ID IMB1_MOUSE Reviewed; 876 AA. AC P70168; Q62117; Q6GTI5; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 27-JUL-2011, sequence version 2. DT 24-JAN-2024, entry version 198. DE RecName: Full=Importin subunit beta-1; DE AltName: Full=Karyopherin subunit beta-1; DE AltName: Full=Nuclear factor p97; DE AltName: Full=Pore targeting complex 97 kDa subunit; DE Short=PTAC97; DE AltName: Full=SCG; GN Name=Kpnb1; Synonyms=Impnb; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Lung; RX PubMed=8812441; DOI=10.1006/geno.1996.0450; RA Matsuda Y., Hamatani K., Itoh M., Takahashi E., Araki R., Abe M.; RT "Localization of the importin-beta gene to mouse chromosome 11D and rat RT chromosome 10q32.1."; RL Genomics 36:213-215(1996). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 74-92; 212-221; 377-389 RP AND 860-867. RC STRAIN=C57BL/6J; TISSUE=Thymus; RX PubMed=7635189; DOI=10.1016/0014-5793(95)00699-a; RA Imamoto N., Shimamoto T., Kose S., Takao T., Tachibana T., Matsubae M., RA Sekimoto T., Shimonishi Y., Yoneda Y.; RT "The nuclear pore-targeting complex binds to nuclear pores after RT association with a karyophile."; RL FEBS Lett. 368:415-419(1995). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S., RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., RA Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of the RT mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Brain, and Limb; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [6] RP FUNCTION, AND INTERACTION WITH HISTONES H2B; H2A; H3 AND H4. RX PubMed=11493596; DOI=10.1093/embo-reports/kve168; RA Muehlhaeusser P., Mueller E.-C., Otto A., Kutay U.; RT "Multiple pathways contribute to nuclear import of core histones."; RL EMBO Rep. 2:690-696(2001). RN [7] RP INTERACTION WITH SRY. RX PubMed=11535586; DOI=10.1074/jbc.m101668200; RA Forwood J.K., Harley V., Jans D.A.; RT "The C-terminal nuclear localization signal of the sex-determining region Y RT (SRY) high mobility group domain mediates nuclear import through importin RT beta 1."; RL J. Biol. Chem. 276:46575-46582(2001). RN [8] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain; RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200; RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.; RT "Comprehensive identification of phosphorylation sites in postsynaptic RT density preparations."; RL Mol. Cell. Proteomics 5:914-922(2006). RN [9] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, RC Pancreas, Spleen, and Testis; RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001; RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.; RT "A tissue-specific atlas of mouse protein phosphorylation and expression."; RL Cell 143:1174-1189(2010). RN [10] RP INTERACTION WITH KPNA7. RC STRAIN=C57BL/6J; TISSUE=Ovary; RX PubMed=20699224; DOI=10.1074/jbc.m110.117044; RA Hu J., Wang F., Yuan Y., Zhu X., Wang Y., Zhang Y., Kou Z., Wang S., RA Gao S.; RT "Novel importin-alpha family member Kpna7 is required for normal fertility RT and fecundity in the mouse."; RL J. Biol. Chem. 285:33113-33122(2010). RN [11] RP INTERACTION WITH RAN. RX PubMed=25946333; DOI=10.1371/journal.pone.0127271; RA Shibano T., Mamada H., Hakuno F., Takahashi S., Taira M.; RT "The inner nuclear membrane protein Nemp1 is a new type of RanGTP-binding RT