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Ephrin type-A receptor 5 (EC 2.7.10.1) (Brain-specific kinase) (EPH homology kinase 1) (EHK-1) (EPH-like kinase 7) (EK7) (hEK7)

 EPHA5_HUMAN             Reviewed;        1037 AA.
P54756; Q7Z3F2;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
22-SEP-2009, sequence version 3.
10-OCT-2018, entry version 186.
RecName: Full=Ephrin type-A receptor 5;
EC=2.7.10.1;
AltName: Full=Brain-specific kinase;
AltName: Full=EPH homology kinase 1;
Short=EHK-1;
AltName: Full=EPH-like kinase 7;
Short=EK7;
Short=hEK7;
Flags: Precursor;
Name=EPHA5; Synonyms=BSK, EHK1, HEK7, TYRO4;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, AND
TISSUE SPECIFICITY.
TISSUE=Brain;
PubMed=9191074; DOI=10.1016/S0169-328X(96)00268-9;
Miescher G.C., Taylor V., Olivieri G., Mindermann T., Shrock E.,
Steck A.J.;
"Extensive splice variation and localization of the EHK-1 receptor
tyrosine kinase in adult human brain and glial tumors.";
Brain Res. Mol. Brain Res. 46:17-24(1997).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
TISSUE=Retina;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 25-1037.
TISSUE=Brain;
PubMed=7898931;
Fox G.M., Holst P.L., Chute H.T., Lindberg R.A., Janssen A.M.,
Basu R., Welcher A.A.;
"cDNA cloning and tissue distribution of five human EPH-like receptor
protein-tyrosine kinases.";
Oncogene 10:897-905(1995).
[5]
IDENTIFICATION OF EFNA5 AS LIGAND, AND PHOSPHORYLATION.
PubMed=7748564; DOI=10.1016/0896-6273(95)90335-6;
Winslow J.W., Moran P., Valverde J., Shih A., Yuan J.Q., Wong S.C.,
Tsai S.P., Goddard A., Henzel W.J., Hefti F., Beck K.D., Caras I.W.;
"Cloning of AL-1, a ligand for an Eph-related tyrosine kinase receptor
involved in axon bundle formation.";
Neuron 14:973-981(1995).
[6]
NOMENCLATURE.
PubMed=9267020;
Eph nomenclature committee;
"Unified nomenclature for Eph family receptors and their ligands, the
ephrins.";
Cell 90:403-404(1997).
[7]
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=10375373; DOI=10.1177/002215549904700702;
Olivieri G., Miescher G.C.;
"Immunohistochemical localization of EphA5 in the adult human central
nervous system.";
J. Histochem. Cytochem. 47:855-861(1999).
[8]
VARIANTS [LARGE SCALE ANALYSIS] THR-81; ALA-235; GLN-330; GLN-417;
LYS-503; CYS-506; GLU-582; THR-672; THR-673; ILE-856; ARG-959 AND
SER-1032.
PubMed=17344846; DOI=10.1038/nature05610;
Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C.,
Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S.,
O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S.,
Bhamra G., Buck G., Choudhury B., Clements J., Cole J., Dicks E.,
Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J.,
Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K.,
Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T.,
West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P.,
Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E.,
DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E.,
Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T.,
Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.;
"Patterns of somatic mutation in human cancer genomes.";
Nature 446:153-158(2007).
-!- FUNCTION: Receptor tyrosine kinase which binds promiscuously GPI-
anchored ephrin-A family ligands residing on adjacent cells,
leading to contact-dependent bidirectional signaling into
neighboring cells. The signaling pathway downstream of the
receptor is referred to as forward signaling while the signaling
pathway downstream of the ephrin ligand is referred to as reverse
signaling. Among GPI-anchored ephrin-A ligands, EFNA5 most
probably constitutes the cognate/functional ligand for EPHA5.
Functions as an axon guidance molecule during development and may
be involved in the development of the retinotectal, entorhino-
hippocampal and hippocamposeptal pathways. Together with EFNA5
plays also a role in synaptic plasticity in adult brain through
regulation of synaptogenesis. In addition to its function in the
nervous system, the interaction of EPHA5 with EFNA5 mediates
communication between pancreatic islet cells to regulate glucose-
stimulated insulin secretion (By similarity). {ECO:0000250}.
-!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a
[protein]-L-tyrosine phosphate. {ECO:0000255|PROSITE-
ProRule:PRU10028}.
