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Elongation factor 1-gamma (EF-1-gamma) (eEF-1B gamma)

 EF1G_HUMAN              Reviewed;         437 AA.
P26641; B4DTG2; Q6PJ62; Q6PK31; Q96CU2; Q9P196;
01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
05-DEC-2018, entry version 210.
RecName: Full=Elongation factor 1-gamma;
Short=EF-1-gamma;
AltName: Full=eEF-1B gamma;
Name=EEF1G; Synonyms=EF1G; ORFNames=PRO1608;
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=1461723; DOI=10.1093/nar/20.22.5907;
Sanders J., Maassen J.A., Moeller W.;
"Elongation factor-1 messenger-RNA levels in cultured cells are high
compared to tissue and are not drastically affected further by
oncogenic transformation.";
Nucleic Acids Res. 20:5907-5910(1992).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=1598220; DOI=10.1093/nar/20.10.2598;
Kumabe T., Schma Y., Yamamoto T.;
"Human cDNAs encoding elongation factor 1 gamma and the ribosomal
protein L19.";
Nucleic Acids Res. 20:2598-2598(1992).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Placenta;
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=16554811; DOI=10.1038/nature04632;
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F.,
Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
Sakaki Y.;
"Human chromosome 11 DNA sequence and analysis including novel gene
identification.";
Nature 440:497-500(2006).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Bone marrow, Eye, Liver, Lung, Muscle, Testis, and Uterus;
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).
[6]
PROTEIN SEQUENCE OF 2-14.
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).
[7]
PROTEIN SEQUENCE OF 2-14, CLEAVAGE OF INITIATOR METHIONINE,
ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=B-cell lymphoma;
Bienvenut W.V.;
Submitted (OCT-2004) to UniProtKB.
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 80-437 (ISOFORM 1).
TISSUE=Pancreatic carcinoma;
PubMed=1372736;
Lew Y., Jones D.V., Mars W.M., Evans D., Byrd D., Frazier M.L.;
"Expression of elongation factor-1 gamma-related sequence in human
pancreatic cancer.";
Pancreas 7:144-152(1992).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 121-437 (ISOFORM 1).
TISSUE=Fetal liver;
Zhang C., Yu Y., Zhang S., Wei H., Zhang Y., Zhou G., Bi J., Liu M.,
He F.;
"Functional prediction of the coding sequences of 79 new genes deduced
by analysis of cDNA clones from human fetal liver.";
Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases.
[10]
IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Lymphoblast;
PubMed=14654843; DOI=10.1038/nature02166;
Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A.,
Mann M.;
"Proteomic characterization of the human centrosome by protein
correlation profiling.";
Nature 426:570-574(2003).
[11]
INDUCTION, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=16548883; DOI=10.1111/j.1462-5822.2005.00644.x;
Leong W.F., Chow V.T.;
"Transcriptomic and proteomic analyses of rhabdomyosarcoma cells
reveal differential cellular gene expression in response to
enterovirus 71 infection.";
Cell. Microbiol. 8:565-580(2006).
[12]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[13]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-147 AND LYS-434, 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).
[14]
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).
[15]
MALONYLATION AT LYS-434.
PubMed=21908771; DOI=10.1074/mcp.M111.012658;
Peng C., Lu Z., Xie Z., Cheng Z., Chen Y., Tan M., Luo H., Zhang Y.,
He W., Yang K., Zwaans B.M., Tishkoff D., Ho L., Lombard D., He T.C.,
Dai J., Verdin E., Ye Y., Zhao Y.;
"The first identification of lysine malonylation substrates and its
regulatory enzyme.";
Mol. Cell. Proteomics 10:M111.012658.01-M111.012658.12(2011).
[16]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[17]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[18]
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).
[19]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-253, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25114211; DOI=10.1073/pnas.1413825111;
Impens F., Radoshevich L., Cossart P., Ribet D.;
"Mapping of SUMO sites and analysis of SUMOylation changes induced by
external stimuli.";
Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
[20]
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).
[21]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-285, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[22]
STRUCTURE BY NMR OF 276-437.
