Variant position: 373 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 508 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 LEATIREVLRLRPVAPMLIP HKANVDSSIGEFAVDKGTEVI
Rhesus macaque LEATIREVLRIRPVAPMLIP HKANVDSSIGEFAVDKGTHVI
Chimpanzee LEATIREVLRLRPVAPMLIP HKANVDSSIGEFAVDKGTQVI
Mouse LEATIREVLRIRPVAPLLIP HKANIDSSIGEFAIPKDTHVI
Rat LEATIREVLRIRPVAPMLIP HKANVDSSIGEFTVPKDTHVV
Pig LEATIREVLRFRPVSPTLIP HRAIIDSSIGEFTIDKDTDVV
Bovine LEATIREVLRIRPVAPTLIP HKAVIDSSIGDLTIDKGTDVV
Goat LEATIREVLRIRPVAPMLIP HKAIIDSSIGDLTIDKGTDVV
Sheep LEATIREVLRIRPVAPMLIP HKAIIDSSIGDLTIDKGTDVV
Cat LEATIREVLRIRPVAPTLIP HKAIMDSSIGEFAVDKGTNVI
Horse LEATIREVLRIRPVAPMLIP HKALVDSSIGEFAVDDGTNVI
Chicken LEATISEGLRIRPVSPLLIP HVSLADTSIGEYSIPKGARVV
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 – 508 Steroid 17-alpha-hydroxylase/17,20 lyase
Mutation of histidine 373 to leucine in cytochrome P450c17 causes 17 alpha-hydroxylase deficiency.
Monno S.; Ogawa H.; Date T.; Fujioka M.; Miller W.L.; Kobayashi M.;
J. Biol. Chem. 268:25811-25817(1993)
Cited for: VARIANT AH5 LEU-373;
A review of the literature on common CYP17A1 mutations in adults with 17-hydroxylase/17,20-lyase deficiency, a case series of such mutations among Koreans and functional characteristics of a novel mutation.
Kim Y.M.; Kang M.; Choi J.H.; Lee B.H.; Kim G.H.; Ohn J.H.; Kim S.Y.; Park M.S.; Yoo H.W.;
Cited for: VARIANTS AH5 GLU-174; LEU-373 AND LEU-406; CHARACTERIZATION OF VARIANT AH5 LEU-406;
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.