Variant position: 408 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 494 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 LQGAHLDETVWERPHEFWPD RFLEPGKNSRALAFGCGARVC
Mouse IQGANLDEMVWELPSKFWPD RFLEPGKNPRTPSFGCGARVC
Rat IQGANLDEMVWELPSKFWPD RFLESGKSPRIPTFGCGARVC
Pig LQGAHLDETVWEQPHEFRPD RFLAPGANPSALAFGCGARVC
Bovine LQGAHLDETVWEQPHEFRPD RFLEPGANPSALAFGCGARVC
Cat LQGAHLDDTVWEQPHEFRPD RFLVPGASPRVLAFGCGARVC
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 – 494 Steroid 21-hydroxylase
428 – 428 Iron (heme axial ligand)
428 – 428 C -> MST. Loss of activity and loss of P450 absorption.
406 – 409
Three novel mutations in CYP21 gene in Brazilian patients with the classical form of 21-hydroxylase deficiency due to a founder effect.
Billerbeck A.E.C.; Mendonca B.B.; Pinto E.M.; Madureira G.; Arnhold I.J.P.; Bachega T.A.S.S.;
J. Clin. Endocrinol. Metab. 87:4314-4317(2002)
Cited for: VARIANTS AH3 CYS-408 AND SER-424;
Inhibition of CYP21A2 enzyme activity caused by novel missense mutations identified in Brazilian and Scandinavian patients.
Soardi F.C.; Barbaro M.; Lau I.F.; Lemos-Marini S.H.; Baptista M.T.; Guerra-Junior G.; Wedell A.; Lajic S.; de Mello M.P.;
J. Clin. Endocrinol. Metab. 93:2416-2420(2008)
Cited for: VARIANTS AH3 ARG-56; LEU-62; ARG-107; PRO-142; ASN-172; TRP-356; CYS-408 AND SER-453; CHARACTERIZATION OF VARIANTS AH3 ARG-56; LEU-62; ARG-107; PRO-142; CYS-408 AND SER-453;
Phenotype-genotype correlations of 13 rare CYP21A2 mutations detected in 46 patients affected with 21-hydroxylase deficiency and in one carrier.
Tardy V.; Menassa R.; Sulmont V.; Lienhardt-Roussie A.; Lecointre C.; Brauner R.; David M.; Morel Y.;
J. Clin. Endocrinol. Metab. 95:1288-1300(2010)
Cited for: VARIANTS AH3 THR-77; PRO-167; ASN-172; THR-230; LYS-233; LEU-281; SER-291; ASP-292; LYS-320; PRO-341; HIS-354; TRP-356; TRP-369; CYS-408; SER-424; HIS-426 AND SER-453; CHARACTERIZATION OF VARIANTS AH3 PRO-167; ASN-172; LEU-281; ASP-292; LYS-320; TRP-369 AND SER-424;
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.