Variant position: 358 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 477 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 S--EDPG-VLGIVYDSVAFPE--------QD GSPPGLR-----VTVMLGGS---------WLQTLE
Mouse S--EDPT-VLGIVYDSVAFPE--------QD GNPPSLR---
Bovine S--EDPV-ILGIVYDSVAFPE--------QD GSLPGLR---
Slime mold K--ENQS-VIGVCFDSNTFPEFVNNNNNNNN DNDNGNEKDQ
Baker's yeast SN-KNPGKLLGVIFDSVIERNFKPLFDKLST NPNALNK--Y
Fission yeast CTPNNPNHVLGIVFDS----E--------QN NPENGSK---
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 – 477 Protoporphyrinogen oxidase
347 – 347 V -> A. Decreases enzyme activity by 45%.
368 – 368 M -> A. Decreases enzyme activity by 52%.
358 – 361
Structural insight into human variegate porphyria disease.
Qin X.; Tan Y.; Wang L.; Wang Z.; Wang B.; Wen X.; Yang G.; Xi Z.; Shen Y.;
FASEB J. 25:653-664(2011)
Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH FAD AND ACIFLUORFEN; CATALYTIC ACTIVITY; FUNCTION; SUBUNIT; CHARACTERIZATION OF VARIANTS VP ASP-11; THR-12; PHE-15; PRO-20; PRO-38; ALA-40; GLU-40; TRP-59; PRO-73; GLY-84; PRO-85; PRO-106; PRO-138; ASP-139; VAL-143; CYS-152; PRO-154; MET-158; HIS-168; VAL-178; VAL-205; CYS-217; GLY-224; ARG-232; ASP-282; ASN-283; PRO-295; ARG-330; ALA-332; GLY-335; CYS-348; ALA-349; PRO-350; ARG-358; ASP-397; PHE-401; PRO-433; PRO-444; ARG-448; PRO-450 AND ARG-453; MUTAGENESIS OF LEU-74; ARG-97; LEU-166; GLY-169; SER-284; VAL-290; PHE-331; LEU-334; VAL-347 AND MET-368;
Molecular characterization of homozygous variegate porphyria.
Roberts A.G.; Puy H.; Dailey T.A.; Morgan R.R.; Whatley S.D.; Dailey H.A.; Martasek P.; Nordmann Y.; Deybach J.C.; Elder G.H.;
Hum. Mol. Genet. 7:1921-1925(1998)
Cited for: VARIANTS VP GLU-169; ALA-349; ARG-358 AND PRO-433; CHARACTERIZATION OF VARIANTS VP GLU-169; ALA-349; ARG-358 AND PRO-433;
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.