IMB1_MOUSE
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 03-AUG-2022, entry version 190.
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, Pancreas,
RC 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}.
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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; 36.
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 iPTMnet; P70168; -.
DR PhosphoSitePlus; P70168; -.
DR SwissPalm; P70168; -.
DR EPD; P70168; -.
DR jPOST; P70168; -.
DR MaxQB; P70168; -.
DR PaxDb; P70168; -.
DR PeptideAtlas; P70168; -.
DR PRIDE; P70168; -.
DR ProteomicsDB; 267130; -.
DR Antibodypedia; 17751; 300 antibodies from 41 providers.
DR DNASU; 16211; -.
DR Ensembl; ENSMUST00000001479; ENSMUSP00000001479; ENSMUSG00000001440.
DR GeneID; 16211; -.
DR KEGG; mmu:16211; -.
DR UCSC; uc007ldu.1; mouse.
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; GRICDII; -.
DR OrthoDB; 769199at2759; -.
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 72 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 270 other tissues.
DR Genevisible; P70168; MM.
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 plate congression; ISO:MGI.
DR GO; GO:0090307; P:mitotic spindle assembly; 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; -; 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; PTHR10527; 1.
DR Pfam; PF03810; IBN_N; 1.
DR SMART; SM00185; ARM; 3.
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; 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
