IMA1_YEAST
ID IMA1_YEAST Reviewed; 542 AA.
AC Q02821; D6W0Z8;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 203.
DE RecName: Full=Importin subunit alpha;
DE AltName: Full=Karyopherin subunit alpha;
DE AltName: Full=Karyopherin-60;
DE AltName: Full=Serine-rich RNA polymerase I suppressor protein;
GN Name=SRP1; Synonyms=KAP60; OrderedLocusNames=YNL189W; ORFNames=N1606;
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].
RX PubMed=1448093; DOI=10.1128/mcb.12.12.5640-5651.1992;
RA Yano R., Oakes M., Yamaghishi M., Dodd J.A., Nomura M.;
RT "Cloning and characterization of SRP1, a suppressor of temperature-
RT sensitive RNA polymerase I mutations, in Saccharomyces cerevisiae.";
RL Mol. Cell. Biol. 12:5640-5651(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 200060 / W303;
RX PubMed=7565597; DOI=10.1007/bf02191602;
RA Kuessel P., Frasch M.;
RT "Yeast Srp1, a nuclear protein related to Drosophila and mouse pendulin, is
RT required for normal migration, division, and integrity of nuclei during
RT mitosis.";
RL Mol. Gen. Genet. 248:351-363(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169873;
RA Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT evolutionary implications.";
RL Nature 387:93-98(1997).
RN [4]
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 [5]
RP MUTAGENESIS.
RX PubMed=8041713; DOI=10.1073/pnas.91.15.6880;
RA Yano R., Oakes M.L., Tabb M.M., Nomura M.;
RT "Yeast Srp1p has homology to armadillo/plakoglobin/beta-catenin and
RT participates in apparently multiple nuclear functions including the
RT maintenance of the nucleolar structure.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:6880-6884(1994).
RN [6]
RP IDENTIFICATION.
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 [7]
RP NUCLEOPORIN REPEAT BINDING REQUIREMENT, AND FUNCTION.
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 [8]
RP FUNCTION, AND INTERACTION WITH STS1.
RX PubMed=10913188; DOI=10.1128/mcb.20.16.6062-6073.2000;
RA Tabb M.M., Tongaonkar P., Vu L., Nomura M.;
RT "Evidence for separable functions of Srp1p, the yeast homolog of importin
RT alpha (Karyopherin alpha): role for Srp1p and Sts1p in protein
RT degradation.";
RL Mol. Cell. Biol. 20:6062-6073(2000).
RN [9]
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 [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 INTERACTION WITH HEH2.
RX PubMed=16929305; DOI=10.1038/nature05075;
RA King M.C., Lusk C.P., Blobel G.;
RT "Karyopherin-mediated import of integral inner nuclear membrane proteins.";
RL Nature 442:1003-1007(2006).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [13]
RP INTERACTION WITH SHE2.
RX PubMed=19244342; DOI=10.1091/mbc.e08-11-1151;
RA Shen Z., Paquin N., Forget A., Chartrand P.;
RT "Nuclear shuttling of She2p couples ASH1 mRNA localization to its
RT translational repression by recruiting Loc1p and Puf6p.";
RL Mol. Biol. Cell 20:2265-2275(2009).
RN [14]
RP FUNCTION, AND INTERACTION WITH STS1.
RX PubMed=21075847; DOI=10.1074/jbc.m110.135863;
RA Chen L., Romero L., Chuang S.M., Tournier V., Joshi K.K., Lee J.A.,
RA Kovvali G., Madura K.;
RT "Sts1 plays a key role in targeting proteasomes to the nucleus.";
RL J. Biol. Chem. 286:3104-3118(2011).
RN [15]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [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 [16]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 89-510.
RX PubMed=9695948; DOI=10.1016/s0092-8674(00)81419-1;
RA Conti E., Uy M., Leighton L., Blobel G., Kuriyan J.;
RT "Crystallographic analysis of the recognition of a nuclear localization
RT signal by the nuclear import factor karyopherin alpha.";
RL Cell 94:193-204(1998).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 87-509 IN COMPLEX WITH NLS
RP PEPTIDE, AND FUNCTION.
