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Nucleoporin NUP159 (Nuclear pore protein NUP159)

 NU159_YEAST             Reviewed;        1460 AA.
P40477; D6VVH2;
01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
01-FEB-1995, sequence version 1.
18-JUL-2018, entry version 171.
RecName: Full=Nucleoporin NUP159;
AltName: Full=Nuclear pore protein NUP159;
Name=NUP159; Synonyms=NUP158, RAT7; OrderedLocusNames=YIL115C;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=7744966; DOI=10.1083/jcb.129.4.939;
Gorsch L.C., Dockendorff T.C., Cole C.N.;
"A conditional allele of the novel repeat-containing yeast nucleoporin
RAT7/NUP159 causes both rapid cessation of mRNA export and reversible
clustering of nuclear pore complexes.";
J. Cell Biol. 129:939-955(1995).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169870;
Churcher C.M., Bowman S., Badcock K., Bankier A.T., Brown D.,
Chillingworth T., Connor R., Devlin K., Gentles S., Hamlin N.,
Harris D.E., Horsnell T., Hunt S., Jagels K., Jones M., Lye G.,
Moule S., Odell C., Pearson D., Rajandream M.A., Rice P., Rowley N.,
Skelton J., Smith V., Walsh S.V., Whitehead S., Barrell B.G.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome IX.";
Nature 387:84-87(1997).
[3]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[4]
FUNCTION, AND INTERACTION WITH NUP82.
PubMed=9736720; DOI=10.1073/pnas.95.19.11241;
Hurwitz M.E., Strambio-de-Castillia C., Blobel G.;
"Two yeast nuclear pore complex proteins involved in mRNA export form
a cytoplasmically oriented subcomplex.";
Proc. Natl. Acad. Sci. U.S.A. 95:11241-11245(1998).
[5]
FUNCTION, AND INTERACTION WITH NSP1.
PubMed=9843582; DOI=10.1091/mbc.9.12.3475;
Belgareh N., Snay-Hodge C., Pasteau F., Dagher S., Cole C.N., Doye V.;
"Functional characterization of a Nup159p-containing nuclear pore
subcomplex.";
Mol. Biol. Cell 9:3475-3492(1998).
[6]
FUNCTION, AND INTERACTION WITH PSE1.
PubMed=9891088; DOI=10.1128/MCB.19.2.1547;
Seedorf M., Damelin M., Kahana J., Taura T., Silver P.A.;
"Interactions between a nuclear transporter and a subset of nuclear
pore complex proteins depend on Ran GTPase.";
Mol. Cell. Biol. 19:1547-1557(1999).
[7]
FUNCTION, AND INTERACTION WITH GLE1; CRM1 AND DBP5.
PubMed=10523319; DOI=10.1093/emboj/18.20.5778;
Hodge C.A., Colot H.V., Stafford P., Cole C.N.;
"Rat8p/Dbp5p is a shuttling transport factor that interacts with
Rat7p/Nup159p and Gle1p and suppresses the mRNA export defect of xpo1-
1 cells.";
EMBO J. 18:5778-5788(1999).
[8]
FUNCTION, AND NUP82 NPC SUBCOMPLEX.
PubMed=10801828; DOI=10.1074/jbc.M001963200;
Bailer S.M., Balduf C., Katahira J., Podtelejnikov A., Rollenhagen C.,
Mann M., Pante N., Hurt E.C.;
"Nup116p associates with the Nup82p-Nsp1p-Nup159p nucleoporin
complex.";
J. Biol. Chem. 275:23540-23548(2000).
[9]
CHARACTERIZATION, AND NPC SUBUNIT LOCATION.
PubMed=10684247; DOI=10.1083/jcb.148.4.635;
Rout M.P., Aitchison J.D., Suprapto A., Hjertaas K., Zhao Y.,
Chait B.T.;
"The yeast nuclear pore complex: composition, architecture, and
transport mechanism.";
J. Cell Biol. 148:635-651(2000).
[10]
FUNCTION, AND INTERACTION WITH MEX67/MTR2 HETERODIMER.
