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Cholesterol side-chain cleavage enzyme, mitochondrial (EC 1.14.15.6) (CYPXIA1) (Cholesterol desmolase) (Cytochrome P450 11A1) (Cytochrome P450(scc))

 CP11A_HUMAN             Reviewed;         521 AA.
P05108; A8K8D5; B3KPU8; G3XAD7; Q15081; Q16805; Q8N1A7;
13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
03-APR-2007, sequence version 2.
12-SEP-2018, entry version 198.
RecName: Full=Cholesterol side-chain cleavage enzyme, mitochondrial;
EC=1.14.15.6;
AltName: Full=CYPXIA1;
AltName: Full=Cholesterol desmolase;
AltName: Full=Cytochrome P450 11A1;
AltName: Full=Cytochrome P450(scc);
Flags: Precursor;
Name=CYP11A1; Synonyms=CYP11A;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=3024157; DOI=10.1073/pnas.83.23.8962;
Chung B.-C., Matteson K.J., Voutilainen R., Mohandas T.K.,
Miller W.L.;
"Human cholesterol side-chain cleavage enzyme, P450scc: cDNA cloning,
assignment of the gene to chromosome 15, and expression in the
placenta.";
Proc. Natl. Acad. Sci. U.S.A. 83:8962-8966(1986).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Placenta;
PubMed=3038854; DOI=10.1093/oxfordjournals.jbchem.a121955;
Morohashi K., Sogawa K., Omura T., Fujii-Kuriyama Y.;
"Gene structure of human cytochrome P-450(SCC), cholesterol
desmolase.";
J. Biochem. 101:879-887(1987).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Placenta, and Testis;
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).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16572171; DOI=10.1038/nature04601;
Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R.,
Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G.,
Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A.,
Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W.,
Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X.,
Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K.,
Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S.,
Nusbaum C.;
"Analysis of the DNA sequence and duplication history of human
chromosome 15.";
Nature 440:671-675(2006).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain;
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).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-89.
Chung B.-C.;
Submitted (JAN-1989) to the EMBL/GenBank/DDBJ databases.
[8]
PROTEIN SEQUENCE OF 51-54, AND INDUCTION.
TISSUE=Choriocarcinoma;
PubMed=1849407; DOI=10.1042/bj2740813;
Hu M.C., Guo I.C., Lin J.H., Chung B.-C.;
"Regulated expression of cytochrome P-450scc (cholesterol-side-chain
cleavage enzyme) in cultured cell lines detected by antibody against
bacterially expressed human protein.";
Biochem. J. 274:813-817(1991).
[9]
NUCLEOTIDE SEQUENCE [MRNA] OF 283-521 (ISOFORM 1).
PubMed=2419119; DOI=10.1210/endo-118-4-1296;
Matteson K.J., Chung B.-C., Urdea M.S., Miller W.L.;
"Study of cholesterol side-chain cleavage (20,22 desmolase) deficiency
causing congenital lipoid adrenal hyperplasia using bovine-sequence
P450scc oligodeoxyribonucleotide probes.";
Endocrinology 118:1296-1305(1986).
[10]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 41-521 IN COMPLEXES WITH
FDX1; HEME AND CHOLESTEROL, FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
PATHWAY, AND INTERACTION WITH FDX1.
PubMed=21636783; DOI=10.1073/pnas.1019441108;
Strushkevich N., MacKenzie F., Cherkesova T., Grabovec I., Usanov S.,
Park H.W.;
"Structural basis for pregnenolone biosynthesis by the mitochondrial
monooxygenase system.";
Proc. Natl. Acad. Sci. U.S.A. 108:10139-10143(2011).
[11]
VARIANT LYS-314.
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).
[12]
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).
[13]
VARIANT AICSR GLY-ASP-271 INS.
