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NADPH--cytochrome P450 reductase (CPR) (P450R) (EC 1.6.2.4)

 NCPR_RAT                Reviewed;         678 AA.
P00388;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
10-OCT-2018, entry version 180.
RecName: Full=NADPH--cytochrome P450 reductase {ECO:0000255|HAMAP-Rule:MF_03212};
Short=CPR {ECO:0000255|HAMAP-Rule:MF_03212};
Short=P450R {ECO:0000255|HAMAP-Rule:MF_03212};
EC=1.6.2.4 {ECO:0000255|HAMAP-Rule:MF_03212};
Name=Por {ECO:0000255|HAMAP-Rule:MF_03212};
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3919392; DOI=10.1073/pnas.82.4.973;
Porter T.D., Kasper C.B.;
"Coding nucleotide sequence of rat NADPH-cytochrome P-450
oxidoreductase cDNA and identification of flavin-binding domains.";
Proc. Natl. Acad. Sci. U.S.A. 82:973-977(1985).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3082610; DOI=10.1089/dna.1986.5.1;
Murakami H., Yabusaki Y., Ohkawa H.;
"Expression of rat NADPH-cytochrome P-450 reductase cDNA in
Saccharomyces cerevisiae.";
DNA 5:1-10(1986).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=Wistar; TISSUE=Liver;
PubMed=2125483; DOI=10.1021/bi00494a009;
Porter T.D., Beck T.W., Kasper C.B.;
"NADPH-cytochrome P-450 oxidoreductase gene organization correlates
with structural domains of the protein.";
Biochemistry 29:9814-9818(1990).
[4]
X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 64-678 IN COMPLEX WITH FAD;
FMN AND NADP.
PubMed=9237990; DOI=10.1073/pnas.94.16.8411;
Wang M., Roberts D.L., Paschke R., Shea T.M., Masters B.S.S.,
Kim J.-J.P.;
"Three-dimensional structure of NADPH-cytochrome P450 reductase:
prototype for FMN- and FAD-containing enzymes.";
Proc. Natl. Acad. Sci. U.S.A. 94:8411-8416(1997).
[5]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 57-678 IN COMPLEX WITH FAD;
FMN AND NADP.
PubMed=11371558; DOI=10.1074/jbc.M101731200;
Hubbard P.A., Shen A.L., Paschke R., Kasper C.B., Kim J.-J.P.;
"NADPH-cytochrome P450 oxidoreductase. Structural basis for hydride
and electron transfer.";
J. Biol. Chem. 276:29163-29170(2001).
[6]
X-RAY CRYSTALLOGRAPHY (3.40 ANGSTROMS) OF 57-678 IN COMPLEX WITH FAD;
FMN AND NADP.
PubMed=19171935; DOI=10.1074/jbc.M807868200;
Hamdane D., Xia C., Im S.C., Zhang H., Kim J.J., Waskell L.;
"Structure and function of an NADPH-cytochrome P450 oxidoreductase in
an open conformation capable of reducing cytochrome P450.";
J. Biol. Chem. 284:11374-11384(2009).
[7]
X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 57-678.
PubMed=21345800; DOI=10.1074/jbc.M111.230532;
Xia C., Hamdane D., Shen A.L., Choi V., Kasper C.B., Pearl N.M.,
Zhang H., Im S.C., Waskell L., Kim J.J.;
"Conformational changes of NADPH-cytochrome P450 oxidoreductase are
essential for catalysis and cofactor binding.";
J. Biol. Chem. 286:16246-16260(2011).
[8]
X-RAY CRYSTALLOGRAPHY (4.30 ANGSTROMS) OF 58-678 IN COMPLEX WITH FAD;
FMN AND NADP.
Sugishima M., Sato H., Higashimoto Y., Harada J., Wada K.,
Fukuyama K., Noguchi M.;
"Structural basis for the electron transfer from an open form of
NADPH-cytochrome P450 oxidoreductase to heme oxygenase.";
Submitted (OCT-2013) to the PDB data bank.
