MUSK_RAT
ID MUSK_RAT Reviewed; 868 AA.
AC Q62838;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Muscle, skeletal receptor tyrosine protein kinase;
DE EC=2.7.10.1;
DE AltName: Full=Muscle-specific tyrosine protein kinase receptor;
DE Short=MuSK;
DE Short=Muscle-specific kinase receptor;
DE Flags: Precursor;
GN Name=Musk;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND
RP INDUCTION BY DENERVATION.
RC TISSUE=Muscle;
RX PubMed=7546737; DOI=10.1016/0896-6273(95)90146-9;
RA Valenzuela D.M., Stitt T.N., DiStefano P.S., Rojas E., Mattsson K.,
RA Compton D.L., Nunez L., Park J.S., Stark J.L., Gies D.R., Thomas S.,
RA LeBeau M.M., Fernald A.A., Copeland N.G., Jenkins N.A., Burden S.J.,
RA Glass D.J., Yancopoulos G.D.;
RT "Receptor tyrosine kinase specific for the skeletal muscle lineage:
RT expression in embryonic muscle, at the neuromuscular junction, and after
RT injury.";
RL Neuron 15:573-584(1995).
RN [2]
RP FUNCTION IN MEMORY FORMATION.
RX PubMed=16870737; DOI=10.1523/jneurosci.1674-06.2006;
RA Garcia-Osta A., Tsokas P., Pollonini G., Landau E.M., Blitzer R.,
RA Alberini C.M.;
RT "MuSK expressed in the brain mediates cholinergic responses, synaptic
RT plasticity, and memory formation.";
RL J. Neurosci. 26:7919-7932(2006).
RN [3]
RP INTERACTION WITH LRP4.
RX PubMed=18848351; DOI=10.1016/j.cell.2008.10.002;
RA Kim N., Stiegler A.L., Cameron T.O., Hallock P.T., Gomez A.M., Huang J.H.,
RA Hubbard S.R., Dustin M.L., Burden S.J.;
RT "Lrp4 is a receptor for Agrin and forms a complex with MuSK.";
RL Cell 135:334-342(2008).
RN [4]
RP INTERACTION WITH DNAJA3.
RX PubMed=19038220; DOI=10.1016/j.neuron.2008.09.025;
RA Linnoila J., Wang Y., Yao Y., Wang Z.Z.;
RT "A mammalian homolog of Drosophila tumorous imaginal discs, Tid1, mediates
RT agrin signaling at the neuromuscular junction.";
RL Neuron 60:625-641(2008).
RN [5]
RP INTERACTION WITH DOK7, ACTIVITY REGULATION, AND PHOSPHORYLATION AT TYR-754.
RX PubMed=20603078; DOI=10.1016/j.molcel.2010.06.007;
RA Bergamin E., Hallock P.T., Burden S.J., Hubbard S.R.;
RT "The cytoplasmic adaptor protein Dok7 activates the receptor tyrosine
RT kinase MuSK via dimerization.";
RL Mol. Cell 39:100-109(2010).
RN [6]
RP FUNCTION, INTERACTION WITH DOK7, PHOSPHORYLATION, AND MUTAGENESIS OF
RP VAL-789 AND MET-834.
RX PubMed=23326516; DOI=10.1371/journal.pone.0053826;
RA Ben Ammar A., Soltanzadeh P., Bauche S., Richard P., Goillot E., Herbst R.,
RA Gaudon K., Huze C., Schaeffer L., Yamanashi Y., Higuchi O., Taly A.,
RA Koenig J., Leroy J.P., Hentati F., Najmabadi H., Kahrizi K., Ilkhani M.,
RA Fardeau M., Eymard B., Hantai D.;
RT "A mutation causes MuSK reduced sensitivity to agrin and congenital
RT myasthenia.";
RL PLoS ONE 8:E53826-E53826(2013).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 560-860.
RX PubMed=12220490; DOI=10.1016/s0969-2126(02)00814-6;
RA Till J.H., Becerra M., Watty A., Lu Y., Ma Y., Neubert T.A., Burden S.J.,
RA Hubbard S.R.;
RT "Crystal structure of the MuSK tyrosine kinase: insights into receptor
RT autoregulation.";
RL Structure 10:1187-1196(2002).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.21 ANGSTROMS) OF 22-212, FUNCTION,
RP PHOSPHORYLATION, SUBUNIT, SUBCELLULAR LOCATION, MUTAGENESIS OF MET-48;
RP LEU-83 AND ILE-96, AND DISULFIDE BONDS.