RX PubMed=10745017; DOI=10.1016/s0969-2126(00)00107-6;
RA Conti E., Kuriyan J.;
RT "Crystallographic analysis of the specific yet versatile recognition of
RT distinct nuclear localization signals by karyopherin alpha.";
RL Structure 8:329-338(2000).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 88-530 IN COMPLEX WITH NUP2.
RX PubMed=14532109; DOI=10.1093/emboj/cdg538;
RA Matsuura Y., Lange A., Harreman M.T., Corbett A.H., Stewart M.;
RT "Structural basis for Nup2p function in cargo release and karyopherin
RT recycling in nuclear import.";
RL EMBO J. 22:5358-5369(2003).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1-530 IN COMPLEX WITH CSE1 AND
RP RANGTP.
RX PubMed=15602554; DOI=10.1038/nature03144;
RA Matsuura Y., Stewart M.;
RT "Structural basis for the assembly of a nuclear export complex.";
RL Nature 432:872-877(2004).
CC -!- FUNCTION: Functions in nuclear protein import as an adapter protein for
CC importin beta nuclear receptors (PubMed:10913188). Binds specifically
CC and directly to substrates containing either a simple or bipartite NLS
CC motif (PubMed:10745017). Promotes docking of import substrates to the
CC nuclear envelope (PubMed:8521485). Together with importin beta KAP95,
CC mediates nuclear import of transcription factor GCN4 (PubMed:14648200).
CC Together with tethering factor STS1, targets the proteasome to the
CC nucleus (PubMed:10913188, PubMed:21075847).
CC {ECO:0000269|PubMed:10745017, ECO:0000269|PubMed:10913188,
CC ECO:0000269|PubMed:14648200, ECO:0000269|PubMed:21075847,
CC ECO:0000269|PubMed:8521485}.
CC -!- SUBUNIT: Forms a complex with an importin beta subunit. In the nucleus,
CC interacts with NUP2 which accelerate release of NLSs, NUP2 is
CC subsequently displaced by CSE1:RanGTP which mediates re-export and
CC recycling. Interacts with HEH2, SHE2, and STS1.
CC {ECO:0000269|PubMed:10745017, ECO:0000269|PubMed:10913188,
CC ECO:0000269|PubMed:14532109, ECO:0000269|PubMed:15602554,
CC ECO:0000269|PubMed:16929305, ECO:0000269|PubMed:19244342,
CC ECO:0000269|PubMed:21075847}.
CC -!- INTERACTION:
CC Q02821; Q08920: CBC2; NbExp=3; IntAct=EBI-1797, EBI-33556;
CC Q02821; P33307: CSE1; NbExp=2; IntAct=EBI-1797, EBI-5168;
CC Q02821; Q03281: HEH2; NbExp=7; IntAct=EBI-1797, EBI-22131;
CC Q02821; P15108: HSC82; NbExp=2; IntAct=EBI-1797, EBI-8666;
CC Q02821; Q06142: KAP95; NbExp=9; IntAct=EBI-1797, EBI-9145;
CC Q02821; P32499: NUP2; NbExp=4; IntAct=EBI-1797, EBI-12401;
CC Q02821; Q03707: SRC1; NbExp=5; IntAct=EBI-1797, EBI-18064;
CC Q02821; P05221; Xeno; NbExp=2; IntAct=EBI-1797, EBI-7261813;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region. Note=Mainly
CC localized at the periphery of the nucleus.
CC -!- DOMAIN: The NLS binding sites are mainly involved in recognition of
CC simple or bipartite NLS motifs. Structurally located within in a
CC helical surface groove they contain several conserved Trp and Asn
CC residues of the corresponding third helices (H3) of ARM repeats which
CC mainly contribute to binding.
CC -!- MISCELLANEOUS: Binds to nucleoporin FxFG but not GLFG repeat regions.
CC Ran-GTP can disrupt the karyopherin heterodimer by binding to the beta
CC subunit and releases both subunits from the docking site.
CC -!- MISCELLANEOUS: Present with 2790 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the importin alpha family. {ECO:0000305}.