protein in eukaryotes."; RL PLoS ONE 10:E0127271-E0127271(2015). RN [12] RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 1-449, AND REPEAT STRUCTURE. RX PubMed=10964573; DOI=10.1006/jmbi.2000.4055; RA Lee S.J., Imamoto N., Sakai H., Nakagawa A., Kose S., Koike M., RA Yamamoto M., Kumasaka T., Yoneda Y., Tsukihara T.; RT "The adoption of a twisted structure of importin-beta is essential for the RT protein-protein interaction required for nuclear transport."; RL J. Mol. Biol. 302:251-264(2000). RN [13] RP X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS), AND REPEAT STRUCTURE. RX PubMed=14645851; DOI=10.1126/science.1088372; RA Lee S.J., Sekimoto T., Yamashita E., Nagoshi E., Nakagawa A., Imamoto N., RA Yoshimura M., Sakai H., Chong K.T., Tsukihara T., Yoneda Y.; RT "The structure of importin-beta bound to SREBP-2: nuclear import of a RT transcription factor."; RL Science 302:1571-1575(2003). CC -!- FUNCTION: Functions in nuclear protein import, either in association CC with an adapter protein, like an importin-alpha subunit, which binds to CC nuclear localization signals (NLS) in cargo substrates, or by acting as CC autonomous nuclear transport receptor. Acting autonomously, serves CC itself as NLS receptor. Docking of the importin/substrate complex to CC the nuclear pore complex (NPC) is mediated by KPNB1 through binding to CC nucleoporin FxFG repeats and the complex is subsequently translocated CC through the pore by an energy requiring, Ran-dependent mechanism. At CC the nucleoplasmic side of the NPC, Ran binds to importin-beta and the CC three components separate and importin-alpha and -beta are re-exported CC from the nucleus to the cytoplasm where GTP hydrolysis releases Ran CC from importin. The directionality of nuclear import is thought to be CC conferred by an asymmetric distribution of the GTP- and GDP-bound forms CC of Ran between the cytoplasm and nucleus. Mediates autonomously the CC nuclear import of ribosomal proteins RPL23A, RPS7 and RPL5. In CC association with IPO7, mediates the nuclear import of H1 histone. In CC vitro, mediates nuclear import of H2A, H2B, H3 and H4 histones. Imports CC SNAI1 and PRKCI into the nucleus (By similarity). CC {ECO:0000250|UniProtKB:Q14974, ECO:0000269|PubMed:11493596}. CC -!- SUBUNIT: Forms a complex with an importin alpha subunit (By CC similarity). Interacts with XPO1 (By similarity). Forms a heterodimer CC with IPO7 (By similarity). The KPNB1/IPO7 heterodimer interacts with H1 CC histone (By similarity). Interacts with SNUPN (By similarity). CC Interacts with H2A, H2B, H3 and H4 histones (PubMed:11493596). CC Component of an import snRNP complex composed of KPNB1, SNUPN, SMN1 and CC ZNF259 (By similarity). Component of a nuclear export receptor complex CC composed of KPNB1, Ran, SNUPN and XPO1 (By similarity). Interacts with CC SRY (PubMed:11535586). Interacts with PRKCI/atypical protein kinase C CC iota (By similarity). Interacts with KPNA2 (By similarity). Interacts CC with KPNA7 (PubMed:20699224). Interacts with SNAI1 (via zinc fingers) CC and SNAI2 (via zinc fingers) (By similarity). Interacts with SLC35G1 CC and STIM1 (By similarity). Interacts with DCAF8 (By similarity). CC Interacts with RAN (PubMed:25946333). Interacts with NUMA1 (via C- CC terminus); this interaction is inhibited by RanGTP (By similarity). CC Interacts with ZBED1/hDREF; required for nuclear import of ZBED1/hDREF CC (By similarity). Interacts with SRP19 (By similarity). Interacts with CC RPL23A (via BIB domain), RPS7 and RPL5 (By similarity). Interacts with CC PARP16 (By similarity). {ECO:0000250|UniProtKB:Q14974, CC ECO:0000269|PubMed:11493596, ECO:0000269|PubMed:11535586, CC ECO:0000269|PubMed:20699224, ECO:0000269|PubMed:25946333}. CC -!