-!- SUBUNIT: Heterotetramer upon binding of the ligand. The
heterotetramer is composed of an ephrin dimer and a receptor
dimer. Oligomerization is probably required to induce biological
responses (By similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10375373};
Single-pass type I membrane protein {ECO:0000255}. Cell
projection, axon {ECO:0000250|UniProtKB:P54757}. Cell projection,
dendrite {ECO:0000269|PubMed:10375373,
ECO:0000269|PubMed:9191074}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Comment=Additional isoforms seem to exist.;
Name=1;
IsoId=P54756-1; Sequence=Displayed;
Name=2;
IsoId=P54756-2; Sequence=VSP_002999;
Name=3;
IsoId=P54756-3; Sequence=VSP_039118, VSP_039119;
-!- TISSUE SPECIFICITY: Almost exclusively expressed in the nervous
system in cortical neurons, cerebellar Purkinje cells and
pyramidal neurons within the cortex and hippocampus. Display an
increasing gradient of expression from the forebrain to hindbrain
and spinal cord. {ECO:0000269|PubMed:10375373,
ECO:0000269|PubMed:9191074}.
-!- PTM: Phosphorylated. Phosphorylation is stimulated by the ligand
EFNA5. Dephosphorylation upon stimulation by glucose, inhibits
EPHA5 forward signaling and results in insulin secretion (By
similarity). {ECO:0000250}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
kinase family. Ephrin receptor subfamily. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
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EMBL; X95425; CAA64700.1; -; mRNA.
EMBL; AC018683; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC104137; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC105923; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC115223; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BX537946; CAD97914.1; -; mRNA.
EMBL; L36644; AAA74245.1; -; mRNA.
CCDS; CCDS3513.1; -. [P54756-1]
CCDS; CCDS3514.1; -. [P54756-2]
RefSeq; NP_001268694.1; NM_001281765.2.
RefSeq; NP_001268695.1; NM_001281766.2.
RefSeq; NP_001305690.1; NM_001318761.1. [P54756-3]
RefSeq; NP_004430.4; NM_004439.7. [P54756-1]
RefSeq; NP_872272.2; NM_182472.4. [P54756-2]
UniGene; Hs.654492; -.
PDB; 2R2P; X-ray; 2.40 A; A=653-939.
PDB; 4ET7; X-ray; 2.60 A; A=59-235.
PDBsum; 2R2P; -.
PDBsum; 4ET7; -.
ProteinModelPortal; P54756; -.
SMR; P54756; -.
BioGrid; 108358; 7.
IntAct; P54756; 2.
MINT; P54756; -.
STRING; 9606.ENSP00000273854; -.
BindingDB; P54756; -.
ChEMBL; CHEMBL3987; -.
GuidetoPHARMACOLOGY; 1825; -.
iPTMnet; P54756; -.
PhosphoSitePlus; P54756; -.
BioMuta; EPHA5; -.
DMDM; 259016353; -.
EPD; P54756; -.
MaxQB; P54756; -.
PaxDb; P54756; -.
PeptideAtlas; P54756; -.
PRIDE; P54756; -.
ProteomicsDB; 56712; -.
ProteomicsDB; 56713; -. [P54756-2]
ProteomicsDB; 56714; -. [P54756-3]
TopDownProteomics; P54756-2; -. [P54756-2]
Ensembl; ENST00000273854; ENSP00000273854; ENSG00000145242. [P54756-1]
Ensembl; ENST00000354839; ENSP00000346899; ENSG00000145242. [P54756-2]
GeneID; 2044; -.
KEGG; hsa:2044; -.
UCSC; uc003hcy.5; human. [P54756-1]
CTD; 2044; -.
DisGeNET; 2044; -.
EuPathDB; HostDB:ENSG00000145242.13; -.
GeneCards; EPHA5; -.
HGNC; HGNC:3389; EPHA5.
MIM; 600004; gene.
neXtProt; NX_P54756; -.
OpenTargets; ENSG00000145242; -.
PharmGKB; PA27821; -.
eggNOG; KOG0196; Eukaryota.
eggNOG; COG0515; LUCA.
GeneTree; ENSGT00760000118975; -.
HOVERGEN; HBG062180; -.
InParanoid; P54756; -.
KO; K05106; -.
PhylomeDB; P54756; -.
TreeFam; TF315608; -.
BRENDA; 2.7.10.1; 2681.
Reactome; R-HSA-2682334; EPH-Ephrin signaling.
Reactome; R-HSA-3928663; EPHA-mediated growth cone collapse.
Reactome; R-HSA-3928665; EPH-ephrin mediated repulsion of cells.
SignaLink; P54756; -.
SIGNOR; P54756; -.
ChiTaRS; EPHA5; human.
EvolutionaryTrace; P54756; -.