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DR EMBL; M75849; AAA35090.1; -; Genomic_DNA.
DR EMBL; Z71465; CAA96083.1; -; Genomic_DNA.
DR EMBL; BK006947; DAA10364.1; -; Genomic_DNA.
DR PIR; S30884; S30884.
DR RefSeq; NP_014210.1; NM_001183027.1.
DR PDB; 1BK5; X-ray; 2.20 A; A/B=89-510.
DR PDB; 1BK6; X-ray; 2.80 A; A/B=89-510.
DR PDB; 1EE4; X-ray; 2.10 A; A/B=87-509.
DR PDB; 1EE5; X-ray; 2.40 A; A=87-510.
DR PDB; 1UN0; X-ray; 2.60 A; A/B=88-530.
DR PDB; 1WA5; X-ray; 2.00 A; B=1-530.
DR PDB; 2C1T; X-ray; 2.60 A; A/B=88-541.
DR PDB; 4PVZ; X-ray; 2.50 A; A/B=88-509.
DR PDB; 4XZR; X-ray; 2.25 A; B=88-509.
DR PDB; 5H2W; X-ray; 2.50 A; A/C=88-510.
DR PDB; 5H2X; X-ray; 2.20 A; A=88-510.
DR PDB; 5T94; X-ray; 2.63 A; B=1-542.
DR PDBsum; 1BK5; -.
DR PDBsum; 1BK6; -.
DR PDBsum; 1EE4; -.
DR PDBsum; 1EE5; -.
DR PDBsum; 1UN0; -.
DR PDBsum; 1WA5; -.
DR PDBsum; 2C1T; -.
DR PDBsum; 4PVZ; -.
DR PDBsum; 4XZR; -.
DR PDBsum; 5H2W; -.
DR PDBsum; 5H2X; -.
DR PDBsum; 5T94; -.
DR AlphaFoldDB; Q02821; -.
DR SMR; Q02821; -.
DR BioGRID; 35644; 442.
DR ComplexPortal; CPX-1068; Importin complex, KAP60-KAP95.
DR DIP; DIP-728N; -.
DR ELM; Q02821; -.
DR IntAct; Q02821; 142.
DR MINT; Q02821; -.
DR STRING; 4932.YNL189W; -.
DR iPTMnet; Q02821; -.
DR MaxQB; Q02821; -.
DR PaxDb; Q02821; -.
DR PRIDE; Q02821; -.
DR EnsemblFungi; YNL189W_mRNA; YNL189W; YNL189W.
DR GeneID; 855532; -.
DR KEGG; sce:YNL189W; -.
DR SGD; S000005133; SRP1.
DR VEuPathDB; FungiDB:YNL189W; -.
DR eggNOG; KOG0166; Eukaryota.
DR GeneTree; ENSGT01050000244950; -.
DR HOGENOM; CLU_018084_6_0_1; -.
DR InParanoid; Q02821; -.
DR OMA; EMIQMLY; -.
DR BioCyc; YEAST:G3O-33200-MON; -.
DR EvolutionaryTrace; Q02821; -.
DR PRO; PR:Q02821; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; Q02821; 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:0005654; C:nucleoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR GO; GO:0097718; F:disordered domain specific 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:0051170; P:import into nucleus; IC:ComplexPortal.
DR GO; GO:0006607; P:NLS-bearing protein import into nucleus; IMP:SGD.
DR GO; GO:0031144; P:proteasome localization; 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 DisProt; DP02227; -.
DR Gene3D; 1.20.5.690; -; 1.
DR Gene3D; 1.25.10.10; -; 1.
DR IDEAL; IID50012; -.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR032413; Arm_3.
DR InterPro; IPR000225; Armadillo.
DR InterPro; IPR002652; Importin-a_IBB.
DR InterPro; IPR036975; Importin-a_IBB_sf.
DR InterPro; IPR024931; Importin_alpha.
DR Pfam; PF00514; Arm; 8.
DR Pfam; PF16186; Arm_3; 1.
DR Pfam; PF01749; IBB; 1.
DR PIRSF; PIRSF005673; Importin_alpha; 1.