RX PubMed=17011580; DOI=10.1016/j.jmb.2006.09.019;
RA Stiegler A.L., Burden S.J., Hubbard S.R.;
RT "Crystal structure of the agrin-responsive immunoglobulin-like domains 1
RT and 2 of the receptor tyrosine kinase MuSK.";
RL J. Mol. Biol. 364:424-433(2006).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 313-494, SUBUNIT, DISULFIDE BONDS,
RP AND GLYCOSYLATION AT ASN-338.
RX PubMed=19664639; DOI=10.1016/j.jmb.2009.07.091;
RA Stiegler A.L., Burden S.J., Hubbard S.R.;
RT "Crystal structure of the frizzled-like cysteine-rich domain of the
RT receptor tyrosine kinase MuSK.";
RL J. Mol. Biol. 393:1-9(2009).
CC -!- FUNCTION: Receptor tyrosine kinase which plays a central role in the
CC formation and the maintenance of the neuromuscular junction (NMJ), the
CC synapse between the motor neuron and the skeletal muscle
CC (PubMed:23326516). Recruitment of AGRIN by LRP4 to the MUSK signaling
CC complex induces phosphorylation and activation of MUSK, the kinase of
CC the complex. The activation of MUSK in myotubes regulates the formation
CC of NMJs through the regulation of different processes including the
CC specific expression of genes in subsynaptic nuclei, the reorganization
CC of the actin cytoskeleton and the clustering of the acetylcholine
CC receptors (AChR) in the postsynaptic membrane. May regulate AChR
CC phosphorylation and clustering through activation of ABL1 and Src
CC family kinases which in turn regulate MUSK. DVL1 and PAK1 that form a
CC ternary complex with MUSK are also important for MUSK-dependent
CC regulation of AChR clustering. May positively regulate Rho family
CC GTPases through FNTA. Mediates the phosphorylation of FNTA which
CC promotes prenylation, recruitment to membranes and activation of RAC1 a
CC regulator of the actin cytoskeleton and of gene expression. Other
CC effectors of the MUSK signaling include DNAJA3 which functions
CC downstream of MUSK. May also play a role within the central nervous
CC system by mediating cholinergic responses, synaptic plasticity and
CC memory formation. {ECO:0000269|PubMed:16870737,
CC ECO:0000269|PubMed:17011580, ECO:0000269|PubMed:23326516}.
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:O15146};
CC -!- ACTIVITY REGULATION: Positively regulated by CK2. {ECO:0000250}.
CC -!- SUBUNIT: Monomer (By similarity). Homodimer (Probable). Interacts with
CC LRP4; the heterodimer forms an AGRIN receptor complex that binds AGRIN
CC resulting in activation of MUSK. Forms a heterotetramer composed of 2
CC DOK7 and 2 MUSK molecules which facilitates MUSK trans-
CC autophosphorylation on tyrosine residue and activation. Interacts (via
CC cytoplasmic part) with DOK7 (via IRS-type PTB domain); requires MUSK
CC phosphorylation. Interacts with DVL1 (via DEP domain); the interaction
CC is direct and mediates the formation of a DVL1, MUSK and PAK1 ternary
CC complex involved in AChR clustering (By similarity). Interacts with
CC PDZRN3; this interaction is enhanced by agrin (By similarity).
CC Interacts with FNTA; the interaction is direct and mediates AGRIN-
CC induced phosphorylation and activation of FNTA (By similarity).
CC Interacts with CSNK2B; mediates regulation by CK2 (By similarity).
CC Interacts (via the cytoplasmic domain) with DNAJA3. Interacts with NSF;
CC may regulate MUSK endocytosis and activity (By similarity). Interacts
CC with CAV3; may regulate MUSK signaling (By similarity). Interacts with
CC RNF31 (By similarity). Interacts with DOK7 (PubMed:23326516).