PubMed=11502818; DOI=10.1210/jcem.86.8.7748;
Tajima T., Fujieda K., Kouda N., Nakae J., Miller W.L.;
"Heterozygous mutation in the cholesterol side chain cleavage enzyme
(P450scc) gene in a patient with 46,XY sex reversal and adrenal
insufficiency.";
J. Clin. Endocrinol. Metab. 86:3820-3825(2001).
[14]
VARIANTS AICSR VAL-189 AND TRP-353.
PubMed=12161514; DOI=10.1210/jcem.87.8.8763;
Katsumata N., Ohtake M., Hojo T., Ogawa E., Hara T., Sato N.,
Tanaka T.;
"Compound heterozygous mutations in the cholesterol side-chain
cleavage enzyme gene (CYP11A) cause congenital adrenal insufficiency
in humans.";
J. Clin. Endocrinol. Metab. 87:3808-3813(2002).
[15]
VARIANT AICSR VAL-359, AND CHARACTERIZATION OF VARIANT AICSR VAL-359.
PubMed=16705068; DOI=10.1210/jc.2005-2230;
al Kandari H., Katsumata N., Alexander S., Rasoul M.A.;
"Homozygous mutation of P450 side-chain cleavage enzyme gene (CYP11A1)
in 46, XY patient with adrenal insufficiency, complete sex reversal,
and agenesis of corpus callosum.";
J. Clin. Endocrinol. Metab. 91:2821-2826(2006).
[16]
VARIANTS AICSR TRP-141 AND GLU-415, AND CHARACTERIZATION OF VARIANTS
AICSR TRP-141 AND GLU-415.
PubMed=18182448; DOI=10.1210/jc.2007-2330;
Kim C.J., Lin L., Huang N., Quigley C.A., Avruskin T.W.,
Achermann J.C., Miller W.L.;
"Severe combined adrenal and gonadal deficiency caused by novel
mutations in the cholesterol side chain cleavage enzyme, P450scc.";
J. Clin. Endocrinol. Metab. 93:696-702(2008).
[17]
VARIANT AICSR PRO-222, AND CHARACTERIZATION OF VARIANT AICSR PRO-222.
PubMed=19116240; DOI=10.1210/jc.2008-1118;
Rubtsov P., Karmanov M., Sverdlova P., Spirin P., Tiulpakov A.;
"A novel homozygous mutation in CYP11A1 gene is associated with late-
onset adrenal insufficiency and hypospadias in a 46,XY patient.";
J. Clin. Endocrinol. Metab. 94:936-939(2009).
-!- FUNCTION: Catalyzes the side-chain cleavage reaction of
cholesterol to pregnenolone, the precursor of most steroid
hormones. {ECO:0000269|PubMed:21636783}.
-!- CATALYTIC ACTIVITY: Cholesterol + 6 reduced adrenodoxin + 3 O(2) +
6 H(+) = pregnenolone + 4-methylpentanal + 6 oxidized adrenodoxin
+ 4 H(2)O. {ECO:0000269|PubMed:21636783}.
-!- COFACTOR:
Name=heme; Xref=ChEBI:CHEBI:30413;
Evidence={ECO:0000269|PubMed:21636783};
-!- PATHWAY: Lipid metabolism; C21-steroid hormone metabolism.
{ECO:0000269|PubMed:21636783}.
-!- SUBUNIT: Interacts with FDX1/adrenodoxin.
{ECO:0000269|PubMed:21636783}.
-!- INTERACTION:
Q9NZ94-2:NLGN3; NbExp=3; IntAct=EBI-7183136, EBI-16423037;
-!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
{ECO:0000250|UniProtKB:P14137}; Peripheral membrane protein
{ECO:0000305}. Note=Localizes to the matrix side of the
mitochondrion inner membrane. {ECO:0000250|UniProtKB:P14137}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P05108-1; Sequence=Displayed;
Name=2;
IsoId=P05108-2; Sequence=VSP_045695;
Note=No experimental confirmation available.;
-!- INDUCTION: By 8-bromo cyclic AMP. {ECO:0000269|PubMed:1849407}.
