EMAL1_HUMAN
ID EMAL1_HUMAN Reviewed; 815 AA.
AC O00423; Q86U15; Q8N536; Q8N5C4; Q8WWL6;
DT 18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 3.
DT 03-AUG-2022, entry version 188.
DE RecName: Full=Echinoderm microtubule-associated protein-like 1;
DE Short=EMAP-1;
DE Short=HuEMAP-1;
GN Name=EML1; Synonyms=EMAP1, EMAPL, EMAPL1;
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), AND VARIANT PRO-556.
RX PubMed=9226380; DOI=10.1006/geno.1997.4779;
RA Eudy J.D., Ma-Edmonds M., Yao S.F., Talmadge C.B., Kelley P.M.,
RA Weston M.D., Kimberling W.J., Sumegi J.;
RT "Isolation of a novel human homologue of the gene coding for echinoderm
RT microtubule-associated protein (EMAP) from the Usher syndrome type 1a locus
RT at 14q32.";
RL Genomics 43:104-106(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT PRO-556.
RA Gerber S., Sumegi J., Rozet J.-M., Perrault I., Ducroq D., Munnich A.,
RA Kaplan J.;
RT "Complete exon-intron structure of human homologue of the gene coding the
RT echinoderm microtubule-associated protein (EMAP).";
RL Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS ASN-552
RP AND PRO-556.
RC TISSUE=Brain, and Uterus;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-500 (ISOFORM 3).
RC TISSUE=Fetal brain;
RA Li W.B., Gruber C., Jessee J., Polayes D.;
RT "Full-length cDNA libraries and normalization.";
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP TISSUE SPECIFICITY.
RX PubMed=10521658; DOI=10.1016/s0378-1119(99)00335-2;
RA Lepley D.M., Palange J.M., Suprenant K.A.;
RT "Sequence and expression patterns of a human EMAP-related protein-2
RT (HuEMAP-2).";
RL Gene 237:343-349(1999).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113, AND IDENTIFICATION BY
RP 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 [7]
RP SUBCELLULAR LOCATION, DOMAIN, AND MUTAGENESIS OF 59-LEU--ASP-61.
RX PubMed=25740311; DOI=10.1042/bj20150039;
RA Richards M.W., O'Regan L., Roth D., Montgomery J.M., Straube A., Fry A.M.,
RA Bayliss R.;
RT "Microtubule association of EML proteins and the EML4-ALK variant 3
RT oncoprotein require an N-terminal trimerization domain.";
RL Biochem. J. 467:529-536(2015).
RN [8]
RP INVOLVEMENT IN BH, VARIANTS BH ARG-225 AND ALA-243, CHARACTERIZATION OF
RP VARIANT BH ALA-243, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=24859200; DOI=10.1038/nn.3729;
RA Kielar M., Tuy F.P., Bizzotto S., Lebrand C., de Juan Romero C.,
RA Poirier K., Oegema R., Mancini G.M., Bahi-Buisson N., Olaso R.,
RA Le Moing A.G., Boutourlinsky K., Boucher D., Carpentier W., Berquin P.,
RA Deleuze J.F., Belvindrah R., Borrell V., Welker E., Chelly J.,
RA Croquelois A., Francis F.;
RT "Mutations in Eml1 lead to ectopic progenitors and neuronal heterotopia in
RT mouse and human.";
RL Nat. Neurosci. 17:923-933(2014).
RN [9]
RP INVOLVEMENT IN BH, AND VARIANT BH 523-ARG--ILE-815 DEL.
RX PubMed=28556411; DOI=10.1002/ana.24964;
RA Shaheen R., Sebai M.A., Patel N., Ewida N., Kurdi W., Altweijri I.,
RA Sogaty S., Almardawi E., Seidahmed M.Z., Alnemri A., Madirevula S.,
RA Ibrahim N., Abdulwahab F., Hashem M., Al-Sheddi T., Alomar R., Alobeid E.,
RA Sallout B., AlBaqawi B., AlAali W., Ajaji N., Lesmana H., Hopkin R.J.,
RA Dupuis L., Mendoza-Londono R., Al Rukban H., Yoon G., Faqeih E.,
RA Alkuraya F.S.;
RT "The genetic landscape of familial congenital hydrocephalus.";
RL Ann. Neurol. 81:890-897(2017).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 167-815, DOMAIN, INTERACTION WITH
RP TUBULIN, AND MUTAGENESIS OF 59-LEU--ASP-61; ARG-192; ARG-194; TRP-547;
RP ASN-626; GLU-627; HIS-646 AND HIS-786.
