NAB2_YEAST
ID NAB2_YEAST Reviewed; 525 AA.
AC P32505; D6VU26;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=Nuclear polyadenylated RNA-binding protein NAB2 {ECO:0000303|PubMed:8474438};
GN Name=NAB2 {ECO:0000303|PubMed:8474438}; OrderedLocusNames=YGL122C;
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 SUBCELLULAR LOCATION.
RC STRAIN=ATCC 208279 / BJ926;
RX PubMed=8474438; DOI=10.1128/mcb.13.5.2730-2741.1993;
RA Anderson J.T., Wilson S.M., Datar K.V., Swanson M.S.;
RT "NAB2: a yeast nuclear polyadenylated RNA-binding protein essential for
RT cell viability.";
RL Mol. Cell. Biol. 13:2730-2741(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(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 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [5]
RP FUNCTION.
RX PubMed=11927564; DOI=10.1093/emboj/21.7.1800;
RA Hector R.E., Nykamp K.R., Dheur S., Anderson J.T., Non P.J., Urbinati C.R.,
RA Wilson S.M., Minvielle-Sebastia L., Swanson M.S.;
RT "Dual requirement for yeast hnRNP Nab2p in mRNA poly(A) tail length control
RT and nuclear export.";
RL EMBO J. 21:1800-1810(2002).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND METHYLATION BY HMT1.
RX PubMed=11779864; DOI=10.1074/jbc.m110053200;
RA Green D.M., Marfatia K.A., Crafton E.B., Zhang X., Cheng X., Corbett A.H.;
RT "Nab2p is required for poly(A) RNA export in Saccharomyces cerevisiae and
RT is regulated by arginine methylation via Hmt1p.";
RL J. Biol. Chem. 277:7752-7760(2002).
RN [7]
RP DOMAIN.
RX PubMed=12496292; DOI=10.1074/jbc.m207571200;
RA Marfatia K.A., Crafton E.B., Green D.M., Corbett A.H.;
RT "Domain analysis of the Saccharomyces cerevisiae heterogeneous nuclear
RT ribonucleoprotein, Nab2p. Dissecting the requirements for Nab2p-facilitated
RT poly(A) RNA export.";
RL J. Biol. Chem. 278:6731-6740(2003).
RN [8]
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 [9]
RP INTERACTION WITH MLP1.
RX PubMed=18682389; DOI=10.1074/jbc.m803649200;
RA Fasken M.B., Stewart M., Corbett A.H.;
RT "Functional significance of the interaction between the mRNA-binding
RT protein, Nab2, and the nuclear pore-associated protein, Mlp1, in mRNA
RT export.";
RL J. Biol. Chem. 283:27130-27143(2008).
RN [10]
RP FUNCTION.
RX PubMed=19840948; DOI=10.1074/jbc.m109.062034;
RA Batisse J., Batisse C., Budd A., Boettcher B., Hurt E.;
RT "Purification of nuclear poly(A)-binding protein Nab2 reveals association
RT with the yeast transcriptome and a messenger ribonucleoprotein core
RT structure.";
RL J. Biol. Chem. 284:34911-34917(2009).
RN [11]
RP SUBCELLULAR LOCATION.
RX PubMed=23222640; DOI=10.1038/nsmb.2468;
RA Mitchell S.F., Jain S., She M., Parker R.;
RT "Global analysis of yeast mRNPs.";
RL Nat. Struct. Mol. Biol. 20:127-133(2013).
RN [12]
RP METHYLATION AT ARG-222.
RX PubMed=26046779; DOI=10.1002/pmic.201500032;
RA Plank M., Fischer R., Geoghegan V., Charles P.D., Konietzny R., Acuto O.,
RA Pears C., Schofield C.J., Kessler B.M.;
RT "Expanding the yeast protein arginine methylome.";
RL Proteomics 15:3232-3243(2015).
RN [13]
RP METHYLATION AT ARG-209, AND PHOSPHORYLATION AT THR-254.
RX PubMed=33856219; DOI=10.1021/acs.jproteome.0c00927;
RA Hamey J.J., Nguyen A., Wilkins M.R.;
RT "Discovery of arginine methylation, phosphorylation, and their co-
RT occurrence in condensate-associated proteins in Saccharomyces cerevisiae.";
RL J. Proteome Res. 20:2420-2434(2021).