GeneWiki; EPH_receptor_A5; -.
GenomeRNAi; 2044; -.
PRO; PR:P54756; -.
Proteomes; UP000005640; Chromosome 4.
Bgee; ENSG00000145242; Expressed in 96 organ(s), highest expression level in frontal cortex.
CleanEx; HS_EPHA5; -.
ExpressionAtlas; P54756; baseline and differential.
Genevisible; P54756; HS.
GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
GO; GO:0030425; C:dendrite; IDA:UniProtKB.
GO; GO:0009897; C:external side of plasma membrane; IDA:UniProtKB.
GO; GO:0005887; C:integral component of plasma membrane; IEA:InterPro.
GO; GO:0043025; C:neuronal cell body; IDA:UniProtKB.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0005791; C:rough endoplasmic reticulum; IDA:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0005003; F:ephrin receptor activity; ISS:UniProtKB.
GO; GO:0005004; F:GPI-linked ephrin receptor activity; ISS:UniProtKB.
GO; GO:0005005; F:transmembrane-ephrin receptor activity; NAS:UniProtKB.
GO; GO:0007411; P:axon guidance; ISS:UniProtKB.
GO; GO:0019933; P:cAMP-mediated signaling; ISS:UniProtKB.
GO; GO:0048013; P:ephrin receptor signaling pathway; ISS:UniProtKB.
GO; GO:0021766; P:hippocampus development; ISS:UniProtKB.
GO; GO:0048666; P:neuron development; IEP:UniProtKB.
GO; GO:0032793; P:positive regulation of CREB transcription factor activity; ISS:UniProtKB.
GO; GO:0032956; P:regulation of actin cytoskeleton organization; ISS:UniProtKB.
GO; GO:0043087; P:regulation of GTPase activity; ISS:UniProtKB.
GO; GO:0061178; P:regulation of insulin secretion involved in cellular response to glucose stimulus; ISS:UniProtKB.
CDD; cd10483; EphR_LBD_A5; 1.
CDD; cd00063; FN3; 2.
Gene3D; 2.60.120.260; -; 1.
Gene3D; 2.60.40.10; -; 2.
InterPro; IPR027936; Eph_TM.
InterPro; IPR034277; EphA5_rcpt_lig-bd.
InterPro; IPR001090; Ephrin_rcpt_lig-bd_dom.
InterPro; IPR003961; FN3_dom.
InterPro; IPR036116; FN3_sf.
InterPro; IPR008979; Galactose-bd-like_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR001660; SAM.
InterPro; IPR013761; SAM/pointed_sf.
InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
InterPro; IPR011641; Tyr-kin_ephrin_A/B_rcpt-like.
InterPro; IPR008266; Tyr_kinase_AS.
InterPro; IPR020635; Tyr_kinase_cat_dom.
InterPro; IPR016257; Tyr_kinase_ephrin_rcpt.
InterPro; IPR001426; Tyr_kinase_rcpt_V_CS.
Pfam; PF14575; EphA2_TM; 1.
Pfam; PF01404; Ephrin_lbd; 1.
Pfam; PF00041; fn3; 2.
Pfam; PF07714; Pkinase_Tyr; 1.
Pfam; PF00536; SAM_1; 1.
PIRSF; PIRSF000666; TyrPK_ephrin_receptor; 1.
PRINTS; PR00109; TYRKINASE.
SMART; SM00615; EPH_lbd; 1.
SMART; SM01411; Ephrin_rec_like; 1.
SMART; SM00060; FN3; 2.
SMART; SM00454; SAM; 1.
SMART; SM00219; TyrKc; 1.
SUPFAM; SSF47769; SSF47769; 1.
SUPFAM; SSF49265; SSF49265; 1.
SUPFAM; SSF49785; SSF49785; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS01186; EGF_2; 1.
PROSITE; PS51550; EPH_LBD; 1.
PROSITE; PS50853; FN3; 2.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PROSITE; PS00790; RECEPTOR_TYR_KIN_V_1; 1.
PROSITE; PS00791; RECEPTOR_TYR_KIN_V_2; 1.
PROSITE; PS50105; SAM_DOMAIN; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; ATP-binding; Cell membrane;
Cell projection; Complete proteome; Glycoprotein; Kinase; Membrane;
Neurogenesis; Nucleotide-binding; Phosphoprotein; Polymorphism;
Receptor; Reference proteome; Repeat; Signal; Transferase;
Transmembrane; Transmembrane helix; Tyrosine-protein kinase.
SIGNAL 1 24 {ECO:0000255}.