RX PubMed=24706829; DOI=10.1073/pnas.1322892111;
RA Richards M.W., Law E.W., Rennalls L.P., Busacca S., O'Regan L., Fry A.M.,
RA Fennell D.A., Bayliss R.;
RT "Crystal structure of EML1 reveals the basis for Hsp90 dependence of
RT oncogenic EML4-ALK by disruption of an atypical beta-propeller domain.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:5195-5200(2014).
CC -!- FUNCTION: Modulates the assembly and organization of the microtubule
CC cytoskeleton, and probably plays a role in regulating the orientation
CC of the mitotic spindle and the orientation of the plane of cell
CC division. Required for normal proliferation of neuronal progenitor
CC cells in the developing brain and for normal brain development. Does
CC not affect neuron migration per se. {ECO:0000250|UniProtKB:Q05BC3}.
CC -!- SUBUNIT: Homotrimer; self-association is mediated by the N-terminal
CC coiled coil (By similarity). Does not interact with EML3
CC (PubMed:25740311). Binds repolymerizing microtubules (PubMed:24859200).
CC Binds unpolymerized tubulins via its WD repeat region
CC (PubMed:24706829). Interacts with TASOR (By similarity).
CC {ECO:0000250|UniProtKB:Q05BC3, ECO:0000250|UniProtKB:Q9HC35,
CC ECO:0000269|PubMed:24706829, ECO:0000269|PubMed:24859200,
CC ECO:0000269|PubMed:25740311}.
CC -!- INTERACTION:
CC O00423; P55212: CASP6; NbExp=3; IntAct=EBI-751327, EBI-718729;
CC O00423; P51114: FXR1; NbExp=2; IntAct=EBI-751327, EBI-713291;
CC O00423; Q9H9L3: ISG20L2; NbExp=3; IntAct=EBI-751327, EBI-751335;
CC O00423; P13473-2: LAMP2; NbExp=3; IntAct=EBI-751327, EBI-21591415;
CC O00423; P31948: STIP1; NbExp=3; IntAct=EBI-751327, EBI-1054052;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q05BC3}.
CC Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q05BC3}.
CC Cytoplasm, cytoskeleton {ECO:0000269|PubMed:24859200,
CC ECO:0000269|PubMed:25740311}. Note=Detected in cytoplasmic punctae. Co-
CC localizes with microtubules (PubMed:24859200, PubMed:25740311).
CC Enriched in perinuclear regions during interphase and in the region of
CC spindle microtubules during metaphase. Enriched at the midzone during
CC telophase and cytokinesis. Detected at growth cones in neurons (By
CC similarity). {ECO:0000250|UniProtKB:Q05BC3,
CC ECO:0000269|PubMed:24859200, ECO:0000269|PubMed:25740311}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O00423-1; Sequence=Displayed;
CC Name=3;
CC IsoId=O00423-3; Sequence=VSP_024476;
CC -!- TISSUE SPECIFICITY: Ubiquitous; expressed in most tissues with the
CC exception of thymus and peripheral blood lymphocytes.
CC {ECO:0000269|PubMed:10521658}.
CC -!- DOMAIN: Contains a tandem atypical propeller in EMLs (TAPE) domain. The
CC N-terminal beta-propeller is formed by canonical WD repeats; in
CC contrast, the second beta-propeller contains one blade that is formed
CC by discontinuous parts of the polypeptide chain.
CC {ECO:0000269|PubMed:24706829}.
CC -!- DOMAIN: The N-terminal coiled coil is required for association with
CC microtubules. {ECO:0000269|PubMed:25740311}.
CC -!- DISEASE: Band heterotopia (BH) [MIM:600348]: A brain malformation of
CC the lissencephaly spectrum, resulting from disordered neuronal
CC migration and characterized by bands of gray matter interposed in the
CC central white matter. Disease features include severe developmental
CC delay with intellectual disability, enlarged head circumference,
CC periventricular and ribbon-like subcortical heterotopia, polymicrogyria
CC and agenesis of the corpus callosum. {ECO:0000269|PubMed:24859200,
CC ECO:0000269|PubMed:28556411}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the WD repeat EMAP family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB57824.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAD62313.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; U97018; AAB57824.1; ALT_FRAME; mRNA.