RN [14] {ECO:0007744|PDB:2JPS, ECO:0007744|PDB:2V75}
RP STRUCTURE BY NMR OF 1-105, AND INTERACTION WITH MLP1.
RX PubMed=18190927; DOI=10.1016/j.jmb.2007.11.087;
RA Grant R.P., Marshall N.J., Yang J.C., Fasken M.B., Kelly S.M.,
RA Harreman M.T., Neuhaus D., Corbett A.H., Stewart M.;
RT "Structure of the N-terminal Mlp1-binding domain of the Saccharomyces
RT cerevisiae mRNA-binding protein, Nab2.";
RL J. Mol. Biol. 376:1048-1059(2008).
RN [15] {ECO:0007744|PDB:3LCN}
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 1-105 IN COMPLEX WITH ZINC.
RX PubMed=20463024; DOI=10.1074/jbc.m110.107276;
RA Zheng C., Fasken M.B., Marshall N.J., Brockmann C., Rubinson M.E.,
RA Wente S.R., Corbett A.H., Stewart M.;
RT "Structural basis for the function of the Saccharomyces cerevisiae Gfd1
RT protein in mRNA nuclear export.";
RL J. Biol. Chem. 285:20704-20715(2010).
RN [16] {ECO:0007744|PDB:2LHN}
RP STRUCTURE BY NMR OF 409-483, AND FUNCTION.
RX PubMed=22560733; DOI=10.1016/j.str.2012.03.011;
RA Brockmann C., Soucek S., Kuhlmann S.I., Mills-Lujan K., Kelly S.M.,
RA Yang J.C., Iglesias N., Stutz F., Corbett A.H., Neuhaus D., Stewart M.;
RT "Structural basis for polyadenosine-RNA binding by Nab2 Zn fingers and its
RT function in mRNA nuclear export.";
RL Structure 20:1007-1018(2012).
RN [17] {ECO:0007744|PDB:4JLQ}
RP X-RAY CRYSTALLOGRAPHY (3.05 ANGSTROMS) OF 205-242.
RX PubMed=23535894; DOI=10.1007/s10969-013-9150-1;
RA Soniat M., Sampathkumar P., Collett G., Gizzi A.S., Banu R.N., Bhosle R.C.,
RA Chamala S., Chowdhury S., Fiser A., Glenn A.S., Hammonds J., Hillerich B.,
RA Khafizov K., Love J.D., Matikainen B., Seidel R.D., Toro R.,
RA Rajesh Kumar P., Bonanno J.B., Chook Y.M., Almo S.C.;
RT "Crystal structure of human Karyopherin beta2 bound to the PY-NLS of
RT Saccharomyces cerevisiae Nab2.";
RL J. Struct. Funct. Genomics 14:31-35(2013).
RN [18] {ECO:0007744|PDB:3ZJ1, ECO:0007744|PDB:3ZJ2}
RP STRUCTURE BY NMR OF 253-333.
RX PubMed=23994011; DOI=10.1016/j.str.2013.07.019;
RA Martinez-Lumbreras S., Santiveri C.M., Mirassou Y., Zorrilla S.,
RA Perez-Canadillas J.M.;
RT "Two singular types of CCCH tandem zinc finger in Nab2p contribute to
RT polyadenosine RNA recognition.";
RL Structure 21:1800-1811(2013).
RN [19] {ECO:0007744|PDB:5L2L}
RP X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 407-483 IN COMPLEX WITH ZINC, AND
RP DOMAIN.
RX PubMed=28180315; DOI=10.1093/nar/gkw1224;
RA Aibara S., Gordon J.M., Riesterer A.S., McLaughlin S.H., Stewart M.;
RT "Structural basis for the dimerization of Nab2 generated by RNA binding
RT provides insight into its contribution to both poly(A) tail length
RT determination and transcript compaction in Saccharomyces cerevisiae.";
RL Nucleic Acids Res. 45:1529-1538(2017).
CC -!- FUNCTION: Essential protein that binds to polyadenylated RNA and
CC single-stranded DNA (PubMed:8474438). It may be involved not only in
CC RNA processing but also in transcription regulation. Associates
CC directly with nascent RNA polymerase II transcripts and remain
CC associated during subsequent nuclear RNA processing reactions
CC (Probable). Involved in mRNA poly(A) tail length control and nuclear
CC export (PubMed:11927564, PubMed:11779864). Functions in surveillance
CC and the packaging leading to generation of export-competent mRNPs.
