EPHB3_HUMAN
ID EPHB3_HUMAN Reviewed; 998 AA.
AC P54753; Q7Z740;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2005, sequence version 2.
DT 03-AUG-2022, entry version 206.
DE RecName: Full=Ephrin type-B receptor 3;
DE EC=2.7.10.1;
DE AltName: Full=EPH-like tyrosine kinase 2;
DE Short=EPH-like kinase 2;
DE AltName: Full=Embryonic kinase 2;
DE Short=EK2;
DE Short=hEK2;
DE AltName: Full=Tyrosine-protein kinase TYRO6;
DE Flags: Precursor;
GN Name=EPHB3; Synonyms=ETK2, HEK2, TYRO6;
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], IDENTIFICATION OF EFNB1 AND EFNB2 AS LIGANDS,
RP AND AUTOPHOSPHORYLATION.
RC TISSUE=Embryo;
RX PubMed=8397371;
RA Boehme B., Holtrich U., Wolf G., Luzius H., Grzeschik K.-H., Strebhardt K.,
RA Ruebsamen-Waigmann H.;
RT "PCR mediated detection of a new human receptor-tyrosine-kinase, HEK 2.";
RL Oncogene 8:2857-2862(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=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 [3]
RP NOMENCLATURE.
RX PubMed=9267020; DOI=10.1016/s0092-8674(00)80500-0;
RG Eph nomenclature committee;
RT "Unified nomenclature for Eph family receptors and their ligands, the
RT ephrins.";
RL Cell 90:403-404(1997).
RN [4]
RP PHOSPHORYLATION AT TYR-614, AND MUTAGENESIS OF TYR-614 AND LYS-665.
RX PubMed=9674711; DOI=10.1038/sj.onc.1201907;
RA Hock B., Boehme B., Karn T., Feller S., Ruebsamen-Waigmann H.,
RA Strebhardt K.;
RT "Tyrosine-614, the major autophosphorylation site of the receptor tyrosine
RT kinase HEK2, functions as multi-docking site for SH2-domain mediated
RT interactions.";
RL Oncogene 17:255-260(1998).
RN [5]
RP AUTOPHOSPHORYLATION, FUNCTION IN CELL ADHESION, FUNCTION IN CELL MIGRATION,
RP AND SUBCELLULAR LOCATION.
RX PubMed=15536074; DOI=10.1074/jbc.m411383200;
RA Miao H., Strebhardt K., Pasquale E.B., Shen T.L., Guan J.L., Wang B.;
RT "Inhibition of integrin-mediated cell adhesion but not directional cell
RT migration requires catalytic activity of EphB3 receptor tyrosine kinase.
RT Role of Rho family small GTPases.";
RL J. Biol. Chem. 280:923-932(2005).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [7]
RP UBIQUITINATION BY RNF186.
RX PubMed=33280498; DOI=10.1080/15548627.2020.1851496;
RA Zhang H., Cui Z., Cheng D., Du Y., Guo X., Gao R., Chen J., Sun W., He R.,
RA Ma X., Peng Q., Martin B.N., Yan W., Rong Y., Wang C.;
RT "RNF186 regulates EFNB1 (ephrin B1)-EPHB2-induced autophagy in the colonic
RT epithelial cells for the maintenance of intestinal homeostasis.";
RL Autophagy 17:3030-3047(2021).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 39-211, AND DISULFIDE BOND.
RG Structural genomics consortium (SGC);
RT "Ligand binding domain of human EPHB3.";
RL Submitted (JAN-2011) to the PDB data bank.
RN [9]
RP VARIANTS [LARGE SCALE ANALYSIS] LEU-168; CYS-440; VAL-579; LEU-601 AND
RP TRP-724.
RX PubMed=17344846; DOI=10.1038/nature05610;
RA Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G.,
RA Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S.,
RA Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.,
RA Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K.,
RA Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D.,
RA Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R.,
RA Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A.,
RA Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F.,
RA Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F.,
RA Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G.,
RA Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R.,
RA Futreal P.A., Stratton M.R.;
RT "Patterns of somatic mutation in human cancer genomes.";
RL Nature 446:153-158(2007).