PubMed=10952996; DOI=10.1083/jcb.150.4.695;
Straesser K., Bassler J., Hurt E.C.;
"Binding of the Mex67p/Mtr2p heterodimer to FXFG, GLFG, and FG repeat
nucleoporins is essential for nuclear mRNA export.";
J. Cell Biol. 150:695-706(2000).
[11]
FUNCTION, AND INTERACTION WITH KARYOPHERINS THROUGH FG REPEATS.
PubMed=11387327; DOI=10.1074/jbc.M102629200;
Allen N.P., Huang L., Burlingame A., Rexach M.;
"Proteomic analysis of nucleoporin interacting proteins.";
J. Biol. Chem. 276:29268-29274(2001).
[12]
FUNCTION, AND PRE-RIBOSOME EXPORT.
PubMed=11739405; DOI=10.1083/jcb.200108142;
Gleizes P.-E., Noaillac-Depeyre J., Leger-Silvestre I., Teulieres F.,
Dauxois J.-Y., Pommet D., Azum-Gelade M.-C., Gas N.;
"Ultrastructural localization of rRNA shows defective nuclear export
of preribosomes in mutants of the Nup82p complex.";
J. Cell Biol. 155:923-936(2001).
[13]
FUNCTION, AND NPC ASSEMBLY.
PubMed=11689687; DOI=10.1128/MCB.21.23.7944-7955.2001;
Bailer S.M., Balduf C., Hurt E.C.;
"The Nsp1p carboxy-terminal domain is organized into functionally
distinct coiled-coil regions required for assembly of nucleoporin
subcomplexes and nucleocytoplasmic transport.";
Mol. Cell. Biol. 21:7944-7955(2001).
[14]
FUNCTION, AND INTERACTION WITH CRM1 AND RNA1.
PubMed=12543930; DOI=10.1074/mcp.T200012-MCP200;
Allen N.P., Patel S.S., Huang L., Chalkley R.J., Burlingame A.,
Lutzmann M., Hurt E.C., Rexach M.;
"Deciphering networks of protein interactions at the nuclear pore
complex.";
Mol. Cell. Proteomics 1:930-946(2002).
[15]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[16]
FUNCTION, AND FG REPEAT STRUCTURE.
PubMed=12604785; DOI=10.1073/pnas.0437902100;
Denning D.P., Patel S.S., Uversky V., Fink A.L., Rexach M.;
"Disorder in the nuclear pore complex: the FG repeat regions of
nucleoporins are natively unfolded.";
Proc. Natl. Acad. Sci. U.S.A. 100:2450-2455(2003).
[17]
FUNCTION, AND FG REPEATS IN NPC TRANSPORT.
PubMed=15039779; DOI=10.1038/ncb1097;
Strawn L.A., Shen T.X., Shulga N., Goldfarb D.S., Wente S.R.;
"Minimal nuclear pore complexes define FG repeat domains essential for
transport.";
Nat. Cell Biol. 6:197-206(2004).
[18]
REVIEW.
PubMed=12791264; DOI=10.1016/S1534-5807(03)00162-X;
Suntharalingam M., Wente S.R.;
"Peering through the pore: nuclear pore complex structure, assembly,
and function.";
Dev. Cell 4:775-789(2003).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-404; SER-735; THR-803;
SER-805 AND SER-819, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
STRAIN=ADR376;
PubMed=17330950; DOI=10.1021/pr060559j;
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
Elias J.E., Gygi S.P.;
"Large-scale phosphorylation analysis of alpha-factor-arrested
Saccharomyces cerevisiae.";
J. Proteome Res. 6:1190-1197(2007).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-657; SER-724; SER-735;
SER-745; SER-805; SER-819; SER-889 AND SER-940, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200;
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth
phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-404; SER-735; THR-803;
SER-805; SER-819 AND SER-940, AND IDENTIFICATION BY MASS SPECTROMETRY
[LARGE SCALE ANALYSIS].