CC {ECO:0000250, ECO:0000269|PubMed:23326516, ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Postsynaptic cell membrane
CC {ECO:0000305|PubMed:17011580}; Single-pass type I membrane protein
CC {ECO:0000305|PubMed:17011580}. Note=Localizes to the postsynaptic cell
CC membrane of the neuromuscular junction. {ECO:0000250|UniProtKB:O15146,
CC ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Muscle specific. {ECO:0000269|PubMed:7546737}.
CC -!- DEVELOPMENTAL STAGE: From E14.0 day, expressed in developing myotomes.
CC Once the muscle is innervated, localized to the neuromuscular junction
CC (NMJ), where its expression is restricted to synaptic nuclei.
CC Expression drops after birth. {ECO:0000269|PubMed:7546737}.
CC -!- INDUCTION: Up-regulated upon denervation (at protein level).
CC {ECO:0000269|PubMed:7546737}.
CC -!- PTM: Ubiquitinated by PDZRN3. Ubiquitination promotes endocytosis and
CC lysosomal degradation (By similarity). {ECO:0000250}.
CC -!- PTM: Phosphorylated (PubMed:23326516). Phosphorylation is induced by
CC AGRIN in a LRP4-dependent manner (PubMed:23326516). Autophosphorylated
CC (By similarity). Autophosphorylation at Tyr-553 is required for
CC interaction with DOK7 which in turn stimulates the phosphorylation and
CC the activation of MUSK (By similarity). {ECO:0000250|UniProtKB:Q61006,
CC ECO:0000269|PubMed:23326516}.
CC -!- PTM: Neddylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; U34985; AAA90956.1; -; mRNA.
DR RefSeq; NP_112323.1; NM_031061.1.
DR PDB; 1LUF; X-ray; 2.05 A; A=529-868.
DR PDB; 2IEP; X-ray; 2.21 A; A/B=22-212.
DR PDB; 3HKL; X-ray; 2.10 A; A/B=313-494.
DR PDBsum; 1LUF; -.
DR PDBsum; 2IEP; -.
DR PDBsum; 3HKL; -.
DR AlphaFoldDB; Q62838; -.
DR SMR; Q62838; -.
DR IntAct; Q62838; 7.
DR MINT; Q62838; -.
DR STRING; 10116.ENSRNOP00000041075; -.
DR GlyGen; Q62838; 3 sites.
DR iPTMnet; Q62838; -.
DR PhosphoSitePlus; Q62838; -.
DR PaxDb; Q62838; -.
DR GeneID; 81725; -.
DR KEGG; rno:81725; -.
DR UCSC; RGD:3211; rat.
DR CTD; 4593; -.
DR RGD; 3211; Musk.
DR eggNOG; KOG1026; Eukaryota.
DR InParanoid; Q62838; -.
DR OrthoDB; 471114at2759; -.
DR EvolutionaryTrace; Q62838; -.
DR PRO; PR:Q62838; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0042995; C:cell projection; IDA:RGD.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:RGD.
DR GO; GO:0005887; C:integral component of plasma membrane; ISO:RGD.
DR GO; GO:0016020; C:membrane; ISO:RGD.
DR GO; GO:0031594; C:neuromuscular junction; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0045211; C:postsynaptic membrane; ISO:RGD.
DR GO; GO:0043235; C:receptor complex; ISO:RGD.
DR GO; GO:0045202; C:synapse; ISO:RGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005518; F:collagen binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030165; F:PDZ domain binding; ISO:RGD.
DR GO; GO:0019901; F:protein kinase binding; IPI:RGD.
DR GO; GO:0004713; F:protein tyrosine kinase activity; IDA:UniProtKB.
DR GO; GO:0038062; F:protein tyrosine kinase collagen receptor activity; IBA:GO_Central.
DR GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IBA:GO_Central.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0090102; P:cochlea development; IEP:RGD.
DR GO; GO:0060291; P:long-term synaptic potentiation; IMP:RGD.
DR GO; GO:0007613; P:memory; IMP:RGD.
DR GO; GO:0010629; P:negative regulation of gene expression; IDA:RGD.
DR GO; GO:0007528; P:neuromuscular junction development; IEP:RGD.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:RGD.
DR GO; GO:0033674; P:positive regulation of kinase activity; IBA:GO_Central.
