Variant position: 843 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 1079 The length of the canonical sequence.
Location on the sequence:
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 LFWVAILMVICSLMALPWYV AATVISIAHIDSLKMETETSA
Mouse LFWVAILMVVCSFMALPWYV AATVISIAHIDSLKMETETSA
Rat LFWVAILMVVCSFMALPWYV AATVISIAHIDSLKMETETSA
Pig LFWVAILMVVCSFMALPWYV AATVISIAHIDSLKMETETSA
Bovine LFWVAILMVVCSFMALPWYV AATVISIAHIDSLKMETETSA
Rabbit LFWVAILMVVCSFMALPWYV AATVISIAHIDSLKMETETSA
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.
Type Positions Description
1 – 1079 Electrogenic sodium bicarbonate cotransporter 1
837 – 837 Extracellular
838 – 855 Discontinuously helical; Name=10
691 – 1079 Missing. In isoform 3.
813 – 896 Missing. In isoform 4.
842 – 842 V -> S. Confers anion exchange activity; when associated with SST-527--529-GFS; D-798; T-844 and R-847.
844 – 844 A -> T. Confers anion exchange activity; when associated with SST-527--529-GFS; D-798; S-842 and R-847.
845 – 845 T -> C. Strongly reduces transporter activity.
847 – 847 I -> R. Abolishes transporter activity. Confers anion exchange activity; when associated with SST-527--529-GFS; D-798; S-842 and T-844.
851 – 851 H -> N. Prevents membrane targeting.
853 – 853 D -> N. Moderate reduction of the sodium-dependent ion transport activity.
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;
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.