Variant position: 352 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 563 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 VVSGTLRSAFEYGGQKCSAC SRLYVPHSLWPQIKGRLLEEH
Mouse VVSGTLRSAFEYGGQKCSAC SRLYVPKSLWPQIKGRLLEEH
Rat VVSGTLRSAFEYGGQKCSAC SRLYVPQSLWPQIKGRLLEEH
Bovine VVSGTLRSAFEYGGQKCSAC SRLYAPRSLWPQIKGRLLEEL
Zebrafish VVTGTIRSAFEYGGQKCSAC SRMYVPDSLWPQIRQGLLDVY
Slime mold FVNNTLRGAFEYQGQKCSAC SRAYIPQSLWPQIKDRLVTGV
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
25 – 563 Delta-1-pyrroline-5-carboxylate dehydrogenase, mitochondrial
348 – 348 Nucleophile
347 – 347 N6-succinyllysine
365 – 365 N6-acetyllysine
352 – 352 S -> A. Reduced affinity for NAD. No effect on enzyme activity.
351 – 357
The three-dimensional structural basis of type II hyperprolinemia.
Srivastava D.; Singh R.K.; Moxley M.A.; Henzl M.T.; Becker D.F.; Tanner J.J.;
J. Mol. Biol. 420:176-189(2012)
Cited for: X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 18-563 OF WILD-TYPE; MUTANT ALA-352 AND VARIANT HYRPRO2 LEU-352; CATALYTIC ACTIVITY; FUNCTION; PATHWAY; BIOPHYSICOCHEMICAL PROPERTIES; SUBUNIT; ACTIVE SITE; CHARACTERIZATION OF VARIANT HYRPRO2 LEU-352; MUTAGENESIS OF SER-352;
Mutations in the Delta1-pyrroline 5-carboxylate dehydrogenase gene cause type II hyperprolinemia.
Geraghty M.T.; Vaughn D.; Nicholson A.J.; Lin W.-W.; Jimenez-Sanchez G.; Obie C.; Flynn M.P.; Valle D.; Hu C.-A.A.;
Hum. Mol. Genet. 7:1411-1415(1998)
Cited for: VARIANT HYRPRO2 LEU-352; VARIANT LEU-16;
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.