CC Controls both mRNP compaction that facilitates movement through nuclear
CC pore complexes and the length of transcript poly(A) tails
CC (PubMed:19840948, PubMed:22560733). {ECO:0000269|PubMed:11779864,
CC ECO:0000269|PubMed:11927564, ECO:0000269|PubMed:19840948,
CC ECO:0000269|PubMed:22560733, ECO:0000269|PubMed:8474438,
CC ECO:0000305|PubMed:8474438}.
CC -!- SUBUNIT: Interacts with MLP1. {ECO:0000269|PubMed:18190927,
CC ECO:0000269|PubMed:18682389}.
CC -!- INTERACTION:
CC P32505; Q04839: GFD1; NbExp=7; IntAct=EBI-11770, EBI-27549;
CC P32505; P38074: HMT1; NbExp=2; IntAct=EBI-11770, EBI-8394;
CC P32505; P38217: KAP104; NbExp=4; IntAct=EBI-11770, EBI-9152;
CC P32505; Q02455: MLP1; NbExp=4; IntAct=EBI-11770, EBI-11009;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11779864,
CC ECO:0000269|PubMed:23222640, ECO:0000269|PubMed:8474438}. Cytoplasm
CC {ECO:0000269|PubMed:11779864}. Note=Localizes to the nucleus at steady-
CC state, it shuttles between nucleus and cytoplasm.
CC {ECO:0000269|PubMed:11779864}.
CC -!- DOMAIN: The N-terminal domain is required for nuclear export of both
CC poly(A) RNA and NAB2. {ECO:0000269|PubMed:12496292}.
CC -!- DOMAIN: The RGG domain is important for NAB2 import.
CC {ECO:0000269|PubMed:12496292}.
CC -!- DOMAIN: Contains seven CCCH Zn fingers that bind to A-rich RNAs and
CC fingers 5 to 7 are critical for these function (PubMed:12496292,
CC PubMed:22560733, PubMed:28180315). Binding A(11)G RNA induces
CC dimerization of Zn fingers 5-7 mediated by the spatial arrangement of
CC the fingers promoting each RNA chain binding two protein chains
CC (PubMed:28180315). {ECO:0000269|PubMed:12496292,
CC ECO:0000269|PubMed:22560733, ECO:0000269|PubMed:28180315}.
CC -!- PTM: Methylated by HMT1. {ECO:0000269|PubMed:11779864}.
CC -!- MISCELLANEOUS: Present with 9670 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the NAB2 family. {ECO:0000305}.
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DR EMBL; L10288; AAA34819.1; -; Genomic_DNA.
DR EMBL; L08079; AAA34820.1; -; Genomic_DNA.
DR EMBL; Z72644; CAA96830.1; -; Genomic_DNA.
DR EMBL; AY723810; AAU09727.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA07987.1; -; Genomic_DNA.
DR PIR; B48058; B48058.
DR RefSeq; NP_011393.3; NM_001180987.3.
DR PDB; 2JPS; NMR; -; A=1-105.
DR PDB; 2LHN; NMR; -; A=409-483.
DR PDB; 2V75; X-ray; 1.80 A; A=1-104.
DR PDB; 3LCN; X-ray; 2.00 A; A/B=1-105.
DR PDB; 3ZJ1; NMR; -; A=253-333.
DR PDB; 3ZJ2; NMR; -; A=333-401.
DR PDB; 4JLQ; X-ray; 3.04 A; B=205-242.
DR PDB; 5L2L; X-ray; 1.55 A; A/B/E/F=409-483.
DR PDBsum; 2JPS; -.
DR PDBsum; 2LHN; -.
DR PDBsum; 2V75; -.
DR PDBsum; 3LCN; -.
DR PDBsum; 3ZJ1; -.
DR PDBsum; 3ZJ2; -.
DR PDBsum; 4JLQ; -.
DR PDBsum; 5L2L; -.
DR AlphaFoldDB; P32505; -.
DR BMRB; P32505; -.
DR SMR; P32505; -.
DR BioGRID; 33129; 2764.
DR DIP; DIP-1331N; -.