-!- FUNCTION: This enzyme is required for electron transfer from NADP
to cytochrome P450 in microsomes. It can also provide electron
transfer to heme oxygenase and cytochrome B5. {ECO:0000255|HAMAP-
Rule:MF_03212}.
-!- CATALYTIC ACTIVITY: NADPH + n oxidized hemoprotein = NADP(+) + n
reduced hemoprotein. {ECO:0000255|HAMAP-Rule:MF_03212}.
-!- COFACTOR:
Name=FAD; Xref=ChEBI:CHEBI:57692;
Evidence={ECO:0000255|HAMAP-Rule:MF_03212,
ECO:0000269|PubMed:9237990};
Note=Binds 1 FAD per monomer. {ECO:0000255|HAMAP-Rule:MF_03212,
ECO:0000269|PubMed:9237990};
-!- COFACTOR:
Name=FMN; Xref=ChEBI:CHEBI:58210;
Evidence={ECO:0000255|HAMAP-Rule:MF_03212,
ECO:0000269|PubMed:9237990};
Note=Binds 1 FMN per monomer. {ECO:0000255|HAMAP-Rule:MF_03212,
ECO:0000269|PubMed:9237990};
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
{ECO:0000255|HAMAP-Rule:MF_03212}; Single-pass membrane protein
{ECO:0000255|HAMAP-Rule:MF_03212}; Cytoplasmic side
{ECO:0000255|HAMAP-Rule:MF_03212}.
-!- SIMILARITY: Belongs to the NADPH--cytochrome P450 reductase
family. {ECO:0000255|HAMAP-Rule:MF_03212}.
-!- SIMILARITY: In the N-terminal section; belongs to the flavodoxin
family. {ECO:0000255|HAMAP-Rule:MF_03212}.
-!- SIMILARITY: In the C-terminal section; belongs to the flavoprotein
pyridine nucleotide cytochrome reductase family.
{ECO:0000255|HAMAP-Rule:MF_03212}.
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EMBL; M10068; AAA41064.1; -; mRNA.
EMBL; M12516; AAA41067.1; -; mRNA.
EMBL; M58937; AAA41683.1; -; Genomic_DNA.
EMBL; M58932; AAA41683.1; JOINED; Genomic_DNA.
EMBL; M58933; AAA41683.1; JOINED; Genomic_DNA.
EMBL; M58934; AAA41683.1; JOINED; Genomic_DNA.
EMBL; M58935; AAA41683.1; JOINED; Genomic_DNA.
EMBL; M58936; AAA41683.1; JOINED; Genomic_DNA.
PIR; A36073; RDRTO4.
RefSeq; NP_113764.1; NM_031576.1.
UniGene; Rn.11359; -.
PDB; 1AMO; X-ray; 2.60 A; A/B=64-678.
PDB; 1J9Z; X-ray; 2.70 A; A/B=57-676.
PDB; 1JA0; X-ray; 2.60 A; A/B=57-676.
PDB; 1JA1; X-ray; 1.80 A; A/B=57-678.
PDB; 3ES9; X-ray; 3.40 A; A/B/C=57-678.
PDB; 3OJW; X-ray; 2.20 A; A=57-678.
PDB; 3OJX; X-ray; 2.50 A; A=57-678.
PDB; 3WKT; X-ray; 4.30 A; A/B=58-678.
PDB; 4Y7C; X-ray; 2.20 A; A/B=57-678.
PDB; 4Y9R; X-ray; 2.40 A; A/B=57-678.
PDB; 4Y9U; X-ray; 1.95 A; A/B=57-678.
PDB; 4YAF; X-ray; 1.91 A; A/B=57-678.
PDB; 4YAL; X-ray; 1.88 A; A/B=57-678.
PDB; 4YAO; X-ray; 2.50 A; A/B=57-678.