DR EMBL; AJ420603; CAD12600.2; -; Genomic_DNA.
DR EMBL; AJ428183; CAD12600.2; JOINED; Genomic_DNA.
DR EMBL; AJ428184; CAD12600.2; JOINED; Genomic_DNA.
DR EMBL; AJ428185; CAD12600.2; JOINED; Genomic_DNA.
DR EMBL; AJ428189; CAD12600.2; JOINED; Genomic_DNA.
DR EMBL; AJ428191; CAD12600.2; JOINED; Genomic_DNA.
DR EMBL; AJ428193; CAD12600.2; JOINED; Genomic_DNA.
DR EMBL; AJ428195; CAD12600.2; JOINED; Genomic_DNA.
DR EMBL; AJ428197; CAD12600.2; JOINED; Genomic_DNA.
DR EMBL; AJ496645; CAD12600.2; JOINED; Genomic_DNA.
DR EMBL; AJ496644; CAD12600.2; JOINED; Genomic_DNA.
DR EMBL; AJ428200; CAD12600.2; JOINED; Genomic_DNA.
DR EMBL; AJ428199; CAD12600.2; JOINED; Genomic_DNA.
DR EMBL; AJ428198; CAD12600.2; JOINED; Genomic_DNA.
DR EMBL; AJ428196; CAD12600.2; JOINED; Genomic_DNA.
DR EMBL; AJ428194; CAD12600.2; JOINED; Genomic_DNA.
DR EMBL; AJ428192; CAD12600.2; JOINED; Genomic_DNA.
DR EMBL; AJ428190; CAD12600.2; JOINED; Genomic_DNA.
DR EMBL; AJ428188; CAD12600.2; JOINED; Genomic_DNA.
DR EMBL; AJ428187; CAD12600.2; JOINED; Genomic_DNA.
DR EMBL; AJ428186; CAD12600.2; JOINED; Genomic_DNA.
DR EMBL; BC032541; AAH32541.1; -; mRNA.
DR EMBL; BC033043; AAH33043.1; -; mRNA.
DR EMBL; BX247979; CAD62313.1; ALT_INIT; mRNA.
DR CCDS; CCDS32154.1; -. [O00423-3]
DR CCDS; CCDS32155.1; -. [O00423-1]
DR RefSeq; NP_001008707.1; NM_001008707.1. [O00423-3]
DR RefSeq; NP_004425.2; NM_004434.2. [O00423-1]
DR PDB; 4CI8; X-ray; 2.60 A; A/B=167-815.
DR PDBsum; 4CI8; -.
DR AlphaFoldDB; O00423; -.
DR SMR; O00423; -.
DR BioGRID; 108324; 28.
DR IntAct; O00423; 16.
DR MINT; O00423; -.
DR STRING; 9606.ENSP00000334314; -.
DR iPTMnet; O00423; -.
DR PhosphoSitePlus; O00423; -.
DR BioMuta; EML1; -.
DR CPTAC; CPTAC-1606; -.
DR EPD; O00423; -.
DR jPOST; O00423; -.
DR MassIVE; O00423; -.
DR MaxQB; O00423; -.
DR PaxDb; O00423; -.
DR PeptideAtlas; O00423; -.
DR PRIDE; O00423; -.
DR ProteomicsDB; 47880; -. [O00423-1]
DR ProteomicsDB; 47881; -. [O00423-3]
DR Antibodypedia; 27460; 87 antibodies from 25 providers.
DR DNASU; 2009; -.
DR Ensembl; ENST00000262233.11; ENSP00000262233.7; ENSG00000066629.18. [O00423-1]
DR Ensembl; ENST00000334192.8; ENSP00000334314.4; ENSG00000066629.18. [O00423-3]
DR GeneID; 2009; -.
DR KEGG; hsa:2009; -.
DR MANE-Select; ENST00000262233.11; ENSP00000262233.7; NM_004434.3; NP_004425.2.