DR IntAct; P32505; 16.
DR MINT; P32505; -.
DR STRING; 4932.YGL122C; -.
DR iPTMnet; P32505; -.
DR MaxQB; P32505; -.
DR PaxDb; P32505; -.
DR PRIDE; P32505; -.
DR EnsemblFungi; YGL122C_mRNA; YGL122C; YGL122C.
DR GeneID; 852755; -.
DR KEGG; sce:YGL122C; -.
DR SGD; S000003090; NAB2.
DR VEuPathDB; FungiDB:YGL122C; -.
DR eggNOG; KOG3702; Eukaryota.
DR GeneTree; ENSGT00440000038430; -.
DR HOGENOM; CLU_037973_1_0_1; -.
DR InParanoid; P32505; -.
DR OMA; VAEYIVL; -.
DR BioCyc; YEAST:G3O-30619-MON; -.
DR EvolutionaryTrace; P32505; -.
DR PRO; PR:P32505; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P32505; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0008097; F:5S rRNA binding; IDA:SGD.
DR GO; GO:0008312; F:7S RNA binding; IDA:SGD.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003729; F:mRNA binding; HDA:SGD.
DR GO; GO:0008143; F:poly(A) binding; IDA:SGD.
DR GO; GO:0033204; F:ribonuclease P RNA binding; IDA:SGD.
DR GO; GO:0000049; F:tRNA binding; IDA:SGD.
DR GO; GO:0006378; P:mRNA polyadenylation; IDA:SGD.
DR GO; GO:1900364; P:negative regulation of mRNA polyadenylation; IBA:GO_Central.
DR GO; GO:1900152; P:negative regulation of nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay; IGI:SGD.
DR GO; GO:0016973; P:poly(A)+ mRNA export from nucleus; IMP:SGD.
DR GO; GO:0045945; P:positive regulation of transcription by RNA polymerase III; IDA:SGD.
DR GO; GO:0043488; P:regulation of mRNA stability; IMP:SGD.
DR Gene3D; 1.10.340.40; -; 1.
DR IDEAL; IID50171; -.
DR InterPro; IPR040366; Nab2/ZC3H14.
DR InterPro; IPR043094; Nab2/ZC3H14_N_sf.
DR InterPro; IPR021083; Nab2_N.
DR InterPro; IPR041044; Nab2p_Zf1.
DR PANTHER; PTHR14738; PTHR14738; 3.
DR Pfam; PF11517; Nab2; 1.
DR Pfam; PF18260; Nab2p_Zf1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Metal-binding; Methylation; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; RNA-binding; Zinc; Zinc-finger.
FT CHAIN 1..525
FT /note="Nuclear polyadenylated RNA-binding protein NAB2"
FT /id="PRO_0000096687"
FT REPEAT 121..124
FT /note="1"
FT /evidence="ECO:0000305"
FT REPEAT 125..128
FT /note="2"
FT /evidence="ECO:0000305"
FT REPEAT 129..132
FT /note="3"
FT /evidence="ECO:0000305"
FT REPEAT 133..136
FT /note="4"
FT /evidence="ECO:0000305"
FT REPEAT 137..140
FT /note="5"
FT /evidence="ECO:0000305"
FT REPEAT 141..144
FT /note="6"
FT /evidence="ECO:0000305"
FT REPEAT 145..148
FT /note="7"
FT /evidence="ECO:0000305"
FT REPEAT 149..152
FT /note="8"
FT /evidence="ECO:0000305"
FT REPEAT 153..156
FT /note="9"
FT /evidence="ECO:0000305"
FT REPEAT 157..160
FT /note="10; approximate"
FT /evidence="ECO:0000305"
FT ZN_FING 262..278
FT /note="C3H1-type 1"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:23994011"
FT ZN_FING 283..300
FT /note="C3H1-type 2"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:23994011"
FT ZN_FING 340..355
FT /note="C3H1-type 3"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:23994011"
FT ZN_FING 371..386
FT /note="C3H1-type 4"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:23994011"
FT ZN_FING 415..430
