IF4A2_HUMAN
ID IF4A2_HUMAN Reviewed; 407 AA.
AC Q14240; D3DNU9; Q53XJ6; Q96B90; Q96EA8;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2004, sequence version 2.
DT 03-AUG-2022, entry version 219.
DE RecName: Full=Eukaryotic initiation factor 4A-II;
DE Short=eIF-4A-II;
DE Short=eIF4A-II;
DE EC=3.6.4.13;
DE AltName: Full=ATP-dependent RNA helicase eIF4A-2;
GN Name=EIF4A2; Synonyms=DDX2B, EIF4F;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Lung;
RX PubMed=8521730; DOI=10.1159/000134145;
RA Sudo K., Takahashi E., Nakamura Y.;
RT "Isolation and mapping of the human EIF4A2 gene homologous to the murine
RT protein synthesis initiation factor 4A-II gene Eif4a2.";
RL Cytogenet. Cell Genet. 71:385-388(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Bone marrow, Brain, Lymph, and Skeletal muscle;
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 INTERACTION WITH EIF4E.
RX PubMed=11408474; DOI=10.1074/jbc.c100284200;
RA Li W., Belsham G.J., Proud C.G.;
RT "Eukaryotic initiation factors 4A (eIF4A) and 4G (eIF4G) mutually interact
RT in a 1:1 ratio in vivo.";
RL J. Biol. Chem. 276:29111-29115(2001).
RN [7]
RP POSSIBLE INTERACTION WITH NOM1.
RX PubMed=15715967; DOI=10.1016/j.gene.2004.12.027;
RA Simmons H.M., Ruis B.L., Kapoor M., Hudacek A.W., Conklin K.F.;
RT "Identification of NOM1, a nucleolar, eIF4A binding protein encoded within
RT the chromosome 7q36 breakpoint region targeted in cases of pediatric acute
RT myeloid leukemia.";
RL Gene 347:137-145(2005).
RN [8]
RP INTERACTION WITH HHV-1 VHS (MICROBIAL INFECTION).
RX PubMed=16014927; DOI=10.1128/jvi.79.15.9651-9664.2005;
RA Feng P., Everly D.N. Jr., Read G.S.;
RT "mRNA decay during herpes simplex virus (HSV) infections: protein-protein
RT interactions involving the HSV virion host shutoff protein and translation
RT factors eIF4H and eIF4A.";
RL J. Virol. 79:9651-9664(2005).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-159, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 22-240.
RX PubMed=20941364; DOI=10.1371/journal.pone.0012791;
RA Schutz P., Karlberg T., van den Berg S., Collins R., Lehtio L., Hogbom M.,
RA Holmberg-Schiavone L., Tempel W., Park H.W., Hammarstrom M., Moche M.,
RA Thorsell A.G., Schuler H.;
RT "Comparative structural analysis of human DEAD-box RNA helicases.";
RL PLoS ONE 5:E12791-E12791(2010).
RN [13]
RP VARIANT [LARGE SCALE ANALYSIS] LEU-181.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: ATP-dependent RNA helicase which is a subunit of the eIF4F
CC complex involved in cap recognition and is required for mRNA binding to
CC ribosome. In the current model of translation initiation, eIF4A unwinds
CC RNA secondary structures in the 5'-UTR of mRNAs which is necessary to
CC allow efficient binding of the small ribosomal subunit, and subsequent
CC scanning for the initiator codon.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
CC -!- SUBUNIT: eIF4F is a multi-subunit complex, the composition of which
CC varies with external and internal environmental conditions. It is
CC composed of at least EIF4A, EIF4E and EIF4G1/EIFFG3 (By similarity).
CC Interacts with EIF4E. May interact with NOM1. {ECO:0000250,
CC ECO:0000269|PubMed:11408474, ECO:0000269|PubMed:16014927}.
CC -!- SUBUNIT: (Microbial infection) Interacts with herpes simplex virus
CC 1/HHV-1 protein Vhs. {ECO:0000269|PubMed:16014927}.
