EFNA1_HUMAN
ID EFNA1_HUMAN Reviewed; 205 AA.
AC P20827; D3DV86; Q5SR60; Q5SR61; Q6I9T9; Q8N578;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2005, sequence version 2.
DT 03-AUG-2022, entry version 202.
DE RecName: Full=Ephrin-A1;
DE AltName: Full=EPH-related receptor tyrosine kinase ligand 1;
DE Short=LERK-1;
DE AltName: Full=Immediate early response protein B61;
DE AltName: Full=Tumor necrosis factor alpha-induced protein 4;
DE Short=TNF alpha-induced protein 4;
DE Contains:
DE RecName: Full=Ephrin-A1, secreted form;
DE Flags: Precursor;
GN Name=EFNA1; Synonyms=EPLG1, LERK1, TNFAIP4;
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 VAL-159.
RX PubMed=2233719; DOI=10.1128/mcb.10.11.5830-5838.1990;
RA Holzman L.B., Marks R.M., Dixit V.M.;
RT "A novel immediate-early response gene of endothelium is induced by
RT cytokines and encodes a secreted protein.";
RL Mol. Cell. Biol. 10:5830-5838(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT VAL-159.
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT VAL-159.
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] (ISOFORM 1), AND VARIANT VAL-159.
RC TISSUE=Liver;
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 PROTEIN SEQUENCE OF 19-33.
RX PubMed=15340161; DOI=10.1110/ps.04682504;
RA Zhang Z., Henzel W.J.;
RT "Signal peptide prediction based on analysis of experimentally verified
RT cleavage sites.";
RL Protein Sci. 13:2819-2824(2004).
RN [7]
RP GPI-ANCHOR.
RX PubMed=7838529;
RA Kozlosky C.J., Maraskovsky E., McGrew J.T., Vanden Bos T., Teepe M.,
RA Lyman S.D., Srinivasan S., Fletcher F.A., Gayle R.B. III, Cerretti D.P.,
RA Beckmann M.P.;
RT "Ligands for the receptor tyrosine kinases hek and elk: isolation of cDNAs
RT encoding a family of proteins.";
RL Oncogene 10:299-306(1995).
RN [8]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=17332925;
RA Liu D.-P., Wang Y., Koeffler H.P., Xie D.;
RT "Ephrin-A1 is a negative regulator in glioma through down-regulation of
RT EphA2 and FAK.";
RL Int. J. Oncol. 30:865-871(2007).
RN [9]
RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND PROTEOLYTIC CLEAVAGE.
RX PubMed=18794797; DOI=10.1038/onc.2008.328;
RA Wykosky J., Palma E., Gibo D.M., Ringler S., Turner C.P., Debinski W.;
RT "Soluble monomeric EphrinA1 is released from tumor cells and is a
RT functional ligand for the EphA2 receptor.";
RL Oncogene 27:7260-7273(2008).
RN [10]
RP GLYCOSYLATION AT ASN-26, AND INTERACTION WITH EPHA2.
RX PubMed=23661698; DOI=10.1074/jbc.m113.464008;
RA Ferluga S., Hantgan R., Goldgur Y., Himanen J.P., Nikolov D.B.,
RA Debinski W.;
RT "Biological and structural characterization of glycosylation on ephrin-A1,
RT a preferred ligand for EphA2 receptor tyrosine kinase.";
RL J. Biol. Chem. 288:18448-18457(2013).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 19-147 IN COMPLEX WITH EPHA2,
RP SUBUNIT, DISULFIDE BOND, AND GLYCOSYLATION AT ASN-26.
RX PubMed=19525919; DOI=10.1038/embor.2009.91;
RA Himanen J.P., Goldgur Y., Miao H., Myshkin E., Guo H., Buck M., Nguyen M.,
RA Rajashankar K.R., Wang B., Nikolov D.B.;
RT "Ligand recognition by A-class Eph receptors: crystal structures of the
RT EphA2 ligand-binding domain and the EphA2/ephrin-A1 complex.";
RL EMBO Rep. 10:722-728(2009).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) OF 19-171 IN COMPLEX WITH EPHA2,
RP SUBUNIT, GLYCOSYLATION AT ASN-26, AND DISULFIDE BONDS.
RX PubMed=20505120; DOI=10.1073/pnas.1004148107;
RA Himanen J.P., Yermekbayeva L., Janes P.W., Walker J.R., Xu K., Atapattu L.,
RA Rajashankar K.R., Mensinga A., Lackmann M., Nikolov D.B., Dhe-Paganon S.;
RT "Architecture of Eph receptor clusters.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:10860-10865(2010).
CC -!- FUNCTION: Cell surface GPI-bound ligand for Eph receptors, a family of
CC receptor tyrosine kinases which are crucial for migration, repulsion
CC and adhesion during neuronal, vascular and epithelial development.
