IMB1_YEAST
ID IMB1_YEAST Reviewed; 861 AA.
AC Q06142; D6VYY6;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 197.
DE RecName: Full=Importin subunit beta-1 {ECO:0000303|PubMed:9321403};
DE AltName: Full=Importin-95 {ECO:0000305};
DE AltName: Full=Karyopherin subunit beta-1 {ECO:0000303|PubMed:7622450};
DE AltName: Full=Karyopherin-95 {ECO:0000303|PubMed:7622450};
GN Name=KAP95 {ECO:0000303|PubMed:7622450, ECO:0000312|SGD:S000004339};
GN OrderedLocusNames=YLR347C {ECO:0000312|SGD:S000004339}; ORFNames=L8300.15;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(1997).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP PROTEIN SEQUENCE OF 819-846, FUNCTION, AND INTERACTION WITH SRP1.
RX PubMed=7622450; DOI=10.1074/jbc.270.28.16499;
RA Enenkel C., Blobel G., Rexach M.;
RT "Identification of a yeast karyopherin heterodimer that targets import
RT substrate to mammalian nuclear pore complexes.";
RL J. Biol. Chem. 270:16499-16502(1995).
RN [4]
RP INTERACTION WITH GSP1.
RX PubMed=8621381; DOI=10.1074/jbc.271.10.5313;
RA Floer M., Blobel G.;
RT "The nuclear transport factor karyopherin beta binds stoichiometrically to
RT Ran-GTP and inhibits the Ran GTPase activating protein.";
RL J. Biol. Chem. 271:5313-5316(1996).
RN [5]
RP FUNCTION, AND INTERACTION WITH NUP1.
RX PubMed=8521485; DOI=10.1016/0092-8674(95)90181-7;
RA Rexach M., Blobel G.;
RT "Protein import into nuclei: association and dissociation reactions
RT involving transport substrate, transport factors, and nucleoporins.";
RL Cell 83:683-692(1995).
RN [6]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH GSP1.
RX PubMed=9321403; DOI=10.1093/emboj/16.20.6237;
RA Schlenstedt G., Smirnova E., Deane R., Solsbacher J., Kutay U.,
RA Goerlich D., Ponstingl H., Bischoff F.R.;
RT "Yrb4p, a yeast ran-GTP-binding protein involved in import of ribosomal
RT protein L25 into the nucleus.";
RL EMBO J. 16:6237-6249(1997).
RN [7]
RP SUBCELLULAR LOCATION.
RX PubMed=10684247; DOI=10.1083/jcb.148.4.635;
RA Rout M.P., Aitchison J.D., Suprapto A., Hjertaas K., Zhao Y., Chait B.T.;
RT "The yeast nuclear pore complex: composition, architecture, and transport
RT mechanism.";
RL J. Cell Biol. 148:635-651(2000).
RN [8]
RP REVIEW.
RX PubMed=11423015; DOI=10.1186/gb-2001-2-6-reviews3008;
RA Stroem A.C., Weis K.;
RT "Importin-beta-like nuclear transport receptors.";
RL Genome Biol. 2:REVIEWS3008.1-REVIEWS3008.9(2001).
RN [9]
RP FUNCTION IN HISTONE H2A/H2B IMPORT.
RX PubMed=11309407; DOI=10.1083/jcb.153.2.251;
RA Mosammaparast N., Jackson K.R., Guo Y., Brame C.J., Shabanowitz J.,
RA Hunt D.F., Pemberton L.F.;
RT "Nuclear import of histone H2A and H2B is mediated by a network of
RT karyopherins.";
RL J. Cell Biol. 153:251-262(2001).
RN [10]
RP FUNCTION.
RC STRAIN=ATCC 200060 / W303 {ECO:0000303|PubMed:14648200};
RX PubMed=14648200; DOI=10.1007/s00438-003-0955-7;
RA Pries R., Boemeke K., Draht O., Kuenzler M., Braus G.H.;
RT "Nuclear import of yeast Gcn4p requires karyopherins Srp1p and Kap95p.";
RL Mol. Genet. Genomics 271:257-266(2004).
RN [11]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-836, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (1.99 ANGSTROMS) IN COMPLEX WITH NUP1, AND REPEAT
RP STRUCTURE.
