GRIK1_RAT
ID GRIK1_RAT Reviewed; 949 AA.
AC P22756;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 3.
DT 03-AUG-2022, entry version 203.
DE RecName: Full=Glutamate receptor ionotropic, kainate 1;
DE Short=GluK1;
DE AltName: Full=Glutamate receptor 5;
DE Short=GluR-5;
DE Short=GluR5;
DE Flags: Precursor;
GN Name=Grik1; Synonyms=Glur5;
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], AND ALTERNATIVE SPLICING.
RC TISSUE=Brain;
RX PubMed=1373382; DOI=10.1002/j.1460-2075.1992.tb05211.x;
RA Sommer B., Burnashev N., Verdoorn T.A., Keinaenen K., Sakmann B.,
RA Seeburg P.H.;
RT "A glutamate receptor channel with high affinity for domoate and kainate.";
RL EMBO J. 11:1651-1656(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=1977421; DOI=10.1016/0896-6273(90)90213-y;
RA Bettler B., Boulter J., Hermans-Borgmeyer I., O'Shea-Greenfield A.,
RA Deneris E.S., Moll C., Borgmeyer U., Hollmann M., Heinemann S.F.;
RT "Cloning of a novel glutamate receptor subunit, GluR5: expression in the
RT nervous system during development.";
RL Neuron 5:583-595(1990).
RN [3]
RP INTERACTION WITH KLHL17.
RX PubMed=17062563; DOI=10.1074/jbc.m608194200;
RA Salinas G.D., Blair L.A., Needleman L.A., Gonzales J.D., Chen Y., Li M.,
RA Singer J.D., Marshall J.;
RT "Actinfilin is a Cul3 substrate adaptor, linking GluR6 kainate receptor
RT subunits to the ubiquitin-proteasome pathway.";
RL J. Biol. Chem. 281:40164-40173(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=1322826; DOI=10.1016/0014-5793(92)80753-4;
RA Lomeli H., Wisden W., Koehler M., Keinaenen K., Sommer B., Seeburg P.H.;
RT "High-affinity kainate and domoate receptors in rat brain.";
RL FEBS Lett. 307:139-143(1992).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 445-820 IN COMPLEX WITH
RP GLUTAMATE, AND SUBUNIT.
RX PubMed=15710405; DOI=10.1016/j.febslet.2005.01.012;
RA Naur P., Vestergaard B., Skov L.K., Egebjerg J., Gajhede M., Kastrup J.S.;
RT "Crystal structure of the kainate receptor GluR5 ligand-binding core in
RT complex with (S)-glutamate.";
RL FEBS Lett. 579:1154-1160(2005).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 446-821 IN COMPLEX WITH GLUTAMATE.
RX PubMed=15721240; DOI=10.1016/j.neuron.2005.01.031;
RA Mayer M.L.;
RT "Crystal structures of the GluR5 and GluR6 ligand binding cores: molecular
RT mechanisms underlying kainate receptor selectivity.";
RL Neuron 45:539-552(2005).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.74 ANGSTROMS) OF 446-820 IN COMPLEXES WITH UBP302
RP AND UBP310, FUNCTION, AND SUBUNIT.
RX PubMed=16540562; DOI=10.1523/jneurosci.0123-06.2005;
RA Mayer M.L., Ghosal A., Dolman N.P., Jane D.E.;
RT "Crystal structures of the kainate receptor GluR5 ligand binding core dimer
RT with novel GluR5-selective antagonists.";
RL J. Neurosci. 26:2852-2861(2006).
CC -!- FUNCTION: Ionotropic glutamate receptor. L-glutamate acts as an
CC excitatory neurotransmitter at many synapses in the central nervous
CC system. Binding of the excitatory neurotransmitter L-glutamate induces
CC a conformation change, leading to the opening of the cation channel,
CC and thereby converts the chemical signal to an electrical impulse. The
CC receptor then desensitizes rapidly and enters a transient inactive
CC state, characterized by the presence of bound agonist. May be involved
CC in the transmission of light information from the retina to the
CC hypothalamus. {ECO:0000269|PubMed:16540562}.
