EI2BB_HUMAN
ID EI2BB_HUMAN Reviewed; 351 AA.
AC P49770; O43201;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 3.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=Translation initiation factor eIF-2B subunit beta;
DE AltName: Full=S20I15;
DE AltName: Full=S20III15;
DE AltName: Full=eIF-2B GDP-GTP exchange factor subunit beta;
GN Name=EIF2B2; Synonyms=EIF2BB;
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 [LARGE SCALE MRNA].
RC TISSUE=Brain;
RA Yu W., Sarginson J., Gibbs R.A.;
RL Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=7596406; DOI=10.1038/375754a0;
RA Sherrington R., Rogaev E.I., Liang Y., Rogaeva E.A., Levesque G., Ikeda M.,
RA Chi H., Lin C., Li G., Holman K., Tsuda T., Mar L., Foncin J.-F.,
RA Bruni A.C., Montesi M.P., Sorbi S., Rainero I., Pinessi L., Nee L.,
RA Chumakov I., Pollen D., Brookes A., Sanseau P., Polinsky R.J., Wasco W.,
RA da Silva H.A.R., Haines J.L., Pericak-Vance M.A., Tanzi R.E., Roses A.D.,
RA Fraser P.E., Rommens J.M., St George-Hyslop P.H.;
RT "Cloning of a gene bearing missense mutations in early-onset familial
RT Alzheimer's disease.";
RL Nature 375:754-760(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12508121; DOI=10.1038/nature01348;
RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H.,
RA Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T.,
RA Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B.,
RA Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D.,
RA Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R.,
RA Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S.,
RA Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C.,
RA Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S.,
RA Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C.,
RA Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P.,
RA Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J.,
RA Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F.,
RA Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F.,
RA Waterston R., Hood L., Weissenbach J.;
RT "The DNA sequence and analysis of human chromosome 14.";
RL Nature 421:601-607(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
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 [5]
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 [6]
RP IDENTIFICATION BY MASS 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 [7]
RP VARIANTS VWM GLY-213; ARG-273; ASP-316 AND VAL-329.
RX PubMed=11704758; DOI=10.1038/ng764;
RA Leegwater P.A.J., Vermeulen G., Koenst A.A.M., Naidu S., Mulders J.,
RA Visser A., Kersbergen P., Mobach D., Fonds D., van Berkel C.G.M.,
RA Lemmers R.J.L.F., Frants R.R., Oudejans C.B.M., Schutgens R.B.H.,
RA Pronk J.C., van der Knaap M.S.;
RT "Subunits of the translation initiation factor eIF2B are mutant in
RT leukoencephalopathy with vanishing white matter.";
RL Nat. Genet. 29:383-388(2001).
RN [8]
RP VARIANTS VWM PHE-171 AND GLY-213.
RX PubMed=12707859; DOI=10.1086/375404;
RA Fogli A., Rodriguez D., Eymard-Pierre E., Bouhour F., Labauge P.,
RA Meaney B.F., Zeesman S., Kaneski C.R., Schiffmann R., Boespflug-Tanguy O.;
RT "Ovarian failure related to eukaryotic initiation factor 2B mutations.";
RL Am. J. Hum. Genet. 72:1544-1550(2003).
RN [9]
RP VARIANTS VWM PHE-171; SER-196; VAL-200 AND GLY-213.
RX PubMed=15776425; DOI=10.1002/humu.9325;
RA Ohlenbusch A., Henneke M., Brockmann K., Goerg M., Hanefeld F.,
RA Kohlschutter A., Gartner J.;
RT "Identification of ten novel mutations in patients with eIF2B-related
RT disorders.";
RL Hum. Mutat. 25:411-411(2005).
RN [10]
RP VARIANT VWM GLU-85.
RX PubMed=21484434; DOI=10.1007/s10048-011-0284-7;
RA Matsukawa T., Wang X., Liu R., Wortham N.C., Onuki Y., Kubota A., Hida A.,
RA Kowa H., Fukuda Y., Ishiura H., Mitsui J., Takahashi Y., Aoki S.,
RA Takizawa S., Shimizu J., Goto J., Proud C.G., Tsuji S.;
RT "Adult-onset leukoencephalopathies with vanishing white matter with novel
RT missense mutations in EIF2B2, EIF2B3, and EIF2B5.";
RL Neurogenetics 12:259-261(2011).
RN [11]
RP VARIANT VWM TYR-268.
RX PubMed=22285377; DOI=10.1016/j.gene.2011.12.047;
RA Alsalem A., Shaheen R., Alkuraya F.S.;
RT "Vanishing white matter disease caused by EIF2B2 mutation with the
RT presentation of an adrenoleukodystrophy phenotype.";
RL Gene 496:141-143(2012).