DR UCSC; uc001ygr.4; human. [O00423-1]
DR CTD; 2009; -.
DR DisGeNET; 2009; -.
DR GeneCards; EML1; -.
DR HGNC; HGNC:3330; EML1.
DR HPA; ENSG00000066629; Low tissue specificity.
DR MalaCards; EML1; -.
DR MIM; 600348; phenotype.
DR MIM; 602033; gene.
DR neXtProt; NX_O00423; -.
DR OpenTargets; ENSG00000066629; -.
DR Orphanet; 99796; Subcortical band heterotopia.
DR PharmGKB; PA27767; -.
DR VEuPathDB; HostDB:ENSG00000066629; -.
DR eggNOG; KOG2106; Eukaryota.
DR GeneTree; ENSGT00940000153887; -.
DR InParanoid; O00423; -.
DR OMA; TTRDIQW; -.
DR OrthoDB; 271572at2759; -.
DR PhylomeDB; O00423; -.
DR TreeFam; TF317832; -.
DR PathwayCommons; O00423; -.
DR SignaLink; O00423; -.
DR BioGRID-ORCS; 2009; 8 hits in 1065 CRISPR screens.
DR ChiTaRS; EML1; human.
DR GeneWiki; EML1; -.
DR GenomeRNAi; 2009; -.
DR Pharos; O00423; Tbio.
DR PRO; PR:O00423; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; O00423; protein.
DR Bgee; ENSG00000066629; Expressed in cortical plate and 193 other tissues.
DR ExpressionAtlas; O00423; baseline and differential.
DR Genevisible; O00423; HS.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005874; C:microtubule; IDA:UniProtKB.
DR GO; GO:0005875; C:microtubule associated complex; TAS:ProtInc.
DR GO; GO:1990023; C:mitotic spindle midzone; IEA:Ensembl.
DR GO; GO:0097431; C:mitotic spindle pole; IEA:Ensembl.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; NAS:UniProtKB.
DR GO; GO:0008017; F:microtubule binding; IMP:UniProtKB.
DR GO; GO:0015631; F:tubulin binding; IDA:UniProtKB.
DR GO; GO:0007420; P:brain development; IMP:UniProtKB.
DR GO; GO:0002244; P:hematopoietic progenitor cell differentiation; IEA:Ensembl.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; ISS:UniProtKB.
DR GO; GO:0007052; P:mitotic spindle organization; ISS:UniProtKB.
DR GO; GO:0007405; P:neuroblast proliferation; ISS:UniProtKB.
DR Gene3D; 2.130.10.10; -; 2.
DR InterPro; IPR005108; HELP.
DR InterPro; IPR011047; Quinoprotein_ADH-like_supfam.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR Pfam; PF03451; HELP; 1.
DR Pfam; PF00400; WD40; 4.
DR SMART; SM00320; WD40; 10.
DR SUPFAM; SSF50978; SSF50978; 1.
DR SUPFAM; SSF50998; SSF50998; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 3.
DR PROSITE; PS50294; WD_REPEATS_REGION; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Coiled coil; Cytoplasm; Cytoskeleton;
KW Disease variant; Epilepsy; Intellectual disability; Lissencephaly;
KW Microtubule; Phosphoprotein; Reference proteome; Repeat; WD repeat.
