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Steroid 21-hydroxylase (EC 1.14.14.16) (21-OHase) (Cytochrome P-450c21) (Cytochrome P450 21) (Cytochrome P450 XXI) (Cytochrome P450-C21) (Cytochrome P450-C21B)

 CP21A_HUMAN             Reviewed;         494 AA.
P08686; A2BHY6; P04033; Q01204; Q08AG8; Q16749; Q16806; Q5ST44;
Q96NU8;
01-NOV-1986, integrated into UniProtKB/Swiss-Prot.
01-JAN-1988, sequence version 1.
25-OCT-2017, entry version 205.
RecName: Full=Steroid 21-hydroxylase;
EC=1.14.14.16 {ECO:0000269|PubMed:16984992, ECO:0000269|PubMed:22014889, ECO:0000269|PubMed:25855791, ECO:0000269|PubMed:27721825};
AltName: Full=21-OHase;
AltName: Full=Cytochrome P-450c21;
AltName: Full=Cytochrome P450 21;
AltName: Full=Cytochrome P450 XXI;
AltName: Full=Cytochrome P450-C21;
AltName: Full=Cytochrome P450-C21B;
Name=CYP21A2; Synonyms=CYP21, CYP21B;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ALLELE CYP21A2*1A).
PubMed=3486422; DOI=10.1073/pnas.83.9.2841;
Higashi Y., Yoshioka H., Yamane M., Gotoh O., Fujii-Kuriyama Y.;
"Complete nucleotide sequence of two steroid 21-hydroxylase genes
tandemly arranged in human chromosome: a pseudogene and a genuine
gene.";
Proc. Natl. Acad. Sci. U.S.A. 83:2841-2845(1986).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ALLELE CYP21A2*1B) (ISOFORM
1).
PubMed=3487786; DOI=10.1073/pnas.83.14.5111;
White P.C., New M.I., Dupont B.;
"Structure of human steroid 21-hydroxylase genes.";
Proc. Natl. Acad. Sci. U.S.A. 83:5111-5115(1986).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT AH3 THR-268, VARIANTS LEU-9
INS; ARG-102 AND SER-493, AND INVOLVEMENT IN AH3.
PubMed=3038528;
Rodrigues N.R., Dunham I., Yu C.Y., Carroll M.C., Porter R.R.,
Campbell R.D.;
"Molecular characterization of the HLA-linked steroid 21-hydroxylase B
gene from an individual with congenital adrenal hyperplasia.";
EMBO J. 6:1653-1661(1987).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT AH3 LEU-281, AND VARIANT
LEU-9 INS.
PubMed=3267225; DOI=10.1172/JCI113562;
Globerman H., Amor M., Parker K.L., New M.I., White P.C.;
"Nonsense mutation causing steroid 21-hydroxylase deficiency.";
J. Clin. Invest. 82:139-144(1988).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS LEU-9 INS; ARG-102 AND
SER-493, AND VARIANTS AH3 HIS-339 AND SER-453.
TISSUE=Peripheral blood;
PubMed=1406709; DOI=10.1210/mend.6.8.1406709;
Helmberg A., Tusie-Luna M.-T., Tabarelli M., Kofler R., White P.C.;
"R339H and P453S: CYP21 mutations associated with nonclassic steroid
21-hydroxylase deficiency that are not apparent gene conversions.";
Mol. Endocrinol. 6:1318-1322(1992).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=19505723; DOI=10.1016/j.molimm.2009.04.033;
Blasko B., Banlaki Z., Gyapay G., Pozsonyi E., Sasvari-Szekely M.,
Rajczy K., Fust G., Szilagyi A.;
"Linkage analysis of the C4A/C4B copy number variation and
polymorphisms of the adjacent steroid 21-hydroxylase gene in a healthy
population.";
Mol. Immunol. 46:2623-2629(2009).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ALLELE CYP21A2*6) (ISOFORM 2).
TISSUE=Adrenal gland;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=14574404; DOI=10.1038/nature02055;
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
"The DNA sequence and analysis of human chromosome 6.";
Nature 425:805-811(2003).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
SER-493.
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[11]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 109-185, AND VARIANT AH3 ASN-172.
PubMed=8485582; DOI=10.1038/ng0393-260;
Collier S., Tassabehji M., Sinnott P., Strachan T.;
"A de novo pathological point mutation at the 21-hydroxylase locus:
implications for gene conversion in the human genome.";
Nat. Genet. 3:260-265(1993).
[12]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 149-182, AND VARIANT AH3 ASN-172.
PubMed=3871526; DOI=10.1073/pnas.82.2.521;
Carroll M.C., Campbell R.D., Porter R.R.;
"Mapping of steroid 21-hydroxylase genes adjacent to complement
component C4 genes in HLA, the major histocompatibility complex in
man.";
Proc. Natl. Acad. Sci. U.S.A. 82:521-525(1985).
[13]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 149-182, AND VARIANT AH3 ASN-172.
PubMed=3257825; DOI=10.1073/pnas.85.5.1600;
Amor M., Parker K.L., Globerman H., New M.I., White P.C.;
"Mutation in the CYP21B gene (Ile-172-->Asn) causes steroid 21-
hydroxylase deficiency.";
Proc. Natl. Acad. Sci. U.S.A. 85:1600-1604(1988).
[14]
NUCLEOTIDE SEQUENCE [MRNA] OF 265-494 (ISOFORM 1), AND VARIANT AH3
LEU-281.
PubMed=3497399; DOI=10.1073/pnas.84.16.5858;
Matteson K.J., Phillips J.A. III, Miller W.L., Chung B.C.,
Orlando P.J., Frisch H., Ferrandez A., Burr I.M.;
"P450XXI (steroid 21-hydroxylase) gene deletions are not found in
family studies of congenital adrenal hyperplasia.";
Proc. Natl. Acad. Sci. U.S.A. 84:5858-5862(1987).
[15]
X-RAY CRYSTALLOGRAPHY (2.64 ANGSTROMS) OF 29-494 IN COMPLEX WITH HEME
AND PROGESTERONE, FUNCTION, COFACTOR, AND CATALYTIC ACTIVITY.
PubMed=25855791; DOI=10.1074/jbc.M115.646307;
Pallan P.S., Wang C., Lei L., Yoshimoto F.K., Auchus R.J.,
Waterman M.R., Guengerich F.P., Egli M.;
"Human Cytochrome P450 21A2, the major steroid 21-hydroxylase:
structure of the enzyme-progesterone substrate complex and rate-
limiting c-h bond cleavage.";
J. Biol. Chem. 290:13128-13143(2015).
[16]
CHARACTERIZATION OF VARIANT AH3 LEU-281, AND MUTAGENESIS OF SER-268
AND CYS-428.
PubMed=1864962; DOI=10.1172/JCI115334;
Wu D.-A., Chung B.-C.;
"Mutations of P450c21 (steroid 21-hydroxylase) at Cys428, Val281, and
Ser268 result in complete, partial, or no loss of enzymatic activity,
respectively.";
J. Clin. Invest. 88:519-523(1991).
[17]
REVIEW ON AH3 VARIANTS.
Gunn S.K., Sherman L.D., Therrell B.L., Owerbach D.I.;
"Molecular genetics of 21-hydroxylase deficient late-onset adrenal
hyperplasia.";
Semin. Reprod. Endocrinol. 11:347-352(1993).
[18]
REVIEW ON AH3 VARIANTS, AND GENE CONVERSION.
PubMed=8081391; DOI=10.1002/humu.1380030408;
White P.C., Tusie-Luna M.-T., New M.I., Speiser P.W.;
"Mutations in steroid 21-hydroxylase (CYP21).";
Hum. Mutat. 3:373-378(1994).
[19]
VARIANTS AH3 LEU-211 AND LEU-281.
PubMed=3260007; DOI=10.1056/NEJM198807073190104;
Speiser P.W., New M.I., White P.C.;
"Molecular genetic analysis of nonclassic steroid 21-hydroxylase
deficiency associated with HLA-B14,DR1.";
N. Engl. J. Med. 319:19-23(1988).
[20]
VARIANTS AH3 ASN-172 AND TRP-356, AND VARIANT LEU-9 INS.
PubMed=2303461;
Chiou S.-H., Hu M.-C., Chung B.-C.;
"A missense mutation at Ile172-->Asn or Arg356-->Trp causes steroid
21-hydroxylase deficiency.";
J. Biol. Chem. 265:3549-3552(1990).
[21]
VARIANT AH3 ASN-172.
PubMed=1937474; DOI=10.1007/BF00201731;
Partanen J., Campbell R.D.;
"Substitution of Ile-172 to Asn in the steroid 21-hydroxylase B
(P450c21B) gene in a Finnish patient with the simple virilizing form
of congenital adrenal hyperplasia.";
Hum. Genet. 87:716-720(1991).
[22]
VARIANT AH3 LEU-30, AND VARIANT THR-268.