CC -!- SUBUNIT: Homotetramer or heterotetramer of pore-forming glutamate
CC receptor subunits. Tetramers may be formed by the dimerization of
CC dimers (Probable). The unedited version (Q) assembles into a functional
CC kainate-gated homomeric channel, whereas the edited version (R) is
CC unable to produce channel activity when expressed alone. Both edited
CC and unedited versions can form functional channels with GRIK4 and
CC GRIK5. Interacts with KLHL17. {ECO:0000269|PubMed:15710405,
CC ECO:0000269|PubMed:15721240, ECO:0000269|PubMed:16540562,
CC ECO:0000269|PubMed:17062563, ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC Postsynaptic cell membrane; Multi-pass membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Comment=Additional isoforms seem to exist.;
CC Name=Glur5-2C;
CC IsoId=P22756-1; Sequence=Displayed;
CC Name=Glur5-2;
CC IsoId=P22756-2; Sequence=VSP_000129, VSP_000130;
CC Name=Glur5-2A;
CC IsoId=P22756-3; Sequence=VSP_000131, VSP_000132;
CC Name=Glur5-2B; Synonyms=Glur5-1;
CC IsoId=P22756-4; Sequence=VSP_000130;
CC -!- TISSUE SPECIFICITY: Expressed in subsets of neurons throughout the
CC developing and adult central and peripheral nervous systems. In the CNS
CC principally in the medial amygdaloid nuclei, medial habenulae, pyriform
CC and cingulate cortices, and Purkinje cell layer. Also highly expressed
CC in embryonic and adult dorsal root ganglia.
CC -!- RNA EDITING: Modified_positions=636; Note=Partially edited.;
CC -!- MISCELLANEOUS: The postsynaptic actions of Glu are mediated by a
CC variety of receptors that are named according to their selective
CC agonists. This receptor binds domoate > kainate > L-glutamate =
CC quisqualate > CNQX = DNQX > AMPA > dihydrokainate > NMDA.
CC -!- SIMILARITY: Belongs to the glutamate-gated ion channel (TC 1.A.10.1)
CC family. GRIK1 subfamily. {ECO:0000305}.
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; M83560; AAA02873.1; -; mRNA.
DR EMBL; M83561; AAA02874.1; -; mRNA.
DR EMBL; Z11712; CAA77775.1; -; mRNA.
DR EMBL; Z11713; CAA77776.1; -; mRNA.
DR EMBL; Z11714; CAA77777.1; -; mRNA.
DR PIR; S19808; S19808.
DR RefSeq; NP_001104584.1; NM_001111114.1.
DR RefSeq; NP_001104587.1; NM_001111117.1.
DR RefSeq; NP_058937.1; NM_017241.2.
DR PDB; 1TXF; X-ray; 2.10 A; A=446-559, A=682-821.
DR PDB; 1VSO; X-ray; 1.85 A; A=445-559, A=682-820.
DR PDB; 1YCJ; X-ray; 1.95 A; A/B=445-559.
DR PDB; 2F34; X-ray; 1.74 A; A/B=446-559, A/B=682-821.
DR PDB; 2F35; X-ray; 1.87 A; A/B=446-559, A/B=682-821.
DR PDB; 2F36; X-ray; 2.11 A; A/B/C/D=446-559, A/B/C/D=682-821.
DR PDB; 2OJT; X-ray; 1.95 A; A/B=446-559, A/B=682-821.
DR PDB; 2PBW; X-ray; 2.50 A; A/B=445-559, A/B=682-820.
DR PDB; 2QS1; X-ray; 1.80 A; A/B=446-559, A/B=682-821.
DR PDB; 2QS2; X-ray; 1.80 A; A/B=446-559, A/B=682-821.
DR PDB; 2QS3; X-ray; 1.76 A; A/B=446-559, A/B=682-821.
DR PDB; 2QS4; X-ray; 1.58 A; A/B/C/D=446-559, A/B/C/D=682-821.
DR PDB; 2WKY; X-ray; 2.20 A; A/B=445-559, A/B=667-806.
DR PDB; 3C31; X-ray; 1.49 A; A/B=446-559, A/B=682-821.