RN [12]
RP VARIANT VWM GLY-213.
RX PubMed=22729508; DOI=10.1007/s10072-012-1129-3;
RA Sambati L., Agati R., Bacci A., Bianchi S., Capellari S.;
RT "Vanishing white matter disease: an Italian case with A638G mutation in
RT exon 5 of EIF2B2 gene, an unusual early onset and a long course.";
RL Neurol. Sci. 34:1235-1238(2013).
RN [13]
RP VARIANT VAL-127.
RX PubMed=26740508; DOI=10.1136/jmedgenet-2015-103568;
RA Lopes F., Barbosa M., Ameur A., Soares G., de Sa J., Dias A.I.,
RA Oliveira G., Cabral P., Temudo T., Calado E., Cruz I.F., Vieira J.P.,
RA Oliveira R., Esteves S., Sauer S., Jonasson I., Syvaenen A.C.,
RA Gyllensten U., Pinto D., Maciel P.;
RT "Identification of novel genetic causes of Rett syndrome-like phenotypes.";
RL J. Med. Genet. 53:190-199(2016).
CC -!- FUNCTION: Catalyzes the exchange of eukaryotic initiation factor 2-
CC bound GDP for GTP.
CC -!- SUBUNIT: Complex of five different subunits; alpha, beta, gamma, delta
CC and epsilon.
CC -!- INTERACTION:
CC P49770; Q96LT7: C9orf72; NbExp=6; IntAct=EBI-718773, EBI-2961725;
CC P49770; Q9UI10: EIF2B4; NbExp=7; IntAct=EBI-718773, EBI-2340132;
CC -!- DISEASE: Leukodystrophy with vanishing white matter (VWM) [MIM:603896]:
CC A leukodystrophy that occurs mainly in children. Neurological signs
CC include progressive cerebellar ataxia, spasticity, inconstant optic
CC atrophy and relatively preserved mental abilities. The disease is
CC chronic-progressive with, in most individuals, additional episodes of
CC rapid deterioration following febrile infections or minor head trauma.
CC While childhood onset is the most common form of the disorder, some
CC severe forms are apparent at birth. A severe, early-onset form seen
CC among the Cree and Chippewayan populations of Quebec and Manitoba is
CC called Cree leukoencephalopathy. Milder forms may not become evident
CC until adolescence or adulthood. Some females with milder forms of the
CC disease who survive to adolescence exhibit ovarian dysfunction. This
CC variant of the disorder is called ovarioleukodystrophy.
CC {ECO:0000269|PubMed:11704758, ECO:0000269|PubMed:12707859,
CC ECO:0000269|PubMed:15776425, ECO:0000269|PubMed:21484434,
CC ECO:0000269|PubMed:22285377, ECO:0000269|PubMed:22729508}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the eIF-2B alpha/beta/delta subunits family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC42002.1; Type=Frameshift; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Mendelian genes eukaryotic translation initiation
CC factor 2B, subunit 2 beta, 39kDa (EIF2B2); Note=Leiden Open Variation
CC Database (LOVD);
CC URL="https://databases.lovd.nl/shared/genes/EIF2B2";
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DR EMBL; AF035280; AAB88176.1; -; mRNA.
DR EMBL; L40395; AAC42002.1; ALT_FRAME; mRNA.
DR EMBL; AC006530; AAD30183.1; -; Genomic_DNA.
DR EMBL; BC011750; AAH11750.1; -; mRNA.
DR CCDS; CCDS9836.1; -.
DR RefSeq; NP_055054.1; NM_014239.3.
DR PDB; 6CAJ; EM; 2.80 A; C/D=2-351.
DR PDB; 6EZO; EM; 4.10 A; C/D=5-351.
DR PDB; 6K71; EM; 4.30 A; C/D=1-351.
DR PDB; 6K72; EM; 4.60 A; C/D=1-351.
DR PDB; 6O81; EM; 3.21 A; C/D=2-351.
DR PDB; 6O85; EM; 3.03 A; C/D=2-351.
DR PDB; 6O9Z; EM; 3.03 A; C/D=2-351.
DR PDB; 7D43; EM; 4.30 A; C/D=1-351.
DR PDB; 7D44; EM; 4.00 A; C/D=1-351.
DR PDB; 7D45; EM; 3.80 A; C/D=1-351.
DR PDB; 7D46; EM; 4.00 A; C/D=1-351.
DR PDB; 7F64; EM; 2.42 A; C/D=1-351.
DR PDB; 7F66; EM; 2.76 A; C/D=1-351.