PubMed=2072928; DOI=10.1210/mend-5-5-685;
Tusie-Luna M.T., Speiser P.W., Dumic M., New M.I., White P.C.;
"A mutation (Pro-30 to Leu) in CYP21 represents a potential nonclassic
steroid 21-hydroxylase deficiency allele.";
Mol. Endocrinol. 5:685-692(1991).
[23]
VARIANTS AH3 LEU-30; ASN-172; ASN-236; GLU-237; LYS-239; LEU-281 AND
TRP-356.
PubMed=1644925; DOI=10.1172/JCI115897;
Speiser P.W., Dupont J., Zhu D., Serrat J., Buegeleisen M.,
Tusie-Luna M.-T., Lesser M., New M.I., White P.C.;
"Disease expression and molecular genotype in congenital adrenal
hyperplasia due to 21-hydroxylase deficiency.";
J. Clin. Invest. 90:584-595(1992).
[24]
VARIANT AH3 SER-453.
PubMed=1406699; DOI=10.1210/mend.6.8.1406699;
Owerbach D., Sherman L., Ballard A.L., Azziz R.;
"Pro-453 to Ser mutation in CYP21 is associated with nonclassic
steroid 21-hydroxylase deficiency.";
Mol. Endocrinol. 6:1211-1215(1992).
[25]
VARIANTS AH3 LEU-105; SER-291 AND SER-453.
PubMed=1496017; DOI=10.1073/pnas.89.15.7232;
Wedell A., Ritzen E.M., Haglund-Stengler B., Luthman H.;
"Steroid 21-hydroxylase deficiency: three additional mutated alleles
and establishment of phenotype-genotype relationships of common
mutations.";
Proc. Natl. Acad. Sci. U.S.A. 89:7232-7236(1992).
[26]
VARIANT AH3 PRO-483.
PubMed=8478006; DOI=10.1007/BF00218263;
Wedell A., Luthman H.;
"Steroid 21-hydroxylase (P450c21): a new allele and spread of
mutations through the pseudogene.";
Hum. Genet. 91:236-240(1993).
[27]
VARIANTS AH3 ASN-172; ASN-236; LEU-281 AND PRO-483, AND VARIANT
SER-493.
PubMed=7749410; DOI=10.1002/humu.1380050205;
Barbat B., Bogyo A., Raux-Demay M.-C., Kuttenn F., Boue J.,
Simon-Bouy B., Serre J.-L., Boue A., Mornet E.;
"Screening of CYP21 gene mutations in 129 French patients affected by
steroid 21-hydroxylase deficiency.";
Hum. Mutat. 5:126-130(1995).
[28]
VARIANT AH3 ASP-380.
PubMed=9067760;
DOI=10.1002/(SICI)1098-1004(1997)9:2<181::AID-HUMU12>3.0.CO;2-Z;
Kirby-Keyser L., Porter C.C., Donohoue P.A.;
"E380D: a novel point mutation of CYP21 in an HLA-homozygous patient
with salt-losing congenital adrenal hyperplasia due to 21-hydroxylase
deficiency.";
Hum. Mutat. 9:181-182(1997).
[29]
VARIANTS AH3 PRO-356 AND GLN-356.
PubMed=9187661; DOI=10.1007/s004390050436;
Lajic S., Levo A., Nikoshkov A., Lundberg Y., Partanen J., Wedell A.;
"A cluster of missense mutations at Arg356 of human steroid 21-
hydroxylase may impair redox partner interaction.";
Hum. Genet. 99:704-709(1997).
[30]
VARIANTS AH3 LEU-105 AND SER-453.
PubMed=8989258; DOI=10.1210/jcem.82.1.3678;
Nikoshkov A., Lajic S., Holst M., Wedell A., Luthman H.;
"Synergistic effect of partially inactivating mutations in steroid 21-
hydroxylase deficiency.";
J. Clin. Endocrinol. Metab. 82:194-199(1997).
[31]
VARIANTS AH3, AND VARIANTS.
PubMed=9580109; DOI=10.1007/s004390050672;
Ordonez-Sanchez M.L., Ramirez-Jimenez S., Lopez-Gutierrez A.U.,
Riba L., Gamboa-Cardiel S., Cerrillo-Hinojosa M.,
Altamirano-Bustamante N., Calzada-Leon R., Robles-Valdes C.,
Mendoza-Morfin F., Tusie-Luna M.T.;
"Molecular genetic analysis of patients carrying steroid 21-
hydroxylase deficiency in the Mexican population: identification of
possible new mutations and high prevalence of apparent germ-line
mutations.";
Hum. Genet. 102:170-177(1998).
[32]
VARIANTS AH3 GLU-196 DEL; SER-291 AND PRO-483.
PubMed=9497336; DOI=10.1074/jbc.273.11.6163;
Nikoshkov A., Lajic S., Vlamis-Gardikas A., Tranebjaerg L., Holst M.,
Wedell A., Luthman H.;
"Naturally occurring mutants of human steroid 21-hydroxylase (P450c21)
pinpoint residues important for enzyme activity and stability.";
J. Biol. Chem. 273:6163-6165(1998).
[33]
VARIANT AH3 GLN-30, CHARACTERIZATION OF VARIANT AH3 GLN-30,
SUBCELLULAR LOCATION, TOPOLOGY, AND DOMAIN.
PubMed=10198222; DOI=10.1006/bbrc.1999.0482;
Lajic S., Nikoshkov A., Holst M., Wedell A.;
"Effects of missense mutations and deletions on membrane anchoring and
enzyme function of human steroid 21-hydroxylase (P450c21).";
Biochem. Biophys. Res. Commun. 257:384-390(1999).
[34]
VARIANTS AH3 LEU-30; VAL-90; ASN-172; ALA-178; LEU-281; CYS-291;
HIS-354; TRP-356 AND SER-453.
PubMed=10364682; DOI=10.1159/000022866;
Lobato M.N., Ordonez-Sanchez M.L., Tusie-Luna M.T., Meseguer A.;
"Mutation analysis in patients with congenital adrenal hyperplasia in
the Spanish population: identification of putative novel steroid 21-
hydroxylase deficiency alleles associated with the classic form of the
disease.";
Hum. Hered. 49:169-175(1999).
[35]
VARIANTS AH3 TYR-169; LEU-281 AND GLN-356.
PubMed=10094562;
DOI=10.1002/(SICI)1098-1004(1999)13:2<172::AID-HUMU17>3.3.CO;2-E;
Witchel S.F., Smith R., Suda-Hartman M.;
"Identification of CYP21 mutations, one novel, by single strand
conformational polymorphism (SSCP) analysis.";
Hum. Mutat. 13:172-172(1999).
[36]
VARIANTS AH3 LEU-30; GLU-64; ASN-172; ASN-236; LEU-281; SER-291;
TRP-356 AND VAL-362.
PubMed=10408778;
DOI=10.1002/(SICI)1098-1004(1999)13:6<482::AID-HUMU8>3.0.CO;2-0;
Ohlsson G., Mueller J., Skakkebaek N.E., Schwartz M.;
"Steroid 21-hydroxylase deficiency: mutational spectrum in Denmark,
three novel mutations, and in vitro expression analysis.";
Hum. Mutat. 13:482-486(1999).
[37]
VARIANTS AH3 LEU-30; ASN-172; ASN-236; GLU-237; LYS-239; LEU-281 AND
TRP-356.
PubMed=10408786;
DOI=10.1002/(SICI)1098-1004(1999)13:6<505::AID-HUMU16>3.0.CO;2-0;
Kapelari K., Ghanaati Z., Wollmann H., Ventz M., Ranke M.B.,
Kofler R., Peters H.;
"A rapid screening for steroid 21-hydroxylase mutations in patients
with congenital adrenal hyperplasia.";
Hum. Mutat. 13:505-505(1999).
[38]
VARIANTS AH3 LEU-281; TRP-356 AND SER-424.
PubMed=10443693; DOI=10.1210/jcem.84.8.5937;
Billerbeck A.E.C., Bachega T.A.S.S., Frazatto E.T., Nishi M.Y.,
Goldberg A.C., Marin M.L.C., Madureira G., Monte O., Arnhold I.J.P.,
Mendonca B.B.;
"A novel missense mutation, GLY424SER, in Brazilian patients with 21-
hydroxylase deficiency.";
J. Clin. Endocrinol. Metab. 84:2870-2872(1999).
[39]
VARIANTS AH3 LEU-30; ASN-172; LEU-281; TRP-356 AND SER-493, AND
VARIANT THR-268.
PubMed=10496074; DOI=10.1007/s100380050167;
Asanuma A., Ohura T., Ogawa E., Sato S., Igarashi Y., Matsubara Y.,
Iinuma K.;
"Molecular analysis of Japanese patients with steroid 21-hydroxylase
deficiency.";
J. Hum. Genet. 44:312-317(1999).
[40]
VARIANTS AH3 ASN-172 AND TRP-356.
PubMed=10051010;
Lako M., Ramsden S., Campbell R.D., Strachan T.;
"Mutation screening in British 21-hydroxylase deficiency families and
development of novel microsatellite based approaches to prenatal
diagnosis.";
J. Med. Genet. 36:119-124(1999).
[41]
VARIANTS AH3 LEU-281 AND SER-453, AND VARIANTS THR-268 AND SER-493.