RX PubMed=15878174; DOI=10.1016/j.jmb.2005.04.003;
RA Liu S.M., Stewart M.;
RT "Structural basis for the high-affinity binding of nucleoporin Nup1p to the
RT Saccharomyces cerevisiae importin-beta homologue, Kap95p.";
RL J. Mol. Biol. 349:515-525(2005).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) IN COMPLEX WITH GSP1, AND FUNCTION.
RX PubMed=15864302; DOI=10.1038/nature03578;
RA Lee S.J., Matsuura Y., Liu S.M., Stewart M.;
RT "Structural basis for nuclear import complex dissociation by RanGTP.";
RL Nature 435:693-696(2005).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) IN COMPLEX WITH GSP1.
RX PubMed=18708071; DOI=10.1016/j.jmb.2008.07.090;
RA Forwood J.K., Lonhienne T.G., Marfori M., Robin G., Meng W., Guncar G.,
RA Liu S.M., Stewart M., Carroll B.J., Kobe B.;
RT "Kap95p binding induces the switch loops of RanGDP to adopt the GTP-bound
RT conformation: implications for nuclear import complex assembly dynamics.";
RL J. Mol. Biol. 383:772-782(2008).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS).
RX PubMed=20826343; DOI=10.1016/j.str.2010.06.015;
RA Forwood J.K., Lange A., Zachariae U., Marfori M., Preast C., Grubmuller H.,
RA Stewart M., Corbett A.H., Kobe B.;
RT "Quantitative structural analysis of importin-beta flexibility: paradigm
RT for solenoid protein structures.";
RL Structure 18:1171-1183(2010).
CC -!- FUNCTION: Importin beta subunit that functions in nuclear protein
CC import through association with the importin alpha subunit, which binds
CC to the classical nuclear localization signal (cNLS) in cargo substrates
CC (PubMed:7622450). Docking of the importin/substrate complex to the
CC nuclear pore complex (NPC) is mediated by importin beta through binding
CC to nucleoporin FxFG repeats and the complex is subsequently
CC translocated through the pore by an energy requiring, Ran-dependent
CC mechanism (PubMed:8521485). At the nucleoplasmic side of the NPC, GTP-
CC Ran binds to importin beta and the three components separate, leading
CC to release of the cargo (PubMed:15864302). Importin alpha and beta are
CC re-exported from the nucleus to the cytoplasm where GTP hydrolysis
CC releases Ran from importin beta. The directionality of nuclear import
CC is thought to be conferred by an asymmetric distribution of the
CC GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus
CC (PubMed:11423015). Mediates the nuclear import of histones H2A and H2B
CC (PubMed:11309407). Mediates the nuclear import of transcription factor
CC GCN4 (PubMed:14648200). {ECO:0000269|PubMed:11309407,
CC ECO:0000269|PubMed:14648200, ECO:0000269|PubMed:15864302,
CC ECO:0000269|PubMed:7622450, ECO:0000269|PubMed:8521485,
CC ECO:0000305|PubMed:11423015}.
CC -!- SUBUNIT: Forms a complex with the importin alpha subunit (SRP1/KAP60)
CC (PubMed:7622450). Interacts with Ran (GSP1); interacts specifically
CC with the GTP-bound form of Ran (GTP-Ran), protecting it from GTP
CC hydrolysis and nucleotide exchange (PubMed:8621381, PubMed:9321403).
CC Interacts with nucleoporin NUP1 (PubMed:8521485, PubMed:15878174).
CC {ECO:0000269|PubMed:15878174, ECO:0000269|PubMed:7622450,
CC ECO:0000269|PubMed:8521485, ECO:0000269|PubMed:8621381,
CC ECO:0000269|PubMed:9321403}.
