Sequence information
Variant position: 419 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 651 The length of the canonical sequence.
Location on the sequence:
FLLFFVLRVRSNVLKGAIQD
R VGLLYQFVGATPYTGMLNAV
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 FLLFF------------------------------------------------VLRV-------------------------------RSNVLKGAIQD----------------------------------------------------------------------------------------------R VGLLYQFVGAT--------------------------------------------------------------------------------------------------------------------------------PYTGM--------LNAV
Mouse FLIFY------------------------------------
Rat FLIFY------------------------------------
Slime mold YIVFFYSVCFFALKYLNFEDKKSKLAVKKLKKKKKVIVCKE
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 – 651
ATP-binding cassette sub-family G member 5
Topological domain
405 – 421
Extracellular
Domain
388 – 645
ABC transmembrane type-2
Mutagenesis
432 – 432
Y -> A. Strongly decreases cholesterol secretion into bile.
Literature citations
Identification of a gene, ABCG5, important in the regulation of dietary cholesterol absorption.
Lee M.-H.; Lu K.; Hazard S.; Yu H.; Shulenin S.; Hidaka H.; Kojima H.; Allikmets R.; Sakuma N.; Pegoraro R.; Srivastava A.K.; Salen G.; Dean M.; Patel S.B.;
Nat. Genet. 27:79-83(2001)
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1); VARIANTS STSL2 HIS-389; HIS-419 AND PRO-419; VARIANT GLU-604; FUNCTION; TISSUE SPECIFICITY;
Two genes that map to the STSL locus cause sitosterolemia: genomic structure and spectrum of mutations involving sterolin-1 and sterolin-2, encoded by ABCG5 and ABCG8, respectively.
Lu K.; Lee M.-H.; Hazard S.; Brooks-Wilson A.; Hidaka H.; Kojima H.; Ose L.; Stalenhoef A.F.H.; Mietinnen T.; Bjorkhem I.; Bruckert E.; Pandya A.; Brewer H.B. Jr.; Salen G.; Dean M.; Srivastava A.K.; Patel S.B.;
Am. J. Hum. Genet. 69:278-290(2001)
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-88 (ISOFORM 1); VARIANTS STSL2 GLN-146; HIS-389; PRO-419; HIS-419 AND SER-550; VARIANT GLU-604;
Missense mutations in ABCG5 and ABCG8 disrupt heterodimerization and trafficking.
Graf G.A.; Cohen J.C.; Hobbs H.H.;
J. Biol. Chem. 279:24881-24888(2004)
Cited for: CHARACTERIZATION OF VARIANTS STSL2 GLN-146; HIS-389; PRO-419; HIS-419 AND LYS-437; FUNCTION;
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.