IMB3_YEAST
ID IMB3_YEAST Reviewed; 1089 AA.
AC P32337; D6W0D5;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 184.
DE RecName: Full=Importin subunit beta-3 {ECO:0000305};
DE AltName: Full=Karyopherin subunit beta-3 {ECO:0000305};
DE AltName: Full=Karyopherin-121 {ECO:0000303|PubMed:9182759};
DE AltName: Full=Protein secretion enhancer 1 {ECO:0000303|PubMed:1522152};
GN Name=PSE1 {ECO:0000303|PubMed:1522152};
GN Synonyms=KAP121 {ECO:0000303|PubMed:9182759};
GN OrderedLocusNames=YMR308C {ECO:0000312|SGD:S000004925};
GN ORFNames=YM9952.10C;
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 [GENOMIC DNA], AND FUNCTION.
RX PubMed=1522152; DOI=10.1242/jcs.101.3.709;
RA Chow T.Y.-K., Ash J.J., Dignard D., Thomas D.Y.;
RT "Screening and identification of a gene, PSE-1, that affects protein
RT secretion in Saccharomyces cerevisiae.";
RL J. Cell Sci. 101:709-719(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169872;
RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL Nature 387:90-93(1997).
RN [3]
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 [4]
RP FUNCTION.
RX PubMed=9182759; DOI=10.1016/s0092-8674(00)80254-8;
RA Rout M.P., Blobel G., Aitchison J.D.;
RT "A distinct nuclear import pathway used by ribosomal proteins.";
RL Cell 89:715-725(1997).
RN [5]
RP FUNCTION, AND INTERACTION WITH GSP1 AND RPL25.
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 [6]
RP SUBCELLULAR LOCATION.
RX PubMed=9238021; DOI=10.1073/pnas.94.16.8590;
RA Seedorf M., Silver P.A.;
RT "Importin/karyopherin protein family members required for mRNA export from
RT the nucleus.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:8590-8595(1997).
RN [7]
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 [8]
RP FUNCTION, AND INTERACTION WITH YAP1.
RX PubMed=11274141; DOI=10.1074/jbc.m009258200;
RA Isoyama T., Murayama A., Nomoto A., Kuge S.;
RT "Nuclear import of the yeast AP-1-like transcription factor Yap1p is
RT mediated by transport receptor Pse1p, and this import step is not affected
RT by oxidative stress.";
RL J. Biol. Chem. 276:21863-21869(2001).
RN [9]
RP FUNCTION, AND INTERACTION WITH HISTONES H3 AND H4.
RX PubMed=11694505; DOI=10.1074/jbc.m106845200;
RA Mosammaparast N., Guo Y., Shabanowitz J., Hunt D.F., Pemberton L.F.;
RT "Pathways mediating the nuclear import of histones H3 and H4 in yeast.";
RL J. Biol. Chem. 277:862-868(2002).
RN [10]
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 [11]
RP FUNCTION, AND INTERACTION WITH NOP1 AND SOF1.
RX PubMed=15367670; DOI=10.1128/mcb.24.19.8487-8503.2004;
RA Leslie D.M., Zhang W., Timney B.L., Chait B.T., Rout M.P., Wozniak R.W.,
RA Aitchison J.D.;
RT "Characterization of karyopherin cargoes reveals unique mechanisms of
RT Kap121p-mediated nuclear import.";
RL Mol. Cell. Biol. 24:8487-8503(2004).
RN [12]
RP INTERACTION WITH ABF1.
RX PubMed=15522095; DOI=10.1111/j.1600-0854.2004.00233.x;
RA Loch C.M., Mosammaparast N., Miyake T., Pemberton L.F., Li R.;
RT "Functional and physical interactions between autonomously replicating
RT sequence-binding factor 1 and the nuclear transport machinery.";
RL Traffic 5:925-935(2004).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-830, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [14]
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 [15]
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 1-1089 IN COMPLEXES WITH STE11;
RP PHO4; NUP53 AND GSP1, AND REPEAT STRUCTURE.