CC -!- INTERACTION:
CC Q06142; P14907: NSP1; NbExp=4; IntAct=EBI-9145, EBI-12265;
CC Q06142; P20676: NUP1; NbExp=6; IntAct=EBI-9145, EBI-12392;
CC Q06142; Q02629: NUP100; NbExp=6; IntAct=EBI-9145, EBI-11698;
CC Q06142; Q02630: NUP116; NbExp=4; IntAct=EBI-9145, EBI-11703;
CC Q06142; P40477: NUP159; NbExp=3; IntAct=EBI-9145, EBI-11747;
CC Q06142; P32499: NUP2; NbExp=5; IntAct=EBI-9145, EBI-12401;
CC Q06142; P49686: NUP42; NbExp=2; IntAct=EBI-9145, EBI-12310;
CC Q06142; Q02199: NUP49; NbExp=2; IntAct=EBI-9145, EBI-12315;
CC Q06142; P48837: NUP57; NbExp=2; IntAct=EBI-9145, EBI-12324;
CC Q06142; P39705: NUP60; NbExp=3; IntAct=EBI-9145, EBI-20731;
CC Q06142; Q02821: SRP1; NbExp=9; IntAct=EBI-9145, EBI-1797;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10684247,
CC ECO:0000269|PubMed:9321403}. Nucleus {ECO:0000269|PubMed:9321403}.
CC Nucleus, nuclear pore complex {ECO:0000269|PubMed:10684247}.
CC -!- MISCELLANEOUS: Binds to nucleoporin FxFG but not GLFG repeat regions.
CC Ran-GTP can disrupt the importin alpha/beta heterodimer by binding to
CC the beta subunit and releases both subunits from the docking site.
CC {ECO:0000269|PubMed:8521485}.
CC -!- MISCELLANEOUS: The stoichiometric complex between importin beta and
CC Ran-GTP renders the latter inaccessible to Ran-specific GTPase
CC activating protein (Ran-GAP) thereby inhibiting GTP hydrolysis
CC stimulated by Ran-GAP. {ECO:0000269|PubMed:8621381}.
CC -!- MISCELLANEOUS: Present with 51700 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the importin beta family. Importin beta-1
CC subfamily. {ECO:0000305}.
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DR EMBL; U19028; AAB67265.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09652.1; -; Genomic_DNA.
DR PIR; S51350; S51350.
DR RefSeq; NP_013451.1; NM_001182236.1.
DR PDB; 2BKU; X-ray; 2.70 A; B/D=1-861.
DR PDB; 3EA5; X-ray; 2.50 A; B/D=1-861.
DR PDB; 3ND2; X-ray; 2.40 A; A=1-861.
DR PDB; 5OWU; X-ray; 2.00 A; A=1-861.
DR PDBsum; 2BKU; -.
DR PDBsum; 3EA5; -.
DR PDBsum; 3ND2; -.
DR PDBsum; 5OWU; -.
DR AlphaFoldDB; Q06142; -.
DR SMR; Q06142; -.
DR BioGRID; 31610; 623.
DR ComplexPortal; CPX-1068; Importin complex, KAP60-KAP95.
DR DIP; DIP-2357N; -.
DR IntAct; Q06142; 69.
DR MINT; Q06142; -.
DR STRING; 4932.YLR347C; -.
DR iPTMnet; Q06142; -.
DR MaxQB; Q06142; -.
DR PaxDb; Q06142; -.
DR PRIDE; Q06142; -.
DR EnsemblFungi; YLR347C_mRNA; YLR347C; YLR347C.
DR GeneID; 851061; -.
DR KEGG; sce:YLR347C; -.
DR SGD; S000004339; KAP95.
DR VEuPathDB; FungiDB:YLR347C; -.
DR eggNOG; KOG1241; Eukaryota.
DR GeneTree; ENSGT00550000074898; -.
DR HOGENOM; CLU_008296_1_0_1; -.
DR InParanoid; Q06142; -.
DR OMA; GRICDII; -.
DR BioCyc; YEAST:G3O-32423-MON; -.
DR Reactome; R-SCE-2995383; Initiation of Nuclear Envelope (NE) Reformation.
DR Reactome; R-SCE-6798695; Neutrophil degranulation.
DR EvolutionaryTrace; Q06142; -.
DR PRO; PR:Q06142; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; Q06142; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0005829; C:cytosol; IDA:ComplexPortal.
DR GO; GO:0042564; C:NLS-dependent protein nuclear import complex; IDA:SGD.
DR GO; GO:0005635; C:nuclear envelope; IDA:ComplexPortal.
DR GO; GO:0005643; C:nuclear pore; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0097718; F:disordered domain specific binding; IPI:CAFA.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IDA:SGD.
DR GO; GO:0061676; F:importin-alpha family protein binding; IPI:CAFA.
DR GO; GO:0061608; F:nuclear import signal receptor activity; IDA:SGD.