CC -!- FUNCTION: Receptor tyrosine kinase which binds promiscuously
CC transmembrane ephrin-B family ligands residing on adjacent cells,
CC leading to contact-dependent bidirectional signaling into neighboring
CC cells. The signaling pathway downstream of the receptor is referred to
CC as forward signaling while the signaling pathway downstream of the
CC ephrin ligand is referred to as reverse signaling. Generally has an
CC overlapping and redundant function with EPHB2. Like EPHB2, functions in
CC axon guidance during development regulating for instance the neurons
CC forming the corpus callosum and the anterior commissure, 2 major
CC interhemispheric connections between the temporal lobes of the cerebral
CC cortex. In addition to its role in axon guidance also plays an
CC important redundant role with other ephrin-B receptors in development
CC and maturation of dendritic spines and the formation of excitatory
CC synapses. Controls other aspects of development through regulation of
CC cell migration and positioning. This includes angiogenesis, palate
CC development and thymic epithelium development for instance. Forward and
CC reverse signaling through the EFNB2/EPHB3 complex also regulate
CC migration and adhesion of cells that tubularize the urethra and septate
CC the cloaca. Finally, plays an important role in intestinal epithelium
CC differentiation segregating progenitor from differentiated cells in the
CC crypt. {ECO:0000269|PubMed:15536074}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.1;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10028};
CC -!- SUBUNIT: Heterotetramer upon binding of the ligand. The heterotetramer
CC is composed of an ephrin dimer and a receptor dimer. Oligomerization is
CC probably required to induce biological responses (By similarity).
CC {ECO:0000250}.
CC -!- INTERACTION:
CC P54753; P37235: HPCAL1; NbExp=3; IntAct=EBI-968308, EBI-749311;
CC P54753; O75031: HSF2BP; NbExp=3; IntAct=EBI-968308, EBI-7116203;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15536074};
CC Single-pass type I membrane protein {ECO:0000269|PubMed:15536074}. Cell
CC projection, dendrite {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- PTM: Phosphorylated. Autophosphorylates upon ligand-binding.
CC Autophosphorylation on Tyr-614 is required for interaction with SH2
CC domain-containing proteins. {ECO:0000269|PubMed:9674711}.
CC -!- PTM: Ubiquitinated by RNF186, mainly through 'Lys-48' and 'Lys-63'-
CC linked polyubiquitin chains. {ECO:0000269|PubMed:33280498}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. Ephrin receptor subfamily. {ECO:0000255|PROSITE-
CC ProRule:PRU00159}.
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DR EMBL; X75208; CAA53021.1; -; mRNA.
DR EMBL; BC052968; AAH52968.1; -; mRNA.
DR CCDS; CCDS3268.1; -.
DR PIR; S37627; S37627.
DR RefSeq; NP_004434.2; NM_004443.3.
DR PDB; 3P1I; X-ray; 2.10 A; A/B/C=39-211.
DR PDB; 3ZFY; X-ray; 2.20 A; A/B=616-910.
DR PDB; 5L6O; X-ray; 1.88 A; A=616-910.
DR PDB; 5L6P; X-ray; 2.26 A; A=616-910.
DR PDBsum; 3P1I; -.
DR PDBsum; 3ZFY; -.
DR PDBsum; 5L6O; -.
DR PDBsum; 5L6P; -.
DR AlphaFoldDB; P54753; -.
DR SMR; P54753; -.
DR BioGRID; 108363; 24.
DR IntAct; P54753; 21.
DR MINT; P54753; -.
DR STRING; 9606.ENSP00000332118; -.
DR BindingDB; P54753; -.
DR ChEMBL; CHEMBL4901; -.
DR DrugCentral; P54753; -.
DR GuidetoPHARMACOLOGY; 1832; -.