PubMed=10391209; DOI=10.1038/10290;
Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N.,
Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L.,
Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q.,
Lander E.S.;
"Characterization of single-nucleotide polymorphisms in coding regions
of human genes.";
Nat. Genet. 22:231-238(1999).
[42]
ERRATUM.
Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N.,
Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L.,
Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q.,
Lander E.S.;
Nat. Genet. 23:373-373(1999).
[43]
VARIANTS AH3 LEU-30; ASN-172; LEU-281; GLY-281; PHE-300; CYS-354;
TRP-356 AND SER-453.
PubMed=10720040; DOI=10.1210/jcem.85.3.6441;
Krone N., Braun A., Roscher A.A., Knorr D., Schwarz H.P.;
"Predicting phenotype in steroid 21-hydroxylase deficiency?
Comprehensive genotyping in 155 unrelated, well defined patients from
southern Germany.";
J. Clin. Endocrinol. Metab. 85:1059-1065(2000).
[44]
VARIANTS AH3 LEU-30; ASN-172; PRO-261; TRP-356 AND PRO-483.
PubMed=11598371; DOI=10.1159/000049992;
Loke K.Y., Lee Y.S., Lee W.W.R., Poh L.K.S.;
"Molecular analysis of CYP-21 mutations for congenital adrenal
hyperplasia in Singapore.";
Horm. Res. 55:179-184(2001).
[45]
VARIANTS AH3 LEU-30; ASN-172; LEU-281; MET-317; TRP-356; CYS-435 AND
SER-453.
PubMed=11232002; DOI=10.1210/jcem.86.1.7131;
Deneux C., Tardy V., Dib A., Mornet E., Billaud L., Charron D.,
Morel Y., Kuttenn F.;
"Phenotype-genotype correlation in 56 women with nonclassical
congenital adrenal hyperplasia due to 21-hydroxylase deficiency.";
J. Clin. Endocrinol. Metab. 86:207-213(2001).
[46]
VARIANTS AH3 LEU-30; ASN-172; LEU-281; SER-291; TRP-356; SER-424;
HIS-426; SER-453 AND PRO-483, AND CHARACTERIZATION OF VARIANT AH3
HIS-426.
PubMed=11600539; DOI=10.1210/jcem.86.10.7898;
Baumgartner-Parzer S.M., Schulze E., Waldhaeusl W., Pauschenwein S.,
Rondot S., Nowotny P., Meyer K., Frisch H., Waldhauser F.,
Vierhapper H.;
"Mutational spectrum of the steroid 21-hydroxylase gene in Austria:
identification of a novel missense mutation.";
J. Clin. Endocrinol. Metab. 86:4771-4775(2001).
[47]
VARIANT AH3 TRP-363.
PubMed=11746135; DOI=10.1002/pd.167;
Levo A., Partanen J.;
"Novel mutations in the human CYP21 gene.";
Prenat. Diagn. 21:885-889(2001).
[48]
VARIANTS AH3 LEU-30; ASN-172; LEU-281; LEU-283; TRP-356 AND SER-453.
PubMed=12222711; DOI=10.1080/080352502760148595;
Ezquieta B., Cueva E., Varela J., Oliver A., Fernandez J., Jariego C.;
"Non-classical 21-hydroxylase deficiency in children: association of
adrenocorticotropic hormone-stimulated 17-hydroxyprogesterone with the
risk of compound heterozygosity with severe mutations.";
Acta Paediatr. 91:892-898(2002).
[49]
VARIANTS HYPERANDROGENISM MET-304; SER-375 AND SER-453, AND
CHARACTERIZATION OF VARIANTS HYPERANDROGENISM MET-304; SER-375 AND
SER-453.
PubMed=12050257; DOI=10.1210/jcem.87.6.8525;
Lajic S., Clauin S., Robins T., Vexiau P., Blanche H.,
Bellanne-Chantelot C., Wedell A.;
"Novel mutations in CYP21 detected in individuals with
hyperandrogenism.";
J. Clin. Endocrinol. Metab. 87:2824-2829(2002).
[50]
VARIANTS AH3 CYS-408 AND SER-424.
PubMed=12213891; DOI=10.1210/jc.2001-011939;
Billerbeck A.E.C., Mendonca B.B., Pinto E.M., Madureira G.,
Arnhold I.J.P., Bachega T.A.S.S.;
"Three novel mutations in CYP21 gene in Brazilian patients with the
classical form of 21-hydroxylase deficiency due to a founder effect.";
J. Clin. Endocrinol. Metab. 87:4314-4317(2002).
[51]
VARIANTS AH3 THR-15; LEU-30; ASN-172; LEU-281 AND SER-453.
PubMed=12887291; DOI=10.1530/eje.0.1490137;
Dolzan V., Stopar-Obreza M., Zerjav-Tansek M., Breskvar K.,
Krzisnik C., Battelino T.;
"Mutational spectrum of congenital adrenal hyperplasia in Slovenian
patients: a novel Ala15Thr mutation and Pro30Leu within a larger gene
conversion associated with a severe form of the disease.";
Eur. J. Endocrinol. 149:137-144(2003).
[52]
VARIANTS AH3 LEU-30; LEU-62; ASN-172; LEU-281; PRO-341; TRP-356;
SER-453 AND PRO-483.
PubMed=12788866; DOI=10.1210/jc.2002-021433;
Pinto G., Tardy V., Trivin C., Thalassinos C., Lortat-Jacob S.,
Nihoul-Fekete C., Morel Y., Brauner R.;
"Follow-up of 68 children with congenital adrenal hyperplasia due to
21-hydroxylase deficiency: relevance of genotype for management.";
J. Clin. Endocrinol. Metab. 88:2624-2633(2003).
[53]
VARIANTS AH3 ASN-172; LEU-281; ARG-291; TYR-301; PRO-341; TRP-356 AND
GLN-483.
PubMed=12915679; DOI=10.1210/jc.2002-021681;
Stikkelbroeck N.M., Hoefsloot L.H., de Wijs I.J., Otten B.J.,
Hermus A.R., Sistermans E.A.;
"CYP21 gene mutation analysis in 198 patients with 21-hydroxylase
deficiency in The Netherlands: six novel mutations and a specific
cluster of four mutations.";
J. Clin. Endocrinol. Metab. 88:3852-3859(2003).
[54]
VARIANTS AH3 ASN-172; TRP-356 AND TRP-483.
PubMed=14715874; DOI=10.1210/jc.2003-031056;
Kharrat M., Tardy V., M'Rad R., Maazoul F., Jemaa L.B., Refai M.,
Morel Y., Chaabouni H.;
"Molecular genetic analysis of Tunisian patients with a classic form
of 21-hydroxylase deficiency: identification of four novel mutations
and high prevalence of Q318X mutation.";
J. Clin. Endocrinol. Metab. 89:368-374(2004).
[55]
VARIANT AH3 HIS-124.
PubMed=14676460; DOI=10.1159/000075587;
Usui T., Nishisho K., Kaji M., Ikuno N., Yorifuji T., Yasuda T.,
Kuzuya H., Shimatsu A.;
"Three novel mutations in Japanese patients with 21-hydroxylase
deficiency.";
Horm. Res. 61:126-132(2004).
[56]
VARIANTS AH3 THR-15; LEU-30; LEU-281 AND SER-482, AND CHARACTERIZATION
OF VARIANTS AH3 THR-15 AND SER-482.
PubMed=15126570; DOI=10.1210/jc.2003-031630;
Barbaro M., Lajic S., Baldazzi L., Balsamo A., Pirazzoli P.,
Cicognani A., Wedell A., Cacciari E.;
"Functional analysis of two recurrent amino acid substitutions in the
CYP21 gene from Italian patients with congenital adrenal
hyperplasia.";
J. Clin. Endocrinol. Metab. 89:2402-2407(2004).
[57]
VARIANTS AH3 LEU-30; ASN-172; ASN-236; GLU-237; LYS-239; LEU-281;
SER-291; GLN-356; TRP-356; TYR-365; SER-453; LEU-479 AND PRO-483, AND
VARIANT ARG-102.
PubMed=15110320; DOI=10.1016/j.ymgme.2004.02.006;
Zeng X., Witchel S.F., Dobrowolski S.F., Moulder P.V., Jarvik J.W.,
Telmer C.A.;
"Detection and assignment of CYP21 mutations using peptide mass
signature genotyping.";
Mol. Genet. Metab. 82:38-47(2004).
[58]
VARIANTS AH3 LEU-30; ASN-172 AND TRP-356.
PubMed=16046588; DOI=10.1210/jc.2005-0379;
Grigorescu Sido A., Weber M.M., Grigorescu Sido P., Clausmeyer S.,
Heinrich U., Schulze E.;
"21-Hydroxylase and 11beta-hydroxylase mutations in Romanian patients
with classic congenital adrenal hyperplasia.";
J. Clin. Endocrinol. Metab. 90:5769-5773(2005).
[59]
VARIANTS AH3 ARG-169; ARG-178; ARG-302 AND CYS-426, CHARACTERIZATION
OF VARIANTS AH3 ARG-169; ARG-178; ARG-302 AND CYS-426, AND CATALYTIC
ACTIVITY.