PDB; 4YAU; X-ray; 2.20 A; A/B=57-678.
PDB; 4YAW; X-ray; 2.00 A; A/B=57-678.
PDB; 5URD; X-ray; 1.90 A; A/B=57-678.
PDB; 5URE; X-ray; 2.30 A; A/B=57-678.
PDB; 5URG; X-ray; 2.30 A; A/B=57-678.
PDB; 5URH; X-ray; 2.50 A; A/B=57-678.
PDB; 5URI; X-ray; 2.70 A; A/B=57-678.
PDBsum; 1AMO; -.
PDBsum; 1J9Z; -.
PDBsum; 1JA0; -.
PDBsum; 1JA1; -.
PDBsum; 3ES9; -.
PDBsum; 3OJW; -.
PDBsum; 3OJX; -.
PDBsum; 3WKT; -.
PDBsum; 4Y7C; -.
PDBsum; 4Y9R; -.
PDBsum; 4Y9U; -.
PDBsum; 4YAF; -.
PDBsum; 4YAL; -.
PDBsum; 4YAO; -.
PDBsum; 4YAU; -.
PDBsum; 4YAW; -.
PDBsum; 5URD; -.
PDBsum; 5URE; -.
PDBsum; 5URG; -.
PDBsum; 5URH; -.
PDBsum; 5URI; -.
ProteinModelPortal; P00388; -.
SMR; P00388; -.
BioGrid; 248088; 1.
STRING; 10116.ENSRNOP00000001961; -.
ChEMBL; CHEMBL2817; -.
iPTMnet; P00388; -.
PhosphoSitePlus; P00388; -.
PaxDb; P00388; -.
PRIDE; P00388; -.
Ensembl; ENSRNOT00000001961; ENSRNOP00000001961; ENSRNOG00000001442.
GeneID; 29441; -.
KEGG; rno:29441; -.
UCSC; RGD:68335; rat.
CTD; 5447; -.
RGD; 68335; Por.
eggNOG; KOG1158; Eukaryota.
eggNOG; COG0369; LUCA.
GeneTree; ENSGT00840000129757; -.
HOGENOM; HOG000282027; -.
HOVERGEN; HBG000432; -.
InParanoid; P00388; -.
KO; K00327; -.
OMA; TKMDVAF; -.
OrthoDB; EOG091G02VT; -.
PhylomeDB; P00388; -.
TreeFam; TF105719; -.
BioCyc; MetaCyc:MONOMER-14290; -.
BRENDA; 1.6.2.4; 5301.
Reactome; R-RNO-211897; Cytochrome P450 - arranged by substrate type.
SABIO-RK; P00388; -.
EvolutionaryTrace; P00388; -.
PRO; PR:P00388; -.
Proteomes; UP000002494; Chromosome 12.
Bgee; ENSRNOG00000001442; Expressed in 10 organ(s), highest expression level in liver.
Genevisible; P00388; RN.
GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:RGD.
GO; GO:0016020; C:membrane; IDA:RGD.
GO; GO:0005739; C:mitochondrion; IDA:RGD.
GO; GO:0004128; F:cytochrome-b5 reductase activity, acting on NAD(P)H; IDA:RGD.
GO; GO:0009055; F:electron transfer activity; IDA:RGD.
GO; GO:0019899; F:enzyme binding; IDA:RGD.
GO; GO:0050660; F:flavin adenine dinucleotide binding; IMP:RGD.
GO; GO:0010181; F:FMN binding; IMP:RGD.
GO; GO:0016787; F:hydrolase activity; IDA:RGD.
GO; GO:0047726; F:iron-cytochrome-c reductase activity; IDA:RGD.
GO; GO:0050661; F:NADP binding; IDA:RGD.
GO; GO:0003958; F:NADPH-hemoprotein reductase activity; IDA:BHF-UCL.
GO; GO:0008941; F:nitric oxide dioxygenase activity; IDA:RGD.