DR PDB; 7F67; EM; 3.59 A; C/D=1-351.
DR PDB; 7KMF; EM; 2.91 A; C/D=1-351.
DR PDB; 7L70; EM; 2.80 A; C/D=2-351.
DR PDB; 7L7G; EM; 3.00 A; C/D=2-351.
DR PDB; 7RLO; EM; 2.60 A; C/D=1-351.
DR PDB; 7VLK; EM; 2.27 A; C/D=1-351.
DR PDBsum; 6CAJ; -.
DR PDBsum; 6EZO; -.
DR PDBsum; 6K71; -.
DR PDBsum; 6K72; -.
DR PDBsum; 6O81; -.
DR PDBsum; 6O85; -.
DR PDBsum; 6O9Z; -.
DR PDBsum; 7D43; -.
DR PDBsum; 7D44; -.
DR PDBsum; 7D45; -.
DR PDBsum; 7D46; -.
DR PDBsum; 7F64; -.
DR PDBsum; 7F66; -.
DR PDBsum; 7F67; -.
DR PDBsum; 7KMF; -.
DR PDBsum; 7L70; -.
DR PDBsum; 7L7G; -.
DR PDBsum; 7RLO; -.
DR PDBsum; 7VLK; -.
DR AlphaFoldDB; P49770; -.
DR SMR; P49770; -.
DR BioGRID; 114409; 121.
DR CORUM; P49770; -.
DR IntAct; P49770; 43.
DR MINT; P49770; -.
DR STRING; 9606.ENSP00000266126; -.
DR iPTMnet; P49770; -.
DR PhosphoSitePlus; P49770; -.
DR SwissPalm; P49770; -.
DR BioMuta; EIF2B2; -.
DR DMDM; 6226858; -.
DR EPD; P49770; -.
DR jPOST; P49770; -.
DR MassIVE; P49770; -.
DR PaxDb; P49770; -.
DR PeptideAtlas; P49770; -.
DR PRIDE; P49770; -.
DR ProteomicsDB; 56113; -.
DR Antibodypedia; 57; 184 antibodies from 30 providers.
DR DNASU; 8892; -.
DR Ensembl; ENST00000266126.10; ENSP00000266126.5; ENSG00000119718.11.
DR GeneID; 8892; -.
DR KEGG; hsa:8892; -.
DR MANE-Select; ENST00000266126.10; ENSP00000266126.5; NM_014239.4; NP_055054.1.
DR CTD; 8892; -.
DR DisGeNET; 8892; -.
DR GeneCards; EIF2B2; -.
DR GeneReviews; EIF2B2; -.
DR HGNC; HGNC:3258; EIF2B2.
DR HPA; ENSG00000119718; Low tissue specificity.
DR MalaCards; EIF2B2; -.
DR MIM; 603896; phenotype.
DR MIM; 606454; gene.
DR neXtProt; NX_P49770; -.
DR OpenTargets; ENSG00000119718; -.
DR Orphanet; 157713; Congenital or early infantile CACH syndrome.
DR Orphanet; 99854; Cree leukoencephalopathy.
DR Orphanet; 157719; Juvenile or adult CACH syndrome.
DR Orphanet; 157716; Late infantile CACH syndrome.
DR Orphanet; 99853; Ovarioleukodystrophy.
DR PharmGKB; PA27689; -.
DR VEuPathDB; HostDB:ENSG00000119718; -.
DR eggNOG; KOG1465; Eukaryota.
DR GeneTree; ENSGT00550000074908; -.
DR HOGENOM; CLU_016218_4_3_1; -.
DR InParanoid; P49770; -.
DR OMA; TSHTSYA; -.
DR OrthoDB; 918011at2759; -.
DR PhylomeDB; P49770; -.
DR TreeFam; TF101506; -.
DR PathwayCommons; P49770; -.
DR Reactome; R-HSA-72731; Recycling of eIF2:GDP.
DR SignaLink; P49770; -.
DR SIGNOR; P49770; -.
DR BioGRID-ORCS; 8892; 810 hits in 1097 CRISPR screens.
DR ChiTaRS; EIF2B2; human.
DR GeneWiki; EIF2B2; -.
DR GenomeRNAi; 8892; -.
DR Pharos; P49770; Tbio.
DR PRO; PR:P49770; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; P49770; protein.
DR Bgee; ENSG00000119718; Expressed in left lobe of thyroid gland and 207 other tissues.
DR ExpressionAtlas; P49770; baseline and differential.