PubMed=16984992; DOI=10.1210/jc.2006-0777;
Grischuk Y., Rubtsov P., Riepe F.G., Groetzinger J., Beljelarskaia S.,
Prassolov V., Kalintchenko N., Semitcheva T., Peterkova V.,
Tiulpakov A., Sippell W.G., Krone N.;
"Four novel missense mutations in the CYP21A2 gene detected in Russian
patients suffering from the classical form of congenital adrenal
hyperplasia: identification, functional characterization, and
structural analysis.";
J. Clin. Endocrinol. Metab. 91:4976-4980(2006).
[60]
VARIANTS AH3 LEU-30; LEU-62; ASN-172; TRP-356 AND SER-453, AND
CHARACTERIZATION OF VARIANTS AH3 LEU-62 AND SER-453.
PubMed=18319307; DOI=10.1210/jc.2007-2701;
Menassa R., Tardy V., Despert F., Bouvattier-Morel C., Brossier J.P.,
Cartigny M., Morel Y.;
"p.H62L, a rare mutation of the CYP21 gene identified in two forms of
21-hydroxylase deficiency.";
J. Clin. Endocrinol. Metab. 93:1901-1908(2008).
[61]
VARIANTS AH3 ARG-56; LEU-62; ARG-107; PRO-142; ASN-172; TRP-356;
CYS-408 AND SER-453, AND CHARACTERIZATION OF VARIANTS AH3 ARG-56;
LEU-62; ARG-107; PRO-142; CYS-408 AND SER-453.
PubMed=18381579; DOI=10.1210/jc.2007-2594;
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.;
"Inhibition of CYP21A2 enzyme activity caused by novel missense
mutations identified in Brazilian and Scandinavian patients.";
J. Clin. Endocrinol. Metab. 93:2416-2420(2008).
[62]
VARIANTS AH3 GLN-121 AND SER-453, AND CHARACTERIZATION OF VARIANT AH3
GLN-121.
PubMed=18445671; DOI=10.1210/jc.2007-2646;
Riepe F.G., Hiort O., Grotzinger J., Sippell W.G., Krone N.,
Holterhus P.M.;
"Functional and structural consequences of a novel point mutation in
the CYP21A2 gene causing congenital adrenal hyperplasia: potential
relevance of helix C for P450 oxidoreductase-21-hydroxylase
interaction.";
J. Clin. Endocrinol. Metab. 93:2891-2895(2008).
[63]
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, AND CHARACTERIZATION OF
VARIANTS AH3 PRO-167; ASN-172; LEU-281; ASP-292; LYS-320; TRP-369 AND
SER-424.
PubMed=20080860; DOI=10.1210/jc.2009-1202;
Tardy V., Menassa R., Sulmont V., Lienhardt-Roussie A., Lecointre C.,
Brauner R., David M., Morel Y.;
"Phenotype-genotype correlations of 13 rare CYP21A2 mutations detected
in 46 patients affected with 21-hydroxylase deficiency and in one
carrier.";
J. Clin. Endocrinol. Metab. 95:1288-1300(2010).
[64]
VARIANT AH3 PHE-198.
PubMed=21169732; DOI=10.3275/7417;
Niceta M., Bono M., Fabiano C., Pojero F., Niceta F., Sammarco P.,
Corsello G., Garofalo P.;
"A large view of CYP21 locus among Sicilians and other populations:
identification of a novel CYP21A2 variant in Sicily.";
J. Endocrinol. Invest. 34:847-854(2011).
[65]
VARIANTS AH3 HIS-191 AND ASN-282, CHARACTERIZATION OF VARIANTS AH3
HIS-191 AND ASN-282, FUNCTION, CATALYTIC ACTIVITY, AND
BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=22014889; DOI=10.1016/j.metabol.2011.08.008;
Concolino P., Mello E., Patrosso M.C., Penco S., Zuppi C.,
Capoluongo E.;
"p.H282N and p.Y191H: 2 novel CYP21A2 mutations in Italian congenital
adrenal hyperplasia patients.";
Metabolism 61:519-524(2012).
[66]
VARIANTS AH3 MET-12; PHE-113; 389-GLN--ALA-391 DEL AND PRO-450,
VARIANTS CYS-16; GLY-202; LEU-267 AND MET-450, CHARACTERIZATION OF
VARIANTS AH3 MET-12; PHE-113; 389-GLN--ALA-391 DEL; PRO-450 AND
SER-482, CHARACTERIZATION OF VARIANTS CYS-16; GLY-202; LEU-267 AND
MET-450, FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL
PROPERTIES.
PubMed=27721825; DOI=10.1155/2016/4209670;
de Paula Michelatto D., Karlsson L., Lusa A.L., Silva C.D.,
Oestberg L.J., Persson B., Guerra-Junior G., de Lemos-Marini S.H.,
Barbaro M., de Mello M.P., Lajic S.;
"Functional and structural consequences of nine CYP21A2 mutations
ranging from very mild to severe effects.";
Int. J. Endocrinol. 2016:4209670-4209670(2016).
-!- FUNCTION: Specifically catalyzes the 21-hydroxylation of steroids.
Required for the adrenal synthesis of mineralocorticoids and
glucocorticoids (PubMed:22014889). {ECO:0000269|PubMed:22014889,
ECO:0000269|PubMed:25855791, ECO:0000269|PubMed:27721825}.
-!- CATALYTIC ACTIVITY: A C(21) steroid + [reduced NADPH--hemoprotein
reductase] + O(2) = a 21-hydroxy-C(21)-steroid + [oxidized NADPH--
hemoprotein reductase] + H(2)O. {ECO:0000269|PubMed:16984992,
ECO:0000269|PubMed:22014889, ECO:0000269|PubMed:25855791,
ECO:0000269|PubMed:27721825}.
-!- COFACTOR:
Name=heme; Xref=ChEBI:CHEBI:30413;
Evidence={ECO:0000269|PubMed:25855791};
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=1.59 uM for 17-hydroxyprogesterone
{ECO:0000269|PubMed:22014889};
KM=12.5 uM for for 17-hydroxyprogesterone (at 37 degrees
Celsius) {ECO:0000269|PubMed:27721825};
KM=1.05 uM for progesterone {ECO:0000269|PubMed:22014889};
Vmax=5.8 nmol/min/mg enzyme {ECO:0000269|PubMed:22014889};
Vmax=0.5 nmol/min/mg enzyme (at 37 degrees Celsius)
{ECO:0000269|PubMed:27721825};
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral
membrane protein {ECO:0000269|PubMed:10198222}. Microsome membrane
{ECO:0000269|PubMed:10198222}; Peripheral membrane protein
{ECO:0000269|PubMed:10198222}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P08686-1; Sequence=Displayed;
Name=2;
IsoId=P08686-2; Sequence=VSP_046264, VSP_046265;
Note=No experimental confirmation available.;
-!- DOMAIN: The leucine-rich hydrophobic amino acid N-terminal region
probably helps to anchor the protein to the microsomal membrane.
{ECO:0000269|PubMed:10198222}.
-!- POLYMORPHISM: Seven non deleterious alleles are known: CYP21A2*1A,
CYP21A2*1B, CYP21A2*2, CYP21A2*3, CYP21A2*4, CYP21A2*5 and
CYP21A2*6. The sequence shown corresponds to allele CYP21A2*1B.
Deleterious alleles are mostly generated by recombinations between
CYP21A2 and the pseudogene CYP21A1P through gene conversion. This
process consists of recombination events that either delete
CYP21A2 or transfer deleterious mutations from CYP21A1P to
CYP21A2.
-!- DISEASE: Adrenal hyperplasia 3 (AH3) [MIM:201910]: A form of
congenital adrenal hyperplasia, a common recessive disease due to
defective synthesis of cortisol. Congenital adrenal hyperplasia is
characterized by androgen excess leading to ambiguous genitalia in
affected females, rapid somatic growth during childhood in both
sexes with premature closure of the epiphyses and short adult
stature. Four clinical types: 'salt wasting' (SW, the most severe
type), 'simple virilizing' (SV, less severely affected patients),
with normal aldosterone biosynthesis, 'non-classic form' or late-
onset (NC or LOAH) and 'cryptic' (asymptomatic).
