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NAD-dependent malic enzyme, mitochondrial (NAD-ME) (EC 1.1.1.38) (Malic enzyme 2)

 MAOM_HUMAN              Reviewed;         584 AA.
P23368; B2R8J2; Q9BWL6; Q9BYG1; Q9H4B2;
01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
01-NOV-1991, sequence version 1.
23-MAY-2018, entry version 191.
RecName: Full=NAD-dependent malic enzyme, mitochondrial;
Short=NAD-ME;
EC=1.1.1.38;
AltName: Full=Malic enzyme 2;
Flags: Precursor;
Name=ME2;
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), AND PARTIAL PROTEIN SEQUENCE.
PubMed=1993674;
Loeber G., Infante A.A., Maurer-Fogy I., Krystek E., Dworkin M.B.;
"Human NAD(+)-dependent mitochondrial malic enzyme. cDNA cloning,
primary structure, and expression in Escherichia coli.";
J. Biol. Chem. 266:3016-3021(1991).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 37-80.
PubMed=11401430; DOI=10.1006/geno.2000.6454;
Yanaihara N., Kohno T., Takakura S., Takei K., Otsuka A., Sunaga N.,
Takahashi M., Yamazaki M., Tashiro H., Fukuzumi Y., Fujimori Y.,
Hagiwara K., Tanaka T., Yokota J.;
"Physical and transcriptional map of a 311-kb segment of chromosome
18q21, a candidate lung tumor suppressor locus.";
Genomics 72:169-179(2001).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Trachea;
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=16177791; DOI=10.1038/nature03983;
Nusbaum C., Zody M.C., Borowsky M.L., Kamal M., Kodira C.D.,
Taylor T.D., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K.,
FitzGerald M.G., Yang X., Abouelleil A., Allen N.R., Anderson S.,
Bloom T., Bugalter B., Butler J., Cook A., DeCaprio D., Engels R.,
Garber M., Gnirke A., Hafez N., Hall J.L., Norman C.H., Itoh T.,
Jaffe D.B., Kuroki Y., Lehoczky J., Lui A., Macdonald P., Mauceli E.,
Mikkelsen T.S., Naylor J.W., Nicol R., Nguyen C., Noguchi H.,
O'Leary S.B., Piqani B., Smith C.L., Talamas J.A., Topham K.,
Totoki Y., Toyoda A., Wain H.M., Young S.K., Zeng Q., Zimmer A.R.,
Fujiyama A., Hattori M., Birren B.W., Sakaki Y., Lander E.S.;
"DNA sequence and analysis of human chromosome 18.";
Nature 437:551-555(2005).
[5]
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.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Placenta;
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 [MRNA] OF 421-584 (ISOFORM 1).
TISSUE=B-cell;
Abts H.;
Thesis (1995), University of Cologne, Germany.
[8]
PROTEIN SEQUENCE OF 19-33.
TISSUE=Platelet;
PubMed=12665801; DOI=10.1038/nbt810;
Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,
Thomas G.R., Vandekerckhove J.;
"Exploring proteomes and analyzing protein processing by mass
spectrometric identification of sorted N-terminal peptides.";
Nat. Biotechnol. 21:566-569(2003).
[9]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-156; LYS-224; LYS-240;
LYS-272 AND LYS-346, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[13]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
PubMed=10467136; DOI=10.1016/S0969-2126(99)80115-4;
Xu Y., Bhargava G., Wu H., Loeber G., Tong L.;
"Crystal structure of human mitochondrial NAD(P)(+)-dependent malic
enzyme: a new class of oxidative decarboxylases.";
Structure 7:877-889(1999).
[14]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 21-584 IN COMPLEX WITH NAD;
DIVALENT METAL ION AND SUBSTRATE ANALOG, AND HOMOTETRAMERIZATION.
PubMed=10700286; DOI=10.1038/73378;
Yang Z., Floyd D.L., Loeber G., Tong L.;
"Structure of a closed form of human malic enzyme and implications for
catalytic mechanism.";
Nat. Struct. Biol. 7:251-257(2000).