DR GlyConnect; 1213; 10 N-Linked glycans (2 sites).
DR GlyGen; P54753; 3 sites, 10 N-linked glycans (2 sites), 1 O-linked glycan (1 site).
DR iPTMnet; P54753; -.
DR PhosphoSitePlus; P54753; -.
DR BioMuta; EPHB3; -.
DR DMDM; 76803655; -.
DR EPD; P54753; -.
DR jPOST; P54753; -.
DR MassIVE; P54753; -.
DR MaxQB; P54753; -.
DR PaxDb; P54753; -.
DR PeptideAtlas; P54753; -.
DR PRIDE; P54753; -.
DR ProteomicsDB; 56711; -.
DR Antibodypedia; 2107; 590 antibodies from 37 providers.
DR DNASU; 2049; -.
DR Ensembl; ENST00000330394.3; ENSP00000332118.2; ENSG00000182580.3.
DR GeneID; 2049; -.
DR KEGG; hsa:2049; -.
DR MANE-Select; ENST00000330394.3; ENSP00000332118.2; NM_004443.4; NP_004434.2.
DR UCSC; uc003foz.4; human.
DR CTD; 2049; -.
DR DisGeNET; 2049; -.
DR GeneCards; EPHB3; -.
DR HGNC; HGNC:3394; EPHB3.
DR HPA; ENSG00000182580; Tissue enhanced (skin).
DR MIM; 601839; gene.
DR neXtProt; NX_P54753; -.
DR OpenTargets; ENSG00000182580; -.
DR PharmGKB; PA27826; -.
DR VEuPathDB; HostDB:ENSG00000182580; -.
DR eggNOG; KOG0196; Eukaryota.
DR GeneTree; ENSGT00940000158024; -.
DR HOGENOM; CLU_000288_141_0_1; -.
DR InParanoid; P54753; -.
DR OMA; TSACSRC; -.
DR OrthoDB; 933071at2759; -.
DR PhylomeDB; P54753; -.
DR TreeFam; TF315608; -.
DR BRENDA; 2.7.10.1; 2681.
DR PathwayCommons; P54753; -.
DR Reactome; R-HSA-2682334; EPH-Ephrin signaling.
DR Reactome; R-HSA-3928662; EPHB-mediated forward signaling.
DR Reactome; R-HSA-3928664; Ephrin signaling.
DR Reactome; R-HSA-3928665; EPH-ephrin mediated repulsion of cells.
DR SignaLink; P54753; -.
DR SIGNOR; P54753; -.
DR BioGRID-ORCS; 2049; 14 hits in 1112 CRISPR screens.
DR ChiTaRS; EPHB3; human.
DR EvolutionaryTrace; P54753; -.
DR GeneWiki; EPHB3; -.
DR GenomeRNAi; 2049; -.
DR Pharos; P54753; Tchem.
DR PRO; PR:P54753; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; P54753; protein.
DR Bgee; ENSG00000182580; Expressed in pancreatic ductal cell and 182 other tissues.
DR Genevisible; P54753; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0043235; C:receptor complex; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008046; F:axon guidance receptor activity; IEA:Ensembl.
DR GO; GO:0005003; F:ephrin receptor activity; IDA:UniProtKB.
DR GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IBA:GO_Central.
DR GO; GO:0005005; F:transmembrane-ephrin receptor activity; IBA:GO_Central.
DR GO; GO:0001525; P:angiogenesis; ISS:UniProtKB.
DR GO; GO:0007411; P:axon guidance; ISS:UniProtKB.
DR GO; GO:0007413; P:axonal fasciculation; ISS:UniProtKB.
DR GO; GO:0016477; P:cell migration; IDA:UniProtKB.
DR GO; GO:0021952; P:central nervous system projection neuron axonogenesis; IEA:Ensembl.
DR GO; GO:0022038; P:corpus callosum development; ISS:UniProtKB.