-!- DISEASE: Adrenal insufficiency, congenital, with 46,XY sex
reversal (AICSR) [MIM:613743]: A rare disorder that can present as
acute adrenal insufficiency in infancy or childhood. ACTH and
plasma renin activity are elevated and adrenal steroids are
inappropriately low or absent; the 46,XY patients have female
external genitalia, sometimes with clitoromegaly. The phenotypic
spectrum ranges from prematurity, complete underandrogenization,
and severe early-onset adrenal failure to term birth with
clitoromegaly and later-onset adrenal failure. Patients with
congenital adrenal insufficiency do not manifest the massive
adrenal enlargement typical of congenital lipoid adrenal
hyperplasia. {ECO:0000269|PubMed:11502818,
ECO:0000269|PubMed:12161514, ECO:0000269|PubMed:16705068,
ECO:0000269|PubMed:18182448, ECO:0000269|PubMed:19116240}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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EMBL; M14565; AAA52162.1; -; mRNA.
EMBL; X05367; CAA28965.1; -; Genomic_DNA.
EMBL; X05368; CAA28965.1; JOINED; Genomic_DNA.
EMBL; X05369; CAA28965.1; JOINED; Genomic_DNA.
EMBL; X05370; CAA28965.1; JOINED; Genomic_DNA.
EMBL; X05371; CAA28965.1; JOINED; Genomic_DNA.
EMBL; X05372; CAA28965.1; JOINED; Genomic_DNA.
EMBL; X05373; CAA28965.1; JOINED; Genomic_DNA.
EMBL; X05374; CAA28965.1; JOINED; Genomic_DNA.
EMBL; AK056794; BAG51810.1; -; mRNA.
EMBL; AK292300; BAF84989.1; -; mRNA.
EMBL; AC090826; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471136; EAW99341.1; -; Genomic_DNA.
EMBL; CH471136; EAW99342.1; -; Genomic_DNA.
EMBL; BC032329; AAH32329.1; -; mRNA.
EMBL; X14257; CAA32471.1; -; Genomic_DNA.
EMBL; M28253; AAA36404.1; -; mRNA.
CCDS; CCDS32291.1; -. [P05108-1]
CCDS; CCDS45303.1; -. [P05108-2]
PIR; A25922; A25922.
RefSeq; NP_000772.2; NM_000781.2. [P05108-1]
RefSeq; NP_001093243.1; NM_001099773.1. [P05108-2]
UniGene; Hs.303980; -.
PDB; 3N9Y; X-ray; 2.10 A; A/B=41-521.
PDB; 3N9Z; X-ray; 2.17 A; A/B=41-521.
PDB; 3NA0; X-ray; 2.50 A; A/B=44-514.
PDB; 3NA1; X-ray; 2.25 A; A/B=41-521.
PDBsum; 3N9Y; -.
PDBsum; 3N9Z; -.
PDBsum; 3NA0; -.
PDBsum; 3NA1; -.
ProteinModelPortal; P05108; -.
SMR; P05108; -.
BioGrid; 107955; 5.
IntAct; P05108; 5.
MINT; P05108; -.
STRING; 9606.ENSP00000268053; -.
BindingDB; P05108; -.
ChEMBL; CHEMBL2033; -.
DrugBank; DB00357; Aminoglutethimide.
DrugBank; DB00169; Cholecalciferol.
DrugBank; DB00882; Clomifene.
DrugBank; DB00257; Clotrimazole.
DrugBank; DB01234; Dexamethasone.
DrugBank; DB01396; Digitoxin.
DrugBank; DB00390; Digoxin.
DrugBank; DB02901; Dihydrotestosterone.
DrugBank; DB00917; Dinoprostone.
DrugBank; DB01437; Glutethimide.
DrugBank; DB01026; Ketoconazole.