DR GO; GO:0043525; P:positive regulation of neuron apoptotic process; ISO:RGD.
DR GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IDA:RGD.
DR GO; GO:2000541; P:positive regulation of protein geranylgeranylation; ISO:RGD.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IDA:RGD.
DR GO; GO:1904395; P:positive regulation of skeletal muscle acetylcholine-gated channel clustering; ISO:RGD.
DR GO; GO:0045887; P:positive regulation of synaptic assembly at neuromuscular junction; IMP:RGD.
DR GO; GO:0032224; P:positive regulation of synaptic transmission, cholinergic; IMP:RGD.
DR GO; GO:0046777; P:protein autophosphorylation; IDA:RGD.
DR GO; GO:0043113; P:receptor clustering; IMP:RGD.
DR GO; GO:0008582; P:regulation of synaptic assembly at neuromuscular junction; ISS:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; ISO:RGD.
DR GO; GO:0048678; P:response to axon injury; IEP:RGD.
DR GO; GO:0051602; P:response to electrical stimulus; IMP:RGD.
DR GO; GO:0014850; P:response to muscle activity; IEP:RGD.
DR GO; GO:0060041; P:retina development in camera-type eye; IEP:RGD.
DR GO; GO:0071340; P:skeletal muscle acetylcholine-gated channel clustering; ISO:RGD.
DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
DR Gene3D; 1.10.2000.10; -; 1.
DR Gene3D; 2.60.40.10; -; 3.
DR InterPro; IPR020067; Frizzled_dom.
DR InterPro; IPR036790; Frizzled_dom_sf.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013098; Ig_I-set.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR InterPro; IPR020635; Tyr_kinase_cat_dom.
DR Pfam; PF01392; Fz; 1.
DR Pfam; PF07679; I-set; 3.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00409; IG; 3.
DR SMART; SM00408; IGc2; 3.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF48726; SSF48726; 3.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50038; FZ; 1.
DR PROSITE; PS50835; IG_LIKE; 3.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cell membrane; Developmental protein;
KW Differentiation; Disulfide bond; Glycoprotein; Immunoglobulin domain;
KW Kinase; Magnesium; Membrane; Metal-binding; Muscle protein;
KW Nucleotide-binding; Phosphoprotein; Postsynaptic cell membrane; Receptor;
KW Reference proteome; Repeat; Signal; Synapse; Transferase; Transmembrane;
KW Transmembrane helix; Tyrosine-protein kinase; Ubl conjugation.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..868
FT /note="Muscle, skeletal receptor tyrosine protein kinase"
FT /id="PRO_0000024448"
FT TOPO_DOM 22..494
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 495..515
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 516..868
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 28..116
FT /note="Ig-like 1"
FT DOMAIN 121..205
FT /note="Ig-like 2"
FT DOMAIN 212..302
FT /note="Ig-like 3"
FT DOMAIN 312..450
FT /note="FZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT DOMAIN 574..855
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 724
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10028"
FT BINDING 580..588
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 608
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 553
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:Q61006"
FT MOD_RES 680
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000250|UniProtKB:Q61006"
FT MOD_RES 697
FT /note="Phosphoserine; by CK2"
FT /evidence="ECO:0000250|UniProtKB:Q61006"
FT MOD_RES 754
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:20603078"
FT CARBOHYD 222
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 338
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19664639"
FT CARBOHYD 459
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 49..99
FT DISULFID 98..112
FT DISULFID 142..190
FT DISULFID 233..282
FT /evidence="ECO:0000250"
FT DISULFID 317..382
FT DISULFID 325..375
FT DISULFID 366..406
FT DISULFID 394..447
FT DISULFID 398..434
FT MUTAGEN 48
FT /note="M->R: Strongly reduced agrin-dependent activation
FT and autophosphorylation."
FT /evidence="ECO:0000269|PubMed:17011580"
FT MUTAGEN 83
FT /note="L->R: Abolishes agrin-dependent activation and
FT autophosphorylation."
FT /evidence="ECO:0000269|PubMed:17011580"
FT MUTAGEN 96
FT /note="I->A: Abolishes agrin-dependent activation and
FT autophosphorylation."
FT /evidence="ECO:0000269|PubMed:17011580"
FT MUTAGEN 789
FT /note="V->M: Reduces interaction with DOK7."