RX PubMed=23541588; DOI=10.1016/j.jmb.2013.02.035;
RA Kobayashi J., Matsuura Y.;
RT "Structural basis for cell-cycle-dependent nuclear import mediated by the
RT karyopherin Kap121p.";
RL J. Mol. Biol. 425:1852-1868(2013).
CC -!- FUNCTION: Functions in nuclear protein import as nuclear transport
CC receptor. Serves as receptor for classical and arginine/glycine-rich
CC nuclear localization signals (cNLS and rg-NLS) in cargo substrates
CC (PubMed:15367670). Its predominant cargo substrate seems to be
CC ribosomal proteins and ribosome biogenesis trans- and cis-acting
CC factors (PubMed:9182759, PubMed:9321403, PubMed:15367670). Required for
CC nuclear transport of YAP1, NOP1 and SOF1 (PubMed:11274141,
CC PubMed:15367670). Mediates the nuclear import of histones H3 and H4
CC (PubMed:11694505). Mediates docking of the importin/substrate complex
CC to the nuclear pore complex (NPC) through binding to repeat-containing
CC nucleoporins. The complex is subsequently translocated through the pore
CC by an energy requiring, Ran-dependent mechanism (PubMed:11423015). At
CC the nucleoplasmic side of the NPC, GTP-Ran binding leads to release of
CC the cargo (PubMed:9321403). The importin is re-exported from the
CC nucleus to the cytoplasm where GTP hydrolysis releases Ran from
CC 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 (PubMed:11423015).
CC {ECO:0000269|PubMed:11274141, ECO:0000269|PubMed:11694505,
CC ECO:0000269|PubMed:15367670, ECO:0000269|PubMed:9182759,
CC ECO:0000269|PubMed:9321403, ECO:0000305|PubMed:11423015}.
CC -!- FUNCTION: Plays a role in protein secretion.
CC {ECO:0000269|PubMed:1522152}.
CC -!- SUBUNIT: Interacts with Ran (GSP1); interacts specifically with the
CC GTP-bound form of Ran (GTP-Ran), protecting it from GTP hydrolysis and
CC nucleotide exchange (PubMed:9321403). Interacts with RPL25; this
CC interaction is dissociated by binding to Ran-GTP (PubMed:9321403).
CC Interacts with YAP1; this interaction is dissociated by binding to Ran-
CC GTP (PubMed:11274141). Interacts with NOP1; via its rg-NLS
CC (PubMed:15367670). Interacts with SOF1; via its cNLS (PubMed:15367670).
CC Interacts with histones H3 and H4; via their NLS (PubMed:11694505).
CC Interacts with ABF1 (PubMed:15522095). {ECO:0000269|PubMed:11274141,
CC ECO:0000269|PubMed:11694505, ECO:0000269|PubMed:15522095,
CC ECO:0000269|PubMed:9321403}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9238021}. Nucleus
CC {ECO:0000269|PubMed:9238021}.
CC -!- MISCELLANEOUS: Present with 15500 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the importin beta family. Importin beta-3
CC subfamily. {ECO:0000305}.
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DR EMBL; Z11538; CAA77639.1; -; Genomic_DNA.
DR EMBL; S45357; AAA10665.1; -; Genomic_DNA.
DR EMBL; Z49212; CAA89141.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA10209.1; -; Genomic_DNA.
DR PIR; S53978; S53978.
DR RefSeq; NP_014039.1; NM_001182819.1.
DR PDB; 3W3T; X-ray; 2.90 A; A=1-1089.
DR PDB; 3W3U; X-ray; 2.60 A; A=1-1089.
DR PDB; 3W3V; X-ray; 3.20 A; A=1-1089.
DR PDB; 3W3W; X-ray; 2.20 A; A=1-1089.
DR PDB; 3W3X; X-ray; 2.90 A; A=1-1089.
DR PDB; 3W3Y; X-ray; 2.80 A; A=1-1089.
DR PDB; 3W3Z; X-ray; 2.70 A; A=1-1089.
DR PDB; 4ZJ7; X-ray; 2.40 A; A=1-1089.
DR PDB; 5H2V; X-ray; 2.80 A; A=1-1089.
DR PDBsum; 3W3T; -.
DR PDBsum; 3W3U; -.