DR Genevisible; P49770; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005851; C:eukaryotic translation initiation factor 2B complex; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
DR GO; GO:0005525; F:GTP binding; IDA:UniProtKB.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
DR GO; GO:0007417; P:central nervous system development; IMP:UniProtKB.
DR GO; GO:0042552; P:myelination; IMP:UniProtKB.
DR GO; GO:0014003; P:oligodendrocyte development; IMP:UniProtKB.
DR GO; GO:0001541; P:ovarian follicle development; IMP:UniProtKB.
DR GO; GO:0050790; P:regulation of catalytic activity; IEA:GOC.
DR GO; GO:0006446; P:regulation of translational initiation; TAS:UniProtKB.
DR GO; GO:0009749; P:response to glucose; ISS:UniProtKB.
DR GO; GO:0009408; P:response to heat; ISS:UniProtKB.
DR GO; GO:0043434; P:response to peptide hormone; ISS:UniProtKB.
DR GO; GO:0050852; P:T cell receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:0006413; P:translational initiation; IDA:UniProtKB.
DR Gene3D; 3.40.50.10470; -; 1.
DR InterPro; IPR000649; IF-2B-related.
DR InterPro; IPR042529; IF_2B-like_C.
DR InterPro; IPR037171; NagB/RpiA_transferase-like.
DR Pfam; PF01008; IF-2B; 1.
DR SUPFAM; SSF100950; SSF100950; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Disease variant; Initiation factor; Leukodystrophy;
KW Protein biosynthesis; Reference proteome.
FT CHAIN 1..351
FT /note="Translation initiation factor eIF-2B subunit beta"
FT /id="PRO_0000156061"
FT VARIANT 85
FT /note="V -> E (in VWM; dbSNP:rs397514648)"
FT /evidence="ECO:0000269|PubMed:21484434"
FT /id="VAR_068451"
FT VARIANT 127
FT /note="A -> V (found in a patient with Rett syndrome-like
FT phenotype; unknown pathological significance;
FT dbSNP:rs150617429)"
FT /evidence="ECO:0000269|PubMed:26740508"
FT /id="VAR_079034"
FT VARIANT 171
FT /note="S -> F (in VWM; with ovarian failure;
FT dbSNP:rs104894428)"
FT /evidence="ECO:0000269|PubMed:12707859,
FT ECO:0000269|PubMed:15776425"
FT /id="VAR_016842"
FT VARIANT 196
FT /note="P -> S (in VWM; dbSNP:rs113994011)"
FT /evidence="ECO:0000269|PubMed:15776425"
FT /id="VAR_068452"
FT VARIANT 200
FT /note="G -> V (in VWM; dbSNP:rs113994012)"
FT /evidence="ECO:0000269|PubMed:15776425"
FT /id="VAR_068453"
FT VARIANT 213
FT /note="E -> G (in VWM; with and without ovarian failure;
FT dbSNP:rs104894425)"
FT /evidence="ECO:0000269|PubMed:11704758,
FT ECO:0000269|PubMed:12707859, ECO:0000269|PubMed:15776425,
FT ECO:0000269|PubMed:22729508"
FT /id="VAR_012289"
FT VARIANT 268
FT /note="C -> Y (in VWM)"
FT /evidence="ECO:0000269|PubMed:22285377"
FT /id="VAR_068454"
FT VARIANT 273
FT /note="K -> R (in VWM; dbSNP:rs113994016)"
FT /evidence="ECO:0000269|PubMed:11704758"
FT /id="VAR_012321"
FT VARIANT 316
FT /note="V -> D (in VWM; dbSNP:rs104894426)"
FT /evidence="ECO:0000269|PubMed:11704758"
FT /id="VAR_012290"
FT VARIANT 329
FT /note="G -> V (in VWM; dbSNP:rs113994020)"
FT /evidence="ECO:0000269|PubMed:11704758"
FT /id="VAR_012322"
FT CONFLICT 6
FT /note="A -> K (in Ref. 2; AAC42002)"
FT /evidence="ECO:0000305"