- INTERACTION: CC P70168; P49790: NUP153; Xeno; NbExp=2; IntAct=EBI-540580, EBI-286779; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus envelope CC {ECO:0000250}. CC -!- PTM: Mono-ADP-ribosylated by PARP16. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the importin beta family. Importin beta-1 CC subfamily. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; D67015; BAA11034.1; -; mRNA. DR EMBL; D45836; BAA08273.1; -; mRNA. DR EMBL; AL627445; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH466556; EDL16074.1; -; Genomic_DNA. DR EMBL; BC052438; AAH52438.1; -; mRNA. DR EMBL; BC055115; AAH55115.1; -; mRNA. DR CCDS; CCDS25316.1; -. DR PIR; S66288; S66288. DR RefSeq; NP_032405.3; NM_008379.3. DR PDB; 1GCJ; X-ray; 2.60 A; A/B=1-449. DR PDB; 1UKL; X-ray; 3.00 A; A/B=1-876. DR PDBsum; 1GCJ; -. DR PDBsum; 1UKL; -. DR AlphaFoldDB; P70168; -. DR SMR; P70168; -. DR BioGRID; 200654; 38. DR ComplexPortal; CPX-1054; Importin complex, KPNA2 variant. DR ComplexPortal; CPX-1056; Importin complex, KPNA1 variant. DR ComplexPortal; CPX-1058; Importin complex, KPNA3 variant. DR ComplexPortal; CPX-1061; Importin complex, KPNA4 variant. DR ComplexPortal; CPX-1065; Importin complex, KPNA6 variant. DR ComplexPortal; CPX-1067; Importin complex, KPNA7 variant. DR ComplexPortal; CPX-1111; Importin complex, Snurportin variant. DR CORUM; P70168; -. DR DIP; DIP-33404N; -. DR IntAct; P70168; 26. DR MINT; P70168; -. DR STRING; 10090.ENSMUSP00000001479; -. DR GlyGen; P70168; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P70168; -. DR MetOSite; P70168; -. DR PhosphoSitePlus; P70168; -. DR SwissPalm; P70168; -. DR EPD; P70168; -. DR jPOST; P70168; -. DR MaxQB; P70168; -. DR PaxDb; 10090-ENSMUSP00000001479; -. DR PeptideAtlas; P70168; -. DR ProteomicsDB; 267130; -. DR Pumba; P70168; -. DR Antibodypedia; 17751; 354 antibodies from 41 providers. DR DNASU; 16211; -. DR Ensembl; ENSMUST00000001479.5; ENSMUSP00000001479.4; ENSMUSG00000001440.6. DR GeneID; 16211; -. DR KEGG; mmu:16211; -. DR UCSC; uc007ldu.1; mouse. DR AGR; MGI:107532; -. DR CTD; 3837; -. DR MGI; MGI:107532; Kpnb1. DR VEuPathDB; HostDB:ENSMUSG00000001440; -. DR eggNOG; KOG1241; Eukaryota. DR GeneTree; ENSGT00550000074898; -. DR HOGENOM; CLU_008296_1_0_1; -. DR InParanoid; P70168; -. DR OMA; QQYQERW; -. DR OrthoDB; 124901at2759; -. DR PhylomeDB; P70168; -. DR TreeFam; TF105655; -. DR Reactome; R-MMU-140342; Apoptosis induced DNA fragmentation. DR Reactome; R-MMU-1655829; Regulation of cholesterol biosynthesis by SREBP (SREBF). DR Reactome; R-MMU-2995383; Initiation of Nuclear Envelope (NE) Reformation. DR Reactome; R-MMU-6798695; Neutrophil degranulation. DR Reactome; R-MMU-68616; Assembly of the ORC complex at the origin of replication. DR Reactome; R-MMU-909733; Interferon alpha/beta signaling. DR BioGRID-ORCS; 16211; 28 hits in 76 CRISPR screens. DR