DR PDBsum; 3W3V; -.
DR PDBsum; 3W3W; -.
DR PDBsum; 3W3X; -.
DR PDBsum; 3W3Y; -.
DR PDBsum; 3W3Z; -.
DR PDBsum; 4ZJ7; -.
DR PDBsum; 5H2V; -.
DR AlphaFoldDB; P32337; -.
DR SMR; P32337; -.
DR BioGRID; 35488; 245.
DR DIP; DIP-1533N; -.
DR IntAct; P32337; 76.
DR MINT; P32337; -.
DR STRING; 4932.YMR308C; -.
DR iPTMnet; P32337; -.
DR MaxQB; P32337; -.
DR PaxDb; P32337; -.
DR PRIDE; P32337; -.
DR EnsemblFungi; YMR308C_mRNA; YMR308C; YMR308C.
DR GeneID; 855356; -.
DR KEGG; sce:YMR308C; -.
DR SGD; S000004925; PSE1.
DR VEuPathDB; FungiDB:YMR308C; -.
DR eggNOG; KOG2171; Eukaryota.
DR GeneTree; ENSGT00940000169161; -.
DR HOGENOM; CLU_003794_0_1_1; -.
DR InParanoid; P32337; -.
DR OMA; PKRFVQE; -.
DR BioCyc; YEAST:G3O-32972-MON; -.
DR PRO; PR:P32337; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; P32337; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0061608; F:nuclear import signal receptor activity; IMP:SGD.
DR GO; GO:0008139; F:nuclear localization sequence binding; IDA:SGD.
DR GO; GO:0006406; P:mRNA export from nucleus; IGI:SGD.
DR GO; GO:0006606; P:protein import into nucleus; IMP:SGD.
DR GO; GO:0007088; P:regulation of mitotic nuclear division; IMP:SGD.
DR GO; GO:0060188; P:regulation of protein desumoylation; IMP:SGD.
DR DisProt; DP02144; -.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR040122; Importin_beta.
DR InterPro; IPR041653; Importin_rep_4.
DR InterPro; IPR040928; Importin_rep_5.
DR InterPro; IPR041389; Importin_rep_6.
DR PANTHER; PTHR10527; PTHR10527; 1.
DR Pfam; PF18808; Importin_rep_4; 1.
DR Pfam; PF18816; Importin_rep_5; 1.
DR Pfam; PF18829; Importin_rep_6; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Nucleus; Phosphoprotein;
KW Protein transport; Reference proteome; Repeat; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..1089
FT /note="Importin subunit beta-3"
FT /id="PRO_0000120774"
FT REPEAT 6..39
FT /note="HEAT 1"
FT /evidence="ECO:0000269|PubMed:23541588"
FT REPEAT 44..78
FT /note="HEAT 2"
FT /evidence="ECO:0000269|PubMed:23541588"
FT REPEAT 96..129
FT /note="HEAT 3"
FT /evidence="ECO:0000269|PubMed:23541588"
FT REPEAT 138..165
FT /note="HEAT 4"
FT /evidence="ECO:0000269|PubMed:23541588"
FT REPEAT 175..207
FT /note="HEAT 5"
FT /evidence="ECO:0000269|PubMed:23541588"
FT REPEAT 216..252
FT /note="HEAT 6"
FT /evidence="ECO:0000269|PubMed:23541588"
FT REPEAT 260..295
FT /note="HEAT 7"
FT /evidence="ECO:0000269|PubMed:23541588"
FT REPEAT 304..359
FT /note="HEAT 8"
FT /evidence="ECO:0000269|PubMed:23541588"