DR GO; GO:0008139; F:nuclear localization sequence binding; IBA:GO_Central.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:SGD.
DR GO; GO:0031267; F:small GTPase binding; IEA:InterPro.
DR GO; GO:0051170; P:import into nucleus; IC:ComplexPortal.
DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR GO; GO:0006607; P:NLS-bearing protein import into nucleus; IMP:SGD.
DR GO; GO:0051292; P:nuclear pore complex assembly; IMP:SGD.
DR GO; GO:0006656; P:phosphatidylcholine biosynthetic process; IMP:SGD.
DR GO; GO:0006606; P:protein import into nucleus; IMP:UniProtKB.
DR GO; GO:0006612; P:protein targeting to membrane; IMP:SGD.
DR GO; GO:0046822; P:regulation of nucleocytoplasmic transport; IDA:SGD.
DR GO; GO:0060188; P:regulation of protein desumoylation; IMP:SGD.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR000225; Armadillo.
DR InterPro; IPR021133; HEAT_type_2.
DR InterPro; IPR001494; Importin-beta_N.
DR InterPro; IPR040122; Importin_beta.
DR PANTHER; PTHR10527; PTHR10527; 1.
DR Pfam; PF03810; IBN_N; 1.
DR SMART; SM00185; ARM; 2.
DR SMART; SM00913; IBN_N; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR PROSITE; PS50077; HEAT_REPEAT; 1.
DR PROSITE; PS50166; IMPORTIN_B_NT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Direct protein sequencing;
KW mRNA transport; Nuclear pore complex; Nucleus; Phosphoprotein;
KW Protein transport; Reference proteome; Repeat; Translocation; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..861
FT /note="Importin subunit beta-1"
FT /id="PRO_0000120764"
FT REPEAT 3..35
FT /note="HEAT 1"
FT /evidence="ECO:0000269|PubMed:15878174"
FT DOMAIN 25..106
FT /note="Importin N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00115"
FT REPEAT 37..66
FT /note="HEAT 2"
FT /evidence="ECO:0000269|PubMed:15878174"
FT REPEAT 90..129
FT /note="HEAT 3"
FT /evidence="ECO:0000269|PubMed:15878174"
FT REPEAT 134..164
FT /note="HEAT 4"
FT /evidence="ECO:0000269|PubMed:15878174"
FT REPEAT 177..208
FT /note="HEAT 5"
FT /evidence="ECO:0000269|PubMed:15878174"
FT REPEAT 219..255
FT /note="HEAT 6"
FT /evidence="ECO:0000269|PubMed:15878174"
FT REPEAT 260..306
FT /note="HEAT 7"
FT /evidence="ECO:0000269|PubMed:15878174"
FT REPEAT 317..362
FT /note="HEAT 8"
FT /evidence="ECO:0000269|PubMed:15878174"
FT REPEAT 367..395
FT /note="HEAT 9"
FT /evidence="ECO:0000269|PubMed:15878174"
FT REPEAT 402..442
FT /note="HEAT 10"
FT /evidence="ECO:0000269|PubMed:15878174"
FT REPEAT 452..484
FT /note="HEAT 11"
FT /evidence="ECO:0000269|PubMed:15878174"
FT REPEAT 496..530
FT /note="HEAT 12"
FT /evidence="ECO:0000269|PubMed:15878174"
FT REPEAT 536..586
FT /note="HEAT 13"
FT /evidence="ECO:0000269|PubMed:15878174"
FT REPEAT 592..629
FT /note="HEAT 14"