DR GO; GO:0060996; P:dendritic spine development; ISS:UniProtKB.
DR GO; GO:0060997; P:dendritic spine morphogenesis; ISS:UniProtKB.
DR GO; GO:0048546; P:digestive tract morphogenesis; ISS:UniProtKB.
DR GO; GO:0048013; P:ephrin receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:0033674; P:positive regulation of kinase activity; IBA:GO_Central.
DR GO; GO:0051965; P:positive regulation of synapse assembly; ISS:UniProtKB.
DR GO; GO:0046777; P:protein autophosphorylation; IDA:UniProtKB.
DR GO; GO:0050770; P:regulation of axonogenesis; ISS:UniProtKB.
DR GO; GO:0022407; P:regulation of cell-cell adhesion; IDA:UniProtKB.
DR GO; GO:0043087; P:regulation of GTPase activity; IDA:UniProtKB.
DR GO; GO:0031290; P:retinal ganglion cell axon guidance; IEA:Ensembl.
DR GO; GO:0060021; P:roof of mouth development; ISS:UniProtKB.
DR GO; GO:0034446; P:substrate adhesion-dependent cell spreading; IDA:UniProtKB.
DR GO; GO:0048538; P:thymus development; ISS:UniProtKB.
DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
DR GO; GO:0001655; P:urogenital system development; ISS:UniProtKB.
DR CDD; cd10478; EphR_LBD_B3; 1.
DR CDD; cd00063; FN3; 2.
DR Gene3D; 1.10.150.50; -; 1.
DR Gene3D; 2.60.40.10; -; 2.
DR InterPro; IPR027936; Eph_TM.
DR InterPro; IPR034245; EphB3_rcpt_lig-bd.
DR InterPro; IPR001090; Ephrin_rcpt_lig-bd_dom.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001660; SAM.
DR InterPro; IPR013761; SAM/pointed_sf.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR011641; Tyr-kin_ephrin_A/B_rcpt-like.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR InterPro; IPR020635; Tyr_kinase_cat_dom.
DR InterPro; IPR016257; Tyr_kinase_ephrin_rcpt.
DR InterPro; IPR001426; Tyr_kinase_rcpt_V_CS.
DR Pfam; PF14575; EphA2_TM; 1.
DR Pfam; PF01404; Ephrin_lbd; 1.
DR Pfam; PF07699; Ephrin_rec_like; 1.
DR Pfam; PF00041; fn3; 2.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF00536; SAM_1; 1.
DR PIRSF; PIRSF000666; TyrPK_ephrin_receptor; 1.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00615; EPH_lbd; 1.
DR SMART; SM00060; FN3; 2.
DR SMART; SM00454; SAM; 1.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF47769; SSF47769; 1.
DR SUPFAM; SSF49265; SSF49265; 1.
DR SUPFAM; SSF49785; SSF49785; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS51550; EPH_LBD; 1.
DR PROSITE; PS50853; FN3; 2.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR PROSITE; PS00790; RECEPTOR_TYR_KIN_V_1; 1.
DR PROSITE; PS00791; RECEPTOR_TYR_KIN_V_2; 1.
DR PROSITE; PS50105; SAM_DOMAIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Angiogenesis; ATP-binding; Cell membrane; Cell projection;
KW Developmental protein; Disulfide bond; Glycoprotein; Kinase; Membrane;
KW Neurogenesis; Nucleotide-binding; Phosphoprotein; Receptor;
KW Reference proteome; Repeat; Signal; Transferase; Transmembrane;
KW Transmembrane helix; Tyrosine-protein kinase; Ubl conjugation.