CHAIN 25 1037 Ephrin type-A receptor 5.
/FTId=PRO_0000016812.
TOPO_DOM 25 573 Extracellular. {ECO:0000255}.
TRANSMEM 574 594 Helical. {ECO:0000255}.
TOPO_DOM 595 1037 Cytoplasmic. {ECO:0000255}.
DOMAIN 60 238 Eph LBD. {ECO:0000255|PROSITE-
ProRule:PRU00883}.
DOMAIN 357 467 Fibronectin type-III 1.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 468 562 Fibronectin type-III 2.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 675 936 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
DOMAIN 965 1029 SAM. {ECO:0000255|PROSITE-
ProRule:PRU00184}.
NP_BIND 681 689 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOTIF 1035 1037 PDZ-binding. {ECO:0000255}.
COMPBIAS 220 354 Cys-rich.
ACT_SITE 800 800 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10028}.
BINDING 707 707 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 650 650 Phosphotyrosine; by autocatalysis.
{ECO:0000250}.
MOD_RES 656 656 Phosphotyrosine; by autocatalysis.
{ECO:0000250}.
MOD_RES 833 833 Phosphotyrosine; by autocatalysis.
{ECO:0000255}.
MOD_RES 982 982 Phosphotyrosine; by autocatalysis.
{ECO:0000250}.
CARBOHYD 264 264 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 299 299 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 369 369 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 423 423 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 436 436 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 461 461 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VAR_SEQ 1 69 Missing (in isoform 3).
{ECO:0000303|PubMed:17974005}.
/FTId=VSP_039118.
VAR_SEQ 563 563 F -> SV (in isoform 3).
{ECO:0000303|PubMed:17974005}.
/FTId=VSP_039119.
VAR_SEQ 597 619 SCCECGCGRASSLCAVAHPSLIW -> R (in isoform
2). {ECO:0000305}.
/FTId=VSP_002999.
VARIANT 81 81 N -> T (in dbSNP:rs33932471).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_042138.
VARIANT 235 235 S -> A (in dbSNP:rs55710198).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_042139.
VARIANT 330 330 E -> Q (in dbSNP:rs56205382).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_042140.
VARIANT 417 417 R -> Q (in a lung adenocarcinoma sample;
somatic mutation; dbSNP:rs199614818).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_042141.
VARIANT 503 503 E -> K (in a lung large cell carcinoma
sample; somatic mutation).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_042142.
VARIANT 506 506 Y -> C (in dbSNP:rs56074660).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_045912.
VARIANT 582 582 G -> E (in a lung adenocarcinoma sample;
somatic mutation; dbSNP:rs1057520012).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_042143.
VARIANT 672 672 A -> T (in dbSNP:rs36050417).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_042144.
VARIANT 673 673 S -> T (in dbSNP:rs56359290).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_042145.
VARIANT 856 856 T -> I (in a lung squamous cell carcinoma
sample; somatic mutation).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_042146.
VARIANT 959 959 H -> R (in dbSNP:rs56312931).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_042147.
VARIANT 1032 1032 N -> S (in a lung large cell carcinoma
sample; somatic mutation).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_042148.
CONFLICT 11 11 R -> H (in Ref. 1; CAA64700).
{ECO:0000305}.
CONFLICT 87 87 G -> D (in Ref. 3; CAD97914).
{ECO:0000305}.
CONFLICT 506 506 Y -> H (in Ref. 1; CAA64700).
{ECO:0000305}.
CONFLICT 611 611 A -> V (in Ref. 3; CAD97914).
{ECO:0000305}.
CONFLICT 616 616 S -> I (in Ref. 1; CAA64700).
{ECO:0000305}.
CONFLICT 820 820 G -> E (in Ref. 3; CAD97914).
{ECO:0000305}.
STRAND 61 65 {ECO:0000244|PDB:4ET7}.
TURN 66 68 {ECO:0000244|PDB:4ET7}.
STRAND 76 89 {ECO:0000244|PDB:4ET7}.
STRAND 95 101 {ECO:0000244|PDB:4ET7}.
STRAND 105 107 {ECO:0000244|PDB:4ET7}.
STRAND 111 114 {ECO:0000244|PDB:4ET7}.
STRAND 126 135 {ECO:0000244|PDB:4ET7}.
HELIX 137 139 {ECO:0000244|PDB:4ET7}.
STRAND 148 157 {ECO:0000244|PDB:4ET7}.
HELIX 166 168 {ECO:0000244|PDB:4ET7}.
STRAND 172 178 {ECO:0000244|PDB:4ET7}.
STRAND 188 192 {ECO:0000244|PDB:4ET7}.