FT REPEAT 361..395
FT /note="HEAT 9"
FT /evidence="ECO:0000269|PubMed:23541588"
FT REPEAT 399..439
FT /note="HEAT 10"
FT /evidence="ECO:0000269|PubMed:23541588"
FT REPEAT 441..481
FT /note="HEAT 11"
FT /evidence="ECO:0000269|PubMed:23541588"
FT REPEAT 484..524
FT /note="HEAT 12"
FT /evidence="ECO:0000269|PubMed:23541588"
FT REPEAT 526..568
FT /note="HEAT 13"
FT /evidence="ECO:0000269|PubMed:23541588"
FT REPEAT 571..613
FT /note="HEAT 14"
FT /evidence="ECO:0000269|PubMed:23541588"
FT REPEAT 615..689
FT /note="HEAT 15"
FT /evidence="ECO:0000269|PubMed:23541588"
FT REPEAT 692..735
FT /note="HEAT 16"
FT /evidence="ECO:0000269|PubMed:23541588"
FT REPEAT 742..781
FT /note="HEAT 17"
FT /evidence="ECO:0000269|PubMed:23541588"
FT REPEAT 788..849
FT /note="HEAT 18"
FT /evidence="ECO:0000269|PubMed:23541588"
FT REPEAT 852..890
FT /note="HEAT 19"
FT /evidence="ECO:0000269|PubMed:23541588"
FT REPEAT 898..930
FT /note="HEAT 20"
FT /evidence="ECO:0000269|PubMed:23541588"
FT REPEAT 938..978
FT /note="HEAT 21"
FT /evidence="ECO:0000269|PubMed:23541588"
FT REPEAT 986..1017
FT /note="HEAT 22"
FT /evidence="ECO:0000269|PubMed:23541588"
FT REPEAT 1028..1063
FT /note="HEAT 23"
FT /evidence="ECO:0000269|PubMed:23541588"
FT REPEAT 1066..1089
FT /note="HEAT 24"
FT /evidence="ECO:0000269|PubMed:23541588"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 830
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT CONFLICT 65
FT /note="A -> S (in Ref. 1; CAA77639/AAA10665)"
FT /evidence="ECO:0000305"
FT CONFLICT 1077
FT /note="P -> A (in Ref. 1; CAA77639/AAA10665)"
FT /evidence="ECO:0000305"
FT HELIX 6..18
FT /evidence="ECO:0007829|PDB:3W3W"
FT HELIX 25..37
FT /evidence="ECO:0007829|PDB:3W3W"
FT STRAND 38..40
FT /evidence="ECO:0007829|PDB:4ZJ7"
FT TURN 41..43
FT /evidence="ECO:0007829|PDB:3W3W"
FT HELIX 44..57
FT /evidence="ECO:0007829|PDB:3W3W"
FT HELIX 61..77
FT /evidence="ECO:0007829|PDB:3W3W"
FT HELIX 91..93
FT /evidence="ECO:0007829|PDB:3W3W"
FT HELIX 96..111
FT /evidence="ECO:0007829|PDB:3W3W"
FT HELIX 116..127
FT /evidence="ECO:0007829|PDB:3W3W"
FT STRAND 132..134
FT /evidence="ECO:0007829|PDB:5H2V"
FT HELIX 138..149
FT /evidence="ECO:0007829|PDB:3W3W"
FT HELIX 153..165
FT /evidence="ECO:0007829|PDB:3W3W"
FT HELIX 168..172
FT /evidence="ECO:0007829|PDB:3W3W"
FT HELIX 175..185
FT /evidence="ECO:0007829|PDB:3W3W"
FT HELIX 191..207
FT /evidence="ECO:0007829|PDB:3W3W"
FT HELIX 210..215
FT /evidence="ECO:0007829|PDB:3W3W"
FT HELIX 217..219
FT /evidence="ECO:0007829|PDB:3W3W"