DR PDB; 3C32; X-ray; 1.72 A; A/B=446-559, A/B=682-821.
DR PDB; 3C33; X-ray; 1.72 A; A/B=446-559, A/B=682-821.
DR PDB; 3C34; X-ray; 1.82 A; A/B=446-559, A/B=682-821.
DR PDB; 3C35; X-ray; 1.97 A; A/B=446-559, A/B=682-821.
DR PDB; 3C36; X-ray; 1.68 A; A/B=446-559, A/B=682-821.
DR PDB; 3GBA; X-ray; 1.35 A; A/B/C/D=445-559, A/B/C/D=667-820.
DR PDB; 3GBB; X-ray; 2.10 A; A/B=445-559, A/B=682-820.
DR PDB; 3S2V; X-ray; 2.50 A; A/B=445-559, A/B=667-805.
DR PDB; 4DLD; X-ray; 2.00 A; A/B=445-559, A/B=667-805.
DR PDB; 4E0X; X-ray; 2.00 A; A/B=682-820.
DR PDB; 4QF9; X-ray; 2.28 A; A/B/C=445-559, A/B/C=682-820.
DR PDB; 4YMB; X-ray; 1.93 A; A/B=445-559, A/B=682-820.
DR PDB; 5M2V; X-ray; 3.18 A; A/B=445-559, A/B=682-820.
DR PDB; 5MFQ; X-ray; 1.90 A; A/B=445-559, A/B=583-818.
DR PDB; 5MFV; X-ray; 2.18 A; A/B=445-559, A/B=583-818.
DR PDB; 5MFW; X-ray; 2.10 A; A/B=445-559, A/B=583-818.
DR PDB; 5NEB; X-ray; 2.05 A; A/B=445-559, A/B=682-820.
DR PDB; 5NF5; X-ray; 2.85 A; A/B=445-559, A/B=682-820.
DR PDB; 6FZ4; X-ray; 1.85 A; A=445-559, A=682-820.
DR PDB; 6SBT; X-ray; 2.30 A; A=445-559, A=682-820.
DR PDB; 7LVT; EM; 4.60 A; A/B/C/D=36-949.
DR PDBsum; 1TXF; -.
DR PDBsum; 1VSO; -.
DR PDBsum; 1YCJ; -.
DR PDBsum; 2F34; -.
DR PDBsum; 2F35; -.
DR PDBsum; 2F36; -.
DR PDBsum; 2OJT; -.
DR PDBsum; 2PBW; -.
DR PDBsum; 2QS1; -.
DR PDBsum; 2QS2; -.
DR PDBsum; 2QS3; -.
DR PDBsum; 2QS4; -.
DR PDBsum; 2WKY; -.
DR PDBsum; 3C31; -.
DR PDBsum; 3C32; -.
DR PDBsum; 3C33; -.
DR PDBsum; 3C34; -.
DR PDBsum; 3C35; -.
DR PDBsum; 3C36; -.
DR PDBsum; 3GBA; -.
DR PDBsum; 3GBB; -.
DR PDBsum; 3S2V; -.
DR PDBsum; 4DLD; -.
DR PDBsum; 4E0X; -.
DR PDBsum; 4QF9; -.
DR PDBsum; 4YMB; -.
DR PDBsum; 5M2V; -.
DR PDBsum; 5MFQ; -.
DR PDBsum; 5MFV; -.
DR PDBsum; 5MFW; -.
DR PDBsum; 5NEB; -.
DR PDBsum; 5NF5; -.
DR PDBsum; 6FZ4; -.
DR PDBsum; 6SBT; -.
DR PDBsum; 7LVT; -.
DR AlphaFoldDB; P22756; -.
DR SMR; P22756; -.
DR BioGRID; 248193; 3.
DR CORUM; P22756; -.
DR DIP; DIP-29257N; -.
DR STRING; 10116.ENSRNOP00000045594; -.
DR BindingDB; P22756; -.
DR ChEMBL; CHEMBL2919; -.
DR DrugCentral; P22756; -.
DR GuidetoPHARMACOLOGY; 450; -.