CC -!- INTERACTION:
CC Q14240; Q7L190: DPPA4; NbExp=3; IntAct=EBI-73473, EBI-710457;
CC Q14240; P04792: HSPB1; NbExp=2; IntAct=EBI-73473, EBI-352682;
CC Q14240; Q9UI26: IPO11; NbExp=3; IntAct=EBI-73473, EBI-748752;
CC Q14240; Q53EL6: PDCD4; NbExp=5; IntAct=EBI-73473, EBI-935824;
CC Q14240; Q7RTY1: SLC16A9; NbExp=3; IntAct=EBI-73473, EBI-10232636;
CC Q14240; Q9Y2D8: SSX2IP; NbExp=3; IntAct=EBI-73473, EBI-2212028;
CC Q14240; Q9NQ86: TRIM36; NbExp=3; IntAct=EBI-73473, EBI-2341518;
CC Q14240; Q9HCM9: TRIM39; NbExp=4; IntAct=EBI-73473, EBI-739510;
CC Q14240; PRO_0000037577 [P27958]; Xeno; NbExp=4; IntAct=EBI-73473, EBI-6904388;
CC Q14240-2; P54253: ATXN1; NbExp=3; IntAct=EBI-10232522, EBI-930964;
CC Q14240-2; Q96D03: DDIT4L; NbExp=3; IntAct=EBI-10232522, EBI-742054;
CC Q14240-2; Q7L190: DPPA4; NbExp=3; IntAct=EBI-10232522, EBI-710457;
CC Q14240-2; P42858: HTT; NbExp=3; IntAct=EBI-10232522, EBI-466029;
CC Q14240-2; Q99750: MDFI; NbExp=3; IntAct=EBI-10232522, EBI-724076;
CC Q14240-2; Q53EL6: PDCD4; NbExp=3; IntAct=EBI-10232522, EBI-935824;
CC Q14240-2; Q8WWB5: PIH1D2; NbExp=3; IntAct=EBI-10232522, EBI-10232538;
CC Q14240-2; Q9Y2D8: SSX2IP; NbExp=3; IntAct=EBI-10232522, EBI-2212028;
CC Q14240-2; Q9NQ86: TRIM36; NbExp=3; IntAct=EBI-10232522, EBI-2341518;
CC Q14240-2; Q9HCM9: TRIM39; NbExp=3; IntAct=EBI-10232522, EBI-739510;
CC Q14240-2; Q6ZNG0: ZNF620; NbExp=3; IntAct=EBI-10232522, EBI-4395669;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q14240-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q14240-2; Sequence=VSP_009629;
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. eIF4A subfamily.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/EIF4A2ID262.html";
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DR EMBL; D30655; BAA06336.1; -; mRNA.
DR EMBL; BT009860; AAP88862.1; -; mRNA.
DR EMBL; AC112907; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471052; EAW78172.1; -; Genomic_DNA.
DR EMBL; CH471052; EAW78177.1; -; Genomic_DNA.
DR EMBL; BC012547; AAH12547.1; -; mRNA.
DR EMBL; BC013708; AAH13708.1; -; mRNA.
DR EMBL; BC015842; AAH15842.1; -; mRNA.
DR EMBL; BC048105; AAH48105.1; -; mRNA.
DR CCDS; CCDS3282.1; -. [Q14240-1]
DR RefSeq; NP_001958.2; NM_001967.3. [Q14240-1]
DR PDB; 3BOR; X-ray; 1.85 A; A=22-240.
DR PDBsum; 3BOR; -.
DR AlphaFoldDB; Q14240; -.
DR SMR; Q14240; -.
DR BioGRID; 108290; 123.
DR ComplexPortal; CPX-5634; Eukaryotic translation initiation factor 4F, EIF4A2 and EIF4G1 variant.
DR ComplexPortal; CPX-5636; Eukaryotic translation initiation factor 4F, EIF4A2 and EIF4G3 variant.
DR IntAct; Q14240; 44.
DR MINT; Q14240; -.
DR STRING; 9606.ENSP00000326381; -.
DR BindingDB; Q14240; -.
DR ChEMBL; CHEMBL4105952; -.