FT /evidence="ECO:0000269|PubMed:15878174"
FT REPEAT 634..669
FT /note="HEAT 15"
FT /evidence="ECO:0000269|PubMed:15878174"
FT REPEAT 675..713
FT /note="HEAT 16"
FT /evidence="ECO:0000269|PubMed:15878174"
FT REPEAT 718..764
FT /note="HEAT 17"
FT /evidence="ECO:0000269|PubMed:15878174"
FT REPEAT 773..812
FT /note="HEAT 18"
FT /evidence="ECO:0000269|PubMed:15878174"
FT REPEAT 819..859
FT /note="HEAT 19"
FT /evidence="ECO:0000269|PubMed:15878174"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 836
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT HELIX 3..15
FT /evidence="ECO:0007829|PDB:5OWU"
FT HELIX 19..35
FT /evidence="ECO:0007829|PDB:5OWU"
FT HELIX 37..48
FT /evidence="ECO:0007829|PDB:5OWU"
FT HELIX 55..67
FT /evidence="ECO:0007829|PDB:5OWU"
FT HELIX 74..87
FT /evidence="ECO:0007829|PDB:5OWU"
FT HELIX 90..104
FT /evidence="ECO:0007829|PDB:5OWU"
FT HELIX 109..126
FT /evidence="ECO:0007829|PDB:5OWU"
FT HELIX 127..129
FT /evidence="ECO:0007829|PDB:5OWU"
FT HELIX 134..142
FT /evidence="ECO:0007829|PDB:5OWU"
FT HELIX 149..165
FT /evidence="ECO:0007829|PDB:5OWU"
FT STRAND 166..169
FT /evidence="ECO:0007829|PDB:3EA5"
FT HELIX 174..176
FT /evidence="ECO:0007829|PDB:5OWU"
FT HELIX 177..188
FT /evidence="ECO:0007829|PDB:5OWU"
FT HELIX 195..208
FT /evidence="ECO:0007829|PDB:5OWU"
FT HELIX 209..211
FT /evidence="ECO:0007829|PDB:5OWU"
FT HELIX 213..216
FT /evidence="ECO:0007829|PDB:5OWU"
FT HELIX 219..233
FT /evidence="ECO:0007829|PDB:5OWU"
FT HELIX 238..255
FT /evidence="ECO:0007829|PDB:5OWU"
FT HELIX 256..258
FT /evidence="ECO:0007829|PDB:5OWU"
FT HELIX 260..265
FT /evidence="ECO:0007829|PDB:5OWU"
FT HELIX 267..274
FT /evidence="ECO:0007829|PDB:5OWU"
FT HELIX 280..306
FT /evidence="ECO:0007829|PDB:5OWU"
FT HELIX 317..332
FT /evidence="ECO:0007829|PDB:5OWU"
FT HELIX 347..362
FT /evidence="ECO:0007829|PDB:5OWU"
FT HELIX 363..366
FT /evidence="ECO:0007829|PDB:5OWU"
FT HELIX 367..377
FT /evidence="ECO:0007829|PDB:5OWU"
FT HELIX 383..395
FT /evidence="ECO:0007829|PDB:5OWU"
FT STRAND 397..400
FT /evidence="ECO:0007829|PDB:5OWU"
FT HELIX 402..418
FT /evidence="ECO:0007829|PDB:5OWU"
FT HELIX 419..421
FT /evidence="ECO:0007829|PDB:5OWU"
FT HELIX 425..442
FT /evidence="ECO:0007829|PDB:5OWU"
FT HELIX 443..445
FT /evidence="ECO:0007829|PDB:5OWU"
FT TURN 448..451
FT /evidence="ECO:0007829|PDB:5OWU"
FT HELIX 452..463
FT /evidence="ECO:0007829|PDB:5OWU"
FT HELIX 467..484
FT /evidence="ECO:0007829|PDB:5OWU"
FT STRAND 487..489
FT /evidence="ECO:0007829|PDB:5OWU"
FT HELIX 491..495
FT /evidence="ECO:0007829|PDB:5OWU"
FT HELIX 496..507
FT /evidence="ECO:0007829|PDB:5OWU"
FT STRAND 509..511
FT /evidence="ECO:0007829|PDB:3ND2"
FT HELIX 513..515
FT /evidence="ECO:0007829|PDB:5OWU"
FT HELIX 516..530