DR TCDB; 1.A.10.1.5; the glutamate-gated ion channel (gic) family of neurotransmitter receptors.
DR GlyGen; P22756; 9 sites.
DR iPTMnet; P22756; -.
DR PhosphoSitePlus; P22756; -.
DR jPOST; P22756; -.
DR PaxDb; P22756; -.
DR PRIDE; P22756; -.
DR GeneID; 29559; -.
DR KEGG; rno:29559; -.
DR UCSC; RGD:2732; rat. [P22756-1]
DR CTD; 2897; -.
DR RGD; 2732; Grik1.
DR eggNOG; KOG1052; Eukaryota.
DR InParanoid; P22756; -.
DR OrthoDB; 188544at2759; -.
DR PhylomeDB; P22756; -.
DR Reactome; R-RNO-451307; Activation of Na-permeable kainate receptors.
DR Reactome; R-RNO-451308; Activation of Ca-permeable Kainate Receptor.
DR EvolutionaryTrace; P22756; -.
DR PRO; PR:P22756; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030425; C:dendrite; IDA:RGD.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0099056; C:integral component of presynaptic membrane; IDA:SynGO.
DR GO; GO:0008328; C:ionotropic glutamate receptor complex; IDA:RGD.
DR GO; GO:0032983; C:kainate selective glutamate receptor complex; ISO:RGD.
DR GO; GO:0016020; C:membrane; ISO:RGD.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0014069; C:postsynaptic density; ISO:RGD.
DR GO; GO:0045211; C:postsynaptic membrane; IBA:GO_Central.
DR GO; GO:0042734; C:presynaptic membrane; ISO:RGD.
DR GO; GO:0043235; C:receptor complex; IDA:UniProtKB.
DR GO; GO:0045202; C:synapse; ISO:RGD.
DR GO; GO:0043195; C:terminal bouton; IDA:RGD.
DR GO; GO:0005234; F:extracellularly glutamate-gated ion channel activity; IDA:RGD.
DR GO; GO:0016595; F:glutamate binding; IDA:RGD.
DR GO; GO:0008066; F:glutamate receptor activity; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IPI:RGD.
DR GO; GO:0004970; F:ionotropic glutamate receptor activity; IDA:RGD.
DR GO; GO:0015277; F:kainate selective glutamate receptor activity; IDA:RGD.
DR GO; GO:0005313; F:L-glutamate transmembrane transporter activity; ISO:RGD.
DR GO; GO:0015276; F:ligand-gated ion channel activity; IBA:GO_Central.
DR GO; GO:0038023; F:signaling receptor activity; IBA:GO_Central.
DR GO; GO:1904315; F:transmitter-gated ion channel activity involved in regulation of postsynaptic membrane potential; IBA:GO_Central.
DR GO; GO:0030534; P:adult behavior; ISO:RGD.
DR GO; GO:0048266; P:behavioral response to pain; ISO:RGD.
DR GO; GO:0007268; P:chemical synaptic transmission; TAS:UniProtKB.
DR GO; GO:0060079; P:excitatory postsynaptic potential; ISO:RGD.
DR GO; GO:0060080; P:inhibitory postsynaptic potential; ISO:RGD.
DR GO; GO:0035235; P:ionotropic glutamate receptor signaling pathway; IDA:RGD.
DR GO; GO:0051899; P:membrane depolarization; ISO:RGD.
DR GO; GO:0050804; P:modulation of chemical synaptic transmission; IBA:GO_Central.
DR GO; GO:0032229; P:negative regulation of synaptic transmission, GABAergic; IDA:RGD.
DR GO; GO:0051967; P:negative regulation of synaptic transmission, glutamatergic; IDA:RGD.
DR GO; GO:0007399; P:nervous system development; IMP:RGD.
DR GO; GO:0014054; P:positive regulation of gamma-aminobutyric acid secretion; ISO:RGD.
DR GO; GO:0032230; P:positive regulation of synaptic transmission, GABAergic; IDA:RGD.
DR GO; GO:0042391; P:regulation of membrane potential; ISO:RGD.
DR GO; GO:0048172; P:regulation of short-term neuronal synaptic plasticity; IDA:RGD.