FT /evidence="ECO:0000269|PubMed:23326516"
FT MUTAGEN 834
FT /note="M->V: Reduces LRP4- and AGRIN-dependent
FT phosphorylation. Reduces DOK7-dependent phosphorylation.
FT Reduces agrin-dependent AChR aggregation in neuromuscular
FT junction. Reduces interaction with DOK7."
FT /evidence="ECO:0000269|PubMed:23326516"
FT STRAND 26..32
FT /evidence="ECO:0007829|PDB:2IEP"
FT STRAND 36..40
FT /evidence="ECO:0007829|PDB:2IEP"
FT STRAND 45..48
FT /evidence="ECO:0007829|PDB:2IEP"
FT STRAND 51..55
FT /evidence="ECO:0007829|PDB:2IEP"
FT STRAND 58..63
FT /evidence="ECO:0007829|PDB:2IEP"
FT STRAND 75..78
FT /evidence="ECO:0007829|PDB:2IEP"
FT HELIX 79..81
FT /evidence="ECO:0007829|PDB:2IEP"
FT STRAND 83..88
FT /evidence="ECO:0007829|PDB:2IEP"
FT HELIX 91..93
FT /evidence="ECO:0007829|PDB:2IEP"
FT STRAND 95..102
FT /evidence="ECO:0007829|PDB:2IEP"
FT STRAND 104..106
FT /evidence="ECO:0007829|PDB:2IEP"
FT STRAND 109..125
FT /evidence="ECO:0007829|PDB:2IEP"
FT STRAND 130..133
FT /evidence="ECO:0007829|PDB:2IEP"
FT STRAND 138..140
FT /evidence="ECO:0007829|PDB:2IEP"
FT STRAND 143..148
FT /evidence="ECO:0007829|PDB:2IEP"
FT STRAND 151..156
FT /evidence="ECO:0007829|PDB:2IEP"
FT STRAND 165..169
FT /evidence="ECO:0007829|PDB:2IEP"
FT STRAND 175..179
FT /evidence="ECO:0007829|PDB:2IEP"
FT HELIX 182..184
FT /evidence="ECO:0007829|PDB:2IEP"
FT STRAND 186..194
FT /evidence="ECO:0007829|PDB:2IEP"
FT STRAND 197..200
FT /evidence="ECO:0007829|PDB:2IEP"
FT STRAND 204..209
FT /evidence="ECO:0007829|PDB:2IEP"
FT STRAND 315..318
FT /evidence="ECO:0007829|PDB:3HKL"
FT STRAND 323..325
FT /evidence="ECO:0007829|PDB:3HKL"
FT TURN 326..328
FT /evidence="ECO:0007829|PDB:3HKL"
FT STRAND 335..338
FT /evidence="ECO:0007829|PDB:3HKL"
FT STRAND 341..343
FT /evidence="ECO:0007829|PDB:3HKL"
FT HELIX 344..359
FT /evidence="ECO:0007829|PDB:3HKL"
FT TURN 364..366
FT /evidence="ECO:0007829|PDB:3HKL"
FT HELIX 367..378
FT /evidence="ECO:0007829|PDB:3HKL"
FT STRAND 384..387
FT /evidence="ECO:0007829|PDB:3HKL"
FT HELIX 395..403
FT /evidence="ECO:0007829|PDB:3HKL"
FT TURN 404..409
FT /evidence="ECO:0007829|PDB:3HKL"
FT HELIX 410..424
FT /evidence="ECO:0007829|PDB:3HKL"
FT HELIX 434..436
FT /evidence="ECO:0007829|PDB:3HKL"
FT TURN 440..442
FT /evidence="ECO:0007829|PDB:3HKL"
FT STRAND 446..448
FT /evidence="ECO:0007829|PDB:3HKL"
FT TURN 451..453
FT /evidence="ECO:0007829|PDB:3HKL"
FT HELIX 562..566