[15]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 20-573 IN COMPLEX WITH ATP;
MANGANESE; ALLOSTERIC ACTIVATOR AND SUBSTRATE ANALOG, MUTAGENESIS OF
ARG-67 AND ARG-91, AND HOMOTETRAMERIZATION.
PubMed=12121650; DOI=10.1016/S0969-2126(02)00788-8;
Yang Z., Lanks C.W., Tong L.;
"Molecular mechanism for the regulation of human mitochondrial
NAD(P)+-dependent malic enzyme by ATP and fumarate.";
Structure 10:951-960(2002).
[16]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 21-584 IN COMPLEX WITH
SUBSTRATE; NAD; MANGANESE AND ALLOSTERIC ACTIVATOR, AND ENZYME
MECHANISM.
PubMed=12962632; DOI=10.1016/S0969-2126(03)00168-0;
Tao X., Yang Z., Tong L.;
"Crystal structures of substrate complexes of malic enzyme and
insights into the catalytic mechanism.";
Structure 11:1141-1150(2003).
-!- CATALYTIC ACTIVITY: (S)-malate + NAD(+) = pyruvate + CO(2) + NADH.
-!- CATALYTIC ACTIVITY: Oxaloacetate = pyruvate + CO(2).
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
Note=Divalent metal cations. Prefers magnesium or manganese.;
-!- ENZYME REGULATION: Subject to allosteric activation by fumarate.
-!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:10700286,
ECO:0000269|PubMed:12121650, ECO:0000269|PubMed:12962632}.
-!- SUBCELLULAR LOCATION: Mitochondrion matrix.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P23368-1; Sequence=Displayed;
Name=2;
IsoId=P23368-2; Sequence=VSP_042717;
Note=No experimental confirmation available.;
-!- MISCELLANEOUS: This isoenzyme can also use NADP(+) but is more
effective with NAD(+).
-!- SIMILARITY: Belongs to the malic enzymes family. {ECO:0000305}.
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EMBL; M55905; AAA36197.1; -; mRNA.
EMBL; AB045122; BAB40980.1; -; Genomic_DNA.
EMBL; AK313391; BAG36189.1; -; mRNA.
EMBL; AC015864; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC087687; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471096; EAW62980.1; -; Genomic_DNA.
EMBL; BC000147; AAH00147.1; -; mRNA.
EMBL; AJ294818; CAC14574.1; -; mRNA.
CCDS; CCDS11948.1; -. [P23368-1]
CCDS; CCDS54187.1; -. [P23368-2]
PIR; A39503; A39503.
RefSeq; NP_001161807.1; NM_001168335.1. [P23368-2]
RefSeq; NP_002387.1; NM_002396.4. [P23368-1]
UniGene; Hs.233119; -.
PDB; 1DO8; X-ray; 2.20 A; A/B/C/D=21-584.
PDB; 1EFK; X-ray; 2.60 A; A/B/C/D=1-584.
PDB; 1EFL; X-ray; 2.60 A; A/B/C/D=1-584.
PDB; 1GZ3; X-ray; 2.30 A; A/B/C/D=20-573.
PDB; 1GZ4; X-ray; 2.20 A; A/B/C/D=23-573.
PDB; 1PJ2; X-ray; 2.30 A; A/B/C/D=21-584.
PDB; 1PJ3; X-ray; 2.10 A; A/B/C/D=21-584.
PDB; 1PJ4; X-ray; 2.30 A; A/B/C/D=21-584.
PDB; 1PJL; X-ray; 2.90 A; A/B/C/D/E/F/G/H=1-584.
PDB; 1QR6; X-ray; 2.10 A; A/B=1-584.
PDBsum; 1DO8; -.
PDBsum; 1EFK; -.
PDBsum; 1EFL; -.
PDBsum; 1GZ3; -.
PDBsum; 1GZ4; -.
PDBsum; 1PJ2; -.
PDBsum; 1PJ3; -.
PDBsum; 1PJ4; -.
PDBsum; 1PJL; -.
PDBsum; 1QR6; -.
ProteinModelPortal; P23368; -.
SMR; P23368; -.
BioGrid; 110364; 5.
IntAct; P23368; 7.
MINT; P23368; -.
STRING; 9606.ENSP00000321070; -.