FT CONFLICT 23
FT /note="K -> T (in Ref. 2; AAC42002)"
FT /evidence="ECO:0000305"
FT CONFLICT 30
FT /note="S -> R (in Ref. 2; AAC42002)"
FT /evidence="ECO:0000305"
FT CONFLICT 35
FT /note="A -> V (in Ref. 2; AAC42002)"
FT /evidence="ECO:0000305"
FT CONFLICT 52
FT /note="S -> R (in Ref. 2; AAC42002)"
FT /evidence="ECO:0000305"
FT CONFLICT 95..101
FT /note="RLHGRSD -> DSMDAAT (in Ref. 2; AAC42002)"
FT /evidence="ECO:0000305"
FT CONFLICT 110
FT /note="H -> D (in Ref. 2; AAC42002)"
FT /evidence="ECO:0000305"
FT HELIX 9..24
FT /evidence="ECO:0007829|PDB:7VLK"
FT STRAND 28..30
FT /evidence="ECO:0007829|PDB:7RLO"
FT HELIX 31..48
FT /evidence="ECO:0007829|PDB:7VLK"
FT HELIX 54..71
FT /evidence="ECO:0007829|PDB:7VLK"
FT HELIX 76..97
FT /evidence="ECO:0007829|PDB:7VLK"
FT HELIX 109..114
FT /evidence="ECO:0007829|PDB:7VLK"
FT HELIX 129..145
FT /evidence="ECO:0007829|PDB:7VLK"
FT HELIX 147..152
FT /evidence="ECO:0007829|PDB:7VLK"
FT TURN 156..158
FT /evidence="ECO:0007829|PDB:7VLK"
FT STRAND 164..169
FT /evidence="ECO:0007829|PDB:7VLK"
FT HELIX 172..181
FT /evidence="ECO:0007829|PDB:7VLK"
FT TURN 182..184
FT /evidence="ECO:0007829|PDB:7VLK"
FT STRAND 188..193
FT /evidence="ECO:0007829|PDB:7VLK"
FT STRAND 195..197
FT /evidence="ECO:0007829|PDB:7VLK"
FT HELIX 200..209
FT /evidence="ECO:0007829|PDB:7VLK"
FT STRAND 213..218
FT /evidence="ECO:0007829|PDB:7VLK"
FT HELIX 219..221
FT /evidence="ECO:0007829|PDB:7VLK"
FT HELIX 222..225
FT /evidence="ECO:0007829|PDB:7VLK"
FT HELIX 226..228
FT /evidence="ECO:0007829|PDB:7VLK"
FT STRAND 230..234
FT /evidence="ECO:0007829|PDB:7VLK"
FT STRAND 237..239
FT /evidence="ECO:0007829|PDB:7VLK"
FT STRAND 241..243
FT /evidence="ECO:0007829|PDB:7L70"
FT STRAND 245..248
FT /evidence="ECO:0007829|PDB:7VLK"
FT HELIX 251..260
FT /evidence="ECO:0007829|PDB:7VLK"
FT STRAND 265..268
FT /evidence="ECO:0007829|PDB:7VLK"
FT HELIX 271..273
FT /evidence="ECO:0007829|PDB:7VLK"
FT TURN 279..281
FT /evidence="ECO:0007829|PDB:6CAJ"
FT STRAND 283..286
FT /evidence="ECO:0007829|PDB:7VLK"
FT HELIX 291..293
FT /evidence="ECO:0007829|PDB:7VLK"
FT HELIX 297..299
FT /evidence="ECO:0007829|PDB:7VLK"
FT HELIX 301..304
FT /evidence="ECO:0007829|PDB:7VLK"
FT STRAND 305..308
FT /evidence="ECO:0007829|PDB:7VLK"
FT STRAND 313..316
FT /evidence="ECO:0007829|PDB:7VLK"
FT HELIX 318..320
FT /evidence="ECO:0007829|PDB:7VLK"
FT STRAND 323..326
FT /evidence="ECO:0007829|PDB:7VLK"
FT STRAND 329..331
FT /evidence="ECO:0007829|PDB:7VLK"
FT HELIX 333..335
FT /evidence="ECO:0007829|PDB:7VLK"
FT HELIX 336..343
FT /evidence="ECO:0007829|PDB:7VLK"
FT HELIX 346..348
FT /evidence="ECO:0007829|PDB:7VLK"
SQ SEQUENCE 351 AA; 38990 MW; C29FE477143F545A CRC64;
MPGSAAKGSE LSERIESFVE TLKRGGGPRS SEEMARETLG LLRQIITDHR WSNAGELMEL
IRREGRRMTA AQPSETTVGN MVRRVLKIIR EEYGRLHGRS DESDQQESLH KLLTSGGLNE
DFSFHYAQLQ SNIIEAINEL LVELEGTMEN IAAQALEHIH SNEVIMTIGF SRTVEAFLKE
AARKRKFHVI VAECAPFCQG HEMAVNLSKA GIETTVMTDA AIFAVMSRVN KVIIGTKTIL
ANGALRAVTG THTLALAAKH HSTPLIVCAP MFKLSPQFPN EEDSFHKFVA PEEVLPFTEG
DILEKVSVHC PVFDYVPPEL ITLFISNIGG NAPSYIYRLM SELYHPDDHV L
