Variant position: 65 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 409 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 G--IFFELYPLFQDVHVMIFVG FGFLMTFLKKYGFSSVGINLL
Mouse D--QFFQLYPLFQDVHVMIFVG FGFLMTFLKKYGFSGVGFN
Rat D--QFFQLYPLFQHVHVMIFVG FGFLMTFLKKYGFSGVGFN
Bovine DVEKTMESYPFFQDVHIMVFAG FGFLMTFLWKYGFSGVGIN
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 – 409 Ammonium transporter Rh type A
52 – 72 Helical
The monovalent cation leak in overhydrated stomatocytic red blood cells results from amino acid substitutions in the Rh-associated glycoprotein.
Bruce L.J.; Guizouarn H.; Burton N.M.; Gabillat N.; Poole J.; Flatt J.F.; Brady R.L.; Borgese F.; Delaunay J.; Stewart G.W.;
Cited for: INVOLVEMENT IN OHST; VARIANTS OHST ARG-61 AND SER-65; CHARACTERIZATION OF VARIANTS OHST ARG-61 AND SER-65; FUNCTION; TISSUE SPECIFICITY; SUBCELLULAR LOCATION; GLYCOSYLATION;
Loss-of-function and gain-of-function phenotypes of stomatocytosis mutant RhAG F65S.
Stewart A.K.; Shmukler B.E.; Vandorpe D.H.; Rivera A.; Heneghan J.F.; Li X.; Hsu A.; Karpatkin M.; O'Neill A.F.; Bauer D.E.; Heeney M.M.; John K.; Kuypers F.A.; Gallagher P.G.; Lux S.E.; Brugnara C.; Westhoff C.M.; Alper S.L.;
Am. J. Physiol. 301:C1325-C1343(2011)
Cited for: VARIANT OHST SER-65; CHARACTERIZATION OF VARIANT OHST SER-65; FUNCTION;
Human RhAG ammonia channel is impaired by the Phe65Ser mutation in overhydrated stomatocytic red cells.
Genetet S.; Ripoche P.; Picot J.; Bigot S.; Delaunay J.; Armari-Alla C.; Colin Y.; Mouro-Chanteloup I.;
Am. J. Physiol. 302:C419-C428(2012)
Cited for: CHARACTERIZATION OF VARIANT OHST SER-65; FUNCTION; SUBCELLULAR LOCATION; GLYCOSYLATION; TISSUE SPECIFICITY;
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.