin 2 water-channel gene.
van Lieburg A.F.; Verdijk M.A.J.; Knoers V.V.A.M.; van Essen A.J.; Proesmans W.; Mallmann R.; Monnens L.A.H.; van Oost B.A.; van Os C.H.; Deen P.M.T.;
Am. J. Hum. Genet. 55:648-652(1994)
Cited for: NUCLEOTIDE SEQUENCE [MRNA]; FUNCTION; SUBCELLULAR LOCATION; VARIANTS NDI2 ARG-64; CYS-187 AND PRO-216; CHARACTERIZATION OF VARIANT NDI2 ARG-64; Mutations in the vasopressin V2 receptor and aquaporin-2 genes in 12 families with congenital nephrogenic diabetes insipidus.
Vargas-Poussou R.; Forestier L.; Dautzenberg M.D.; Niaudet P.; Dechaux M.; Antignac C.;
J. Am. Soc. Nephrol. 8:1855-1862(1997)
Cited for: VARIANTS NDI2 MET-168 AND PRO-216;
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.