CC Binds promiscuously Eph receptors residing on adjacent cells, leading
CC to contact-dependent bidirectional signaling into neighboring cells.
CC Plays an important role in angiogenesis and tumor neovascularization.
CC The recruitment of VAV2, VAV3 and PI3-kinase p85 subunit by
CC phosphorylated EPHA2 is critical for EFNA1-induced RAC1 GTPase
CC activation and vascular endothelial cell migration and assembly. Exerts
CC anti-oncogenic effects in tumor cells through activation and down-
CC regulation of EPHA2. Activates EPHA2 by inducing tyrosine
CC phosphorylation which leads to its internalization and degradation.
CC Acts as a negative regulator in the tumorigenesis of gliomas by down-
CC regulating EPHA2 and FAK. Can evoke collapse of embryonic neuronal
CC growth cone and regulates dendritic spine morphogenesis.
CC {ECO:0000269|PubMed:17332925, ECO:0000269|PubMed:18794797}.
CC -!- SUBUNIT: Monomer. Homodimer. Forms heterodimers with EPHA2. Binds to
CC the receptor tyrosine kinases EPHA2, EPHA3, EPHA4, EPHA5, EPHA6 and
CC EPHA7. Also binds with low affinity to EPHA1.
CC {ECO:0000269|PubMed:18794797, ECO:0000269|PubMed:19525919,
CC ECO:0000269|PubMed:20505120}.
CC -!- INTERACTION:
CC P20827; P29317: EPHA2; NbExp=9; IntAct=EBI-715194, EBI-702104;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18794797};
CC Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:18794797}.
CC -!- SUBCELLULAR LOCATION: [Ephrin-A1, secreted form]: Secreted
CC {ECO:0000269|PubMed:18794797}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P20827-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P20827-2; Sequence=VSP_017543;
CC -!- TISSUE SPECIFICITY: Brain. Down-regulated in primary glioma tissues
CC compared to the normal tissues. The soluble monomeric form is expressed
CC in the glioblastoma multiforme (GBM) and breast cancer cells (at
CC protein level). {ECO:0000269|PubMed:17332925}.
CC -!- INDUCTION: By TNF and IL1B/interleukin-1 beta.
CC -!- PTM: Undergoes proteolysis by a metalloprotease to give rise to a
CC soluble monomeric form.
CC -!- PTM: N-Glycosylation is required for binding to EPHA2 receptor and
CC inducing its internalization. {ECO:0000269|PubMed:23661698}.
CC -!- SIMILARITY: Belongs to the ephrin family. {ECO:0000255|PROSITE-
CC ProRule:PRU00884}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M57730; AAA58388.1; -; mRNA.
DR EMBL; CR457416; CAG33697.1; -; mRNA.
DR EMBL; AL691442; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471121; EAW53131.1; -; Genomic_DNA.
DR EMBL; CH471121; EAW53132.1; -; Genomic_DNA.
DR EMBL; BC032698; AAH32698.1; -; mRNA.
DR EMBL; BC095432; AAH95432.1; -; mRNA.
DR CCDS; CCDS1091.1; -. [P20827-1]
DR CCDS; CCDS1092.1; -. [P20827-2]
DR PIR; A36377; A36377.
DR RefSeq; NP_004419.2; NM_004428.2. [P20827-1]
DR RefSeq; NP_872626.1; NM_182685.1. [P20827-2]
DR PDB; 3CZU; X-ray; 2.65 A; B=17-171.
DR PDB; 3HEI; X-ray; 2.00 A; B/D/F/H/J/L/N/P=18-147.
DR PDB; 3MBW; X-ray; 2.81 A; B=17-171.
DR PDBsum; 3CZU; -.
DR PDBsum; 3HEI; -.
DR PDBsum; 3MBW; -.
DR AlphaFoldDB; P20827; -.
DR SMR; P20827; -.
DR BioGRID; 108262; 11.
DR DIP; DIP-98N; -.
DR IntAct; P20827; 10.
DR MINT; P20827; -.
DR STRING; 9606.ENSP00000357392; -.
DR GlyConnect; 1209; 4 N-Linked glycans (1 site).
DR GlyGen; P20827; 2 sites, 5 N-linked glycans (1 site), 1 O-linked glycan (1 site).
DR iPTMnet; P20827; -.
DR PhosphoSitePlus; P20827; -.
DR BioMuta; EFNA1; -.
DR DMDM; 73920206; -.
DR EPD; P20827; -.
DR jPOST; P20827; -.
DR MassIVE; P20827; -.
DR MaxQB; P20827; -.
DR PaxDb; P20827; -.
DR PeptideAtlas; P20827; -.