GO; GO:0009437; P:carnitine metabolic process; IEP:RGD.
GO; GO:0090346; P:cellular organofluorine metabolic process; IEA:Ensembl.
GO; GO:0071372; P:cellular response to follicle-stimulating hormone stimulus; IEP:RGD.
GO; GO:0071371; P:cellular response to gonadotropin stimulus; IEP:RGD.
GO; GO:0071375; P:cellular response to peptide hormone stimulus; IEP:RGD.
GO; GO:0070988; P:demethylation; IDA:RGD.
GO; GO:0019395; P:fatty acid oxidation; IDA:RGD.
GO; GO:0009812; P:flavonoid metabolic process; IEP:RGD.
GO; GO:0018393; P:internal peptidyl-lysine acetylation; IDA:RGD.
GO; GO:0043066; P:negative regulation of apoptotic process; IMP:RGD.
GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; IMP:RGD.
GO; GO:0060192; P:negative regulation of lipase activity; IDA:RGD.
GO; GO:0043602; P:nitrate catabolic process; IDA:RGD.
GO; GO:0046210; P:nitric oxide catabolic process; IDA:RGD.
GO; GO:0055114; P:oxidation-reduction process; IDA:BHF-UCL.
GO; GO:0045542; P:positive regulation of cholesterol biosynthetic process; IMP:RGD.
GO; GO:0032332; P:positive regulation of chondrocyte differentiation; IMP:RGD.
GO; GO:0032770; P:positive regulation of monooxygenase activity; IEA:Ensembl.
GO; GO:0045880; P:positive regulation of smoothened signaling pathway; IMP:RGD.
GO; GO:0090031; P:positive regulation of steroid hormone biosynthetic process; IDA:RGD.
GO; GO:0090181; P:regulation of cholesterol metabolic process; IMP:RGD.
GO; GO:0003420; P:regulation of growth plate cartilage chondrocyte proliferation; IMP:RGD.
GO; GO:0042493; P:response to drug; IEP:RGD.
GO; GO:0007584; P:response to nutrient; IEP:RGD.
Gene3D; 1.20.990.10; -; 4.
Gene3D; 3.40.50.360; -; 1.
Gene3D; 3.40.50.80; -; 1.
HAMAP; MF_03212; NCPR; 1.
InterPro; IPR003097; CysJ-like_FAD-binding.
InterPro; IPR017927; FAD-bd_FR_type.
InterPro; IPR001094; Flavdoxin-like.
InterPro; IPR008254; Flavodoxin/NO_synth.
InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
InterPro; IPR029039; Flavoprotein-like_sf.
InterPro; IPR039261; FNR_nucleotide-bd.
InterPro; IPR023173; NADPH_Cyt_P450_Rdtase_alpha.
InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
InterPro; IPR023208; P450R.
InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
Pfam; PF00667; FAD_binding_1; 1.
Pfam; PF00258; Flavodoxin_1; 1.
Pfam; PF00175; NAD_binding_1; 1.
PIRSF; PIRSF000208; P450R; 1.
PRINTS; PR00369; FLAVODOXIN.
PRINTS; PR00371; FPNCR.
SUPFAM; SSF52218; SSF52218; 1.
SUPFAM; SSF52343; SSF52343; 1.
SUPFAM; SSF63380; SSF63380; 1.
PROSITE; PS51384; FAD_FR; 1.
PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Complete proteome; Endoplasmic reticulum;
FAD; Flavoprotein; FMN; Membrane; NADP; Oxidoreductase;
Reference proteome; Transmembrane; Transmembrane helix.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:P16435}.
CHAIN 2 678 NADPH--cytochrome P450 reductase.
/FTId=PRO_0000167600.
TOPO_DOM 2 22 Lumenal. {ECO:0000255|HAMAP-
Rule:MF_03212}.
TRANSMEM 23 43 Helical. {ECO:0000255|HAMAP-
Rule:MF_03212}.