DrugBank; DB03589; Alpha-Ketomalonic Acid.
DrugBank; DB01677; Fumarate.
DrugBank; DB03499; Malate Ion.
DrugBank; DB00157; NADH.
DrugBank; DB03680; Tartronate.
CarbonylDB; P23368; -.
iPTMnet; P23368; -.
PhosphoSitePlus; P23368; -.
SwissPalm; P23368; -.
BioMuta; ME2; -.
DMDM; 126733; -.
EPD; P23368; -.
MaxQB; P23368; -.
PaxDb; P23368; -.
PeptideAtlas; P23368; -.
PRIDE; P23368; -.
DNASU; 4200; -.
Ensembl; ENST00000321341; ENSP00000321070; ENSG00000082212. [P23368-1]
Ensembl; ENST00000382927; ENSP00000372384; ENSG00000082212. [P23368-2]
GeneID; 4200; -.
KEGG; hsa:4200; -.
UCSC; uc002ley.4; human. [P23368-1]
CTD; 4200; -.
DisGeNET; 4200; -.
EuPathDB; HostDB:ENSG00000082212.11; -.
GeneCards; ME2; -.
HGNC; HGNC:6984; ME2.
HPA; HPA008247; -.
HPA; HPA008880; -.
MIM; 154270; gene.
neXtProt; NX_P23368; -.
OpenTargets; ENSG00000082212; -.
PharmGKB; PA30724; -.
eggNOG; KOG1257; Eukaryota.
eggNOG; COG0281; LUCA.
GeneTree; ENSGT00390000000754; -.
HOGENOM; HOG000042486; -.
HOVERGEN; HBG000746; -.
InParanoid; P23368; -.
KO; K00027; -.
OMA; FRYPEPE; -.
OrthoDB; EOG091G04H9; -.
PhylomeDB; P23368; -.
TreeFam; TF300537; -.
BRENDA; 1.1.1.38; 2681.
Reactome; R-HSA-71403; Citric acid cycle (TCA cycle).
SABIO-RK; P23368; -.
ChiTaRS; ME2; human.
EvolutionaryTrace; P23368; -.
GeneWiki; ME2; -.
GeneWiki; ME2_(gene); -.
GenomeRNAi; 4200; -.
PRO; PR:P23368; -.
Proteomes; UP000005640; Chromosome 18.
Bgee; ENSG00000082212; -.
CleanEx; HS_ME2; -.
ExpressionAtlas; P23368; baseline and differential.
Genevisible; P23368; HS.
GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
GO; GO:0005739; C:mitochondrion; IDA:HPA.
GO; GO:0009055; F:electron transfer activity; TAS:UniProtKB.
GO; GO:0004471; F:malate dehydrogenase (decarboxylating) (NAD+) activity; TAS:Reactome.
GO; GO:0004473; F:malate dehydrogenase (decarboxylating) (NADP+) activity; IBA:GO_Central.
GO; GO:0004470; F:malic enzyme activity; IMP:CACAO.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0051287; F:NAD binding; IEA:InterPro.
GO; GO:0008948; F:oxaloacetate decarboxylase activity; IEA:UniProtKB-EC.
GO; GO:0006108; P:malate metabolic process; IBA:GO_Central.
GO; GO:0006090; P:pyruvate metabolic process; IBA:GO_Central.
GO; GO:1902031; P:regulation of NADP metabolic process; IMP:CACAO.
GO; GO:0006099; P:tricarboxylic acid cycle; TAS:Reactome.
Gene3D; 3.40.50.10380; -; 1.
InterPro; IPR015884; Malic_enzyme_CS.
InterPro; IPR012301; Malic_N_dom.
InterPro; IPR037062; Malic_N_dom_sf.
InterPro; IPR012302; Malic_NAD-bd.
InterPro; IPR001891; Malic_OxRdtase.
InterPro; IPR036291; NAD(P)-bd_dom_sf.
Pfam; PF00390; malic; 1.
Pfam; PF03949; Malic_M; 1.
PIRSF; PIRSF000106; ME; 1.
PRINTS; PR00072; MALOXRDTASE.
SMART; SM01274; malic; 1.
SMART; SM00919; Malic_M; 1.