PubMed=19779198; DOI=10.1126/science.1172867;
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
"Global analysis of Cdk1 substrate phosphorylation sites provides
insights into evolution.";
Science 325:1682-1686(2009).
[22]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 2-387, FUNCTION, AND
INTERACTION WITH DBP5.
PubMed=15574330; DOI=10.1016/j.molcel.2004.10.032;
Weirich C.S., Erzberger J.P., Berger J.M., Weis K.;
"The N-terminal domain of Nup159 forms a beta-propeller that functions
in mRNA export by tethering the helicase Dbp5 to the nuclear pore.";
Mol. Cell 16:749-760(2004).
[23]
X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 1425-1460 IN COMPLEX WITH
NUP82 AND NUP116, AND SUBUNIT.
PubMed=21930948; DOI=10.1073/pnas.1112846108;
Yoshida K., Seo H.S., Debler E.W., Blobel G., Hoelz A.;
"Structural and functional analysis of an essential nucleoporin
heterotrimer on the cytoplasmic face of the nuclear pore complex.";
Proc. Natl. Acad. Sci. U.S.A. 108:16571-16576(2011).
[24]
X-RAY CRYSTALLOGRAPHY (3.4 ANGSTROMS) OF 1425-1460 IN COMPLEX WITH
NUP82 AND THE MOUSE ORTHOLOG OF NUP145, AND SUBUNIT.
PubMed=22480613; DOI=10.1016/j.jmb.2012.03.024;
Stuwe T., von Borzyskowski L.S., Davenport A.M., Hoelz A.;
"Molecular basis for the anchoring of proto-oncoprotein Nup98 to the
cytoplasmic face of the nuclear pore complex.";
J. Mol. Biol. 419:330-346(2012).
-!- FUNCTION: Functions as a component of the nuclear pore complex
(NPC). NPC components, collectively referred to as nucleoporins
(NUPs), can play the role of both NPC structural components and of
docking or interaction partners for transiently associated nuclear
transport factors. Active directional transport is assured by
both, a Phe-Gly (FG) repeat affinity gradient for these transport
factors across the NPC and a transport cofactor concentration
gradient across the nuclear envelope (GSP1 and GSP2 GTPases
associated predominantly with GTP in the nucleus, with GDP in the
cytoplasm). NUP159 plays an important role in several nuclear
export pathways including poly(A)+ RNA, pre-ribosome, and protein
export. {ECO:0000269|PubMed:10523319, ECO:0000269|PubMed:10801828,
ECO:0000269|PubMed:10952996, ECO:0000269|PubMed:11387327,
ECO:0000269|PubMed:11689687, ECO:0000269|PubMed:11739405,
ECO:0000269|PubMed:12543930, ECO:0000269|PubMed:12604785,
ECO:0000269|PubMed:15039779, ECO:0000269|PubMed:15574330,
ECO:0000269|PubMed:9736720, ECO:0000269|PubMed:9843582,
ECO:0000269|PubMed:9891088}.