DrugBank; DB00338; Omeprazole.
DrugBank; DB01232; Saquinavir.
DrugBank; DB00857; Terbinafine.
DrugBank; DB00624; Testosterone.
SwissLipids; SLP:000001196; -.
iPTMnet; P05108; -.
PhosphoSitePlus; P05108; -.
BioMuta; CYP11A1; -.
DMDM; 143811381; -.
PaxDb; P05108; -.
PeptideAtlas; P05108; -.
PRIDE; P05108; -.
ProteomicsDB; 51794; -.
DNASU; 1583; -.
Ensembl; ENST00000268053; ENSP00000268053; ENSG00000140459. [P05108-1]
Ensembl; ENST00000358632; ENSP00000351455; ENSG00000140459. [P05108-2]
GeneID; 1583; -.
KEGG; hsa:1583; -.
UCSC; uc002axs.3; human. [P05108-1]
CTD; 1583; -.
DisGeNET; 1583; -.
EuPathDB; HostDB:ENSG00000140459.17; -.
GeneCards; CYP11A1; -.
HGNC; HGNC:2590; CYP11A1.
HPA; HPA016436; -.
MalaCards; CYP11A1; -.
MIM; 118485; gene.
MIM; 613743; phenotype.
neXtProt; NX_P05108; -.
OpenTargets; ENSG00000140459; -.
Orphanet; 168558; 46,XY disorder of sex development - adrenal insufficiency due to CYP11A1 deficiency.
Orphanet; 289548; Inherited isolated adrenal insufficiency due to CYP11A1 deficiency.
PharmGKB; PA27089; -.
eggNOG; KOG0159; Eukaryota.
eggNOG; COG2124; LUCA.
GeneTree; ENSGT00900000140779; -.
HOGENOM; HOG000013161; -.
HOVERGEN; HBG051098; -.
InParanoid; P05108; -.
KO; K00498; -.
OMA; WGVRQCL; -.
OrthoDB; EOG091G04MV; -.
PhylomeDB; P05108; -.
TreeFam; TF105094; -.
BioCyc; MetaCyc:HS06719-MONOMER; -.
BRENDA; 1.14.15.6; 2681.
Reactome; R-HSA-196108; Pregnenolone biosynthesis.
Reactome; R-HSA-211976; Endogenous sterols.
Reactome; R-HSA-5579026; Defective CYP11A1 causes Adrenal insufficiency, congenital, with 46,XY sex reversal (AICSR).
SABIO-RK; P05108; -.
SIGNOR; P05108; -.
UniPathway; UPA00229; -.
ChiTaRS; CYP11A1; human.
EvolutionaryTrace; P05108; -.
GeneWiki; Cholesterol_side-chain_cleavage_enzyme; -.
GenomeRNAi; 1583; -.
PRO; PR:P05108; -.
Proteomes; UP000005640; Chromosome 15.
Bgee; ENSG00000140459; Expressed in 98 organ(s), highest expression level in right adrenal gland.
CleanEx; HS_CYP11A1; -.
ExpressionAtlas; P05108; baseline and differential.
Genevisible; P05108; HS.
GO; GO:0005743; C:mitochondrial inner membrane; ISS:UniProtKB.
GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
GO; GO:0008386; F:cholesterol monooxygenase (side-chain-cleaving) activity; IDA:UniProtKB.
GO; GO:0020037; F:heme binding; IDA:UniProtKB.
GO; GO:0005506; F:iron ion binding; IEA:InterPro.
GO; GO:0006700; P:C21-steroid hormone biosynthetic process; IDA:UniProtKB.
GO; GO:0008203; P:cholesterol metabolic process; IDA:UniProtKB.
GO; GO:0016125; P:sterol metabolic process; TAS:Reactome.
GO; GO:0042359; P:vitamin D metabolic process; ISS:UniProtKB.
Gene3D; 1.10.630.10; -; 1.