FT SIGNAL 1..33
FT /evidence="ECO:0000255"
FT CHAIN 34..998
FT /note="Ephrin type-B receptor 3"
FT /id="PRO_0000016831"
FT TOPO_DOM 34..559
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 560..580
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 581..998
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 39..217
FT /note="Eph LBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00883"
FT DOMAIN 339..451
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 452..545
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 633..896
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 925..989
FT /note="SAM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
FT MOTIF 996..998
FT /note="PDZ-binding"
FT /evidence="ECO:0000255"
FT ACT_SITE 758
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10028"
FT BINDING 639..647
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 665
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 614
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:9674711"
FT CARBOHYD 351
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 445
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 81..199
FT /evidence="ECO:0000269|Ref.8"
FT VARIANT 168
FT /note="R -> L (in a lung small cell carcinoma sample;
FT somatic mutation)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_042176"
FT VARIANT 440
FT /note="R -> C (in dbSNP:rs56029711)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_042177"
FT VARIANT 579
FT /note="I -> V (in dbSNP:rs56103851)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_042178"
FT VARIANT 601
FT /note="I -> L (in dbSNP:rs56129875)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_042179"
FT VARIANT 724
FT /note="R -> W (in a lung neuroendocrine carcinoma sample;
FT somatic mutation; dbSNP:rs371378866)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_042180"
FT MUTAGEN 614
FT /note="Y->F: Partial loss of phosphorylation and loss of
FT interaction with SH2-containing proteins."
FT /evidence="ECO:0000269|PubMed:9674711"
FT MUTAGEN 665
FT /note="K->R: Kinase-dead. Loss of autophosphorylation."
FT /evidence="ECO:0000269|PubMed:9674711"
FT CONFLICT 367
FT /note="G -> V (in Ref. 1; CAA53021)"
FT /evidence="ECO:0000305"
FT CONFLICT 406..408
FT /note="TER -> SEP (in Ref. 1; CAA53021)"
FT /evidence="ECO:0000305"
FT CONFLICT 412
FT /note="I -> T (in Ref. 1; CAA53021)"
FT /evidence="ECO:0000305"
FT STRAND 39..44
FT /evidence="ECO:0007829|PDB:3P1I"
FT HELIX 45..47
FT /evidence="ECO:0007829|PDB:3P1I"
FT STRAND 55..58
FT /evidence="ECO:0007829|PDB:3P1I"
FT STRAND 63..68
FT /evidence="ECO:0007829|PDB:3P1I"
FT STRAND 74..80
FT /evidence="ECO:0007829|PDB:3P1I"
FT STRAND 85..87
FT /evidence="ECO:0007829|PDB:3P1I"
FT STRAND 90..93
FT /evidence="ECO:0007829|PDB:3P1I"
FT STRAND 103..114
FT /evidence="ECO:0007829|PDB:3P1I"