STRAND 196 202 {ECO:0000244|PDB:4ET7}.
STRAND 207 219 {ECO:0000244|PDB:4ET7}.
STRAND 221 230 {ECO:0000244|PDB:4ET7}.
HELIX 663 665 {ECO:0000244|PDB:2R2P}.
HELIX 672 674 {ECO:0000244|PDB:2R2P}.
STRAND 675 683 {ECO:0000244|PDB:2R2P}.
STRAND 685 694 {ECO:0000244|PDB:2R2P}.
STRAND 702 708 {ECO:0000244|PDB:2R2P}.
HELIX 715 728 {ECO:0000244|PDB:2R2P}.
STRAND 739 743 {ECO:0000244|PDB:2R2P}.
STRAND 745 748 {ECO:0000244|PDB:2R2P}.
STRAND 750 754 {ECO:0000244|PDB:2R2P}.
HELIX 761 766 {ECO:0000244|PDB:2R2P}.
TURN 767 770 {ECO:0000244|PDB:2R2P}.
HELIX 774 793 {ECO:0000244|PDB:2R2P}.
HELIX 803 805 {ECO:0000244|PDB:2R2P}.
STRAND 806 808 {ECO:0000244|PDB:2R2P}.
STRAND 814 816 {ECO:0000244|PDB:2R2P}.
HELIX 842 844 {ECO:0000244|PDB:2R2P}.
HELIX 847 852 {ECO:0000244|PDB:2R2P}.
HELIX 857 873 {ECO:0000244|PDB:2R2P}.
TURN 878 881 {ECO:0000244|PDB:2R2P}.
HELIX 884 893 {ECO:0000244|PDB:2R2P}.
HELIX 905 914 {ECO:0000244|PDB:2R2P}.
HELIX 919 921 {ECO:0000244|PDB:2R2P}.
HELIX 925 936 {ECO:0000244|PDB:2R2P}.
SEQUENCE 1037 AA; 114803 MW; 578C2F4D950DE419 CRC64;
MRGSGPRGAG RRRPPSGGGD TPITPASLAG CYSAPRRAPL WTCLLLCAAL RTLLASPSNE
VNLLDSRTVM GDLGWIAFPK NGWEEIGEVD ENYAPIHTYQ VCKVMEQNQN NWLLTSWISN
EGASRIFIEL KFTLRDCNSL PGGLGTCKET FNMYYFESDD QNGRNIKENQ YIKIDTIAAD
ESFTELDLGD RVMKLNTEVR DVGPLSKKGF YLAFQDVGAC IALVSVRVYY KKCPSVVRHL
AVFPDTITGA DSSQLLEVSG SCVNHSVTDE PPKMHCSAEG EWLVPIGKCM CKAGYEEKNG
TCQVCRPGFF KASPHIQSCG KCPPHSYTHE EASTSCVCEK DYFRRESDPP TMACTRPPSA
PRNAISNVNE TSVFLEWIPP ADTGGRKDVS YYIACKKCNS HAGVCEECGG HVRYLPRQSG
LKNTSVMMVD LLAHTNYTFE IEAVNGVSDL SPGARQYVSV NVTTNQAAPS PVTNVKKGKI
AKNSISLSWQ EPDRPNGIIL EYEIKYFEKD QETSYTIIKS KETTITAEGL KPASVYVFQI
RARTAAGYGV FSRRFEFETT PVFAASSDQS QIPVIAVSVT VGVILLAVVI GVLLSGSCCE
CGCGRASSLC AVAHPSLIWR CGYSKAKQDP EEEKMHFHNG HIKLPGVRTY IDPHTYEDPN
QAVHEFAKEI EASCITIERV IGAGEFGEVC SGRLKLPGKR ELPVAIKTLK VGYTEKQRRD
FLGEASIMGQ FDHPNIIHLE GVVTKSKPVM IVTEYMENGS LDTFLKKNDG QFTVIQLVGM
LRGISAGMKY LSDMGYVHRD LAARNILINS NLVCKVSDFG LSRVLEDDPE AAYTTRGGKI
PIRWTAPEAI AFRKFTSASD VWSYGIVMWE VVSYGERPYW EMTNQDVIKA VEEGYRLPSP
MDCPAALYQL MLDCWQKERN SRPKFDEIVN MLDKLIRNPS SLKTLVNASC RVSNLLAEHS
PLGSGAYRSV GEWLEAIKMG RYTEIFMENG YSSMDAVAQV TLEDLRRLGV TLVGHQKKIM
NSLQEMKVQL VNGMVPL


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