TOPO_DOM 44 678 Cytoplasmic. {ECO:0000255|HAMAP-
Rule:MF_03212}.
DOMAIN 80 224 Flavodoxin-like. {ECO:0000255|HAMAP-
Rule:MF_03212}.
DOMAIN 279 521 FAD-binding FR-type. {ECO:0000255|HAMAP-
Rule:MF_03212}.
NP_BIND 86 91 FMN. {ECO:0000255|HAMAP-Rule:MF_03212,
ECO:0000269|PubMed:11371558,
ECO:0000269|PubMed:19171935,
ECO:0000269|PubMed:21345800,
ECO:0000269|PubMed:9237990,
ECO:0000269|Ref.8}.
NP_BIND 138 141 FMN. {ECO:0000255|HAMAP-Rule:MF_03212,
ECO:0000269|PubMed:11371558,
ECO:0000269|PubMed:19171935,
ECO:0000269|PubMed:21345800,
ECO:0000269|PubMed:9237990,
ECO:0000269|Ref.8}.
NP_BIND 173 182 FMN. {ECO:0000255|HAMAP-Rule:MF_03212,
ECO:0000269|PubMed:11371558,
ECO:0000269|PubMed:19171935,
ECO:0000269|PubMed:21345800,
ECO:0000269|PubMed:9237990,
ECO:0000269|Ref.8}.
NP_BIND 454 457 FAD. {ECO:0000255|HAMAP-Rule:MF_03212,
ECO:0000269|PubMed:11371558,
ECO:0000269|PubMed:19171935,
ECO:0000269|PubMed:21345800,
ECO:0000269|PubMed:9237990,
ECO:0000269|Ref.8}.
NP_BIND 472 474 FAD. {ECO:0000255|HAMAP-Rule:MF_03212,
ECO:0000269|PubMed:11371558,
ECO:0000269|PubMed:19171935,
ECO:0000269|PubMed:9237990,
ECO:0000269|Ref.8}.
NP_BIND 488 491 FAD. {ECO:0000255|HAMAP-Rule:MF_03212,
ECO:0000269|PubMed:11371558,
ECO:0000269|PubMed:19171935,
ECO:0000269|PubMed:21345800,
ECO:0000269|PubMed:9237990,
ECO:0000269|Ref.8}.
NP_BIND 596 597 NADP. {ECO:0000255|HAMAP-Rule:MF_03212,
ECO:0000269|PubMed:11371558,
ECO:0000269|PubMed:19171935,
ECO:0000269|PubMed:21345800,
ECO:0000269|PubMed:9237990,
ECO:0000269|Ref.8}.
NP_BIND 602 606 NADP. {ECO:0000255|HAMAP-Rule:MF_03212,
ECO:0000269|PubMed:11371558,
ECO:0000269|PubMed:19171935,
ECO:0000269|PubMed:21345800,
ECO:0000269|PubMed:9237990,
ECO:0000269|Ref.8}.
BINDING 208 208 FMN. {ECO:0000255|HAMAP-Rule:MF_03212,
ECO:0000269|PubMed:11371558,
ECO:0000269|PubMed:21345800,
ECO:0000269|PubMed:9237990}.
BINDING 298 298 NADP. {ECO:0000255|HAMAP-Rule:MF_03212,
ECO:0000269|PubMed:11371558,
ECO:0000269|PubMed:19171935,
ECO:0000269|PubMed:21345800,
ECO:0000269|PubMed:9237990}.
BINDING 424 424 FAD. {ECO:0000255|HAMAP-Rule:MF_03212,
ECO:0000269|PubMed:11371558,
ECO:0000269|PubMed:19171935,
ECO:0000269|PubMed:21345800,
ECO:0000269|Ref.8}.
BINDING 478 478 FAD. {ECO:0000255|HAMAP-Rule:MF_03212,
ECO:0000269|PubMed:11371558,
ECO:0000269|PubMed:19171935,
ECO:0000269|PubMed:21345800,
ECO:0000269|PubMed:9237990,
ECO:0000269|Ref.8}.