SUPFAM; SSF51735; SSF51735; 1.
PROSITE; PS00331; MALIC_ENZYMES; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Allosteric enzyme; Alternative splicing;
Complete proteome; Direct protein sequencing; Metal-binding;
Mitochondrion; NAD; Oxidoreductase; Polymorphism; Reference proteome;
Transit peptide.
TRANSIT 1 18 Mitochondrion.
{ECO:0000269|PubMed:12665801}.
CHAIN 19 584 NAD-dependent malic enzyme,
mitochondrial.
/FTId=PRO_0000018537.
NP_BIND 165 173 NAD. {ECO:0000269|PubMed:10700286,
ECO:0000269|PubMed:12962632}.
NP_BIND 311 328 NAD. {ECO:0000269|PubMed:10700286,
ECO:0000269|PubMed:12962632}.
ACT_SITE 112 112 Proton donor.
ACT_SITE 183 183 Proton acceptor.
METAL 255 255 Divalent metal cation.
METAL 256 256 Divalent metal cation.
METAL 279 279 Divalent metal cation.
BINDING 67 67 Allosteric activator.
{ECO:0000269|PubMed:12121650,
ECO:0000269|PubMed:12962632}.
BINDING 91 91 Allosteric activator.
{ECO:0000269|PubMed:12121650,
ECO:0000269|PubMed:12962632}.
BINDING 165 165 Substrate. {ECO:0000269|PubMed:12962632}.
BINDING 259 259 NAD. {ECO:0000269|PubMed:10700286,
ECO:0000269|PubMed:12962632}.
BINDING 421 421 Substrate. {ECO:0000269|PubMed:12962632}.
BINDING 466 466 Substrate. {ECO:0000269|PubMed:12962632}.
SITE 279 279 Important for activity. {ECO:0000250}.
MOD_RES 156 156 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 224 224 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 240 240 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 272 272 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 346 346 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
VAR_SEQ 474 584 VALAVILCNTRHISDSVFLEAAKALTSQLTDEELAQGRLYP
PLANIQEVSINIAIKVTEYLYANKMAFRYPEPEDKAKYVKE
RTWRSEYDSLLPDVYEWPESASSPPVITE -> YRIPIC
(in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_042717.
VARIANT 114 114 P -> L (in dbSNP:rs16952692).
/FTId=VAR_034104.
VARIANT 450 450 G -> E (in dbSNP:rs649224).
/FTId=VAR_050017.
MUTAGEN 67 67 R->S: Abolishes activation by fumarate.
{ECO:0000269|PubMed:12121650}.
MUTAGEN 91 91 R->T: Abolishes activation by fumarate.
{ECO:0000269|PubMed:12121650}.
CONFLICT 263 263 F -> Y (in Ref. 3; BAG36189).
{ECO:0000305}.
HELIX 27 30 {ECO:0000244|PDB:1PJ3}.
TURN 32 34 {ECO:0000244|PDB:1PJ3}.
HELIX 37 39 {ECO:0000244|PDB:1PJ3}.
HELIX 42 47 {ECO:0000244|PDB:1PJ3}.
TURN 51 53 {ECO:0000244|PDB:1PJ3}.
HELIX 61 74 {ECO:0000244|PDB:1PJ3}.
HELIX 78 89 {ECO:0000244|PDB:1PJ3}.
HELIX 93 102 {ECO:0000244|PDB:1PJ3}.
HELIX 104 111 {ECO:0000244|PDB:1PJ3}.
HELIX 115 121 {ECO:0000244|PDB:1PJ3}.
HELIX 123 126 {ECO:0000244|PDB:1PJ3}.
STRAND 132 136 {ECO:0000244|PDB:1PJ3}.
HELIX 137 139 {ECO:0000244|PDB:1PJ3}.
TURN 140 142 {ECO:0000244|PDB:1PJL}.
HELIX 143 147 {ECO:0000244|PDB:1PJ3}.
STRAND 157 161 {ECO:0000244|PDB:1PJ3}.
STRAND 163 165 {ECO:0000244|PDB:1PJ3}.
TURN 167 169 {ECO:0000244|PDB:1QR6}.