DR SMART; SM00185; ARM; 8.
DR SUPFAM; SSF48371; SSF48371; 1.
DR PROSITE; PS50176; ARM_REPEAT; 2.
DR PROSITE; PS51214; IBB; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Protein transport;
KW Reference proteome; Repeat; Transport.
FT CHAIN 1..542
FT /note="Importin subunit alpha"
FT /id="PRO_0000120744"
FT DOMAIN 1..65
FT /note="IBB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00561"
FT REPEAT 89..122
FT /note="ARM 1; truncated"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00259,
FT ECO:0000269|PubMed:8521485"
FT REPEAT 123..162
FT /note="ARM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00259,
FT ECO:0000269|PubMed:8521485"
FT REPEAT 163..204
FT /note="ARM 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00259,
FT ECO:0000269|PubMed:8521485"
FT REPEAT 205..251
FT /note="ARM 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00259,
FT ECO:0000269|PubMed:8521485"
FT REPEAT 252..288
FT /note="ARM 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00259,
FT ECO:0000269|PubMed:8521485"
FT REPEAT 289..330
FT /note="ARM 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00259,
FT ECO:0000269|PubMed:8521485"
FT REPEAT 331..372
FT /note="ARM 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00259,
FT ECO:0000269|PubMed:8521485"
FT REPEAT 373..417
FT /note="ARM 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00259,
FT ECO:0000269|PubMed:8521485"
FT REPEAT 418..471
FT /note="ARM 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00259,
FT ECO:0000269|PubMed:8521485"
FT REPEAT 472..508
FT /note="ARM 10; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00259,
FT ECO:0000269|PubMed:8521485"
FT REGION 1..77
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 209..335
FT /note="NLS binding site 1"
FT REGION 419..505
FT /note="NLS binding site 2"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..56
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MUTAGEN 116
FT /note="S->F: In SRP1-31; temperature-sensitive mutant;
FT reduced growth rate and chromosome loss."
FT /evidence="ECO:0000269|PubMed:8041713"
FT MUTAGEN 145
FT /note="E->K: In SRP1-49; temperature-sensitive mutant;
FT alteration in nucleolar and microtubule morphology."
FT /evidence="ECO:0000269|PubMed:8041713"
FT MUTAGEN 219
FT /note="P->Q: In SRP1-1; temperature-sensitive mutant."
FT /evidence="ECO:0000269|PubMed:8041713"
FT MUTAGEN 286
FT /note="D->N: In SRP1-3; temperature-sensitive mutant."
FT /evidence="ECO:0000269|PubMed:8041713"
FT MUTAGEN 360
FT /note="E->K: In SRP1-2; temperature-sensitive mutant."
FT /evidence="ECO:0000269|PubMed:8041713"
FT MUTAGEN 459
FT /note="G->V: In SRP1-54; temperature-sensitive mutant;
FT reduced growth rate."