BINDING 535 535 NADP. {ECO:0000255|HAMAP-Rule:MF_03212,
ECO:0000269|PubMed:11371558,
ECO:0000269|PubMed:19171935,
ECO:0000269|PubMed:21345800,
ECO:0000269|PubMed:9237990,
ECO:0000269|Ref.8}.
BINDING 639 639 NADP. {ECO:0000255|HAMAP-Rule:MF_03212,
ECO:0000269|PubMed:11371558,
ECO:0000269|PubMed:19171935,
ECO:0000269|PubMed:21345800,
ECO:0000269|PubMed:9237990}.
BINDING 677 677 FAD. {ECO:0000255|HAMAP-Rule:MF_03212,
ECO:0000269|PubMed:11371558,
ECO:0000269|PubMed:19171935,
ECO:0000269|PubMed:21345800,
ECO:0000269|PubMed:9237990,
ECO:0000269|Ref.8}.
MOD_RES 2 2 N-acetylglycine.
{ECO:0000250|UniProtKB:P16435}.
CONFLICT 255 255 V -> A (in Ref. 3; AAA41683).
{ECO:0000305}.
HELIX 69 76 {ECO:0000244|PDB:1JA1}.
STRAND 80 85 {ECO:0000244|PDB:1JA1}.
STRAND 87 89 {ECO:0000244|PDB:1JA1}.
HELIX 90 101 {ECO:0000244|PDB:1JA1}.
HELIX 102 105 {ECO:0000244|PDB:1JA1}.
STRAND 109 112 {ECO:0000244|PDB:1JA1}.
HELIX 114 116 {ECO:0000244|PDB:1JA1}.
HELIX 119 127 {ECO:0000244|PDB:1JA1}.
STRAND 132 140 {ECO:0000244|PDB:1JA1}.
TURN 141 143 {ECO:0000244|PDB:1JA1}.
HELIX 147 149 {ECO:0000244|PDB:1JA1}.
HELIX 150 158 {ECO:0000244|PDB:1JA1}.
STRAND 167 174 {ECO:0000244|PDB:1JA1}.
STRAND 176 180 {ECO:0000244|PDB:1JA1}.
HELIX 183 194 {ECO:0000244|PDB:1JA1}.
STRAND 198 201 {ECO:0000244|PDB:1JA1}.
STRAND 204 207 {ECO:0000244|PDB:1JA1}.
TURN 208 210 {ECO:0000244|PDB:1JA1}.
HELIX 212 231 {ECO:0000244|PDB:1JA1}.
STRAND 244 249 {ECO:0000244|PDB:1JA1}.
HELIX 255 257 {ECO:0000244|PDB:1JA1}.
STRAND 258 261 {ECO:0000244|PDB:1JA1}.
STRAND 263 265 {ECO:0000244|PDB:1JA1}.
TURN 266 270 {ECO:0000244|PDB:1JA1}.
STRAND 277 280 {ECO:0000244|PDB:5URD}.
STRAND 282 291 {ECO:0000244|PDB:1JA1}.
STRAND 294 298 {ECO:0000244|PDB:1JA1}.
STRAND 300 306 {ECO:0000244|PDB:1JA1}.
TURN 308 311 {ECO:0000244|PDB:5URG}.
STRAND 319 322 {ECO:0000244|PDB:1JA1}.
HELIX 328 337 {ECO:0000244|PDB:1JA1}.
STRAND 345 351 {ECO:0000244|PDB:1JA1}.
STRAND 360 366 {ECO:0000244|PDB:1JA1}.
HELIX 367 373 {ECO:0000244|PDB:1JA1}.
HELIX 383 389 {ECO:0000244|PDB:1JA1}.
HELIX 390 392 {ECO:0000244|PDB:1JA1}.