DR PRIDE; P20827; -.
DR ProteomicsDB; 53809; -. [P20827-1]
DR ProteomicsDB; 53810; -. [P20827-2]
DR Antibodypedia; 34167; 371 antibodies from 37 providers.
DR DNASU; 1942; -.
DR Ensembl; ENST00000368406.2; ENSP00000357391.2; ENSG00000169242.12. [P20827-2]
DR Ensembl; ENST00000368407.8; ENSP00000357392.3; ENSG00000169242.12. [P20827-1]
DR GeneID; 1942; -.
DR KEGG; hsa:1942; -.
DR MANE-Select; ENST00000368407.8; ENSP00000357392.3; NM_004428.3; NP_004419.2.
DR UCSC; uc001fhh.4; human. [P20827-1]
DR CTD; 1942; -.
DR DisGeNET; 1942; -.
DR GeneCards; EFNA1; -.
DR HGNC; HGNC:3221; EFNA1.
DR HPA; ENSG00000169242; Tissue enhanced (liver).
DR MIM; 191164; gene.
DR neXtProt; NX_P20827; -.
DR OpenTargets; ENSG00000169242; -.
DR PharmGKB; PA27656; -.
DR VEuPathDB; HostDB:ENSG00000169242; -.
DR eggNOG; KOG3858; Eukaryota.
DR GeneTree; ENSGT00940000159919; -.
DR HOGENOM; CLU_081598_2_0_1; -.
DR InParanoid; P20827; -.
DR OMA; GQNSAMR; -.
DR OrthoDB; 1094764at2759; -.
DR PhylomeDB; P20827; -.
DR PathwayCommons; P20827; -.
DR Reactome; R-HSA-2682334; EPH-Ephrin signaling.
DR Reactome; R-HSA-3928663; EPHA-mediated growth cone collapse.
DR Reactome; R-HSA-3928665; EPH-ephrin mediated repulsion of cells.
DR SignaLink; P20827; -.
DR SIGNOR; P20827; -.
DR BioGRID-ORCS; 1942; 11 hits in 1079 CRISPR screens.
DR ChiTaRS; EFNA1; human.
DR EvolutionaryTrace; P20827; -.
DR GeneWiki; Ephrin_A1; -.
DR GenomeRNAi; 1942; -.
DR Pharos; P20827; Tbio.
DR PRO; PR:P20827; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; P20827; protein.
DR Bgee; ENSG00000169242; Expressed in right lobe of liver and 186 other tissues.
DR Genevisible; P20827; HS.
DR GO; GO:0046658; C:anchored component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0046875; F:ephrin receptor binding; IPI:UniProtKB.
DR GO; GO:0005102; F:signaling receptor binding; TAS:ProtInc.
DR GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
DR GO; GO:0003180; P:aortic valve morphogenesis; ISS:BHF-UCL.
DR GO; GO:0007411; P:axon guidance; IBA:GO_Central.
DR GO; GO:0016477; P:cell migration; IDA:UniProtKB.
DR GO; GO:0007267; P:cell-cell signaling; TAS:ProtInc.
DR GO; GO:0003199; P:endocardial cushion to mesenchymal transition involved in heart valve formation; ISS:BHF-UCL.
DR GO; GO:0048013; P:ephrin receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:0003183; P:mitral valve morphogenesis; ISS:BHF-UCL.
DR GO; GO:0061002; P:negative regulation of dendritic spine morphogenesis; ISS:UniProtKB.
DR GO; GO:0010719; P:negative regulation of epithelial to mesenchymal transition; ISS:BHF-UCL.
DR GO; GO:0043409; P:negative regulation of MAPK cascade; IEA:Ensembl.
DR GO; GO:1903051; P:negative regulation of proteolysis involved in protein catabolic process; IGI:ARUK-UCL.
DR GO; GO:0070244; P:negative regulation of thymocyte apoptotic process; IEA:Ensembl.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:BHF-UCL.
DR GO; GO:0014028; P:notochord formation; IEA:Ensembl.
DR GO; GO:1902004; P:positive regulation of amyloid-beta formation; IDA:ARUK-UCL.
DR GO; GO:1902961; P:positive regulation of aspartic-type endopeptidase activity involved in amyloid precursor protein catabolic process; IGI:ARUK-UCL.
DR GO; GO:0043410; P:positive regulation of MAPK cascade; IEA:Ensembl.
DR GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IDA:UniProtKB.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IGI:ARUK-UCL.
DR GO; GO:0061098; P:positive regulation of protein tyrosine kinase activity; IGI:ARUK-UCL.
DR GO; GO:0050821; P:protein stabilization; IGI:ARUK-UCL.
DR GO; GO:0045765; P:regulation of angiogenesis; IEA:Ensembl.