FT CHAIN 1..815
FT /note="Echinoderm microtubule-associated protein-like 1"
FT /id="PRO_0000050961"
FT REPEAT 261..310
FT /note="WD 1"
FT REPEAT 315..358
FT /note="WD 2"
FT REPEAT 363..400
FT /note="WD 3"
FT REPEAT 409..446
FT /note="WD 4"
FT REPEAT 450..489
FT /note="WD 5"
FT REPEAT 493..530
FT /note="WD 6"
FT REPEAT 535..572
FT /note="WD 7"
FT REPEAT 578..613
FT /note="WD 8"
FT REPEAT 617..655
FT /note="WD 9"
FT REPEAT 664..701
FT /note="WD 10"
FT REPEAT 709..768
FT /note="WD 11"
FT REPEAT 775..814
FT /note="WD 12"
FT REGION 77..179
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 176..815
FT /note="Tandem atypical propeller in EMLs"
FT COILED 31..72
FT /evidence="ECO:0000255"
FT COMPBIAS 89..108
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 126..142
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 153..169
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 113
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT VAR_SEQ 127
FT /note="K -> KRLNRSVSLLNACKLNRSTP (in isoform 3)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_024476"
FT VARIANT 225
FT /note="W -> R (in BH; dbSNP:rs886037937)"
FT /evidence="ECO:0000269|PubMed:24859200"
FT /id="VAR_071075"
FT VARIANT 243
FT /note="T -> A (in BH; decreased microtubule-binding;
FT dbSNP:rs886037936)"
FT /evidence="ECO:0000269|PubMed:24859200"
FT /id="VAR_071076"
FT VARIANT 377
FT /note="A -> V (in dbSNP:rs34198557)"
FT /id="VAR_031720"
FT VARIANT 523..815
FT /note="Missing (in BH)"
FT /evidence="ECO:0000269|PubMed:28556411"
FT /id="VAR_081119"
FT VARIANT 552
FT /note="H -> N (in dbSNP:rs17853154)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_031721"
FT VARIANT 556
FT /note="S -> P (in dbSNP:rs2250718)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:9226380, ECO:0000269|Ref.2"
FT /id="VAR_031722"
FT MUTAGEN 59..61
FT /note="LAD->AAA: No effect on tubulin binding. Does not
FT disrupt self-association. Decreased association with
FT microtubules."
FT /evidence="ECO:0000269|PubMed:24706829,
FT ECO:0000269|PubMed:25740311"
FT MUTAGEN 192
FT /note="R->S: Abolishes tubulin binding; when associated
FT with S-194; A-547; T-626; S-627; A-646 and A-786."
FT /evidence="ECO:0000269|PubMed:24706829"
FT MUTAGEN 194
FT /note="R->S: Abolishes tubulin binding; when associated
FT with S-192; A-547; T-626; S-627; A-646 and A-786."
FT /evidence="ECO:0000269|PubMed:24706829"
FT MUTAGEN 547
FT /note="W->A: Abolishes tubulin binding; when associated
FT with S-192; S-194; T-626; S-627; A-646 and A-786."
FT /evidence="ECO:0000269|PubMed:24706829"
FT MUTAGEN 626
FT /note="N->T: Abolishes tubulin binding; when associated
FT with S-192; S-194; A-547; S-627; A-646 and A-786."
FT /evidence="ECO:0000269|PubMed:24706829"
FT MUTAGEN 627
FT /note="E->S: Abolishes tubulin binding; when associated
FT with S-192; S-194; A-547; T-626; A-646 and A-786."
FT /evidence="ECO:0000269|PubMed:24706829"
FT MUTAGEN 646
FT /note="H->A: Abolishes tubulin binding; when associated
FT with S-192; S-194; A-547; T-626; S-627 and A-786."
FT /evidence="ECO:0000269|PubMed:24706829"
FT MUTAGEN 786
FT /note="H->A: Abolishes tubulin binding; when associated
FT with S-192; S-194; A-547; T-626; S-627 and A-646."