DR iPTMnet; Q14240; -.
DR MetOSite; Q14240; -.
DR PhosphoSitePlus; Q14240; -.
DR SwissPalm; Q14240; -.
DR BioMuta; EIF4A2; -.
DR DMDM; 45645183; -.
DR EPD; Q14240; -.
DR jPOST; Q14240; -.
DR MassIVE; Q14240; -.
DR MaxQB; Q14240; -.
DR PaxDb; Q14240; -.
DR PeptideAtlas; Q14240; -.
DR PRIDE; Q14240; -.
DR ProteomicsDB; 59936; -. [Q14240-1]
DR ProteomicsDB; 59937; -. [Q14240-2]
DR Antibodypedia; 3189; 313 antibodies from 33 providers.
DR DNASU; 1974; -.
DR Ensembl; ENST00000323963.10; ENSP00000326381.5; ENSG00000156976.17. [Q14240-1]
DR Ensembl; ENST00000440191.6; ENSP00000398370.2; ENSG00000156976.17. [Q14240-2]
DR GeneID; 1974; -.
DR KEGG; hsa:1974; -.
DR MANE-Select; ENST00000323963.10; ENSP00000326381.5; NM_001967.4; NP_001958.2.
DR UCSC; uc003fqs.4; human. [Q14240-1]
DR CTD; 1974; -.
DR DisGeNET; 1974; -.
DR GeneCards; EIF4A2; -.
DR HGNC; HGNC:3284; EIF4A2.
DR HPA; ENSG00000156976; Low tissue specificity.
DR MIM; 601102; gene.
DR neXtProt; NX_Q14240; -.
DR OpenTargets; ENSG00000156976; -.
DR PharmGKB; PA27712; -.
DR VEuPathDB; HostDB:ENSG00000156976; -.
DR eggNOG; KOG0327; Eukaryota.
DR GeneTree; ENSGT00940000153783; -.
DR HOGENOM; CLU_003041_1_0_1; -.
DR InParanoid; Q14240; -.
DR OMA; EHKDGQR; -.
DR OrthoDB; 726081at2759; -.
DR PhylomeDB; Q14240; -.
DR TreeFam; TF101524; -.
DR PathwayCommons; Q14240; -.
DR Reactome; R-HSA-1169408; ISG15 antiviral mechanism.
DR Reactome; R-HSA-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR Reactome; R-HSA-429947; Deadenylation of mRNA.
DR Reactome; R-HSA-72649; Translation initiation complex formation.
DR Reactome; R-HSA-72662; Activation of the mRNA upon binding of the cap-binding complex and eIFs, and subsequent binding to 43S.
DR Reactome; R-HSA-72702; Ribosomal scanning and start codon recognition.
DR Reactome; R-HSA-72706; GTP hydrolysis and joining of the 60S ribosomal subunit.
DR SignaLink; Q14240; -.
DR SIGNOR; Q14240; -.
DR BioGRID-ORCS; 1974; 12 hits in 1071 CRISPR screens.
DR ChiTaRS; EIF4A2; human.
DR EvolutionaryTrace; Q14240; -.
DR GeneWiki; EIF4A2; -.
DR GenomeRNAi; 1974; -.
DR Pharos; Q14240; Tbio.
DR PRO; PR:Q14240; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q14240; protein.
DR Bgee; ENSG00000156976; Expressed in secondary oocyte and 208 other tissues.
DR ExpressionAtlas; Q14240; baseline and differential.
DR Genevisible; Q14240; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0016281; C:eukaryotic translation initiation factor 4F complex; TAS:ProtInc.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:AgBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IDA:AgBase.
DR GO; GO:0004386; F:helicase activity; TAS:ProtInc.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0003743; F:translation initiation factor activity; IBA:GO_Central.
DR GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEA:Ensembl.
DR GO; GO:0002183; P:cytoplasmic translational initiation; IBA:GO_Central.
DR GO; GO:1900260; P:negative regulation of RNA-directed 5'-3' RNA polymerase activity; IDA:AgBase.
DR GO; GO:0006446; P:regulation of translational initiation; TAS:ProtInc.