-!- SUBUNIT: The nuclear pore complex (NPC) constitutes the exclusive
means of nucleocytoplasmic transport. NPCs allow the passive
diffusion of ions and small molecules and the active, nuclear
transport receptor-mediated bidirectional transport of
macromolecules such as proteins, RNAs, ribonucleoparticles (RNPs),
and ribosomal subunits across the nuclear envelope. The 55-60 MDa
NPC is composed of at least 31 different subunits: ASM4, CDC31,
GLE1, GLE2, NDC1, NIC96, NSP1, NUP1, NUP2, NUP100, NUP116, NUP120,
NUP133, NUP145, NUP157, NUP159, NUP170, NUP188, NUP192, NUP42,
NUP49, NUP53, NUP57, NUP60, NUP82, NUP84, NUP85, POM152, POM34,
SEC13 and SEH1. Due to its 8-fold rotational symmetry, all
subunits are present with 8 copies or multiples thereof. NUP159 is
part of the NUP82 subcomplex (NUP82, NSP1, NUP159) interacting
with NUP82 through its C-terminal coiled coil. This subcomplex is
the base for interactions with NUP116 and GLE2 and with NUP42 and
GLE1. Interacts through its FG repeats with karyopherins, such as
heterodimeric mRNA transport factor MEX67/MTR2, CRM1 (XPO1), and
PSE1 (GSP1-GDP dependent). Interaction with CRM1 (XPO1) is GSP1-
GTP dependent and stimulated by RNA1. NUP159 also interacts with
GLE1 and the ATP-dependent RNA helicase DBP5.
{ECO:0000269|PubMed:10523319, ECO:0000269|PubMed:10952996,
ECO:0000269|PubMed:11387327, ECO:0000269|PubMed:12543930,
ECO:0000269|PubMed:15574330, ECO:0000269|PubMed:21930948,
ECO:0000269|PubMed:22480613, ECO:0000269|PubMed:9736720,
ECO:0000269|PubMed:9843582, ECO:0000269|PubMed:9891088}.
-!- INTERACTION:
P20449:DBP5; NbExp=4; IntAct=EBI-11747, EBI-5617;
Q06142:KAP95; NbExp=3; IntAct=EBI-11747, EBI-9145;
P14907:NSP1; NbExp=9; IntAct=EBI-11747, EBI-12265;
P36161:NUP133; NbExp=3; IntAct=EBI-11747, EBI-11722;
P40368:NUP82; NbExp=8; IntAct=EBI-11747, EBI-12331;
P16521:YEF3; NbExp=3; IntAct=EBI-11747, EBI-6338;
-!- SUBCELLULAR LOCATION: Nucleus, nuclear pore complex. Nucleus
membrane; Peripheral membrane protein; Cytoplasmic side.
-!- DOMAIN: Contains FG repeats. FG repeats are interaction sites for
karyopherins (importins, exportins) and form probably an affinity
gradient, guiding the transport proteins unidirectionally with
their cargo through the NPC. FG repeat regions are highly flexible
and lack ordered secondary structure. The overall conservation of
FG repeats regarding exact sequence, spacing, and repeat unit
length is limited. FG repeat types and their physico-chemical
environment change across the NPC from the nucleoplasmic to the
cytoplasmic side: SXFG/PXFG repeats are especially abundant in
NUPs on the cytoplasmic side.
-!- MISCELLANEOUS: Present with 1230 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
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EMBL; L40634; AAC41652.1; -; Genomic_DNA.
EMBL; Z38125; CAA86265.1; -; Genomic_DNA.
EMBL; BK006942; DAA08438.1; -; Genomic_DNA.
PIR; S48457; S48457.
RefSeq; NP_012151.1; NM_001179463.1.
PDB; 1XIP; X-ray; 2.50 A; A=2-387.
PDB; 3PBP; X-ray; 2.60 A; C/F/I/L=1425-1460.
PDB; 3RRM; X-ray; 2.88 A; C=2-387.
PDB; 3TKN; X-ray; 3.40 A; B/E/H=1425-1460.
PDB; 4DS1; X-ray; 1.85 A; B/D=1116-1126.
PDBsum; 1XIP; -.
PDBsum; 3PBP; -.
PDBsum; 3RRM; -.
PDBsum; 3TKN; -.
PDBsum; 4DS1; -.
DisProt; DP01078; -.
ProteinModelPortal; P40477; -.
SMR; P40477; -.
BioGrid; 34876; 240.
ComplexPortal; CPX-824; Nuclear pore complex.
DIP; DIP-2314N; -.
IntAct; P40477; 29.
MINT; P40477; -.
STRING; 4932.YIL115C; -.