FT /evidence="ECO:0000269|PubMed:24706829"
FT CONFLICT 93..95
FT /note="LRT -> FRS (in Ref. 1; AAB57824)"
FT /evidence="ECO:0000305"
FT CONFLICT 106
FT /note="K -> I (in Ref. 1; AAB57824)"
FT /evidence="ECO:0000305"
FT CONFLICT 117
FT /note="V -> F (in Ref. 1; AAB57824)"
FT /evidence="ECO:0000305"
FT CONFLICT 120
FT /note="E -> D (in Ref. 1; AAB57824)"
FT /evidence="ECO:0000305"
FT CONFLICT 189
FT /note="M -> L (in Ref. 1; AAB57824)"
FT /evidence="ECO:0000305"
FT CONFLICT 464..465
FT /note="FA -> SP (in Ref. 1; AAB57824 and 2; CAD12600)"
FT /evidence="ECO:0000305"
FT CONFLICT 499..500
FT /note="IP -> VS (in Ref. 4; CAD62313)"
FT /evidence="ECO:0000305"
FT STRAND 179..181
FT /evidence="ECO:0007829|PDB:4CI8"
FT TURN 182..185
FT /evidence="ECO:0007829|PDB:4CI8"
FT STRAND 186..199
FT /evidence="ECO:0007829|PDB:4CI8"
FT HELIX 202..205
FT /evidence="ECO:0007829|PDB:4CI8"
FT STRAND 220..227
FT /evidence="ECO:0007829|PDB:4CI8"
FT STRAND 238..240
FT /evidence="ECO:0007829|PDB:4CI8"
FT STRAND 246..250
FT /evidence="ECO:0007829|PDB:4CI8"
FT STRAND 253..258
FT /evidence="ECO:0007829|PDB:4CI8"
FT TURN 259..262
FT /evidence="ECO:0007829|PDB:4CI8"
FT STRAND 263..267
FT /evidence="ECO:0007829|PDB:4CI8"
FT STRAND 274..279
FT /evidence="ECO:0007829|PDB:4CI8"
FT STRAND 283..291
FT /evidence="ECO:0007829|PDB:4CI8"
FT STRAND 305..309
FT /evidence="ECO:0007829|PDB:4CI8"
FT TURN 310..312
FT /evidence="ECO:0007829|PDB:4CI8"
FT STRAND 315..319
FT /evidence="ECO:0007829|PDB:4CI8"
FT TURN 321..323
FT /evidence="ECO:0007829|PDB:4CI8"
FT STRAND 326..333
FT /evidence="ECO:0007829|PDB:4CI8"
FT STRAND 335..339
FT /evidence="ECO:0007829|PDB:4CI8"
FT STRAND 342..346
FT /evidence="ECO:0007829|PDB:4CI8"
FT STRAND 348..350
FT /evidence="ECO:0007829|PDB:4CI8"
FT STRAND 352..357
FT /evidence="ECO:0007829|PDB:4CI8"
FT HELIX 358..360
FT /evidence="ECO:0007829|PDB:4CI8"
FT STRAND 362..368
FT /evidence="ECO:0007829|PDB:4CI8"
FT STRAND 374..379
FT /evidence="ECO:0007829|PDB:4CI8"
FT STRAND 386..392
FT /evidence="ECO:0007829|PDB:4CI8"
FT STRAND 394..401
FT /evidence="ECO:0007829|PDB:4CI8"
FT STRAND 404..409
FT /evidence="ECO:0007829|PDB:4CI8"
FT STRAND 419..426
FT /evidence="ECO:0007829|PDB:4CI8"
FT STRAND 432..436
FT /evidence="ECO:0007829|PDB:4CI8"
FT STRAND 441..444
FT /evidence="ECO:0007829|PDB:4CI8"
FT STRAND 449..455
FT /evidence="ECO:0007829|PDB:4CI8"
FT STRAND 458..461
FT /evidence="ECO:0007829|PDB:4CI8"
FT STRAND 463..468
FT /evidence="ECO:0007829|PDB:4CI8"
FT STRAND 474..478
FT /evidence="ECO:0007829|PDB:4CI8"
FT TURN 479..481
FT /evidence="ECO:0007829|PDB:4CI8"
FT STRAND 483..487
FT /evidence="ECO:0007829|PDB:4CI8"
FT STRAND 493..498
FT /evidence="ECO:0007829|PDB:4CI8"
FT TURN 501..503
FT /evidence="ECO:0007829|PDB:4CI8"
FT STRAND 505..511