DR GO; GO:0006413; P:translational initiation; IC:ComplexPortal.
DR CDD; cd18046; DEADc_EIF4AII_EIF4AI_DDX2; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR044728; EIF4A_DEADc.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000629; RNA-helicase_DEAD-box_CS.
DR InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00039; DEAD_ATP_HELICASE; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS51195; Q_MOTIF; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; ATP-binding; Helicase;
KW Host-virus interaction; Hydrolase; Initiation factor; Nucleotide-binding;
KW Phosphoprotein; Protein biosynthesis; Reference proteome; RNA-binding.
FT CHAIN 1..407
FT /note="Eukaryotic initiation factor 4A-II"
FT /id="PRO_0000054938"
FT DOMAIN 64..235
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 246..407
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 33..61
FT /note="Q motif"
FT MOTIF 183..186
FT /note="DEAD box"
FT BINDING 77..84
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 159
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 9
FT /note="N -> NS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_009629"
FT VARIANT 93
FT /note="Q -> H (in dbSNP:rs11538616)"
FT /id="VAR_052158"
FT VARIANT 181
FT /note="V -> L (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035838"
FT CONFLICT 27
FT /note="N -> S (in Ref. 5; AAH15842)"
FT /evidence="ECO:0000305"
FT CONFLICT 212..213
FT /note="LL -> FA (in Ref. 1; BAA06336)"
FT /evidence="ECO:0000305"
FT HELIX 35..37
FT /evidence="ECO:0007829|PDB:3BOR"
FT HELIX 42..51
FT /evidence="ECO:0007829|PDB:3BOR"
FT HELIX 58..68
FT /evidence="ECO:0007829|PDB:3BOR"
FT STRAND 73..75
FT /evidence="ECO:0007829|PDB:3BOR"
FT HELIX 81..94
FT /evidence="ECO:0007829|PDB:3BOR"
FT STRAND 104..107
FT /evidence="ECO:0007829|PDB:3BOR"
FT HELIX 111..124
FT /evidence="ECO:0007829|PDB:3BOR"
FT TURN 125..129
FT /evidence="ECO:0007829|PDB:3BOR"
FT STRAND 132..135
FT /evidence="ECO:0007829|PDB:3BOR"
FT STRAND 154..158
FT /evidence="ECO:0007829|PDB:3BOR"
FT HELIX 160..168
FT /evidence="ECO:0007829|PDB:3BOR"
FT STRAND 179..184
FT /evidence="ECO:0007829|PDB:3BOR"
FT HELIX 185..190
FT /evidence="ECO:0007829|PDB:3BOR"
FT HELIX 194..203
FT /evidence="ECO:0007829|PDB:3BOR"
FT STRAND 209..213
FT /evidence="ECO:0007829|PDB:3BOR"
FT HELIX 219..228
FT /evidence="ECO:0007829|PDB:3BOR"
FT STRAND 233..235
FT /evidence="ECO:0007829|PDB:3BOR"
SQ SEQUENCE 407 AA; 46402 MW; FAA7D3BA9D8C6DA0 CRC64;
MSGGSADYNR EHGGPEGMDP DGVIESNWNE IVDNFDDMNL KESLLRGIYA YGFEKPSAIQ
QRAIIPCIKG YDVIAQAQSG TGKTATFAIS ILQQLEIEFK ETQALVLAPT RELAQQIQKV
ILALGDYMGA TCHACIGGTN VRNEMQKLQA EAPHIVVGTP GRVFDMLNRR YLSPKWIKMF
VLDEADEMLS RGFKDQIYEI FQKLNTSIQV VLLSATMPTD VLEVTKKFMR DPIRILVKKE
ELTLEGIKQF YINVEREEWK LDTLCDLYET LTITQAVIFL NTRRKVDWLT EKMHARDFTV
SALHGDMDQK ERDVIMREFR SGSSRVLITT DLLARGIDVQ QVSLVINYDL PTNRENYIHR
IGRGGRFGRK GVAINFVTEE DKRILRDIET FYNTTVEEMP MNVADLI