{ECO:0000269|PubMed:10051010, ECO:0000269|PubMed:10094562,
ECO:0000269|PubMed:10198222, ECO:0000269|PubMed:10364682,
ECO:0000269|PubMed:10391209, ECO:0000269|PubMed:10408778,
ECO:0000269|PubMed:10408786, ECO:0000269|PubMed:10443693,
ECO:0000269|PubMed:10496074, ECO:0000269|PubMed:10720040,
ECO:0000269|PubMed:11232002, ECO:0000269|PubMed:11598371,
ECO:0000269|PubMed:11600539, ECO:0000269|PubMed:11746135,
ECO:0000269|PubMed:12213891, ECO:0000269|PubMed:12222711,
ECO:0000269|PubMed:12788866, ECO:0000269|PubMed:12887291,
ECO:0000269|PubMed:12915679, ECO:0000269|PubMed:1406699,
ECO:0000269|PubMed:1406709, ECO:0000269|PubMed:14676460,
ECO:0000269|PubMed:14715874, ECO:0000269|PubMed:1496017,
ECO:0000269|PubMed:15110320, ECO:0000269|PubMed:15126570,
ECO:0000269|PubMed:16046588, ECO:0000269|PubMed:1644925,
ECO:0000269|PubMed:16984992, ECO:0000269|PubMed:18319307,
ECO:0000269|PubMed:18381579, ECO:0000269|PubMed:18445671,
ECO:0000269|PubMed:1864962, ECO:0000269|PubMed:1937474,
ECO:0000269|PubMed:20080860, ECO:0000269|PubMed:2072928,
ECO:0000269|PubMed:21169732, ECO:0000269|PubMed:22014889,
ECO:0000269|PubMed:2303461, ECO:0000269|PubMed:27721825,
ECO:0000269|PubMed:3038528, ECO:0000269|PubMed:3257825,
ECO:0000269|PubMed:3260007, ECO:0000269|PubMed:3267225,
ECO:0000269|PubMed:3497399, ECO:0000269|PubMed:3871526,
ECO:0000269|PubMed:7749410, ECO:0000269|PubMed:8478006,
ECO:0000269|PubMed:8485582, ECO:0000269|PubMed:8989258,
ECO:0000269|PubMed:9067760, ECO:0000269|PubMed:9187661,
ECO:0000269|PubMed:9497336, ECO:0000269|PubMed:9580109}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
-!- WEB RESOURCE: Name=Cytochrome P450 Allele Nomenclature Committee;
Note=CYP21A2 alleles;
URL="http://www.cypalleles.ki.se/cyp21.htm";
-!- WEB RESOURCE: Name=SHMPD; Note=The Singapore human mutation and
polymorphism database;
URL="http://shmpd.bii.a-star.edu.sg/gene.php?genestart=A&genename=CYP21A2";
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EMBL; M12792; AAB59440.1; -; Genomic_DNA.
EMBL; M13936; AAA59695.1; -; Genomic_DNA.
EMBL; M26856; AAA52064.1; -; Genomic_DNA.
EMBL; X58906; CAA41709.1; -; Genomic_DNA.
EMBL; GQ222286; ACT35412.1; -; Genomic_DNA.
EMBL; GQ222296; ACT35422.1; -; Genomic_DNA.
EMBL; GQ222301; ACT35427.1; -; Genomic_DNA.
EMBL; AK054616; BAB70774.1; -; mRNA.
EMBL; AL645922; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL662828; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL662849; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL844853; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL929593; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BX679671; CAM26070.1; -; Genomic_DNA.
EMBL; CR753845; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471081; EAX03570.1; -; Genomic_DNA.
EMBL; CR936924; CAQ07659.1; -; Genomic_DNA.
EMBL; BC125182; AAI25183.1; -; mRNA.
EMBL; K02771; AAA59706.1; -; Genomic_DNA.
EMBL; M19711; AAA83248.1; -; Genomic_DNA.
EMBL; M17252; AAA59985.1; -; mRNA.
CCDS; CCDS47406.1; -. [P08686-2]
PIR; A25446; O4HUC2.
RefSeq; NP_000491.4; NM_000500.7.
RefSeq; NP_001122062.3; NM_001128590.3.
UniGene; Hs.654479; -.
PDB; 2GEG; Model; -; C=27-494.
PDB; 4Y8W; X-ray; 2.64 A; A/B/C=29-494.
PDBsum; 2GEG; -.
PDBsum; 4Y8W; -.
ProteinModelPortal; P08686; -.
SMR; P08686; -.
STRING; 9606.ENSP00000408860; -.
BindingDB; P08686; -.
ChEMBL; CHEMBL2759; -.
DrugBank; DB01026; Ketoconazole.
SwissLipids; SLP:000001618; -.
iPTMnet; P08686; -.
PhosphoSitePlus; P08686; -.
BioMuta; CYP21A2; -.
DMDM; 117275; -.
PaxDb; P08686; -.
PeptideAtlas; P08686; -.
PRIDE; P08686; -.
Ensembl; ENST00000383321; ENSP00000372811; ENSG00000206338.
Ensembl; ENST00000434026; ENSP00000392321; ENSG00000232414.
Ensembl; ENST00000435122; ENSP00000415043; ENSG00000231852.
Ensembl; ENST00000436607; ENSP00000403721; ENSG00000235134. [P08686-1]
Ensembl; ENST00000448314; ENSP00000398594; ENSG00000198457. [P08686-1]
Ensembl; ENST00000452386; ENSP00000403230; ENSG00000233151.
GeneID; 1589; -.
KEGG; hsa:1589; -.
UCSC; uc003nzf.3; human. [P08686-1]
CTD; 1589; -.
DisGeNET; 1589; -.
EuPathDB; HostDB:ENSG00000231852.6; -.
GeneCards; CYP21A2; -.
H-InvDB; HIX0057724; -.
H-InvDB; HIX0166983; -.
HGNC; HGNC:2600; CYP21A2.
HPA; HPA048979; -.
HPA; HPA053371; -.
MalaCards; CYP21A2; -.
MIM; 201910; phenotype.
MIM; 613815; gene.
neXtProt; NX_P08686; -.
Orphanet; 315306; Classic congenital adrenal hyperplasia due to 21-hydroxylase deficiency, salt wasting form.
Orphanet; 315311; Classic congenital adrenal hyperplasia due to 21-hydroxylase deficiency, simple virilizing form.
Orphanet; 95698; Non-classic congenital adrenal hyperplasia due to 21-hydroxylase deficiency.
PharmGKB; PA27096; -.
eggNOG; KOG0156; Eukaryota.
eggNOG; COG2124; LUCA.
HOGENOM; HOG000036991; -.
HOVERGEN; HBG106944; -.
InParanoid; P08686; -.
KO; K00513; -.
OrthoDB; EOG091G074I; -.
PhylomeDB; P08686; -.
BioCyc; MetaCyc:HS09769-MONOMER; -.
BRENDA; 1.14.99.10; 2681.
Reactome; R-HSA-193993; Mineralocorticoid biosynthesis.
Reactome; R-HSA-194002; Glucocorticoid biosynthesis.
Reactome; R-HSA-211976; Endogenous sterols.
GeneWiki; 21-Hydroxylase; -.
GenomeRNAi; 1589; -.
PRO; PR:P08686; -.
Proteomes; UP000005640; Chromosome 6.
Bgee; ENSG00000231852; -.
CleanEx; HS_CYP21A2; -.
ExpressionAtlas; P08686; baseline and differential.
Genevisible; P08686; HS.
GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
GO; GO:0031090; C:organelle membrane; IEA:UniProtKB-SubCell.
GO; GO:0020037; F:heme binding; IDA:UniProtKB.
GO; GO:0005506; F:iron ion binding; IEA:InterPro.
GO; GO:0004509; F:steroid 21-monooxygenase activity; IDA:UniProtKB.
GO; GO:0005496; F:steroid binding; IEA:UniProtKB-KW.
GO; GO:0008395; F:steroid hydroxylase activity; IMP:UniProtKB.
GO; GO:0006704; P:glucocorticoid biosynthetic process; TAS:Reactome.
GO; GO:0006705; P:mineralocorticoid biosynthetic process; TAS:Reactome.
GO; GO:0006694; P:steroid biosynthetic process; IDA:UniProtKB.
GO; GO:0008202; P:steroid metabolic process; IMP:UniProtKB.
GO; GO:0016125; P:sterol metabolic process; TAS:Reactome.
Gene3D; 1.10.630.10; -; 1.
InterPro; IPR001128; Cyt_P450.
InterPro; IPR017972; Cyt_P450_CS.
InterPro; IPR002401; Cyt_P450_E_grp-I.
InterPro; IPR036396; Cyt_P450_sf.
Pfam; PF00067; p450; 1.
PRINTS; PR00463; EP450I.
PRINTS; PR00385; P450.
SUPFAM; SSF48264; SSF48264; 1.
PROSITE; PS00086; CYTOCHROME_P450; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome;
Congenital adrenal hyperplasia; Disease mutation;
Endoplasmic reticulum; Heme; Iron; Lipid-binding; Membrane;
Metal-binding; Microsome; Monooxygenase; Oxidoreductase; Polymorphism;
Reference proteome; Steroid-binding; Steroidogenesis.
CHAIN 1 494 Steroid 21-hydroxylase.
/FTId=PRO_0000051976.
REGION 342 358 Steroid-binding. {ECO:0000250}.
METAL 428 428 Iron (heme axial ligand).
{ECO:0000269|PubMed:25855791}.