HELIX 173 177 {ECO:0000244|PDB:1PJ3}.
HELIX 178 191 {ECO:0000244|PDB:1PJ3}.
HELIX 195 197 {ECO:0000244|PDB:1PJ3}.
STRAND 198 205 {ECO:0000244|PDB:1PJ3}.
HELIX 212 214 {ECO:0000244|PDB:1PJ3}.
HELIX 229 246 {ECO:0000244|PDB:1PJ3}.
STRAND 251 254 {ECO:0000244|PDB:1PJ3}.
HELIX 259 269 {ECO:0000244|PDB:1PJ3}.
TURN 270 272 {ECO:0000244|PDB:1PJ3}.
STRAND 273 277 {ECO:0000244|PDB:1PJ3}.
HELIX 278 298 {ECO:0000244|PDB:1PJ3}.
HELIX 302 304 {ECO:0000244|PDB:1PJ3}.
STRAND 307 310 {ECO:0000244|PDB:1PJ3}.
HELIX 314 329 {ECO:0000244|PDB:1PJ3}.
HELIX 334 339 {ECO:0000244|PDB:1PJ3}.
STRAND 341 345 {ECO:0000244|PDB:1PJ3}.
TURN 360 362 {ECO:0000244|PDB:1PJ3}.
HELIX 363 365 {ECO:0000244|PDB:1PJ3}.
HELIX 377 384 {ECO:0000244|PDB:1PJ3}.
STRAND 387 391 {ECO:0000244|PDB:1PJ3}.
STRAND 394 396 {ECO:0000244|PDB:1GZ3}.
HELIX 401 410 {ECO:0000244|PDB:1PJ3}.
STRAND 415 418 {ECO:0000244|PDB:1PJ3}.
HELIX 423 425 {ECO:0000244|PDB:1PJ3}.
STRAND 426 428 {ECO:0000244|PDB:1QR6}.
HELIX 430 436 {ECO:0000244|PDB:1PJ3}.
TURN 437 439 {ECO:0000244|PDB:1PJ3}.
STRAND 442 447 {ECO:0000244|PDB:1PJ3}.
HELIX 467 469 {ECO:0000244|PDB:1PJ3}.
HELIX 471 480 {ECO:0000244|PDB:1PJ3}.
HELIX 488 499 {ECO:0000244|PDB:1PJ3}.
HELIX 504 508 {ECO:0000244|PDB:1PJ3}.
HELIX 516 518 {ECO:0000244|PDB:1PJ3}.
HELIX 519 536 {ECO:0000244|PDB:1PJ3}.
HELIX 549 555 {ECO:0000244|PDB:1PJ3}.
SEQUENCE 584 AA; 65444 MW; 4CEF9AF89B07D93D CRC64;
MLSRLRVVST TCTLACRHLH IKEKGKPLML NPRTNKGMAF TLQERQMLGL QGLLPPKIET
QDIQALRFHR NLKKMTSPLE KYIYIMGIQE RNEKLFYRIL QDDIESLMPI VYTPTVGLAC
SQYGHIFRRP KGLFISISDR GHVRSIVDNW PENHVKAVVV TDGERILGLG DLGVYGMGIP
VGKLCLYTAC AGIRPDRCLP VCIDVGTDNI ALLKDPFYMG LYQKRDRTQQ YDDLIDEFMK
AITDRYGRNT LIQFEDFGNH NAFRFLRKYR EKYCTFNDDI QGTAAVALAG LLAAQKVISK
PISEHKILFL GAGEAALGIA NLIVMSMVEN GLSEQEAQKK IWMFDKYGLL VKGRKAKIDS
YQEPFTHSAP ESIPDTFEDA VNILKPSTII GVAGAGRLFT PDVIRAMASI NERPVIFALS
NPTAQAECTA EEAYTLTEGR CLFASGSPFG PVKLTDGRVF TPGQGNNVYI FPGVALAVIL
CNTRHISDSV FLEAAKALTS QLTDEELAQG RLYPPLANIQ EVSINIAIKV TEYLYANKMA
FRYPEPEDKA KYVKERTWRS EYDSLLPDVY EWPESASSPP VITE


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