Sequence information
Variant position: 868 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 911 The length of the canonical sequence.
Location on the sequence:
WVVKSTPASLALPFVLILTV
P LRRVLLPLIFRNVELQCLDA
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 WVVKSTPASLALPFVLILTVP LRRVLLPLIFRNVELQCLDA
Mouse WVVKSTPASLALPFVLILTVP LRRLILPLIFRELELQCLDG
Rat WVVKSTPASLALPFVLILTVP LRRLLLPLIFRELELQCLDG
Chicken WGVKVSPASLRCPFVLVLTVP LRRLLLPRIFSEIELKCLDT
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
Chain
1 – 911
Band 3 anion transport protein
Intramembrane
839 – 869
Discontinuously helical
Helix
859 – 873
Literature citations
A substrate access tunnel in the cytosolic domain is not an essential feature of the solute carrier 4 (SLC4) family of bicarbonate transporters.
Shnitsar V.; Li J.; Li X.; Calmettes C.; Basu A.; Casey J.R.; Moraes T.F.; Reithmeier R.A.;
J. Biol. Chem. 288:33848-33860(2013)
Cited for: X-RAY CRYSTALLOGRAPHY (2.23 ANGSTROMS) OF 51-356; FUNCTION; SUBCELLULAR LOCATION; GLYCOSYLATION AT ASN-642; MUTAGENESIS OF GLU-85; ARG-283; ASN-642 AND GLU-681; CHARACTERIZATION OF VARIANT ACANTHOCYTOSIS LEU-868;
Band 3 HT, a human red-cell variant associated with acanthocytosis and increased anion transport, carries the mutation Pro-868-->Leu in the membrane domain of band 3.
Bruce L.J.; Kay M.M.; Lawrence C.; Tanner M.J.;
Biochem. J. 293:317-320(1993)
Cited for: VARIANT ACANTHOCYTOSIS LEU-868;
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.