Expasy logo

UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot Q9Y6R1: Variant p.Thr529Ser

Electrogenic sodium bicarbonate cotransporter 1
Gene: SLC4A4
Feedback?
Variant information Variant position: help 529 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 Threonine (T) to Serine (S) at position 529 (T529S, p.Thr529Ser). 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 medium size and polar (T) to small size and polar (S) 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 pRTA-OA; decreased cotransporter activity; mediates electroneutral sodium/bicarbonate cotransport rather than electrogenic sodium/bicarbonate cotransport; no effect on cell membrane localization. Any additional useful information about the variant.


Sequence information Variant position: help 529 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 1079 The length of the canonical sequence.
Location on the sequence: help AVSGAIFCLFAGQPLTILSS T GPVLVFERLLFNFSKDNNFD 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                         AVSGAIFCLFAGQPLTILSSTGPVLVFERLLFNFSKDNNFD

Mouse                         AVSGAIFCLFAGQPLTILSSTGPVLVFERLLFNFSKDHNFD

Rat                           AVSGAIFCLFAGQPLTILSSTGPVLVFERLLFNFSKDHSFD

Pig                           AVSGAVFCLFAGQPLTILSSTGPVLVFERLLFNFSKDHNFD

Bovine                        AVSGAIFCLFAGQPLTILSSTGPVLVFERLLFNFSKDHNFD

Rabbit                        AVSGAIFCLFAGQPLTILSSTGPVLVFERLLFNFSKDHNFD
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 – 1079 Electrogenic sodium bicarbonate cotransporter 1
Topological domain 521 – 521 Cytoplasmic
Transmembrane 522 – 542 Discontinuously helical; Name=3
Mutagenesis 527 – 529 SST -> GFS. Confers anion exchange activity; when associated with E-798; S-842; T-844 and R-847.
Mutagenesis 527 – 527 S -> C. Severely reduces transporter activity.
Mutagenesis 536 – 536 E -> Q. Prevents membrane targeting.



Literature citations
Functional analysis of NBC1 mutants associated with proximal renal tubular acidosis and ocular abnormalities.
Horita S.; Yamada H.; Inatomi J.; Moriyama N.; Sekine T.; Igarashi T.; Endo Y.; Dasouki M.; Ekim M.; Al-Gazali L.; Shimadzu M.; Seki G.; Fujita T.;
J. Am. Soc. Nephrol. 16:2270-2278(2005)
Cited for: VARIANTS PRTA-OA SER-342; SER-529; HIS-554; VAL-843 AND CYS-925; CHARACTERIZATION OF VARIANTS PRTA-OA SER-342; SER-529; HIS-554; VAL-843 AND CYS-925; FUNCTION; TRANSPORTER ACTIVITY; SUBCELLULAR LOCATION; Functional analysis of a novel missense NBC1 mutation and of other mutations causing proximal renal tubular acidosis.
Suzuki M.; Vaisbich M.H.; Yamada H.; Horita S.; Li Y.; Sekine T.; Moriyama N.; Igarashi T.; Endo Y.; Cardoso T.P.; de Sa L.C.; Koch V.H.; Seki G.; Fujita T.;
Pflugers Arch. 455:583-593(2008)
Cited for: VARIANT PRTA-OA ARG-530; CHARACTERIZATION OF VARIANTS PRTA-OA SER-342 SER-529; ARG-530 AND PRO-566; FUNCTION; SUBCELLULAR LOCATION; TRANSPORTER ACTIVITY; Missense mutation T485S alters NBCe1-A electrogenicity causing proximal renal tubular acidosis.
Zhu Q.; Shao X.M.; Kao L.; Azimov R.; Weinstein A.M.; Newman D.; Liu W.; Kurtz I.;
Am. J. Physiol. 305:C392-C405(2013)
Cited for: CHARACTERIZATION OF VARIANTS PRTA-OA SER-529 AND ARG-530; FUNCTION; TRANSPORTER ACTIVITY; 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.