DR GO; GO:0050770; P:regulation of axonogenesis; IEA:Ensembl.
DR GO; GO:0043535; P:regulation of blood vessel endothelial cell migration; IEA:Ensembl.
DR GO; GO:0033628; P:regulation of cell adhesion mediated by integrin; IDA:UniProtKB.
DR GO; GO:0050730; P:regulation of peptidyl-tyrosine phosphorylation; ISS:UniProtKB.
DR GO; GO:0034446; P:substrate adhesion-dependent cell spreading; IDA:UniProtKB.
DR CDD; cd10425; Ephrin-A_Ectodomain; 1.
DR Gene3D; 2.60.40.420; -; 1.
DR InterPro; IPR008972; Cupredoxin.
DR InterPro; IPR031328; Ephrin.
DR InterPro; IPR034252; Ephrin-A_Ecto.
DR InterPro; IPR019765; Ephrin_CS.
DR InterPro; IPR001799; Ephrin_RBD.
DR PANTHER; PTHR11304; PTHR11304; 1.
DR Pfam; PF00812; Ephrin; 1.
DR PRINTS; PR01347; EPHRIN.
DR SUPFAM; SSF49503; SSF49503; 1.
DR PROSITE; PS01299; EPHRIN_RBD_1; 1.
DR PROSITE; PS51551; EPHRIN_RBD_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Angiogenesis; Cell membrane;
KW Direct protein sequencing; Disulfide bond; Glycoprotein; GPI-anchor;
KW Lipoprotein; Membrane; Reference proteome; Secreted; Signal;
KW Tumor suppressor.
FT SIGNAL 1..18
FT /evidence="ECO:0000269|PubMed:15340161"
FT CHAIN 19..182
FT /note="Ephrin-A1"
FT /id="PRO_0000008353"
FT CHAIN 19..?
FT /note="Ephrin-A1, secreted form"
FT /id="PRO_0000389630"
FT PROPEP 183..205
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000008354"
FT DOMAIN 19..151
FT /note="Ephrin RBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00884"
FT LIPID 182
FT /note="GPI-anchor amidated serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 26
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:20505120,
FT ECO:0000269|PubMed:23661698"
FT DISULFID 51..92
FT /evidence="ECO:0000269|PubMed:19525919,
FT ECO:0000269|PubMed:20505120, ECO:0007744|PDB:3HEI"
FT DISULFID 80..140
FT /evidence="ECO:0000269|PubMed:19525919,
FT ECO:0000269|PubMed:20505120, ECO:0007744|PDB:3HEI"
FT VAR_SEQ 131..152
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_017543"
FT VARIANT 159
FT /note="D -> V (in dbSNP:rs4745)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:2233719, ECO:0000269|Ref.2,
FT ECO:0000269|Ref.4"
FT /id="VAR_014791"
FT CONFLICT 180
FT /note="G -> A (in Ref. 5; AAH32698)"
FT /evidence="ECO:0000305"
FT STRAND 20..24
FT /evidence="ECO:0007829|PDB:3HEI"
FT HELIX 30..32
FT /evidence="ECO:0007829|PDB:3HEI"
FT STRAND 38..41
FT /evidence="ECO:0007829|PDB:3HEI"
FT STRAND 46..50
FT /evidence="ECO:0007829|PDB:3HEI"
FT HELIX 61..63
FT /evidence="ECO:0007829|PDB:3HEI"
FT STRAND 67..72
FT /evidence="ECO:0007829|PDB:3HEI"
FT HELIX 74..79
FT /evidence="ECO:0007829|PDB:3HEI"
FT HELIX 85..87
FT /evidence="ECO:0007829|PDB:3HEI"
FT STRAND 88..92
FT /evidence="ECO:0007829|PDB:3HEI"
FT STRAND 98..100
FT /evidence="ECO:0007829|PDB:3MBW"
FT STRAND 103..107
FT /evidence="ECO:0007829|PDB:3HEI"
FT STRAND 125..134
FT /evidence="ECO:0007829|PDB:3HEI"
FT STRAND 142..147
FT /evidence="ECO:0007829|PDB:3HEI"
SQ SEQUENCE 205 AA; 23787 MW; EFF026BF4C12461F CRC64;
MEFLWAPLLG LCCSLAAADR HTVFWNSSNP KFRNEDYTIH VQLNDYVDII CPHYEDHSVA
DAAMEQYILY LVEHEEYQLC QPQSKDQVRW QCNRPSAKHG PEKLSEKFQR FTPFTLGKEF
KEGHSYYYIS KPIHQHEDRC LRLKVTVSGK ITHSPQAHDN PQEKRLAADD PEVRVLHSIG
HSAAPRLFPL AWTVLLLPLL LLQTP