FT HELIX 220..226
FT /evidence="ECO:0007829|PDB:3W3W"
FT HELIX 228..232
FT /evidence="ECO:0007829|PDB:3W3W"
FT HELIX 236..252
FT /evidence="ECO:0007829|PDB:3W3W"
FT HELIX 254..260
FT /evidence="ECO:0007829|PDB:3W3W"
FT HELIX 261..273
FT /evidence="ECO:0007829|PDB:3W3W"
FT HELIX 279..295
FT /evidence="ECO:0007829|PDB:3W3W"
FT HELIX 297..301
FT /evidence="ECO:0007829|PDB:3W3W"
FT HELIX 304..318
FT /evidence="ECO:0007829|PDB:3W3W"
FT HELIX 329..332
FT /evidence="ECO:0007829|PDB:3W3W"
FT HELIX 343..359
FT /evidence="ECO:0007829|PDB:3W3W"
FT HELIX 361..376
FT /evidence="ECO:0007829|PDB:3W3W"
FT HELIX 381..394
FT /evidence="ECO:0007829|PDB:3W3W"
FT TURN 395..398
FT /evidence="ECO:0007829|PDB:3W3W"
FT HELIX 399..402
FT /evidence="ECO:0007829|PDB:3W3W"
FT HELIX 406..413
FT /evidence="ECO:0007829|PDB:3W3W"
FT HELIX 414..418
FT /evidence="ECO:0007829|PDB:3W3W"
FT HELIX 422..438
FT /evidence="ECO:0007829|PDB:3W3W"
FT TURN 439..441
FT /evidence="ECO:0007829|PDB:3W3W"
FT HELIX 442..458
FT /evidence="ECO:0007829|PDB:3W3W"
FT HELIX 465..480
FT /evidence="ECO:0007829|PDB:3W3W"
FT HELIX 484..487
FT /evidence="ECO:0007829|PDB:3W3W"
FT HELIX 488..490
FT /evidence="ECO:0007829|PDB:3W3W"
FT HELIX 491..502
FT /evidence="ECO:0007829|PDB:3W3W"
FT HELIX 507..524
FT /evidence="ECO:0007829|PDB:3W3W"
FT HELIX 525..531
FT /evidence="ECO:0007829|PDB:3W3W"
FT HELIX 532..544
FT /evidence="ECO:0007829|PDB:3W3W"
FT HELIX 551..568
FT /evidence="ECO:0007829|PDB:3W3W"
FT HELIX 570..573
FT /evidence="ECO:0007829|PDB:3W3W"
FT TURN 574..576
FT /evidence="ECO:0007829|PDB:3W3W"
FT HELIX 577..588
FT /evidence="ECO:0007829|PDB:3W3W"
FT HELIX 597..613
FT /evidence="ECO:0007829|PDB:3W3W"
FT HELIX 614..620
FT /evidence="ECO:0007829|PDB:3W3W"
FT HELIX 621..632
FT /evidence="ECO:0007829|PDB:3W3W"
FT STRAND 638..641
FT /evidence="ECO:0007829|PDB:3W3W"
FT STRAND 646..648
FT /evidence="ECO:0007829|PDB:3W3W"
FT HELIX 649..651
FT /evidence="ECO:0007829|PDB:3W3W"
FT STRAND 655..668
FT /evidence="ECO:0007829|PDB:3W3W"
FT HELIX 669..689
FT /evidence="ECO:0007829|PDB:3W3W"
FT HELIX 690..693
FT /evidence="ECO:0007829|PDB:3W3W"
FT HELIX 694..703
FT /evidence="ECO:0007829|PDB:3W3W"
FT HELIX 705..709
FT /evidence="ECO:0007829|PDB:3W3W"
FT HELIX 715..734
FT /evidence="ECO:0007829|PDB:3W3W"
FT HELIX 742..757
FT /evidence="ECO:0007829|PDB:3W3W"
FT TURN 758..760
FT /evidence="ECO:0007829|PDB:3W3W"
FT HELIX 764..781
FT /evidence="ECO:0007829|PDB:3W3W"
FT HELIX 788..809
FT /evidence="ECO:0007829|PDB:3W3W"
FT HELIX 829..849