FT HELIX 116..118
FT /evidence="ECO:0007829|PDB:3P1I"
FT STRAND 130..139
FT /evidence="ECO:0007829|PDB:3P1I"
FT STRAND 155..160
FT /evidence="ECO:0007829|PDB:3P1I"
FT STRAND 175..181
FT /evidence="ECO:0007829|PDB:3P1I"
FT STRAND 186..198
FT /evidence="ECO:0007829|PDB:3P1I"
FT STRAND 200..210
FT /evidence="ECO:0007829|PDB:3P1I"
FT STRAND 633..640
FT /evidence="ECO:0007829|PDB:5L6O"
FT STRAND 646..652
FT /evidence="ECO:0007829|PDB:5L6O"
FT STRAND 655..657
FT /evidence="ECO:0007829|PDB:5L6P"
FT STRAND 660..666
FT /evidence="ECO:0007829|PDB:5L6O"
FT HELIX 673..687
FT /evidence="ECO:0007829|PDB:5L6O"
FT STRAND 697..701
FT /evidence="ECO:0007829|PDB:5L6O"
FT STRAND 703..706
FT /evidence="ECO:0007829|PDB:5L6O"
FT STRAND 708..712
FT /evidence="ECO:0007829|PDB:5L6O"
FT HELIX 719..725
FT /evidence="ECO:0007829|PDB:5L6O"
FT TURN 726..728
FT /evidence="ECO:0007829|PDB:5L6O"
FT HELIX 732..751
FT /evidence="ECO:0007829|PDB:5L6O"
FT HELIX 761..763
FT /evidence="ECO:0007829|PDB:5L6O"
FT STRAND 764..766
FT /evidence="ECO:0007829|PDB:5L6O"
FT STRAND 772..774
FT /evidence="ECO:0007829|PDB:5L6O"
FT STRAND 791..793
FT /evidence="ECO:0007829|PDB:5L6O"
FT STRAND 796..798
FT /evidence="ECO:0007829|PDB:5L6P"
FT HELIX 802..804
FT /evidence="ECO:0007829|PDB:5L6O"
FT HELIX 807..812
FT /evidence="ECO:0007829|PDB:5L6O"
FT HELIX 817..832
FT /evidence="ECO:0007829|PDB:5L6O"
FT TURN 838..841
FT /evidence="ECO:0007829|PDB:5L6O"
FT HELIX 844..852
FT /evidence="ECO:0007829|PDB:5L6O"
FT HELIX 865..874
FT /evidence="ECO:0007829|PDB:5L6O"
FT TURN 879..881
FT /evidence="ECO:0007829|PDB:5L6O"
FT HELIX 885..897
FT /evidence="ECO:0007829|PDB:5L6O"
FT HELIX 899..902
FT /evidence="ECO:0007829|PDB:5L6O"
SQ SEQUENCE 998 AA; 110330 MW; 9B65A4EF58B27407 CRC64;
MARARPPPPP SPPPGLLPLL PPLLLLPLLL LPAGCRALEE TLMDTKWVTS ELAWTSHPES
GWEEVSGYDE AMNPIRTYQV CNVRESSQNN WLRTGFIWRR DVQRVYVELK FTVRDCNSIP
NIPGSCKETF NLFYYEADSD VASASSPFWM ENPYVKVDTI APDESFSRLD AGRVNTKVRS
FGPLSKAGFY LAFQDQGACM SLISVRAFYK KCASTTAGFA LFPETLTGAE PTSLVIAPGT
CIPNAVEVSV PLKLYCNGDG EWMVPVGACT CATGHEPAAK ESQCRPCPPG SYKAKQGEGP
CLPCPPNSRT TSPAASICTC HNNFYRADSD SADSACTTVP SPPRGVISNV NETSLILEWS
EPRDLGGRDD LLYNVICKKC HGAGGASACS RCDDNVEFVP RQLGLTERRV HISHLLAHTR
YTFEVQAVNG VSGKSPLPPR YAAVNITTNQ AAPSEVPTLR LHSSSGSSLT LSWAPPERPN
GVILDYEMKY FEKSEGIAST VTSQMNSVQL DGLRPDARYV VQVRARTVAG YGQYSRPAEF
ETTSERGSGA QQLQEQLPLI VGSATAGLVF VVAVVVIAIV CLRKQRHGSD SEYTEKLQQY
IAPGMKVYID PFTYEDPNEA VREFAKEIDV SCVKIEEVIG AGEFGEVCRG RLKQPGRREV
FVAIKTLKVG YTERQRRDFL SEASIMGQFD HPNIIRLEGV VTKSRPVMIL TEFMENCALD
SFLRLNDGQF TVIQLVGMLR GIAAGMKYLS EMNYVHRDLA ARNILVNSNL VCKVSDFGLS
RFLEDDPSDP TYTSSLGGKI PIRWTAPEAI AYRKFTSASD VWSYGIVMWE VMSYGERPYW
DMSNQDVINA VEQDYRLPPP MDCPTALHQL MLDCWVRDRN LRPKFSQIVN TLDKLIRNAA
SLKVIASAQS GMSQPLLDRT VPDYTTFTTV GDWLDAIKMG RYKESFVSAG FASFDLVAQM
TAEDLLRIGV TLAGHQKKIL SSIQDMRLQM NQTLPVQV