FT /note="C3H1-type 5"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:22560733"
FT ZN_FING 437..452
FT /note="C3H1-type 6"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:22560733"
FT ZN_FING 458..473
FT /note="C3H1-type 7"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:22560733"
FT REGION 102..160
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 121..156
FT /note="10 X 4 AA tandem repeats of Q-Q-Q-P"
FT /evidence="ECO:0000305"
FT REGION 196..236
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 209..239
FT /note="PY-NLS nuclear localization signal"
FT /evidence="ECO:0000305|PubMed:23535894"
FT REGION 209..228
FT /note="RNA-binding RGG-box"
FT /evidence="ECO:0000250"
FT REGION 503..525
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 507..525
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 209
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000269|PubMed:33856219"
FT MOD_RES 222
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000269|PubMed:26046779"
FT MOD_RES 254
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:33856219"
FT VARIANT 130..157
FT /note="Missing (in YJA512)"
FT HELIX 7..18
FT /evidence="ECO:0007829|PDB:2V75"
FT HELIX 28..40
FT /evidence="ECO:0007829|PDB:2V75"
FT HELIX 45..55
FT /evidence="ECO:0007829|PDB:2V75"
FT HELIX 61..79
FT /evidence="ECO:0007829|PDB:2V75"
FT HELIX 84..93
FT /evidence="ECO:0007829|PDB:2V75"
FT TURN 269..273
FT /evidence="ECO:0007829|PDB:3ZJ1"
FT TURN 293..295
FT /evidence="ECO:0007829|PDB:3ZJ1"
FT STRAND 297..299
FT /evidence="ECO:0007829|PDB:3ZJ1"
FT STRAND 301..303
FT /evidence="ECO:0007829|PDB:3ZJ1"
FT HELIX 305..326
FT /evidence="ECO:0007829|PDB:3ZJ1"
FT STRAND 328..330
FT /evidence="ECO:0007829|PDB:3ZJ1"
FT HELIX 343..345
FT /evidence="ECO:0007829|PDB:3ZJ2"
FT STRAND 353..355
FT /evidence="ECO:0007829|PDB:3ZJ2"
FT HELIX 374..376
FT /evidence="ECO:0007829|PDB:3ZJ2"
FT STRAND 384..387
FT /evidence="ECO:0007829|PDB:3ZJ2"
FT HELIX 390..393
FT /evidence="ECO:0007829|PDB:3ZJ2"
FT STRAND 412..414
FT /evidence="ECO:0007829|PDB:5L2L"
FT HELIX 418..420
FT /evidence="ECO:0007829|PDB:5L2L"
FT STRAND 427..429
FT /evidence="ECO:0007829|PDB:2LHN"
FT STRAND 433..436
FT /evidence="ECO:0007829|PDB:5L2L"
FT HELIX 440..442
FT /evidence="ECO:0007829|PDB:5L2L"
FT STRAND 455..457
FT /evidence="ECO:0007829|PDB:5L2L"
FT HELIX 461..463
FT /evidence="ECO:0007829|PDB:5L2L"
FT STRAND 470..472
FT /evidence="ECO:0007829|PDB:2LHN"
SQ SEQUENCE 525 AA; 58321 MW; 40335C3D4658DD91 CRC64;
MSQEQYTENL KVIVAEKLAG IPNFNEDIKY VAEYIVLLIV NGGTVESVVD ELASLFDSVS
RDTLANVVQT AFFALEALQQ GESAENIVSK IRMMNAQSLG QSDIAQQQQQ QQQQQQPDIA
QQQPQQQPQQ QPQQQPQQQP QQQPQQQPQQ QPQQQPQLQP LQPQLGTQNA MQTDAPATPS
PISAFSGVVN AAAPPQFAPV DNSQRFTQRG GGAVGKNRRG GRGGNRGGRN NNSTRFNPLA
KALGMAGESN MNFTPTKKEG RCRLFPHCPL GRSCPHAHPT KVCNEYPNCP KPPGTCEFLH
PNEDEELMKE MERTREEFQK RKADLLAAKR KPVQTGIVLC KFGALCSNPS CPFGHPTPAN
EDAKVIDLMW CDKNLTCDNP ECRKAHSSLS KIKEVKPISQ KKAAPPPVEK SLEQCKFGTH
CTNKRCKYRH ARSHIMCREG ANCTRIDCLF GHPINEDCRF GVNCKNIYCL FRHPPGRVLP
EKKGAAPNSN VPTNERPFAL PENAIIENAP PQTSFTHQEQ DTEMN
