Sequence information
Variant position: 133 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 310 The length of the canonical sequence.
Location on the sequence:
YEHIKEKLAGLEIGILVNNV
G MLPNLLPSHFLNAPDEIQSL
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 YEHIKEKLAGLEIGILVNNVG MLPNLLPSHFLNAPD---EIQSL
Mouse YDHIKEHLEGLEIGILVNNVG MLPSFFPSHFLSTSG---ES
Rat YDHIEEQLKGLEIGVLVNNVG MLPNLLPSHFLSTSG---ES
Zebrafish YGHITENIEGLDIGVLVNNVG ILPSQIPCKLLETSDLEERI
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 – 310
17-beta-hydroxysteroid dehydrogenase type 3
Mutagenesis
133 – 133
G -> A. Has 70% of wild-type testosterone 17-beta-dehydrogenase (NADP(+)) activity.
Mutagenesis
133 – 133
G -> F. Almost complete loss of testosterone 17-beta-dehydrogenase (NADP(+)) activity.
Mutagenesis
133 – 133
G -> Q. Almost complete loss of testosterone 17-beta-dehydrogenase (NADP(+)) activity.
Literature citations
Biochemical analyses and molecular modeling explain the functional loss of 17beta-hydroxysteroid dehydrogenase 3 mutant G133R in three Tunisian patients with 46, XY Disorders of Sex Development.
Engeli R.T.; Rhouma B.B.; Sager C.P.; Tsachaki M.; Birk J.; Fakhfakh F.; Keskes L.; Belguith N.; Odermatt A.;
J. Steroid Biochem. Mol. Biol. 155:147-154(2016)
Cited for: VARIANT MPH ARG-133; CHARACTERIZATION OF VARIANT MPH ARG-133; FUNCTION; CATALYTIC ACTIVITY; SUBCELLULAR LOCATION; MUTAGENESIS OF GLY-133;
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.