BINDING 233 233 Substrate. {ECO:0000269|PubMed:25855791}.
VAR_SEQ 6 6 L -> LL (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_046264.
VAR_SEQ 68 102 VVVLNSKRTIEEAMVKKWADFAGRPEPLTYKLVSK -> KL
VSR (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_046265.
VARIANT 9 9 L -> LL (in allele CYP21A2*2).
{ECO:0000269|PubMed:1406709,
ECO:0000269|PubMed:2303461,
ECO:0000269|PubMed:3038528,
ECO:0000269|PubMed:3267225}.
/FTId=VAR_018363.
VARIANT 12 12 L -> M (in AH3; non-classic form; unknown
pathological significance; no effect on
steroid 21-monooxygenase activity).
{ECO:0000269|PubMed:27721825}.
/FTId=VAR_077582.
VARIANT 15 15 A -> T (in AH3; salt wasting form;
unknown pathological significance; no
significant difference in steroid 21-
monooxygenase activity;
dbSNP:rs63749090).
{ECO:0000269|PubMed:12887291,
ECO:0000269|PubMed:15126570}.
/FTId=VAR_026059.
VARIANT 16 16 R -> C (decreased steroid 21-
monooxygenase activity;
dbSNP:rs757608533).
{ECO:0000269|PubMed:27721825}.
/FTId=VAR_077583.
VARIANT 30 30 P -> L (in AH3; non-classic form; 10% of
non-classic AH3 Texan patients; 50%
steroid 21-monooxygenase activity;
dbSNP:rs9378251).
{ECO:0000269|PubMed:10364682,
ECO:0000269|PubMed:10408778,
ECO:0000269|PubMed:10408786,
ECO:0000269|PubMed:10496074,
ECO:0000269|PubMed:10720040,
ECO:0000269|PubMed:11232002,
ECO:0000269|PubMed:11598371,
ECO:0000269|PubMed:11600539,
ECO:0000269|PubMed:12222711,
ECO:0000269|PubMed:12788866,
ECO:0000269|PubMed:12887291,
ECO:0000269|PubMed:15110320,
ECO:0000269|PubMed:15126570,
ECO:0000269|PubMed:16046588,
ECO:0000269|PubMed:1644925,
ECO:0000269|PubMed:18319307,
ECO:0000269|PubMed:2072928}.
/FTId=VAR_001281.
VARIANT 30 30 P -> Q (in AH3; does not affect membrane
binding; enzyme function abolished).
{ECO:0000269|PubMed:10198222}.
/FTId=VAR_026060.
VARIANT 56 56 G -> R (in AH3; loss of activity).
{ECO:0000269|PubMed:18381579}.
/FTId=VAR_065668.
VARIANT 62 62 H -> L (in AH3; non-classic form; simple
virilizing form when associated with a
second mild mutation such as S-453 or L-
30; activity is significantly reduced in
association with S-453; dbSNP:rs9378252).
{ECO:0000269|PubMed:12788866,
ECO:0000269|PubMed:18319307,
ECO:0000269|PubMed:18381579}.
/FTId=VAR_018364.
VARIANT 64 64 G -> E (in AH3; no activity).
{ECO:0000269|PubMed:10408778}.
/FTId=VAR_007923.
VARIANT 77 77 I -> T (in AH3; simple virilizing form).
{ECO:0000269|PubMed:20080860}.
/FTId=VAR_065669.
VARIANT 90 90 G -> V (in AH3).
{ECO:0000269|PubMed:10364682}.
/FTId=VAR_026061.
VARIANT 98 98 K -> R.
/FTId=VAR_001282.
VARIANT 102 102 K -> R (in allele CYP21A2*3;
dbSNP:rs6474).
{ECO:0000269|PubMed:1406709,
ECO:0000269|PubMed:15110320,
ECO:0000269|PubMed:3038528}.
/FTId=VAR_001283.
VARIANT 105 105 P -> L (in AH3; dbSNP:rs550051210).
{ECO:0000269|PubMed:1496017,
ECO:0000269|PubMed:8989258}.
/FTId=VAR_001284.
VARIANT 107 107 L -> R (in AH3; loss of activity).
{ECO:0000269|PubMed:18381579}.
/FTId=VAR_065670.
VARIANT 113 113 S -> F (in AH3; non-classic form; loss of
steroid 21-monooxygenase activity).
{ECO:0000269|PubMed:27721825}.
/FTId=VAR_077584.
VARIANT 121 121 K -> Q (in AH3; non-classic form; reduced
activity; decreased affinity for 17-
hydroxyprogesterone and progesterone;
dbSNP:rs547552654).
{ECO:0000269|PubMed:18445671}.
/FTId=VAR_065671.
VARIANT 124 124 R -> H (in AH3; dbSNP:rs72552750).
{ECO:0000269|PubMed:14676460}.
/FTId=VAR_026062.
VARIANT 142 142 L -> P (in AH3; loss of activity).
{ECO:0000269|PubMed:18381579}.
/FTId=VAR_065672.
VARIANT 167 167 L -> P (in AH3; salt wasting form; loss
of activity).
{ECO:0000269|PubMed:20080860}.
/FTId=VAR_065673.
VARIANT 169 169 C -> R (in AH3; exhibits low hydroxylase
activity toward 17-hydroxyprogesterone
and progesterone).
{ECO:0000269|PubMed:16984992}.
/FTId=VAR_075372.
VARIANT 169 169 C -> Y (in AH3).
{ECO:0000269|PubMed:10094562}.
/FTId=VAR_001285.
VARIANT 172 172 I -> N (in AH3; simple virilizing form;
1-4% activity; dbSNP:rs6475).
{ECO:0000269|PubMed:10051010,
ECO:0000269|PubMed:10364682,
ECO:0000269|PubMed:10408778,
ECO:0000269|PubMed:10408786,
ECO:0000269|PubMed:10496074,
ECO:0000269|PubMed:10720040,
ECO:0000269|PubMed:11232002,
ECO:0000269|PubMed:11598371,
ECO:0000269|PubMed:11600539,
ECO:0000269|PubMed:12222711,
ECO:0000269|PubMed:12788866,
ECO:0000269|PubMed:12887291,
ECO:0000269|PubMed:12915679,
ECO:0000269|PubMed:14715874,
ECO:0000269|PubMed:15110320,
ECO:0000269|PubMed:16046588,
ECO:0000269|PubMed:1644925,
ECO:0000269|PubMed:18319307,
ECO:0000269|PubMed:18381579,
ECO:0000269|PubMed:1937474,
ECO:0000269|PubMed:20080860,
ECO:0000269|PubMed:2303461,
ECO:0000269|PubMed:3257825,
ECO:0000269|PubMed:3871526,
ECO:0000269|PubMed:7749410,
ECO:0000269|PubMed:8485582}.
/FTId=VAR_001286.
VARIANT 178 178 G -> A (in AH3; dbSNP:rs72552751).
{ECO:0000269|PubMed:10364682}.
/FTId=VAR_026063.
VARIANT 178 178 G -> R (in AH3; exhibits low enzymatic
activity toward 17-hydroxyprogesterone
and progesterone; dbSNP:rs772317717).
{ECO:0000269|PubMed:16984992}.
/FTId=VAR_075373.
VARIANT 183 183 D -> E (in allele CYP21A2*4;
dbSNP:rs1040310).
/FTId=VAR_001287.
VARIANT 191 191 Y -> H (in AH3; exhibits low enzymatic
activity toward 17-hydroxyprogesterone
and progesterone).
{ECO:0000269|PubMed:22014889}.
/FTId=VAR_075374.
VARIANT 196 196 Missing (in AH3; moderate).
{ECO:0000269|PubMed:9497336}.
/FTId=VAR_008688.
VARIANT 198 198 L -> F (in AH3; dbSNP:rs143240527).
{ECO:0000269|PubMed:21169732}.
/FTId=VAR_075375.
VARIANT 202 202 S -> G (decreased steroid 21-
monooxygenase activity;
dbSNP:rs372964292).
{ECO:0000269|PubMed:27721825}.
/FTId=VAR_077585.
VARIANT 211 211 V -> L (in AH3; non-classic form;
pathogenicity uncertain).
{ECO:0000269|PubMed:3260007}.
/FTId=VAR_026064.
VARIANT 230 230 I -> T (in AH3).
{ECO:0000269|PubMed:20080860}.
/FTId=VAR_065674.
VARIANT 233 233 R -> K (in AH3).
{ECO:0000269|PubMed:20080860}.
/FTId=VAR_065675.
VARIANT 236 236 I -> N (in AH3; salt wasting form;
dbSNP:rs111647200).
{ECO:0000269|PubMed:10408778,
ECO:0000269|PubMed:10408786,
ECO:0000269|PubMed:15110320,
ECO:0000269|PubMed:1644925,
ECO:0000269|PubMed:7749410}.
/FTId=VAR_001288.
VARIANT 237 237 V -> E (in AH3; salt wasting form;
dbSNP:rs12530380).