FT /evidence="ECO:0007829|PDB:5OWU"
FT HELIX 533..535
FT /evidence="ECO:0007829|PDB:5OWU"
FT HELIX 536..553
FT /evidence="ECO:0007829|PDB:5OWU"
FT HELIX 558..560
FT /evidence="ECO:0007829|PDB:5OWU"
FT HELIX 563..586
FT /evidence="ECO:0007829|PDB:5OWU"
FT HELIX 588..590
FT /evidence="ECO:0007829|PDB:5OWU"
FT HELIX 592..594
FT /evidence="ECO:0007829|PDB:5OWU"
FT HELIX 595..607
FT /evidence="ECO:0007829|PDB:5OWU"
FT STRAND 608..610
FT /evidence="ECO:0007829|PDB:3EA5"
FT HELIX 611..613
FT /evidence="ECO:0007829|PDB:5OWU"
FT HELIX 615..629
FT /evidence="ECO:0007829|PDB:5OWU"
FT HELIX 630..636
FT /evidence="ECO:0007829|PDB:5OWU"
FT HELIX 637..649
FT /evidence="ECO:0007829|PDB:5OWU"
FT HELIX 655..669
FT /evidence="ECO:0007829|PDB:5OWU"
FT HELIX 671..674
FT /evidence="ECO:0007829|PDB:5OWU"
FT HELIX 675..689
FT /evidence="ECO:0007829|PDB:5OWU"
FT HELIX 698..713
FT /evidence="ECO:0007829|PDB:5OWU"
FT HELIX 714..717
FT /evidence="ECO:0007829|PDB:5OWU"
FT HELIX 718..732
FT /evidence="ECO:0007829|PDB:5OWU"
FT STRAND 737..740
FT /evidence="ECO:0007829|PDB:5OWU"
FT HELIX 741..764
FT /evidence="ECO:0007829|PDB:5OWU"
FT TURN 765..767
FT /evidence="ECO:0007829|PDB:5OWU"
FT HELIX 769..772
FT /evidence="ECO:0007829|PDB:5OWU"
FT HELIX 773..775
FT /evidence="ECO:0007829|PDB:5OWU"
FT HELIX 776..788
FT /evidence="ECO:0007829|PDB:5OWU"
FT HELIX 790..793
FT /evidence="ECO:0007829|PDB:5OWU"
FT HELIX 796..812
FT /evidence="ECO:0007829|PDB:5OWU"
FT STRAND 816..818
FT /evidence="ECO:0007829|PDB:2BKU"
FT HELIX 819..821
FT /evidence="ECO:0007829|PDB:5OWU"
FT HELIX 825..836
FT /evidence="ECO:0007829|PDB:5OWU"
FT STRAND 837..840
FT /evidence="ECO:0007829|PDB:3EA5"
FT HELIX 842..860
FT /evidence="ECO:0007829|PDB:5OWU"
SQ SEQUENCE 861 AA; 94776 MW; ED530F5313E75B06 CRC64;
MSTAEFAQLL ENSILSPDQN IRLTSETQLK KLSNDNFLQF AGLSSQVLID ENTKLEGRIL
AALTLKNELV SKDSVKTQQF AQRWITQVSP EAKNQIKTNA LTALVSIEPR IANAAAQLIA
AIADIELPHG AWPELMKIMV DNTGAEQPEN VKRASLLALG YMCESADPQS QALVSSSNNI
LIAIVQGAQS TETSKAVRLA ALNALADSLI FIKNNMEREG ERNYLMQVVC EATQAEDIEV
QAAAFGCLCK IMSLYYTFMK PYMEQALYAL TIATMKSPND KVASMTVEFW STICEEEIDI
AYELAQFPQS PLQSYNFALS SIKDVVPNLL NLLTRQNEDP EDDDWNVSMS AGACLQLFAQ
NCGNHILEPV LEFVEQNITA DNWRNREAAV MAFGSIMDGP DKVQRTYYVH QALPSILNLM
NDQSLQVKET TAWCIGRIAD SVAESIDPQQ HLPGVVQACL IGLQDHPKVA TNCSWTIINL
VEQLAEATPS PIYNFYPALV DGLIGAANRI DNEFNARASA FSALTTMVEY ATDTVAETSA
SISTFVMDKL GQTMSVDENQ LTLEDAQSLQ ELQSNILTVL AAVIRKSPSS VEPVADMLMG
LFFRLLEKKD SAFIEDDVFY AISALAASLG KGFEKYLETF SPYLLKALNQ VDSPVSITAV
GFIADISNSL EEDFRRYSDA MMNVLAQMIS NPNARRELKP AVLSVFGDIA SNIGADFIPY
LNDIMALCVA AQNTKPENGT LEALDYQIKV LEAVLDAYVG IVAGLHDKPE ALFPYVGTIF
QFIAQVAEDP QLYSEDATSR AAVGLIGDIA AMFPDGSIKQ FYGQDWVIDY IKRTRSGQLF
SQATKDTARW AREQQKRQLS L