FT /evidence="ECO:0007829|PDB:1LUF"
FT HELIX 571..573
FT /evidence="ECO:0007829|PDB:1LUF"
FT STRAND 575..582
FT /evidence="ECO:0007829|PDB:1LUF"
FT STRAND 587..594
FT /evidence="ECO:0007829|PDB:1LUF"
FT STRAND 600..609
FT /evidence="ECO:0007829|PDB:1LUF"
FT HELIX 616..630
FT /evidence="ECO:0007829|PDB:1LUF"
FT STRAND 640..644
FT /evidence="ECO:0007829|PDB:1LUF"
FT STRAND 646..649
FT /evidence="ECO:0007829|PDB:1LUF"
FT STRAND 651..655
FT /evidence="ECO:0007829|PDB:1LUF"
FT HELIX 662..668
FT /evidence="ECO:0007829|PDB:1LUF"
FT HELIX 698..717
FT /evidence="ECO:0007829|PDB:1LUF"
FT HELIX 727..729
FT /evidence="ECO:0007829|PDB:1LUF"
FT STRAND 730..732
FT /evidence="ECO:0007829|PDB:1LUF"
FT HELIX 734..736
FT /evidence="ECO:0007829|PDB:1LUF"
FT STRAND 738..740
FT /evidence="ECO:0007829|PDB:1LUF"
FT HELIX 746..749
FT /evidence="ECO:0007829|PDB:1LUF"
FT HELIX 751..753
FT /evidence="ECO:0007829|PDB:1LUF"
FT HELIX 765..767
FT /evidence="ECO:0007829|PDB:1LUF"
FT HELIX 770..775
FT /evidence="ECO:0007829|PDB:1LUF"
FT HELIX 780..795
FT /evidence="ECO:0007829|PDB:1LUF"
FT TURN 796..798
FT /evidence="ECO:0007829|PDB:1LUF"
FT TURN 801..804
FT /evidence="ECO:0007829|PDB:1LUF"
FT HELIX 807..815
FT /evidence="ECO:0007829|PDB:1LUF"
FT HELIX 828..837
FT /evidence="ECO:0007829|PDB:1LUF"
FT HELIX 842..844
FT /evidence="ECO:0007829|PDB:1LUF"
FT HELIX 848..857
FT /evidence="ECO:0007829|PDB:1LUF"
SQ SEQUENCE 868 AA; 96822 MW; C146B4E74EE25B24 CRC64;
MRELVNIPLL QMLTLVAFSG TEKLPKAPVI TTPLETVDAL VEEVATFMCA VESYPQPEIS
WTRNKILIKL FDTRYSIREN GQLLTILSVE DSDDGIYCCT ANNGVGGAVE SCGALQVKMK
PKITRPPINV KIIEGLKAVL PCTTMGNPKP SVSWIKGDSA LRENSRIAVL ESGSLRIHNV
QKEDAGQYRC VAKNSLGTAY SKLVKLEVEV FARILRAPES HNVTFGSFVT LRCTAIGMPV
PTISWIENGN AVSSGSIQEN VKDRVIDSRL QLFITKPGLY TCIATNKHGE KFSTAKAAAT
VSIAEWSKSQ KESKGYCAQY RGEVCDAVLV KDSLVFFNTS YPDPEEAQEL LIHTAWNELK
AVSPLCRPAA EALLCNHLFQ ECSPGVLPTP MPICREYCLA VKELFCAKEW LAMEGKTHRG
LYRSGMHFLP VPECSKLPSM HQDPTACTRL PYLDYKKENI TTFPSITSSK PSVDIPNLPA
STSSFAVSPA YSMTVIISIM SCFAVFALLT ITTLYCCRRR REWKNKKRES AAVTLTTLPS
ELLLDRLHPN PMYQRMPLLL NPKLLSLEYP RNNIEYVRDI GEGAFGRVFQ ARAPGLLPYE
PFTMVAVKML KEEASADMQA DFQREAALMA EFDNPNIVKL LGVCAVGKPM CLLFEYMAYG
DLNEFLRSMS PHTVCSLSHS DLSTRARVSS PGPPPLSCAE QLCIARQVAA GMAYLSERKF
VHRDLATRNC LVGENMVVKI ADFGLSRNIY SADYYKADGN DAIPIRWMPP ESIFYNRYTT
ESDVWAYGVV LWEIFSYGLQ PYYGMAHEEV IYYVRDGNIL ACPENCPLEL YNLMRLCWSK
LPADRPSFCS IHRILQRMCE RAEGTVGV