STRAND 393 395 {ECO:0000244|PDB:3OJX}.
HELIX 396 403 {ECO:0000244|PDB:1JA1}.
HELIX 404 406 {ECO:0000244|PDB:1JA1}.
STRAND 408 410 {ECO:0000244|PDB:1JA1}.
HELIX 411 419 {ECO:0000244|PDB:1JA1}.
TURN 420 424 {ECO:0000244|PDB:1JA1}.
HELIX 427 433 {ECO:0000244|PDB:1JA1}.
HELIX 441 447 {ECO:0000244|PDB:1JA1}.
STRAND 454 457 {ECO:0000244|PDB:1JA1}.
TURN 462 464 {ECO:0000244|PDB:1JA1}.
STRAND 468 474 {ECO:0000244|PDB:1JA1}.
STRAND 477 479 {ECO:0000244|PDB:1JA1}.
STRAND 483 487 {ECO:0000244|PDB:1JA1}.
HELIX 489 496 {ECO:0000244|PDB:1JA1}.
STRAND 508 514 {ECO:0000244|PDB:1JA1}.
STRAND 528 531 {ECO:0000244|PDB:1JA1}.
HELIX 534 537 {ECO:0000244|PDB:1JA1}.
HELIX 538 552 {ECO:0000244|PDB:1JA1}.
STRAND 560 567 {ECO:0000244|PDB:1JA1}.
TURN 569 571 {ECO:0000244|PDB:1JA1}.
HELIX 576 584 {ECO:0000244|PDB:1JA1}.
STRAND 587 595 {ECO:0000244|PDB:1JA1}.
STRAND 598 601 {ECO:0000244|PDB:1JA1}.
HELIX 605 611 {ECO:0000244|PDB:1JA1}.
HELIX 613 621 {ECO:0000244|PDB:1JA1}.
STRAND 626 632 {ECO:0000244|PDB:1JA1}.
TURN 633 635 {ECO:0000244|PDB:1JA1}.
HELIX 636 651 {ECO:0000244|PDB:1JA1}.
HELIX 656 668 {ECO:0000244|PDB:1JA1}.
STRAND 671 677 {ECO:0000244|PDB:1JA1}.
SEQUENCE 678 AA; 76963 MW; AF3087E4D7A352D6 CRC64;
MGDSHEDTSA TMPEAVAEEV SLFSTTDMVL FSLIVGVLTY WFIFRKKKEE IPEFSKIQTT
APPVKESSFV EKMKKTGRNI IVFYGSQTGT AEEFANRLSK DAHRYGMRGM SADPEEYDLA
DLSSLPEIDK SLVVFCMATY GEGDPTDNAQ DFYDWLQETD VDLTGVKFAV FGLGNKTYEH
FNAMGKYVDQ RLEQLGAQRI FELGLGDDDG NLEEDFITWR EQFWPAVCEF FGVEATGEES
SIRQYELVVH EDMDVAKVYT GEMGRLKSYE NQKPPFDAKN PFLAAVTANR KLNQGTERHL
MHLELDISDS KIRYESGDHV AVYPANDSAL VNQIGEILGA DLDVIMSLNN LDEESNKKHP
FPCPTTYRTA LTYYLDITNP PRTNVLYELA QYASEPSEQE HLHKMASSSG EGKELYLSWV
VEARRHILAI LQDYPSLRPP IDHLCELLPR LQARYYSIAS SSKVHPNSVH ICAVAVEYEA
KSGRVNKGVA TSWLRAKEPA GENGGRALVP MFVRKSQFRL PFKSTTPVIM VGPGTGIAPF
MGFIQERAWL REQGKEVGET LLYYGCRRSD EDYLYREELA RFHKDGALTQ LNVAFSREQA
HKVYVQHLLK RDREHLWKLI HEGGAHIYVC GDARNMAKDV QNTFYDIVAE FGPMEHTQAV
DYVKKLMTKG RYSLDVWS


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