InterPro; IPR033283; CYP11A1.
InterPro; IPR001128; Cyt_P450.
InterPro; IPR017972; Cyt_P450_CS.
InterPro; IPR002401; Cyt_P450_E_grp-I.
InterPro; IPR036396; Cyt_P450_sf.
PANTHER; PTHR24279:SF3; PTHR24279:SF3; 1.
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; Cholesterol metabolism;
Complete proteome; Direct protein sequencing; Disease mutation; Heme;
Iron; Lipid metabolism; Membrane; Metal-binding; Mitochondrion;
Mitochondrion inner membrane; Monooxygenase; Oxidoreductase;
Polymorphism; Reference proteome; Steroid metabolism; Steroidogenesis;
Sterol metabolism; Transit peptide.
TRANSIT 1 39 Mitochondrion.
{ECO:0000250|UniProtKB:P00189}.
CHAIN 40 521 Cholesterol side-chain cleavage enzyme,
mitochondrial.
/FTId=PRO_0000003585.
METAL 462 462 Iron (heme axial ligand).
{ECO:0000244|PDB:3N9Y,
ECO:0000244|PDB:3N9Z,
ECO:0000244|PDB:3NA0,
ECO:0000244|PDB:3NA1,
ECO:0000269|PubMed:21636783}.
VAR_SEQ 1 158 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_045695.
VARIANT 141 141 L -> W (in AICSR; reduced activity;
dbSNP:rs121912813).
{ECO:0000269|PubMed:18182448}.
/FTId=VAR_065241.
VARIANT 189 189 A -> V (in AICSR; no loss of activity;
dbSNP:rs121912811).
{ECO:0000269|PubMed:12161514}.
/FTId=VAR_016949.
VARIANT 222 222 L -> P (in AICSR; markedly reduced
activity; dbSNP:rs387906601).
{ECO:0000269|PubMed:19116240}.
/FTId=VAR_065242.
VARIANT 271 271 D -> DGD (in AICSR; complete loss of
activity). {ECO:0000269|PubMed:11502818}.
/FTId=VAR_016950.
VARIANT 314 314 E -> K (in dbSNP:rs6161).
{ECO:0000269|PubMed:10391209}.
/FTId=VAR_013944.
VARIANT 353 353 R -> W (in AICSR; loss of activity;
dbSNP:rs72547508).
{ECO:0000269|PubMed:12161514}.
/FTId=VAR_016951.
VARIANT 359 359 A -> V (in AICSR; markedly reduced
activity; dbSNP:rs121912812).
{ECO:0000269|PubMed:16705068}.
/FTId=VAR_065243.
VARIANT 415 415 V -> E (in AICSR; complete loss of
activity; dbSNP:rs121912814).
{ECO:0000269|PubMed:18182448}.
/FTId=VAR_065244.
CONFLICT 16 16 C -> Y (in Ref. 1; AAA52162).
{ECO:0000305}.
CONFLICT 274 274 F -> L (in Ref. 2; CAA28965).
{ECO:0000305}.
CONFLICT 283 283 N -> H (in Ref. 9; AAA36404).
{ECO:0000305}.
CONFLICT 301 301 I -> M (in Ref. 1; AAA52162 and 9;
AAA36404). {ECO:0000305}.
CONFLICT 505 505 K -> E (in Ref. 3; BAG51810).
{ECO:0000305}.
HELIX 48 50 {ECO:0000244|PDB:3N9Y}.
HELIX 58 68 {ECO:0000244|PDB:3N9Y}.
HELIX 71 73 {ECO:0000244|PDB:3N9Y}.
HELIX 74 85 {ECO:0000244|PDB:3N9Y}.
STRAND 87 93 {ECO:0000244|PDB:3N9Y}.
STRAND 96 101 {ECO:0000244|PDB:3N9Y}.
HELIX 104 112 {ECO:0000244|PDB:3N9Y}.