PubMed=12766415; DOI=10.1023/A:1023504611632;
Vanwetswinkel S., Kriek J., Andersen G.R., Dijk J., Siegal G.;
"1H, 15N and 13C resonance assignments of the highly conserved 19 kDa
C-terminal domain from human elongation factor 1Bgamma.";
J. Biomol. NMR 26:189-190(2003).
-!- FUNCTION: Probably plays a role in anchoring the complex to other
cellular components.
-!- SUBUNIT: EF-1 is composed of four subunits: alpha, beta, delta,
and gamma.
-!- INTERACTION:
F4ZW62:-; NbExp=3; IntAct=EBI-10177695, EBI-10177680;
P24534:EEF1B2; NbExp=5; IntAct=EBI-351467, EBI-354334;
P29692:EEF1D; NbExp=3; IntAct=EBI-351467, EBI-358607;
P29692-2:EEF1D; NbExp=3; IntAct=EBI-10177695, EBI-5280572;
Q658K8:EEF1DP3; NbExp=4; IntAct=EBI-10177695, EBI-10248874;
O94889:KLHL18; NbExp=3; IntAct=EBI-10177695, EBI-2510096;
Q04695:KRT17; NbExp=2; IntAct=EBI-351467, EBI-297873;
Q9HBL7:PLGRKT; NbExp=3; IntAct=EBI-10177695, EBI-714824;
P78332:RBM6; NbExp=3; IntAct=EBI-10177695, EBI-2692323;
Q969Q1:TRIM63; NbExp=2; IntAct=EBI-351467, EBI-5661333;
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P26641-1; Sequence=Displayed;
Name=2;
IsoId=P26641-2; Sequence=VSP_056204;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Highly expressed in pancreatic tumor tissue
and to a lesser extent in normal kidney, intestine, pancreas,
stomach, lung, brain, spleen and liver.
-!- INDUCTION: Down-regulated in response to enterovirus 71 (EV71)
infection. {ECO:0000269|PubMed:16548883}.
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EMBL; X63526; CAA45089.1; -; mRNA.
EMBL; Z11531; CAA77630.1; -; mRNA.
EMBL; AK300203; BAG61974.1; -; mRNA.
EMBL; AP001363; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AP002990; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC000384; AAH00384.1; -; mRNA.
EMBL; BC006509; AAH06509.1; -; mRNA.
EMBL; BC006520; AAH06520.1; -; mRNA.
EMBL; BC007949; AAH07949.2; -; mRNA.
EMBL; BC009865; AAH09865.1; -; mRNA.
EMBL; BC013918; AAH13918.1; -; mRNA.
EMBL; BC015813; AAH15813.1; -; mRNA.
EMBL; BC021974; AAH21974.2; -; mRNA.
EMBL; BC028179; AAH28179.1; -; mRNA.
EMBL; BC031012; AAH31012.1; -; mRNA.
EMBL; BC067738; AAH67738.1; -; mRNA.
EMBL; M55409; AAC18414.1; -; mRNA.
EMBL; AF119850; AAF69604.1; -; mRNA.
CCDS; CCDS44626.1; -. [P26641-1]
PIR; S22655; S22655.
RefSeq; NP_001395.1; NM_001404.4. [P26641-1]
UniGene; Hs.144835; -.
UniGene; Hs.444467; -.
PDB; 1PBU; NMR; -; A=276-437.
PDB; 5DQS; X-ray; 2.10 A; A=2-218.
PDB; 5JPO; X-ray; 2.00 A; A/B/C/D=1-218.
PDBsum; 1PBU; -.
PDBsum; 5DQS; -.
PDBsum; 5JPO; -.
ProteinModelPortal; P26641; -.
SMR; P26641; -.
BioGrid; 108257; 186.
CORUM; P26641; -.
DIP; DIP-32516N; -.
IntAct; P26641; 161.
MINT; P26641; -.
STRING; 9606.ENSP00000331901; -.
iPTMnet; P26641; -.
PhosphoSitePlus; P26641; -.
SwissPalm; P26641; -.
BioMuta; EEF1G; -.
DMDM; 119165; -.
OGP; P26641; -.
EPD; P26641; -.
PaxDb; P26641; -.
PeptideAtlas; P26641; -.