FT /evidence="ECO:0000269|PubMed:8041713"
FT HELIX 15..17
FT /evidence="ECO:0007829|PDB:1WA5"
FT HELIX 89..97
FT /evidence="ECO:0007829|PDB:1WA5"
FT HELIX 101..115
FT /evidence="ECO:0007829|PDB:1WA5"
FT STRAND 118..120
FT /evidence="ECO:0007829|PDB:1EE4"
FT HELIX 123..128
FT /evidence="ECO:0007829|PDB:1WA5"
FT HELIX 132..137
FT /evidence="ECO:0007829|PDB:1WA5"
FT STRAND 140..143
FT /evidence="ECO:0007829|PDB:5T94"
FT HELIX 145..158
FT /evidence="ECO:0007829|PDB:1WA5"
FT HELIX 163..171
FT /evidence="ECO:0007829|PDB:1WA5"
FT HELIX 175..184
FT /evidence="ECO:0007829|PDB:1WA5"
FT HELIX 187..201
FT /evidence="ECO:0007829|PDB:1WA5"
FT HELIX 205..213
FT /evidence="ECO:0007829|PDB:1WA5"
FT HELIX 217..222
FT /evidence="ECO:0007829|PDB:1WA5"
FT HELIX 223..225
FT /evidence="ECO:0007829|PDB:1WA5"
FT HELIX 229..243
FT /evidence="ECO:0007829|PDB:1WA5"
FT STRAND 246..248
FT /evidence="ECO:0007829|PDB:1WA5"
FT HELIX 252..255
FT /evidence="ECO:0007829|PDB:1WA5"
FT HELIX 256..258
FT /evidence="ECO:0007829|PDB:1WA5"
FT HELIX 259..265
FT /evidence="ECO:0007829|PDB:1WA5"
FT HELIX 271..284
FT /evidence="ECO:0007829|PDB:1WA5"
FT STRAND 286..288
FT /evidence="ECO:0007829|PDB:1WA5"
FT HELIX 289..297
FT /evidence="ECO:0007829|PDB:1WA5"
FT HELIX 301..306
FT /evidence="ECO:0007829|PDB:1WA5"
FT HELIX 307..309
FT /evidence="ECO:0007829|PDB:1WA5"
FT HELIX 313..326
FT /evidence="ECO:0007829|PDB:1WA5"
FT HELIX 331..339
FT /evidence="ECO:0007829|PDB:1WA5"
FT HELIX 342..349
FT /evidence="ECO:0007829|PDB:1WA5"
FT HELIX 355..369
FT /evidence="ECO:0007829|PDB:1WA5"
FT HELIX 373..381
FT /evidence="ECO:0007829|PDB:1WA5"
FT HELIX 385..394
FT /evidence="ECO:0007829|PDB:1WA5"
FT HELIX 397..413
FT /evidence="ECO:0007829|PDB:1WA5"
FT TURN 414..416
FT /evidence="ECO:0007829|PDB:1WA5"
FT HELIX 418..426
FT /evidence="ECO:0007829|PDB:1WA5"
FT HELIX 430..436
FT /evidence="ECO:0007829|PDB:1WA5"
FT TURN 437..439
FT /evidence="ECO:0007829|PDB:1WA5"
FT HELIX 442..466
FT /evidence="ECO:0007829|PDB:1WA5"
FT HELIX 472..479
FT /evidence="ECO:0007829|PDB:1WA5"
FT HELIX 482..488
FT /evidence="ECO:0007829|PDB:1WA5"
FT HELIX 489..491
FT /evidence="ECO:0007829|PDB:1WA5"
FT STRAND 492..494
FT /evidence="ECO:0007829|PDB:2C1T"
FT HELIX 495..508
FT /evidence="ECO:0007829|PDB:1WA5"
FT TURN 510..512
FT /evidence="ECO:0007829|PDB:1UN0"
SQ SEQUENCE 542 AA; 60441 MW; 8D3A0CB76F2E7C00 CRC64;
MDNGTDSSTS KFVPEYRRTN FKNKGRFSAD ELRRRRDTQQ VELRKAKRDE ALAKRRNFIP
PTDGADSDEE DESSVSADQQ FYSQLQQELP QMTQQLNSDD MQEQLSATVK FRQILSREHR
PPIDVVIQAG VVPRLVEFMR ENQPEMLQLE AAWALTNIAS GTSAQTKVVV DADAVPLFIQ
LLYTGSVEVK EQAIWALGNV AGDSTDYRDY VLQCNAMEPI LGLFNSNKPS LIRTATWTLS
NLCRGKKPQP DWSVVSQALP TLAKLIYSMD TETLVDACWA ISYLSDGPQE AIQAVIDVRI
PKRLVELLSH ESTLVQTPAL RAVGNIVTGN DLQTQVVINA GVLPALRLLL SSPKENIKKE
ACWTISNITA GNTEQIQAVI DANLIPPLVK LLEVAEYKTK KEACWAISNA SSGGLQRPDI
IRYLVSQGCI KPLCDLLEIA DNRIIEVTLD ALENILKMGE ADKEARGLNI NENADFIEKA
GGMEKIFNCQ QNENDKIYEK AYKIIETYFG EEEDAVDETM APQNAGNTFG FGSNVNQQFN
FN
