GRIK3_RAT
ID GRIK3_RAT Reviewed; 919 AA.
AC P42264; O35420;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 182.
DE RecName: Full=Glutamate receptor ionotropic, kainate 3;
DE Short=GluK3;
DE AltName: Full=Glutamate receptor 7;
DE Short=GluR-7;
DE Short=GluR7;
DE Flags: Precursor;
GN Name=Grik3; Synonyms=Glur7;
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] (ISOFORM GLUR7A).
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 [2]
RP SEQUENCE REVISION.
RA Sprengel R.;
RL Submitted (APR-1994) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM GLUR7B).
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RX PubMed=9390526; DOI=10.1016/s0896-6273(00)80404-3;
RA Schiffer H.H., Swanson G.T., Heinemann S.F.;
RT "Rat GluR7 and a carboxy-terminal splice variant, GluR7b, are functional
RT kainate receptor subunits with a low sensitivity to glutamate.";
RL Neuron 19:1141-1146(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 32-919 (ISOFORM GLUR7A).
RX PubMed=1371217; DOI=10.1016/0896-6273(92)90292-l;
RA Bettler B., Egebjerg J., Sharma G., Pecht G., Hermans-Borgmeyer I.,
RA Moll C., Stevens C.F., Heinemann S.F.;
RT "Cloning of a putative glutamate receptor: a low affinity kainate-binding
RT subunit.";
RL Neuron 8:257-265(1992).
RN [5]
RP INTERACTION WITH PRKCABP.
RX PubMed=11122333; DOI=10.1046/j.1460-9568.2000.01309.x;
RA El Far O., Airas J., Wischmeyer E., Nehring R.B., Karschin A., Betz H.;
RT "Interaction of the C-terminal tail region of the metabotropic glutamate
RT receptor 7 with the protein kinase C substrate PICK1.";
RL Eur. J. Neurosci. 12:4215-4221(2000).
RN [6]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-278, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=24090084; DOI=10.1021/pr400783j;
RA Parker B.L., Thaysen-Andersen M., Solis N., Scott N.E., Larsen M.R.,
RA Graham M.E., Packer N.H., Cordwell S.J.;
RT "Site-specific glycan-peptide analysis for determination of N-glycoproteome
RT heterogeneity.";
RL J. Proteome Res. 12:5791-5800(2013).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) OF 32-423, PROTEIN SEQUENCE OF
RP N-TERMINUS, SUBUNIT, MEMBRANE TOPOLOGY, DISULFIDE BOND, GLYCOSYLATION AT
RP ASN-70; ASN-278 AND ASN-381, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=20951142; DOI=10.1016/j.jmb.2010.10.006;
RA Kumar J., Mayer M.L.;
RT "Crystal structures of the glutamate receptor ion channel GluK3 and GluK5
RT amino-terminal domains.";
RL J. Mol. Biol. 404:680-696(2010).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 432-806 IN COMPLEX WITH GLUTAMATE,
RP FUNCTION, AND SUBUNIT.
RX PubMed=21907808; DOI=10.1016/j.jsb.2011.08.014;
RA Venskutonyte R., Frydenvang K., Gajhede M., Bunch L., Pickering D.S.,
RA Kastrup J.S.;
RT "Binding site and interlobe interactions of the ionotropic glutamate
RT receptor GluK3 ligand binding domain revealed by high resolution crystal
RT structure in complex with (S)-glutamate.";
RL J. Struct. Biol. 176:307-314(2011).
CC -!- FUNCTION: Receptor for glutamate that functions as ligand-gated ion
CC channel in the central nervous system and plays an important role in
CC excitatory synaptic transmission. L-glutamate acts as an excitatory
CC neurotransmitter at many synapses in the central nervous system. The
CC postsynaptic actions of Glu are mediated by a variety of receptors that
CC are named according to their selective agonists. This receptor binds
CC domoate > kainate >> L-glutamate = quisqualate >> AMPA = NMDA.
CC {ECO:0000269|PubMed:21907808}.
CC -!- SUBUNIT: Homotetramer, and heterotetramer with GRIK4 or GRIK5.
CC Homomeric GLUR7A and GLUR7B form functional kainate receptors. GLUR7A
CC receptors have a very low sensitivity to glutamate. GLUR7A can also
CC coassemble with either GRIK4 or GRIK5 to form heteromeric receptors.
CC Interacts with PRKCABP. Interacts with NETO2 (By similarity).
CC {ECO:0000250}.
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=2;
CC Name=GluR7A;
CC IsoId=P42264-1; Sequence=Displayed;
CC Name=GluR7B;
CC IsoId=P42264-2; Sequence=VSP_000135;
CC -!- TISSUE SPECIFICITY: Expressed in the deep cortical layers, dentate
CC gyrus, reticular thalamic nucleus, mammillary bodies, pons, and
CC cerebellum of the adult.
CC -!- DEVELOPMENTAL STAGE: Expressed in both adult and embryonic CNS.
CC -!- PTM: Mass spectrometry data suggest the protein is N-glycosylated at
CC five distinct sites. {ECO:0000269|PubMed:20951142}.