PRIDE; P26641; -.
ProteomicsDB; 54359; -.
TopDownProteomics; P26641-1; -. [P26641-1]
DNASU; 1937; -.
Ensembl; ENST00000329251; ENSP00000331901; ENSG00000254772. [P26641-1]
GeneID; 1937; -.
KEGG; hsa:1937; -.
CTD; 1937; -.
DisGeNET; 1937; -.
EuPathDB; HostDB:ENSG00000254772.9; -.
GeneCards; EEF1G; -.
HGNC; HGNC:3213; EEF1G.
HPA; HPA040688; -.
HPA; HPA055316; -.
MIM; 130593; gene.
neXtProt; NX_P26641; -.
OpenTargets; ENSG00000254772; -.
PharmGKB; PA27649; -.
eggNOG; KOG0867; Eukaryota.
eggNOG; KOG1627; Eukaryota.
eggNOG; COG0625; LUCA.
GeneTree; ENSGT00390000007552; -.
HOGENOM; HOG000235245; -.
HOVERGEN; HBG051444; -.
InParanoid; P26641; -.
KO; K03233; -.
OMA; DYEVYDW; -.
OrthoDB; EOG091G06QR; -.
PhylomeDB; P26641; -.
TreeFam; TF314343; -.
Reactome; R-HSA-156842; Eukaryotic Translation Elongation.
ChiTaRS; EEF1G; human.
EvolutionaryTrace; P26641; -.
GeneWiki; EEF1G; -.
GenomeRNAi; 1937; -.
PRO; PR:P26641; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000254772; Expressed in 89 organ(s), highest expression level in muscle of leg.
CleanEx; HS_EEF1G; -.
ExpressionAtlas; P26641; baseline and differential.
Genevisible; P26641; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0016020; C:membrane; HDA:UniProtKB.
GO; GO:0005634; C:nucleus; HDA:UniProtKB.
GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW.
GO; GO:0009615; P:response to virus; IEP:UniProtKB.
GO; GO:0006414; P:translational elongation; IBA:GO_Central.
Gene3D; 3.30.70.1010; -; 1.
InterPro; IPR001662; EF1B_G_C.
InterPro; IPR036433; EF1B_G_C_sf.
InterPro; IPR010987; Glutathione-S-Trfase_C-like.
InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
InterPro; IPR040079; Glutathione_S-Trfase.
InterPro; IPR004045; Glutathione_S-Trfase_N.
InterPro; IPR004046; GST_C.
InterPro; IPR036249; Thioredoxin-like_sf.
Pfam; PF00647; EF1G; 1.
Pfam; PF00043; GST_C; 1.
Pfam; PF02798; GST_N; 1.
SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1.
SMART; SM01183; EF1G; 1.
SUPFAM; SSF47616; SSF47616; 1.
SUPFAM; SSF52833; SSF52833; 1.
SUPFAM; SSF89942; SSF89942; 1.
PROSITE; PS50040; EF1G_C; 1.
PROSITE; PS50405; GST_CTER; 1.
PROSITE; PS50404; GST_NTER; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Complete proteome;
Direct protein sequencing; Elongation factor; Isopeptide bond;
Protein biosynthesis; Reference proteome; Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378,
ECO:0000269|PubMed:12665801,
ECO:0000269|Ref.7}.
CHAIN 2 437 Elongation factor 1-gamma.
/FTId=PRO_0000208813.
DOMAIN 2 87 GST N-terminal.
DOMAIN 88 216 GST C-terminal.
DOMAIN 276 437 EF-1-gamma C-terminal.
{ECO:0000255|PROSITE-ProRule:PRU00519}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378,
ECO:0000269|Ref.7}.
MOD_RES 147 147 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 212 212 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q9D8N0}.
MOD_RES 401 401 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q9D8N0}.
MOD_RES 434 434 N6-acetyllysine; alternate.
{ECO:0000244|PubMed:19608861}.
MOD_RES 434 434 N6-malonyllysine; alternate.
{ECO:0000269|PubMed:21908771}.
CROSSLNK 253 253 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1).
{ECO:0000244|PubMed:25114211}.