HELIX 124 132 {ECO:0000244|PDB:3N9Y}.
HELIX 139 141 {ECO:0000244|PDB:3N9Y}.
HELIX 144 158 {ECO:0000244|PDB:3N9Y}.
HELIX 161 164 {ECO:0000244|PDB:3N9Y}.
HELIX 167 189 {ECO:0000244|PDB:3N9Y}.
STRAND 190 196 {ECO:0000244|PDB:3N9Y}.
HELIX 199 215 {ECO:0000244|PDB:3N9Y}.
STRAND 223 225 {ECO:0000244|PDB:3N9Y}.
HELIX 228 244 {ECO:0000244|PDB:3N9Y}.
HELIX 245 247 {ECO:0000244|PDB:3N9Y}.
HELIX 252 258 {ECO:0000244|PDB:3N9Y}.
HELIX 260 291 {ECO:0000244|PDB:3N9Y}.
HELIX 301 307 {ECO:0000244|PDB:3N9Y}.
HELIX 313 328 {ECO:0000244|PDB:3N9Y}.
HELIX 330 344 {ECO:0000244|PDB:3N9Y}.
HELIX 346 362 {ECO:0000244|PDB:3N9Y}.
TURN 363 365 {ECO:0000244|PDB:3N9Y}.
HELIX 367 370 {ECO:0000244|PDB:3N9Y}.
HELIX 375 387 {ECO:0000244|PDB:3N9Y}.
STRAND 390 397 {ECO:0000244|PDB:3N9Y}.
STRAND 402 404 {ECO:0000244|PDB:3N9Y}.
STRAND 407 409 {ECO:0000244|PDB:3N9Y}.
STRAND 414 418 {ECO:0000244|PDB:3N9Y}.
HELIX 419 423 {ECO:0000244|PDB:3N9Y}.
TURN 426 428 {ECO:0000244|PDB:3N9Y}.
STRAND 429 431 {ECO:0000244|PDB:3N9Y}.
HELIX 437 440 {ECO:0000244|PDB:3N9Y}.
TURN 449 451 {ECO:0000244|PDB:3N9Y}.
HELIX 458 460 {ECO:0000244|PDB:3N9Y}.
HELIX 465 482 {ECO:0000244|PDB:3N9Y}.
STRAND 483 486 {ECO:0000244|PDB:3N9Y}.
STRAND 495 505 {ECO:0000244|PDB:3N9Y}.
STRAND 509 513 {ECO:0000244|PDB:3N9Y}.
SEQUENCE 521 AA; 60102 MW; AB0501E7A5665D8B CRC64;
MLAKGLPPRS VLVKGCQTFL SAPREGLGRL RVPTGEGAGI STRSPRPFNE IPSPGDNGWL
NLYHFWRETG THKVHLHHVQ NFQKYGPIYR EKLGNVESVY VIDPEDVALL FKSEGPNPER
FLIPPWVAYH QYYQRPIGVL LKKSAAWKKD RVALNQEVMA PEATKNFLPL LDAVSRDFVS
VLHRRIKKAG SGNYSGDISD DLFRFAFESI TNVIFGERQG MLEEVVNPEA QRFIDAIYQM
FHTSVPMLNL PPDLFRLFRT KTWKDHVAAW DVIFSKADIY TQNFYWELRQ KGSVHHDYRG
ILYRLLGDSK MSFEDIKANV TEMLAGGVDT TSMTLQWHLY EMARNLKVQD MLRAEVLAAR
HQAQGDMATM LQLVPLLKAS IKETLRLHPI SVTLQRYLVN DLVLRDYMIP AKTLVQVAIY
ALGREPTFFF DPENFDPTRW LSKDKNITYF RNLGFGWGVR QCLGRRIAEL EMTIFLINML
ENFRVEIQHL SDVGTTFNLI LMPEKPISFT FWPFNQEATQ Q


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