FT /evidence="ECO:0007829|PDB:4CI8"
FT STRAND 517..521
FT /evidence="ECO:0007829|PDB:4CI8"
FT STRAND 526..529
FT /evidence="ECO:0007829|PDB:4CI8"
FT STRAND 536..539
FT /evidence="ECO:0007829|PDB:4CI8"
FT STRAND 546..551
FT /evidence="ECO:0007829|PDB:4CI8"
FT STRAND 553..562
FT /evidence="ECO:0007829|PDB:4CI8"
FT STRAND 565..571
FT /evidence="ECO:0007829|PDB:4CI8"
FT TURN 572..575
FT /evidence="ECO:0007829|PDB:4CI8"
FT STRAND 576..582
FT /evidence="ECO:0007829|PDB:4CI8"
FT STRAND 587..592
FT /evidence="ECO:0007829|PDB:4CI8"
FT STRAND 596..612
FT /evidence="ECO:0007829|PDB:4CI8"
FT TURN 613..615
FT /evidence="ECO:0007829|PDB:4CI8"
FT STRAND 618..623
FT /evidence="ECO:0007829|PDB:4CI8"
FT STRAND 625..627
FT /evidence="ECO:0007829|PDB:4CI8"
FT STRAND 629..634
FT /evidence="ECO:0007829|PDB:4CI8"
FT STRAND 638..645
FT /evidence="ECO:0007829|PDB:4CI8"
FT STRAND 650..656
FT /evidence="ECO:0007829|PDB:4CI8"
FT TURN 657..660
FT /evidence="ECO:0007829|PDB:4CI8"
FT STRAND 661..668
FT /evidence="ECO:0007829|PDB:4CI8"
FT STRAND 675..681
FT /evidence="ECO:0007829|PDB:4CI8"
FT STRAND 687..691
FT /evidence="ECO:0007829|PDB:4CI8"
FT STRAND 697..700
FT /evidence="ECO:0007829|PDB:4CI8"
FT HELIX 701..703
FT /evidence="ECO:0007829|PDB:4CI8"
FT HELIX 710..713
FT /evidence="ECO:0007829|PDB:4CI8"
FT STRAND 724..726
FT /evidence="ECO:0007829|PDB:4CI8"
FT TURN 727..731
FT /evidence="ECO:0007829|PDB:4CI8"
FT STRAND 741..747
FT /evidence="ECO:0007829|PDB:4CI8"
FT STRAND 749..758
FT /evidence="ECO:0007829|PDB:4CI8"
FT STRAND 763..768
FT /evidence="ECO:0007829|PDB:4CI8"
FT STRAND 772..774
FT /evidence="ECO:0007829|PDB:4CI8"
FT STRAND 778..780
FT /evidence="ECO:0007829|PDB:4CI8"
FT STRAND 789..792
FT /evidence="ECO:0007829|PDB:4CI8"
FT STRAND 796..802
FT /evidence="ECO:0007829|PDB:4CI8"
FT STRAND 809..815
FT /evidence="ECO:0007829|PDB:4CI8"
SQ SEQUENCE 815 AA; 89861 MW; A1476F75F3537205 CRC64;
MEDGFSSYSS LYDTSSLLQF CNDDSASAAS SMEVTDRIAS LEQRVQMQED DIQLLKSALA
DVVRRLNITE EQQAVLNRKG PTKARPLMQT LPLRTTVNNG TVLPKKPTGS LPSPSGVRKE
TAVPATKSNI KRTSSSERVS PGGRRESNGD SRGNRNRTGS TSSSSSGKKN SESKPKEPVF
SAEEGYVKMF LRGRPVTMYM PKDQVDSYSL EAKVELPTKR LKLEWVYGYR GRDCRNNLYL
LPTGETVYFI ASVVVLYNVE EQLQRHYAGH NDDVKCLAVH PDRITIATGQ VAGTSKDGKQ
LPPHVRIWDS VTLNTLHVIG IGFFDRAVTC IAFSKSNGGT NLCAVDDSND HVLSVWDWQK
EEKLADVKCS NEAVFAADFH PTDTNIIVTC GKSHLYFWTL EGSSLNKKQG LFEKQEKPKF
VLCVTFSENG DTITGDSSGN ILVWGKGTNR ISYAVQGAHE GGIFALCMLR DGTLVSGGGK
DRKLISWSGN YQKLRKTEIP EQFGPIRTVA EGKGDVILIG TTRNFVLQGT LSGDFTPITQ
GHTDELWGLA IHASKSQFLT CGHDKHATLW DAVGHRPVWD KIIEDPAQSS GFHPSGSVVA
VGTLTGRWFV FDTETKDLVT VHTDGNEQLS VMRYSPDGNF LAIGSHDNCI YIYGVSDNGR
KYTRVGKCSG HSSFITHLDW SVNSQFLVSN SGDYEILYWV PSACKQVVSV ETTRDIEWAT
YTCTLGFHVF GVWPEGSDGT DINAVCRAHE KKLLSTGDDF GKVHLFSYPC SQFRAPSHIY
GGHSSHVTNV DFLCEDSHLI STGGKDTSIM QWRVI