CROSSLNK 285 285 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VAR_SEQ 1 4 MAAG -> MAERWVAPAVLRRARFASTFFLSPQIYAHKDGD
LRSAFFILSFKRGEFIPFLNW (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_056204.
CONFLICT 102 102 A -> V (in Ref. 5; AAH13918).
{ECO:0000305}.
STRAND 3 7 {ECO:0000244|PDB:5JPO}.
HELIX 13 25 {ECO:0000244|PDB:5JPO}.
STRAND 28 32 {ECO:0000244|PDB:5JPO}.
TURN 35 37 {ECO:0000244|PDB:5JPO}.
TURN 40 42 {ECO:0000244|PDB:5JPO}.
HELIX 43 45 {ECO:0000244|PDB:5JPO}.
HELIX 47 52 {ECO:0000244|PDB:5JPO}.
STRAND 58 63 {ECO:0000244|PDB:5JPO}.
HELIX 72 78 {ECO:0000244|PDB:5JPO}.
HELIX 82 85 {ECO:0000244|PDB:5JPO}.
HELIX 89 105 {ECO:0000244|PDB:5JPO}.
HELIX 107 117 {ECO:0000244|PDB:5JPO}.
HELIX 125 145 {ECO:0000244|PDB:5JPO}.
TURN 146 148 {ECO:0000244|PDB:5JPO}.
STRAND 150 153 {ECO:0000244|PDB:5JPO}.
HELIX 159 174 {ECO:0000244|PDB:5JPO}.
HELIX 178 181 {ECO:0000244|PDB:5JPO}.
HELIX 185 195 {ECO:0000244|PDB:5JPO}.
HELIX 198 204 {ECO:0000244|PDB:5JPO}.
HELIX 279 281 {ECO:0000244|PDB:1PBU}.
HELIX 290 299 {ECO:0000244|PDB:1PBU}.
HELIX 302 304 {ECO:0000244|PDB:1PBU}.
HELIX 306 311 {ECO:0000244|PDB:1PBU}.
TURN 316 318 {ECO:0000244|PDB:1PBU}.
STRAND 320 324 {ECO:0000244|PDB:1PBU}.
HELIX 329 331 {ECO:0000244|PDB:1PBU}.
HELIX 338 348 {ECO:0000244|PDB:1PBU}.
HELIX 349 351 {ECO:0000244|PDB:1PBU}.
HELIX 353 355 {ECO:0000244|PDB:1PBU}.
STRAND 356 358 {ECO:0000244|PDB:1PBU}.
STRAND 361 364 {ECO:0000244|PDB:1PBU}.
STRAND 370 381 {ECO:0000244|PDB:1PBU}.
HELIX 384 386 {ECO:0000244|PDB:1PBU}.
HELIX 388 390 {ECO:0000244|PDB:1PBU}.
HELIX 394 396 {ECO:0000244|PDB:1PBU}.
HELIX 408 418 {ECO:0000244|PDB:1PBU}.
TURN 424 426 {ECO:0000244|PDB:1PBU}.
SEQUENCE 437 AA; 50119 MW; A6110663110CF3FC CRC64;
MAAGTLYTYP ENWRAFKALI AAQYSGAQVR VLSAPPHFHF GQTNRTPEFL RKFPAGKVPA
FEGDDGFCVF ESNAIAYYVS NEELRGSTPE AAAQVVQWVS FADSDIVPPA STWVFPTLGI
MHHNKQATEN AKEEVRRILG LLDAYLKTRT FLVGERVTLA DITVVCTLLW LYKQVLEPSF
RQAFPNTNRW FLTCINQPQF RAVLGEVKLC EKMAQFDAKK FAETQPKKDT PRKEKGSREE
KQKPQAERKE EKKAAAPAPE EEMDECEQAL AAEPKAKDPF AHLPKSTFVL DEFKRKYSNE
DTLSVALPYF WEHFDKDGWS LWYSEYRFPE ELTQTFMSCN LITGMFQRLD KLRKNAFASV
ILFGTNNSSS ISGVWVFRGQ ELAFPLSPDW QVDYESYTWR KLDPGSEETQ TLVREYFSWE
GAFQHVGKAF NQGKIFK


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