TCDB; 1.I.1.1.1; the eukaryotic nuclear pore complex (e-npc) family.
iPTMnet; P40477; -.
MaxQB; P40477; -.
PaxDb; P40477; -.
PRIDE; P40477; -.
DNASU; 854691; -.
EnsemblFungi; YIL115C; YIL115C; YIL115C.
GeneID; 854691; -.
KEGG; sce:YIL115C; -.
EuPathDB; FungiDB:YIL115C; -.
SGD; S000001377; NUP159.
GeneTree; ENSGT00730000113975; -.
HOGENOM; HOG000113875; -.
InParanoid; P40477; -.
KO; K18715; -.
OMA; FGESAFG; -.
OrthoDB; EOG092C0CCA; -.
BioCyc; YEAST:G3O-31369-MONOMER; -.
EvolutionaryTrace; P40477; -.
PRO; PR:P40477; -.
Proteomes; UP000002311; Chromosome IX.
GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
GO; GO:0005643; C:nuclear pore; IDA:SGD.
GO; GO:0044613; C:nuclear pore central transport channel; IDA:SGD.
GO; GO:0044614; C:nuclear pore cytoplasmic filaments; IDA:SGD.
GO; GO:0000774; F:adenyl-nucleotide exchange factor activity; IDA:SGD.
GO; GO:0017056; F:structural constituent of nuclear pore; IPI:SGD.
GO; GO:0003714; F:transcription corepressor activity; IBA:GO_Central.
GO; GO:0097064; P:ncRNA export from nucleus; IMP:SGD.
GO; GO:0006607; P:NLS-bearing protein import into nucleus; IGI:SGD.
GO; GO:0031081; P:nuclear pore distribution; IMP:SGD.
GO; GO:0016973; P:poly(A)+ mRNA export from nucleus; IMP:SGD.
GO; GO:0006611; P:protein export from nucleus; IMP:SGD.
GO; GO:0000055; P:ribosomal large subunit export from nucleus; IMP:SGD.
GO; GO:0000056; P:ribosomal small subunit export from nucleus; IMP:SGD.
Gene3D; 2.130.10.10; -; 1.
InterPro; IPR037686; Nup159/Nup146.
InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
PANTHER; PTHR21243:SF14; PTHR21243:SF14; 1.
1: Evidence at protein level;
3D-structure; Coiled coil; Complete proteome; Membrane;
mRNA transport; Nuclear pore complex; Nucleus; Phosphoprotein;
Protein transport; Reference proteome; Repeat; Translocation;
Transport.
CHAIN 1 1460 Nucleoporin NUP159.
/FTId=PRO_0000204849.
REPEAT 228 231 FG 1.
REPEAT 267 270 PXFG 1.
REPEAT 462 470 SXFGXPXFG 1.
REPEAT 503 511 SXFGXPXFG 2; approximate.
REPEAT 522 530 SXFGXPXFG 3; approximate.
REPEAT 532 535 PXFG 2.
REPEAT 548 556 SXFGXPXFG 4.
REPEAT 558 561 PXFG 3.
REPEAT 574 582 SXFGXPXFG 5.
REPEAT 584 587 PXFG 4.
REPEAT 600 608 SXFGXPXFG 6.
REPEAT 610 613 SXFG 1.
REPEAT 624 632 SXFGXPXFG 7; approximate.
REPEAT 642 645 FG 2.
REPEAT 687 690 FG 3.
REPEAT 704 707 FXFG 1.
REPEAT 709 712 SXFG 2.
REPEAT 728 731 FXFG 2.
REPEAT 842 845 PXFG 5.
REPEAT 873 876 FXFG 3.
REGION 1 500 Interaction with DBP5.
REGION 497 701 Interactions with CRM1 and GLE1.
REGION 1223 1460 Interaction with NUP82.
{ECO:0000269|PubMed:9736720}.
COILED 1279 1320
COILED 1383 1418
COMPBIAS 455 766 Ser-rich.