DR GO; GO:0048167; P:regulation of synaptic plasticity; TAS:UniProtKB.
DR GO; GO:0035249; P:synaptic transmission, glutamatergic; ISO:RGD.
DR InterPro; IPR001828; ANF_lig-bd_rcpt.
DR InterPro; IPR019594; Glu/Gly-bd.
DR InterPro; IPR001508; Iono_rcpt_met.
DR InterPro; IPR001320; Iontro_rcpt.
DR InterPro; IPR028082; Peripla_BP_I.
DR Pfam; PF01094; ANF_receptor; 1.
DR Pfam; PF00060; Lig_chan; 1.
DR Pfam; PF10613; Lig_chan-Glu_bd; 1.
DR PRINTS; PR00177; NMDARECEPTOR.
DR SMART; SM00918; Lig_chan-Glu_bd; 1.
DR SMART; SM00079; PBPe; 1.
DR SUPFAM; SSF53822; SSF53822; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane; Glycoprotein;
KW Ion channel; Ion transport; Ligand-gated ion channel; Membrane;
KW Phosphoprotein; Postsynaptic cell membrane; Receptor; Reference proteome;
KW RNA editing; Signal; Synapse; Transmembrane; Transmembrane helix;
KW Transport.
FT SIGNAL 1..30
FT /evidence="ECO:0000255"
FT CHAIN 31..949
FT /note="Glutamate receptor ionotropic, kainate 1"
FT /id="PRO_0000011543"
FT TOPO_DOM 31..576
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 577..597
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 598..653
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 654..674
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 675..834
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 835..855
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 856..949
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT BINDING 531..533
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT BINDING 538
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000269|PubMed:15710405,
FT ECO:0000269|PubMed:15721240"
FT BINDING 704..705
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT BINDING 753
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000269|PubMed:15710405,
FT ECO:0000269|PubMed:15721240"
FT MOD_RES 725
FT /note="Phosphoserine; by PKC"
FT /evidence="ECO:0000255"
FT MOD_RES 761
FT /note="Phosphothreonine; by PKC"
FT /evidence="ECO:0000255"
FT CARBOHYD 68
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 74
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 276
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 379
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 428
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 439
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 446
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 561
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 766
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 402..416
FT /note="Missing (in isoform Glur5-2)"
FT /evidence="ECO:0000305"
FT /id="VSP_000129"
FT VAR_SEQ 870..898
FT /note="Missing (in isoform Glur5-2B and isoform Glur5-2)"
FT /evidence="ECO:0000305"
FT /id="VSP_000130"
FT VAR_SEQ 870..871
FT /note="KG -> HY (in isoform Glur5-2A)"
FT /evidence="ECO:0000305"
FT /id="VSP_000131"
FT VAR_SEQ 872..949
FT /note="Missing (in isoform Glur5-2A)"