FT /evidence="ECO:0007829|PDB:3W3W"
FT TURN 850..853
FT /evidence="ECO:0007829|PDB:3W3W"
FT HELIX 854..857
FT /evidence="ECO:0007829|PDB:3W3W"
FT HELIX 858..860
FT /evidence="ECO:0007829|PDB:3W3W"
FT HELIX 861..868
FT /evidence="ECO:0007829|PDB:3W3W"
FT STRAND 870..872
FT /evidence="ECO:0007829|PDB:5H2V"
FT HELIX 873..887
FT /evidence="ECO:0007829|PDB:3W3W"
FT HELIX 891..893
FT /evidence="ECO:0007829|PDB:3W3U"
FT HELIX 895..909
FT /evidence="ECO:0007829|PDB:3W3W"
FT HELIX 914..930
FT /evidence="ECO:0007829|PDB:3W3W"
FT TURN 933..935
FT /evidence="ECO:0007829|PDB:3W3W"
FT HELIX 936..949
FT /evidence="ECO:0007829|PDB:3W3W"
FT HELIX 958..960
FT /evidence="ECO:0007829|PDB:3W3W"
FT HELIX 961..977
FT /evidence="ECO:0007829|PDB:3W3W"
FT TURN 978..980
FT /evidence="ECO:0007829|PDB:3W3W"
FT HELIX 987..993
FT /evidence="ECO:0007829|PDB:3W3W"
FT HELIX 1002..1013
FT /evidence="ECO:0007829|PDB:3W3W"
FT STRAND 1023..1027
FT /evidence="ECO:0007829|PDB:5H2V"
FT HELIX 1029..1041
FT /evidence="ECO:0007829|PDB:3W3W"
FT HELIX 1053..1062
FT /evidence="ECO:0007829|PDB:3W3W"
FT HELIX 1066..1071
FT /evidence="ECO:0007829|PDB:3W3W"
FT HELIX 1072..1075
FT /evidence="ECO:0007829|PDB:3W3W"
FT HELIX 1078..1085
FT /evidence="ECO:0007829|PDB:3W3W"
SQ SEQUENCE 1089 AA; 121031 MW; 9C5F7FB5B8824C37 CRC64;
MSALPEEVNR TLLQIVQAFA SPDNQIRSVA EKALSEEWIT ENNIEYLLTF LAEQAAFSQD
TTVAALSAVL FRKLALKAPP SSKLMIMSKN ITHIRKEVLA QIRSSLLKGF LSERADSIRH
KLSDAIAECV QDDLPAWPEL LQALIESLKS GNPNFRESSF RILTTVPYLI TAVDINSILP
IFQSGFTDAS DNVKIAAVTA FVGYFKQLPK SEWSKLGILL PSLLNSLPRF LDDGKDDALA
SVFESLIELV ELAPKLFKDM FDQIIQFTDM VIKNKDLEPP ARTTALELLT VFSENAPQMC
KSNQNYGQTL VMVTLIMMTE VSIDDDDAAE WIESDDTDDE EEVTYDHARQ ALDRVALKLG
GEYLAAPLFQ YLQQMITSTE WRERFAAMMA LSSAAEGCAD VLIGEIPKIL DMVIPLINDP
HPRVQYGCCN VLGQISTDFS PFIQRTAHDR ILPALISKLT SECTSRVQTH AAAALVNFSE
FASKDILEPY LDSLLTNLLV LLQSNKLYVQ EQALTTIAFI AEAAKNKFIK YYDTLMPLLL
NVLKVNNKDN SVLKGKCMEC ATLIGFAVGK EKFHEHSQEL ISILVALQNS DIDEDDALRS
YLEQSWSRIC RILGDDFVPL LPIVIPPLLI TAKATQDVGL IEEEEAANFQ QYPDWDVVQV
QGKHIAIHTS VLDDKVSAME LLQSYATLLR GQFAVYVKEV MEEIALPSLD FYLHDGVRAA
GATLIPILLS CLLAATGTQN EELVLLWHKA SSKLIGGLMS EPMPEITQVY HNSLVNGIKV
MGDNCLSEDQ LAAFTKGVSA NLTDTYERMQ DRHGDGDEYN ENIDEEEDFT DEDLLDEINK
SIAAVLKTTN GHYLKNLENI WPMINTFLLD NEPILVIFAL VVIGDLIQYG GEQTASMKNA
FIPKVTECLI SPDARIRQAA SYIIGVCAQY APSTYADVCI PTLDTLVQIV DFPGSKLEEN
RSSTENASAA IAKILYAYNS NIPNVDTYTA NWFKTLPTIT DKEAASFNYQ FLSQLIENNS
PIVCAQSNIS AVVDSVIQAL NERSLTEREG QTVISSVKKL LGFLPSSDAM AIFNRYPADI
MEKVHKWFA