MOD_RES 404 404 Phosphoserine.
{ECO:0000244|PubMed:17330950,
ECO:0000244|PubMed:19779198}.
MOD_RES 657 657 Phosphoserine.
{ECO:0000244|PubMed:18407956}.
MOD_RES 724 724 Phosphoserine.
{ECO:0000244|PubMed:18407956}.
MOD_RES 735 735 Phosphoserine.
{ECO:0000244|PubMed:17330950,
ECO:0000244|PubMed:18407956,
ECO:0000244|PubMed:19779198}.
MOD_RES 745 745 Phosphoserine.
{ECO:0000244|PubMed:18407956}.
MOD_RES 803 803 Phosphothreonine.
{ECO:0000244|PubMed:17330950,
ECO:0000244|PubMed:19779198}.
MOD_RES 805 805 Phosphoserine.
{ECO:0000244|PubMed:17330950,
ECO:0000244|PubMed:18407956,
ECO:0000244|PubMed:19779198}.
MOD_RES 819 819 Phosphoserine.
{ECO:0000244|PubMed:17330950,
ECO:0000244|PubMed:18407956,
ECO:0000244|PubMed:19779198}.
MOD_RES 889 889 Phosphoserine.
{ECO:0000244|PubMed:18407956}.
MOD_RES 940 940 Phosphoserine.
{ECO:0000244|PubMed:18407956,
ECO:0000244|PubMed:19779198}.
STRAND 10 15 {ECO:0000244|PDB:1XIP}.
STRAND 17 25 {ECO:0000244|PDB:1XIP}.
STRAND 42 45 {ECO:0000244|PDB:1XIP}.
TURN 46 49 {ECO:0000244|PDB:1XIP}.
STRAND 50 55 {ECO:0000244|PDB:1XIP}.
STRAND 58 63 {ECO:0000244|PDB:1XIP}.
HELIX 64 72 {ECO:0000244|PDB:1XIP}.
STRAND 73 75 {ECO:0000244|PDB:1XIP}.
STRAND 81 85 {ECO:0000244|PDB:1XIP}.
STRAND 89 95 {ECO:0000244|PDB:1XIP}.
STRAND 98 114 {ECO:0000244|PDB:1XIP}.
STRAND 118 123 {ECO:0000244|PDB:1XIP}.
STRAND 128 133 {ECO:0000244|PDB:1XIP}.
STRAND 135 142 {ECO:0000244|PDB:1XIP}.
STRAND 145 151 {ECO:0000244|PDB:1XIP}.
TURN 152 154 {ECO:0000244|PDB:1XIP}.
STRAND 157 169 {ECO:0000244|PDB:1XIP}.
STRAND 171 178 {ECO:0000244|PDB:1XIP}.
STRAND 183 189 {ECO:0000244|PDB:1XIP}.
STRAND 192 199 {ECO:0000244|PDB:1XIP}.
HELIX 203 206 {ECO:0000244|PDB:1XIP}.
TURN 210 212 {ECO:0000244|PDB:1XIP}.
STRAND 213 231 {ECO:0000244|PDB:1XIP}.
STRAND 245 253 {ECO:0000244|PDB:1XIP}.
STRAND 256 265 {ECO:0000244|PDB:1XIP}.
STRAND 278 284 {ECO:0000244|PDB:1XIP}.
STRAND 286 288 {ECO:0000244|PDB:1XIP}.
STRAND 292 298 {ECO:0000244|PDB:1XIP}.
STRAND 305 307 {ECO:0000244|PDB:1XIP}.
STRAND 309 317 {ECO:0000244|PDB:1XIP}.
HELIX 318 320 {ECO:0000244|PDB:1XIP}.
TURN 328 330 {ECO:0000244|PDB:1XIP}.
STRAND 336 342 {ECO:0000244|PDB:1XIP}.
STRAND 364 369 {ECO:0000244|PDB:1XIP}.