ChiTaRS; Kpnb1; mouse. DR EvolutionaryTrace; P70168; -. DR PRO; PR:P70168; -. DR Proteomes; UP000000589; Chromosome 11. DR RNAct; P70168; Protein. DR Bgee; ENSMUSG00000001440; Expressed in optic fissure and 274 other cell types or tissues. DR GO; GO:0005737; C:cytoplasm; ISO:MGI. DR GO; GO:0010494; C:cytoplasmic stress granule; IDA:ARUK-UCL. DR GO; GO:0005829; C:cytosol; ISO:MGI. DR GO; GO:0071782; C:endoplasmic reticulum tubular network; ISO:MGI. DR GO; GO:0042564; C:NLS-dependent protein nuclear import complex; ISO:MGI. DR GO; GO:0005635; C:nuclear envelope; ISO:MGI. DR GO; GO:0031965; C:nuclear membrane; ISO:MGI. DR GO; GO:0005643; C:nuclear pore; ISO:MGI. DR GO; GO:0005654; C:nucleoplasm; ISO:MGI. DR GO; GO:0005634; C:nucleus; IBA:GO_Central. DR GO; GO:0032991; C:protein-containing complex; IDA:MGI. DR GO; GO:0019899; F:enzyme binding; ISO:MGI. DR GO; GO:0051879; F:Hsp90 protein binding; IDA:MGI. DR GO; GO:0061676; F:importin-alpha family protein binding; IPI:MGI. DR GO; GO:0019894; F:kinesin binding; ISO:MGI. DR GO; GO:0061608; F:nuclear import signal receptor activity; IDA:MGI. DR GO; GO:0008139; F:nuclear localization sequence binding; IBA:GO_Central. DR GO; GO:0019904; F:protein domain specific binding; ISO:MGI. DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI. DR GO; GO:0031267; F:small GTPase binding; IEA:InterPro. DR GO; GO:0030953; P:astral microtubule organization; ISO:MGI. DR GO; GO:0040001; P:establishment of mitotic spindle localization; ISO:MGI. DR GO; GO:0045184; P:establishment of protein localization; ISO:MGI. DR GO; GO:0007079; P:mitotic chromosome movement towards spindle pole; ISO:MGI. DR GO; GO:0007080; P:mitotic metaphase chromosome alignment; ISO:MGI. DR GO; GO:0090307; P:mitotic spindle assembly; ISO:MGI. DR GO; GO:0006607; P:NLS-bearing protein import into nucleus; ISO:MGI. DR GO; GO:0006606; P:protein import into nucleus; IDA:MGI. DR GO; GO:0031291; P:Ran protein signal transduction; ISO:MGI. DR GO; GO:0006610; P:ribosomal protein import into nucleus; IDA:MGI. DR GO; GO:0006404; P:RNA import into nucleus; ISO:MGI. DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1. DR IDEAL; IID50146; -. 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; IMPORTIN BETA; 1. DR PANTHER; PTHR10527:SF1; IMPORTIN SUBUNIT BETA-1; 1. DR Pfam; PF13513; HEAT_EZ; 1. DR Pfam; PF03810; IBN_N; 1. DR SMART; SM00185; ARM; 3. DR SMART; SM00913; IBN_N; 1. DR SUPFAM; SSF48371; ARM repeat; 1. DR PROSITE; PS50077; HEAT_REPEAT; 1. DR PROSITE; PS50166; IMPORTIN_B_NT; 1. DR Genevisible; P70168; MM. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; ADP-ribosylation; Cytoplasm; KW Direct protein sequencing; Nucleus; Phosphoprotein; Protein transport; KW Reference proteome; Repeat; Transport. FT CHAIN 1..876 FT /note="Importin subunit beta-1" FT /id="PRO_0000120746" FT REPEAT 3..29 FT /note="HEAT 1" FT /evidence="ECO:0000269|PubMed:10964573" FT DOMAIN 21..101 FT /note="Importin N-terminal" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00115" FT REPEAT 32..62 FT /note="HEAT 2" FT /evidence="ECO:0000269|PubMed:10964573" FT REPEAT 85..120 FT /note="HEAT 3" FT /evidence="ECO:0000269|PubMed:10964573" FT REPEAT 129..160 FT /note="HEAT 4" FT /evidence="ECO:0000269|PubMed:10964573" FT REPEAT 170..201 FT /note="HEAT 5" FT /evidence="ECO:0000269|PubMed:10964573" FT REPEAT 212..247 FT /note="HEAT 6" FT /evidence="ECO:0000269|PubMed:10964573" FT REPEAT 260..302 FT /note="HEAT 7" FT /evidence="ECO:0000269|PubMed:10964573" FT REPEAT 314..359 FT /note="HEAT 8" FT /evidence="ECO:0000269|PubMed:10964573" FT REPEAT 363..392 FT /note="HEAT 9" FT /evidence="ECO:0000269|PubMed:10964573" FT REPEAT 399..438 FT /note="HEAT 10" FT /evidence="ECO:0000269|PubMed:10964573" FT REPEAT 449..485 FT /note="HEAT 11" FT /evidence="ECO:0000269|PubMed:14645851" FT REPEAT 500..537 FT /note="HEAT 12" FT /evidence="ECO:0000269|PubMed:14645851" FT REPEAT 544..592 FT /note="HEAT 13" FT /evidence="ECO:0000269|PubMed:14645851" FT REPEAT 597..639 FT /note="HEAT 14" FT /evidence="ECO:0000269|PubMed:14645851" FT REPEAT 644..680 FT /note="HEAT 15" FT /evidence="ECO:0000269|PubMed:14645851" FT REPEAT 686..724 FT /note="HEAT 16" FT /evidence="ECO:0000269|PubMed:14645851" FT REPEAT 729..777 FT /note="HEAT 17" FT /evidence="ECO:0000269|PubMed:14645851" FT REPEAT 785..828 FT /note="HEAT 18" FT /evidence="ECO:0000269|PubMed:14645851" FT REPEAT 834..875 FT /note="HEAT 19" FT /evidence="ECO:0000269|PubMed:14645851" FT REGION 286..462 FT /note="Essential for high affinity interaction with RPL23A" FT /evidence="ECO:0000250|UniProtKB:Q14974" FT REGION 329..342 FT /note="IAB-binding" FT REGION 334..419 FT /note="Ran-GTP binding" FT /evidence="ECO:0000250" FT MOD_RES 1 FT /note="N-acetylmethionine" FT /evidence="ECO:0000250|UniProtKB:Q14974" FT MOD_RES 12 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q14974" FT MOD_RES 211 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q14974" FT MOD_RES 835 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q14974" FT MOD_RES 867 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q14974" FT CONFLICT 388 FT /note="M -> V (in Ref. 1; BAA11034)" FT /evidence="ECO:0000305" FT HELIX 1..7 FT /evidence="ECO:0007829|PDB:1GCJ" FT TURN 8..11 FT /evidence="ECO:0007829|PDB:1GCJ" FT HELIX 15..45 FT /evidence="ECO:0007829|PDB:1GCJ" FT STRAND 47..49 FT /evidence="ECO:0007829|PDB:1UKL" FT HELIX 51..62 FT /evidence="ECO:0007829|PDB:1GCJ" FT TURN 63..65 FT /evidence="ECO:0007829|PDB:1GCJ" FT HELIX 70..82 FT /evidence="ECO:0007829|PDB:1GCJ" FT HELIX 85..98 FT /evidence="ECO:0007829|PDB:1GCJ" FT STRAND 104..106 FT /evidence="ECO:0007829|PDB:1GCJ" FT HELIX 108..120 FT /evidence="ECO:0007829|PDB:1GCJ" FT HELIX 121..123 FT /evidence="ECO:0007829|PDB:1GCJ" FT HELIX 129..138 FT /evidence="ECO:0007829|PDB:1GCJ" FT HELIX 144..160 FT /evidence="ECO:0007829|PDB:1GCJ" FT HELIX 163..166 FT /evidence="ECO:0007829|PDB:1GCJ" FT HELIX 167..169 FT /evidence="ECO:0007829|PDB:1GCJ" FT HELIX 170..181 FT /evidence="ECO:0007829|PDB:1GCJ" FT HELIX 188..201 FT /evidence="ECO:0007829|PDB:1GCJ" FT TURN 202..204 FT /evidence="ECO:0007829|PDB:1GCJ" FT HELIX 206..209 FT /evidence="ECO:0007829|PDB:1GCJ" FT HELIX 212..225 FT /evidence="ECO:0007829|PDB:1GCJ" FT HELIX 231..247 FT /evidence="ECO:0007829|PDB:1GCJ" FT HELIX 249..254 FT /evidence="ECO:0007829|PDB:1GCJ" FT TURN 255..259 FT /evidence="ECO:0007829|PDB:1GCJ" FT HELIX 260..268 FT /evidence="ECO:0007829|PDB:1GCJ" FT HELIX 273..302 FT /evidence="ECO:0007829|PDB:1GCJ" FT HELIX 314..329 FT /evidence="ECO:0007829|PDB:1GCJ" FT HELIX 330..332 FT /evidence="ECO:0007829|PDB:1GCJ" FT