FT /evidence="ECO:0000305"
FT /id="VSP_000132"
FT VARIANT 636
FT /note="Q -> R (in RNA edited version)"
FT CONFLICT 282
FT /note="K -> L (in Ref. 2; AAA02874)"
FT /evidence="ECO:0000305"
FT CONFLICT 354..355
FT /note="CA -> WR (in Ref. 2; AAA02874)"
FT /evidence="ECO:0000305"
FT CONFLICT 477
FT /note="A -> G (in Ref. 2; AAA02874)"
FT /evidence="ECO:0000305"
FT STRAND 449..453
FT /evidence="ECO:0007829|PDB:3GBA"
FT TURN 457..459
FT /evidence="ECO:0007829|PDB:3GBA"
FT STRAND 460..462
FT /evidence="ECO:0007829|PDB:3GBA"
FT HELIX 471..474
FT /evidence="ECO:0007829|PDB:3GBA"
FT STRAND 475..477
FT /evidence="ECO:0007829|PDB:3GBA"
FT HELIX 478..490
FT /evidence="ECO:0007829|PDB:3GBA"
FT STRAND 494..498
FT /evidence="ECO:0007829|PDB:3GBA"
FT HELIX 515..521
FT /evidence="ECO:0007829|PDB:3GBA"
FT STRAND 526..528
FT /evidence="ECO:0007829|PDB:3GBA"
FT HELIX 536..539
FT /evidence="ECO:0007829|PDB:3GBA"
FT STRAND 542..544
FT /evidence="ECO:0007829|PDB:3GBA"
FT STRAND 548..551
FT /evidence="ECO:0007829|PDB:3GBA"
FT STRAND 553..559
FT /evidence="ECO:0007829|PDB:3GBA"
FT HELIX 686..690
FT /evidence="ECO:0007829|PDB:3GBA"
FT STRAND 693..698
FT /evidence="ECO:0007829|PDB:3GBA"
FT HELIX 704..711
FT /evidence="ECO:0007829|PDB:3GBA"
FT HELIX 715..724
FT /evidence="ECO:0007829|PDB:3GBA"
FT HELIX 726..729
FT /evidence="ECO:0007829|PDB:6FZ4"
FT STRAND 731..735
FT /evidence="ECO:0007829|PDB:3GBA"
FT HELIX 736..745
FT /evidence="ECO:0007829|PDB:3GBA"
FT STRAND 746..753
FT /evidence="ECO:0007829|PDB:3GBA"
FT HELIX 754..763
FT /evidence="ECO:0007829|PDB:3GBA"
FT STRAND 767..771
FT /evidence="ECO:0007829|PDB:3GBA"
FT STRAND 777..779
FT /evidence="ECO:0007829|PDB:3GBA"
FT STRAND 782..784
FT /evidence="ECO:0007829|PDB:3GBA"
FT HELIX 789..802
FT /evidence="ECO:0007829|PDB:3GBA"
FT HELIX 805..813
FT /evidence="ECO:0007829|PDB:3GBA"
SQ SEQUENCE 949 AA; 107840 MW; 020660BDD00054E0 CRC64;
MERSTVLIQP GLWTRDTSWT LLYFLCYILP QTSPQVLRIG GIFETVENEP VNVEELAFKF
AVTSINRNRT LMPNTTLTYD IQRINLFDSF EASRRACDQL ALGVAALFGP SHSSSVSAVQ
SICNALEVPH IQTRWKHPSV DSRDLFYINL YPDYAAISRA VLDLVLYYNW KTVTVVYEDS
TGLIRLQELI KAPSRYNIKI KIRQLPPANK DAKPLLKEMK KSKEFYVIFD CSHETAAEIL
KQILFMGMMT EYYHYFFTTL DLFALDLELY RYSGVNMTGF RKLNIDNPHV SSIIEKWSME
RLQAPPRPET GLLDGMMTTE AALMYDAVYM VAIASHRASQ LTVSSLQCHR HKPCALGPRF
MNLIKEARWD GLTGRITFNK TDGLRKDFDL DIISLKEEGT EKASGEVSKH LYKVWKKIGI
WNSNSGLNMT DGNRDRSNNI TDSLANRTLI VTTILEEPYV MYRKSDKPLY GNDRFEAYCL
DLLKELSNIL GFLYDVKLVP DGKYGAQNDK GEWNGMVKEL IDHRADLAVA PLTITYVREK
VIDFSKPFMT LGISILYRKP NGTNPGVFSF LNPLSPDIWM YVLLACLGVS CVLFVIARFT
PYEWYNPHPC NPDSDVVENN FTLLNSFWFG VGALMQQGSE LMPKALSTRI VGGIWWFFTL
IIISSYTANL AAFLTVERME SPIDSADDLA KQTKIEYGAV RDGSTMTFFK KSKISTYEKM
WAFMSSRQQS ALVKNSDEGI QRVLTTDYAL LMESTSIEYV TQRNCNLTQI GGLIDSKGYG
VGTPIGSPYR DKITIAILQL QEEGKLHMMK EKWWRGNGCP EEDSKEASAL GVENIGGIFI
VLAAGLVLSV FVAIGEFLYK SRKNNDVEQK GKSSRLRFYF RNKVRFHGSK KESLGVEKCL
SFNAIMEELG ISLKNQKKLK KKSRTKGKSS FTSILTCHQR RTQRKETVA