{ECO:0000269|PubMed:10408786,
ECO:0000269|PubMed:15110320,
ECO:0000269|PubMed:1644925}.
/FTId=VAR_001289.
VARIANT 239 239 M -> K (in AH3; salt wasting form;
dbSNP:rs6476).
{ECO:0000269|PubMed:10408786,
ECO:0000269|PubMed:15110320,
ECO:0000269|PubMed:1644925}.
/FTId=VAR_001290.
VARIANT 261 261 L -> P (in AH3; dbSNP:rs750337015).
{ECO:0000269|PubMed:11598371}.
/FTId=VAR_026065.
VARIANT 267 267 P -> L (decreased steroid 21-
monooxygenase activity; dbSNP:rs61732108
and dbSNP:rs142028935).
{ECO:0000269|PubMed:27721825}.
/FTId=VAR_077586.
VARIANT 268 268 S -> T (in allele CYP21A2*5;
dbSNP:rs6472).
{ECO:0000269|PubMed:10391209,
ECO:0000269|PubMed:10496074,
ECO:0000269|PubMed:2072928,
ECO:0000269|PubMed:3038528}.
/FTId=VAR_001291.
VARIANT 281 281 V -> G (in AH3; salt wasting form).
{ECO:0000269|PubMed:10720040}.
/FTId=VAR_026066.
VARIANT 281 281 V -> L (in AH3; non-classic form; 50%
activity; most common variant; normal KM
but 20% reduced Vmax; dbSNP:rs6471).
{ECO:0000269|PubMed:10094562,
ECO:0000269|PubMed:10364682,
ECO:0000269|PubMed:10391209,
ECO:0000269|PubMed:10408778,
ECO:0000269|PubMed:10408786,
ECO:0000269|PubMed:10443693,
ECO:0000269|PubMed:10496074,
ECO:0000269|PubMed:10720040,
ECO:0000269|PubMed:11232002,
ECO:0000269|PubMed:11600539,
ECO:0000269|PubMed:12222711,
ECO:0000269|PubMed:12788866,
ECO:0000269|PubMed:12887291,
ECO:0000269|PubMed:12915679,
ECO:0000269|PubMed:15110320,
ECO:0000269|PubMed:15126570,
ECO:0000269|PubMed:1644925,
ECO:0000269|PubMed:1864962,
ECO:0000269|PubMed:20080860,
ECO:0000269|PubMed:3260007,
ECO:0000269|PubMed:3267225,
ECO:0000269|PubMed:3497399,
ECO:0000269|PubMed:7749410}.
/FTId=VAR_001292.
VARIANT 282 282 H -> N (in AH3; exhibits low enzymatic
activity toward 17-hydroxyprogesterone
and progesterone).
{ECO:0000269|PubMed:22014889}.
/FTId=VAR_075376.
VARIANT 283 283 M -> L (in AH3).
{ECO:0000269|PubMed:12222711}.
/FTId=VAR_026067.
VARIANT 291 291 G -> C (in AH3).
{ECO:0000269|PubMed:10364682}.
/FTId=VAR_026068.
VARIANT 291 291 G -> R (in AH3; dbSNP:rs201552310).
{ECO:0000269|PubMed:12915679}.
/FTId=VAR_018365.
VARIANT 291 291 G -> S (in AH3; salt wasting form; less
then 1% activity; dbSNP:rs201552310).
{ECO:0000269|PubMed:10408778,
ECO:0000269|PubMed:11600539,
ECO:0000269|PubMed:1496017,
ECO:0000269|PubMed:15110320,
ECO:0000269|PubMed:20080860,
ECO:0000269|PubMed:9497336}.
/FTId=VAR_001293.
VARIANT 292 292 G -> D (in AH3; salt wasting form; less
then 1% activity).
{ECO:0000269|PubMed:20080860}.
/FTId=VAR_065676.
VARIANT 300 300 L -> F (in AH3; salt wasting form;
dbSNP:rs765001985).
{ECO:0000269|PubMed:10720040}.
/FTId=VAR_026069.
VARIANT 301 301 S -> Y (in AH3).
{ECO:0000269|PubMed:12915679}.
/FTId=VAR_018366.
VARIANT 302 302 W -> R (in AH3; exhibits low enzymatic
activity toward 17-hydroxyprogesterone
and progesterone).
{ECO:0000269|PubMed:16984992}.
/FTId=VAR_075377.
VARIANT 304 304 V -> M (in hyperandrogenism; due to 21-
hydroxylase deficiency; non-classic type;
residual activity of 46% for conversion
of 17-hydroxyprogesterone and 26% for
conversion of progesterone compared with
the normal enzyme; dbSNP:rs151344505).
{ECO:0000269|PubMed:12050257}.
/FTId=VAR_026070.
VARIANT 317 317 L -> M (in AH3).
{ECO:0000269|PubMed:11232002}.
/FTId=VAR_026071.
VARIANT 320 320 E -> K (in AH3; simple virilizing form;
4% activity).
{ECO:0000269|PubMed:20080860}.
/FTId=VAR_065677.
VARIANT 339 339 R -> H (in AH3; non-classic form; 50%
activity; dbSNP:rs72552754).
{ECO:0000269|PubMed:1406709}.
/FTId=VAR_001294.
VARIANT 341 341 R -> P (in AH3; simple virilizing form).
{ECO:0000269|PubMed:12788866,
ECO:0000269|PubMed:12915679,
ECO:0000269|PubMed:20080860}.
/FTId=VAR_018367.
VARIANT 341 341 R -> W (in AH3; non-classic form; mild;
dbSNP:rs777860817).
/FTId=VAR_001295.
VARIANT 354 354 R -> C (in AH3; salt wasting form;
dbSNP:rs772900496).
{ECO:0000269|PubMed:10720040}.
/FTId=VAR_026072.
VARIANT 354 354 R -> H (in AH3; salt wasting form;
dbSNP:rs760216630).
{ECO:0000269|PubMed:10364682,
ECO:0000269|PubMed:20080860}.
/FTId=VAR_026073.
VARIANT 356 356 R -> P (in AH3; salt wasting form; 0.15%
activity). {ECO:0000269|PubMed:9187661}.
/FTId=VAR_001296.
VARIANT 356 356 R -> Q (in AH3; simple virilizing form;
mild; 0.65% activity; dbSNP:rs574370139).
{ECO:0000269|PubMed:10094562,
ECO:0000269|PubMed:15110320,
ECO:0000269|PubMed:9187661}.
/FTId=VAR_001297.
VARIANT 356 356 R -> W (in AH3; salt wasting form;
dbSNP:rs7769409).
{ECO:0000269|PubMed:10051010,
ECO:0000269|PubMed:10364682,
ECO:0000269|PubMed:10408778,
ECO:0000269|PubMed:10408786,
ECO:0000269|PubMed:10443693,
ECO:0000269|PubMed:10496074,
ECO:0000269|PubMed:10720040,
ECO:0000269|PubMed:11232002,
ECO:0000269|PubMed:11598371,
ECO:0000269|PubMed:11600539,
ECO:0000269|PubMed:12222711,
ECO:0000269|PubMed:12788866,
ECO:0000269|PubMed:12915679,
ECO:0000269|PubMed:14715874,
ECO:0000269|PubMed:15110320,
ECO:0000269|PubMed:16046588,
ECO:0000269|PubMed:1644925,
ECO:0000269|PubMed:18319307,
ECO:0000269|PubMed:18381579,
ECO:0000269|PubMed:20080860,
ECO:0000269|PubMed:2303461}.
/FTId=VAR_001298.
VARIANT 362 362 A -> V (in AH3; no activity).
{ECO:0000269|PubMed:10408778}.
/FTId=VAR_007924.
VARIANT 363 363 L -> W (in AH3).
{ECO:0000269|PubMed:11746135}.
/FTId=VAR_026074.
VARIANT 365 365 H -> Y (in AH3).
{ECO:0000269|PubMed:15110320}.
/FTId=VAR_026075.
VARIANT 369 369 R -> W (in AH3; dbSNP:rs781074931).
{ECO:0000269|PubMed:20080860}.
/FTId=VAR_065678.
VARIANT 375 375 G -> S (in hyperandrogenism; due to 21-
hydroxylase deficiency; almost completely
abolished enzyme activity;
dbSNP:rs151344506).
{ECO:0000269|PubMed:12050257}.
/FTId=VAR_026076.
VARIANT 380 380 E -> D (in AH3; salt wasting form;
dbSNP:rs72552756).
{ECO:0000269|PubMed:9067760}.
/FTId=VAR_001299.
VARIANT 389 391 Missing (in AH3; salt wasting form; loss
of steroid 21-monooxygenase activity).
{ECO:0000269|PubMed:27721825}.
/FTId=VAR_077587.
VARIANT 408 408 R -> C (in AH3; very low residual
activity; dbSNP:rs72552757).
{ECO:0000269|PubMed:12213891,
ECO:0000269|PubMed:18381579,
ECO:0000269|PubMed:20080860}.
/FTId=VAR_026077.