STRAND 338..340 FT /evidence="ECO:0007829|PDB:1GCJ" FT HELIX 344..359 FT /evidence="ECO:0007829|PDB:1GCJ" FT HELIX 360..362 FT /evidence="ECO:0007829|PDB:1GCJ" FT HELIX 363..374 FT /evidence="ECO:0007829|PDB:1GCJ" FT HELIX 380..392 FT /evidence="ECO:0007829|PDB:1GCJ" FT STRAND 394..397 FT /evidence="ECO:0007829|PDB:1GCJ" FT HELIX 399..416 FT /evidence="ECO:0007829|PDB:1GCJ" FT HELIX 422..438 FT /evidence="ECO:0007829|PDB:1GCJ" FT HELIX 440..444 FT /evidence="ECO:0007829|PDB:1GCJ" FT STRAND 447..449 FT /evidence="ECO:0007829|PDB:1GCJ" FT HELIX 464..485 FT /evidence="ECO:0007829|PDB:1UKL" FT HELIX 486..488 FT /evidence="ECO:0007829|PDB:1UKL" FT STRAND 491..495 FT /evidence="ECO:0007829|PDB:1UKL" FT HELIX 500..514 FT /evidence="ECO:0007829|PDB:1UKL" FT TURN 517..520 FT /evidence="ECO:0007829|PDB:1UKL" FT HELIX 521..523 FT /evidence="ECO:0007829|PDB:1UKL" FT HELIX 524..537 FT /evidence="ECO:0007829|PDB:1UKL" FT HELIX 544..563 FT /evidence="ECO:0007829|PDB:1UKL" FT HELIX 564..567 FT /evidence="ECO:0007829|PDB:1UKL" FT HELIX 571..592 FT /evidence="ECO:0007829|PDB:1UKL" FT HELIX 597..616 FT /evidence="ECO:0007829|PDB:1UKL" FT HELIX 625..639 FT /evidence="ECO:0007829|PDB:1UKL" FT TURN 640..643 FT /evidence="ECO:0007829|PDB:1UKL" FT HELIX 644..648 FT /evidence="ECO:0007829|PDB:1UKL" FT HELIX 651..659 FT /evidence="ECO:0007829|PDB:1UKL" FT HELIX 661..663 FT /evidence="ECO:0007829|PDB:1UKL" FT HELIX 664..680 FT /evidence="ECO:0007829|PDB:1UKL" FT HELIX 682..685 FT /evidence="ECO:0007829|PDB:1UKL" FT HELIX 686..701 FT /evidence="ECO:0007829|PDB:1UKL" FT STRAND 703..705 FT /evidence="ECO:0007829|PDB:1UKL" FT HELIX 709..724 FT /evidence="ECO:0007829|PDB:1UKL" FT HELIX 725..728 FT /evidence="ECO:0007829|PDB:1UKL" FT HELIX 729..743 FT /evidence="ECO:0007829|PDB:1UKL" FT HELIX 753..777 FT /evidence="ECO:0007829|PDB:1UKL" FT STRAND 779..782 FT /evidence="ECO:0007829|PDB:1UKL" FT HELIX 785..790 FT /evidence="ECO:0007829|PDB:1UKL" FT HELIX 793..806 FT /evidence="ECO:0007829|PDB:1UKL" FT HELIX 812..828 FT /evidence="ECO:0007829|PDB:1UKL" FT HELIX 834..838 FT /evidence="ECO:0007829|PDB:1UKL" FT HELIX 841..849 FT /evidence="ECO:0007829|PDB:1UKL" FT HELIX 856..871 FT /evidence="ECO:0007829|PDB:1UKL" FT HELIX 872..875 FT /evidence="ECO:0007829|PDB:1UKL" SQ SEQUENCE 876 AA; 97184 MW; 00D6B15023A30598 CRC64; MELITILEKT VSPDRLELEA AQKFLERAAV ENLPTFLVEL SRVLANPGNS QVARVAAGLQ IKNSLTSKDP DIKAQYQQRW LAIDANARRE VKNYVLQTLG TETYRPSSAS QCVAGIACAE IPVSQWPELI PQLVANVTNP NSTEHMKEST LEAIGYICQD IDPEQLQDKS NEILTAIIQG MRKEEPSNNV KLAATNALLN SLEFTKANFD KESERHFIMQ VVCEATQCPD TRVRVAALQN LVKIMSLYYQ YMETYMGPAL FAITIEAMKS DIDEVALQGI EFWSNVCDEE MDLAIEASEA AEQGRPPEHT SKFYAKGALQ YLVPILTQTL TKQDENDDDD DWNPCKAAGV CLMLLSTCCE DDIVPHVLPF IKEHIKNPDW RYRDAAVMAF GSILEGPEPN QLKPLVIQAM PTLIELMKDP SVVVRDTTAW TVGRICELLP EAAINDVYLA PLLQCLIEGL SAEPRVASNV CWAFSSLAEA AYEAADVADD QEEPATYCLS SSFELIVQKL LETTDRPDGH QNNLRSSAYE SLMEIVKNSA KDCYPAVQKT TLVIMERLQQ VLQMESHIQS TSDRIQFNDL QSLLCATLQN VLRKVQHQDA LQISDVVMAS LLRMFQSTAG SGGVQEDALM AVSTLVEVLG GEFLKYMEAF KPFLGIGLKN YAEYQVCLAA VGLVGDLCRA LQSNILPFCD EVMQLLLENL GNENVHRSVK PQILSVFGDI ALAIGGEFKK YLEVVLNTLQ QASQAQVDKS DFDMVDYLNE LRESCLEAYT GIVQGLKGDQ ENVHPDVMLV QPRVEFILSF IDHIAGDEDH TDGVVACAAG LIGDLCTAFG KDVLKLVEAR PMIHELLTEG RRSKTNKAKT LATWATKELR KLKNQA //