STRAND 372 380 {ECO:0000244|PDB:1XIP}.
STRAND 1118 1123 {ECO:0000244|PDB:4DS1}.
HELIX 1436 1454 {ECO:0000244|PDB:3PBP}.
SEQUENCE 1460 AA; 158908 MW; A33FFA52378F8205 CRC64;
MSSLKDEVPT ETSEDFGFKF LGQKQILPSF NEKLPFASLQ NLDISNSKSL FVAASGSKAV
VGELQLLRDH ITSDSTPLTF KWEKEIPDVI FVCFHGDQVL VSTRNALYSL DLEELSEFRT
VTSFEKPVFQ LKNVNNTLVI LNSVNDLSAL DLRTKSTKQL AQNVTSFDVT NSQLAVLLKD
RSFQSFAWRN GEMEKQFEFS LPSELEELPV EEYSPLSVTI LSPQDFLAVF GNVISETDDE
VSYDQKMYII KHIDGSASFQ ETFDITPPFG QIVRFPYMYK VTLSGLIEPD ANVNVLASSC
SSEVSIWDSK QVIEPSQDSE RAVLPISEET DKDTNPIGVA VDVVTSGTIL EPCSGVDTIE
RLPLVYILNN EGSLQIVGLF HVAAIKSGHY SINLESLEHE KSLSPTSEKI PIAGQEQEEK
KKNNESSKAL SENPFTSANT SGFTFLKTQP AAANSLQSQS SSTFGAPSFG SSAFKIDLPS
VSSTSTGVAS SEQDATDPAS AKPVFGKPAF GAIAKEPSTS EYAFGKPSFG APSFGSGKSS
VESPASGSAF GKPSFGTPSF GSGNSSVEPP ASGSAFGKPS FGTPSFGSGN SSAEPPASGS
AFGKPSFGTS AFGTASSNET NSGSIFGKAA FGSSSFAPAN NELFGSNFTI SKPTVDSPKE
VDSTSPFPSS GDQSEDESKS DVDSSSTPFG TKPNTSTKPK TNAFDFGSSS FGSGFSKALE
SVGSDTTFKF GTQASPFSSQ LGNKSPFSSF TKDDTENGSL SKGSTSEIND DNEEHESNGP
NVSGNDLTDS TVEQTSSTRL PETPSDEDGE VVEEEAQKSP IGKLTETIKK SANIDMAGLK
NPVFGNHVKA KSESPFSAFA TNITKPSSTT PAFSFGNSTM NKSNTSTVSP MEEADTKETS
EKGPITLKSV ENPFLPAKEE RTGESSKKDH NDDPKDGYVS GSEISVRTSE SAFDTTANEE
IPKSQDVNNH EKSETDPKYS QHAVVDHDNK SKEMNETSKN NERSGQPNHG VQGDGIALKK
DNEKENFDSN MAIKQFEDHQ SSEEDASEKD SRQSSEVKES DDNMSLNSDR DESISESYDK
LEDINTDELP HGGEAFKARE VSASADFDVQ TSLEDNYAES GIQTDLSESS KENEVQTDAI
PVKHNSTQTV KKEAVDNGLQ TEPVETCNFS VQTFEGDENY LAEQCKPKQL KEYYTSAKVS
NIPFVSQNST LRLIESTFQT VEAEFTVLME NIRNMDTFFT DQSSIPLVKR TVRSINNLYT
WRIPEAEILL NIQNNIKCEQ MQITNANIQD LKEKVTDYVR KDIAQITEDV ANAKEEYLFL
MHFDDASSGY VKDLSTHQFR MQKTLRQKLF DVSAKINHTE ELLNILKLFT VKNKRLDDNP
LVAKLAKESL ARDGLLKEIK LLREQVSRLQ LEEKGKKASS FDASSSITKD MKGFKVVEVG
LAMNTKKQIG DFFKNLNMAK


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