VARIANT 424 424 G -> S (in AH3; very low activity;
dbSNP:rs72552758).
{ECO:0000269|PubMed:10443693,
ECO:0000269|PubMed:11600539,
ECO:0000269|PubMed:12213891,
ECO:0000269|PubMed:20080860}.
/FTId=VAR_026078.
VARIANT 426 426 R -> C (in AH3; exhibits low enzymatic
activity toward 17-hydroxyprogesterone
and progesterone).
{ECO:0000269|PubMed:16984992}.
/FTId=VAR_075378.
VARIANT 426 426 R -> H (in AH3; exhibits low enzymatic
activity toward 17-hydroxyprogesterone;
dbSNP:rs151344504).
{ECO:0000269|PubMed:11600539,
ECO:0000269|PubMed:20080860}.
/FTId=VAR_026079.
VARIANT 435 435 R -> C (in AH3; dbSNP:rs767333157).
{ECO:0000269|PubMed:11232002}.
/FTId=VAR_026080.
VARIANT 450 450 T -> M (decreased steroid 21-
monooxygenase activity).
{ECO:0000269|PubMed:27721825}.
/FTId=VAR_077588.
VARIANT 450 450 T -> P (in AH3; salt wasting form; loss
of steroid 21-monooxygenase activity).
{ECO:0000269|PubMed:27721825}.
/FTId=VAR_077589.
VARIANT 453 453 P -> S (in AH3; non-classic form; simple
virilizing form when associated with L-
62; 50% of activity; almost completely
abolished enzyme activity when associated
with S-375; dbSNP:rs6445).
{ECO:0000269|PubMed:10364682,
ECO:0000269|PubMed:10391209,
ECO:0000269|PubMed:10720040,
ECO:0000269|PubMed:11232002,
ECO:0000269|PubMed:11600539,
ECO:0000269|PubMed:12050257,
ECO:0000269|PubMed:12222711,
ECO:0000269|PubMed:12788866,
ECO:0000269|PubMed:12887291,
ECO:0000269|PubMed:1406699,
ECO:0000269|PubMed:1406709,
ECO:0000269|PubMed:1496017,
ECO:0000269|PubMed:15110320,
ECO:0000269|PubMed:18319307,
ECO:0000269|PubMed:18381579,
ECO:0000269|PubMed:18445671,
ECO:0000269|PubMed:20080860,
ECO:0000269|PubMed:8989258}.
/FTId=VAR_001300.
VARIANT 479 479 R -> L (in AH3; dbSNP:rs184649564).
{ECO:0000269|PubMed:15110320}.
/FTId=VAR_026081.
VARIANT 482 482 P -> S (in AH3; reduced enzyme activity
to 70% of normal; dbSNP:rs776989258).
{ECO:0000269|PubMed:15126570,
ECO:0000269|PubMed:27721825}.
/FTId=VAR_026082.
VARIANT 483 483 R -> P (in AH3; moderate; 1-2% of
activity; dbSNP:rs200005406).
{ECO:0000269|PubMed:11598371,
ECO:0000269|PubMed:11600539,
ECO:0000269|PubMed:12788866,
ECO:0000269|PubMed:15110320,
ECO:0000269|PubMed:7749410,
ECO:0000269|PubMed:8478006,
ECO:0000269|PubMed:9497336}.
/FTId=VAR_001301.
VARIANT 483 483 R -> Q (in AH3; dbSNP:rs200005406).
{ECO:0000269|PubMed:12915679}.
/FTId=VAR_018368.
VARIANT 483 483 R -> W (in AH3; salt wasting form;
dbSNP:rs759736443).
{ECO:0000269|PubMed:14715874}.
/FTId=VAR_026083.
VARIANT 493 493 N -> S (in allele CYP21A2*6;
dbSNP:rs6473).
{ECO:0000269|PubMed:10391209,
ECO:0000269|PubMed:10496074,
ECO:0000269|PubMed:1406709,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:3038528,
ECO:0000269|PubMed:7749410}.
/FTId=VAR_001302.
MUTAGEN 268 268 S->C,M,T: No loss of function.
{ECO:0000269|PubMed:1864962}.
MUTAGEN 281 281 V->I: Normal KM but 50% reduced Vmax.
MUTAGEN 281 281 V->T: Normal KM but 10% reduced Vmax.
MUTAGEN 428 428 C->M,S,T: Loss of activity and loss of
P450 absorption.
{ECO:0000269|PubMed:1864962}.
CONFLICT 155 155 G -> D (in Ref. 7; BAB70774).
{ECO:0000305}.
CONFLICT 242 242 R -> G (in Ref. 7; BAB70774).
{ECO:0000305}.
CONFLICT 277 277 L -> Q (in Ref. 7; BAB70774).
{ECO:0000305}.
CONFLICT 304 304 V -> A (in Ref. 7; BAB70774).
{ECO:0000305}.
CONFLICT 311 311 P -> L (in Ref. 14; AAA59985).
{ECO:0000305}.
CONFLICT 346 346 N -> I (in Ref. 14; AAA59985).
{ECO:0000305}.
CONFLICT 426 426 R -> P (in Ref. 1; AAB59440).
{ECO:0000305}.
CONFLICT 437 437 E -> D (in Ref. 1; AAB59440).
{ECO:0000305}.
HELIX 38 40 {ECO:0000244|PDB:4Y8W}.
HELIX 44 50 {ECO:0000244|PDB:4Y8W}.
HELIX 52 55 {ECO:0000244|PDB:4Y8W}.
STRAND 57 63 {ECO:0000244|PDB:4Y8W}.
STRAND 66 71 {ECO:0000244|PDB:4Y8W}.
HELIX 74 81 {ECO:0000244|PDB:4Y8W}.
TURN 82 84 {ECO:0000244|PDB:4Y8W}.
HELIX 85 88 {ECO:0000244|PDB:4Y8W}.
HELIX 95 99 {ECO:0000244|PDB:4Y8W}.
HELIX 114 128 {ECO:0000244|PDB:4Y8W}.
TURN 129 134 {ECO:0000244|PDB:4Y8W}.
HELIX 135 150 {ECO:0000244|PDB:4Y8W}.
HELIX 160 177 {ECO:0000244|PDB:4Y8W}.
HELIX 179 182 {ECO:0000244|PDB:4Y8W}.
TURN 183 185 {ECO:0000244|PDB:4Y8W}.
HELIX 187 201 {ECO:0000244|PDB:4Y8W}.
HELIX 204 211 {ECO:0000244|PDB:4Y8W}.
HELIX 213 216 {ECO:0000244|PDB:4Y8W}.
HELIX 223 245 {ECO:0000244|PDB:4Y8W}.
HELIX 256 261 {ECO:0000244|PDB:4Y8W}.
HELIX 278 309 {ECO:0000244|PDB:4Y8W}.
HELIX 311 324 {ECO:0000244|PDB:4Y8W}.
TURN 336 338 {ECO:0000244|PDB:4Y8W}.
HELIX 343 355 {ECO:0000244|PDB:4Y8W}.
STRAND 369 373 {ECO:0000244|PDB:4Y8W}.
STRAND 376 378 {ECO:0000244|PDB:4Y8W}.
STRAND 383 386 {ECO:0000244|PDB:4Y8W}.
HELIX 388 392 {ECO:0000244|PDB:4Y8W}.
TURN 395 397 {ECO:0000244|PDB:4Y8W}.
STRAND 398 400 {ECO:0000244|PDB:4Y8W}.
HELIX 406 409 {ECO:0000244|PDB:4Y8W}.
HELIX 431 446 {ECO:0000244|PDB:4Y8W}.
STRAND 449 457 {ECO:0000244|PDB:4Y8W}.
STRAND 478 482 {ECO:0000244|PDB:4Y8W}.
SEQUENCE 494 AA; 55887 MW; 7E1FF83B59FBA136 CRC64;
MLLLGLLLLP LLAGARLLWN WWKLRSLHLP PLAPGFLHLL QPDLPIYLLG LTQKFGPIYR
LHLGLQDVVV LNSKRTIEEA MVKKWADFAG RPEPLTYKLV SKNYPDLSLG DYSLLWKAHK
KLTRSALLLG IRDSMEPVVE QLTQEFCERM RAQPGTPVAI EEEFSLLTCS IICYLTFGDK
IKDDNLMPAY YKCIQEVLKT WSHWSIQIVD VIPFLRFFPN PGLRRLKQAI EKRDHIVEMQ
LRQHKESLVA GQWRDMMDYM LQGVAQPSME EGSGQLLEGH VHMAAVDLLI GGTETTANTL
SWAVVFLLHH PEIQQRLQEE LDHELGPGAS SSRVPYKDRA RLPLLNATIA EVLRLRPVVP
LALPHRTTRP SSISGYDIPE GTVIIPNLQG AHLDETVWER PHEFWPDRFL EPGKNSRALA
FGCGARVCLG EPLARLELFV VLTRLLQAFT LLPSGDALPS LQPLPHCSVI LKMQPFQVRL
QPRGMGAHSP GQNQ


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