CC -!- SIMILARITY: Belongs to the glutamate-gated ion channel (TC 1.A.10.1)
CC family. GRIK3 subfamily. {ECO:0000305}.
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DR EMBL; Z11716; CAA77779.1; -; mRNA.
DR EMBL; AF027331; AAC53462.1; -; mRNA.
DR EMBL; M83552; AAC80577.1; -; mRNA.
DR PIR; I53474; I53474.
DR PIR; S19810; S19810.
DR RefSeq; NP_001106187.1; NM_001112716.1.
DR RefSeq; NP_852038.2; NM_181373.3.
DR PDB; 3OLZ; X-ray; 2.75 A; A/B=32-423.
DR PDB; 3S9E; X-ray; 1.60 A; A/B=432-546, A/B=669-806.
DR PDB; 3U92; X-ray; 1.90 A; A/B=433-546, A/B=669-807.
DR PDB; 3U93; X-ray; 1.88 A; A/B=433-546, A/B=669-807.
DR PDB; 3U94; X-ray; 1.96 A; A/B/C/D=433-546, A/B/C/D=669-807.
DR PDB; 4E0W; X-ray; 2.35 A; A=432-546, A=669-806.
DR PDB; 4G8N; X-ray; 2.30 A; A=432-546, A=669-806.
DR PDB; 4IGR; X-ray; 2.65 A; A=432-546, A=669-806.
DR PDB; 4MH5; X-ray; 1.65 A; A=432-546, A=669-806.
DR PDB; 4NWC; X-ray; 2.01 A; A=432-546, A=669-806.
DR PDB; 4NWD; X-ray; 2.60 A; A=432-546, A=669-806.
DR PDB; 5NF6; X-ray; 2.55 A; A/B=432-546, A/B=669-806.
DR PDB; 5O4F; X-ray; 2.10 A; A/B=432-546, A/B=669-806.
DR PDB; 6F28; X-ray; 2.40 A; A/B=432-546, A/B=669-806.
DR PDB; 6F29; X-ray; 2.60 A; A=432-546, A=669-806.
DR PDB; 6JFY; EM; 7.40 A; A/B/C/D=32-840.
DR PDB; 6JFZ; EM; 7.60 A; A/B/C/D=32-840.
DR PDB; 6JMV; X-ray; 1.83 A; A/B=433-546, A/B=669-807.
DR PDB; 6KZM; EM; 9.60 A; A/B/C/D=34-855.
DR PDB; 6L6F; EM; 10.60 A; A/B/C/D=32-855.
DR PDBsum; 3OLZ; -.
DR PDBsum; 3S9E; -.
DR PDBsum; 3U92; -.
DR PDBsum; 3U93; -.
DR PDBsum; 3U94; -.
DR PDBsum; 4E0W; -.
DR PDBsum; 4G8N; -.
DR PDBsum; 4IGR; -.
DR PDBsum; 4MH5; -.
DR PDBsum; 4NWC; -.
DR PDBsum; 4NWD; -.
DR PDBsum; 5NF6; -.
DR PDBsum; 5O4F; -.
DR PDBsum; 6F28; -.
DR PDBsum; 6F29; -.
DR PDBsum; 6JFY; -.
DR PDBsum; 6JFZ; -.
DR PDBsum; 6JMV; -.
DR PDBsum; 6KZM; -.
DR PDBsum; 6L6F; -.
DR AlphaFoldDB; P42264; -.
DR SMR; P42264; -.
DR STRING; 10116.ENSRNOP00000048216; -.
DR BindingDB; P42264; -.
DR ChEMBL; CHEMBL3744; -.
DR DrugCentral; P42264; -.
DR GuidetoPHARMACOLOGY; 452; -.
DR GlyGen; P42264; 10 sites.
DR iPTMnet; P42264; -.
DR PhosphoSitePlus; P42264; -.
DR PaxDb; P42264; -.
DR PRIDE; P42264; -.
DR GeneID; 298521; -.
DR KEGG; rno:298521; -.
DR UCSC; RGD:71027; rat. [P42264-1]
DR CTD; 2899; -.
DR RGD; 71027; Grik3.
DR eggNOG; KOG1052; Eukaryota.
DR InParanoid; P42264; -.
DR OrthoDB; 188544at2759; -.
DR PhylomeDB; P42264; -.
DR Reactome; R-RNO-451308; Activation of Ca-permeable Kainate Receptor.
DR Reactome; R-RNO-500657; Presynaptic function of Kainate receptors.
DR PRO; PR:P42264; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030424; C:axon; IDA:RGD.
DR GO; GO:0030425; C:dendrite; IDA:UniProtKB.
DR GO; GO:0032839; C:dendrite cytoplasm; IDA:RGD.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:RGD.
DR GO; GO:0005887; C:integral component of plasma membrane; ISO:RGD.
DR GO; GO:0032983; C:kainate selective glutamate receptor complex; IBA:GO_Central.
DR GO; GO:0043204; C:perikaryon; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0045211; C:postsynaptic membrane; IBA:GO_Central.
DR GO; GO:0042734; C:presynaptic membrane; IBA:GO_Central.
DR GO; GO:0043195; C:terminal bouton; IDA:RGD.
DR GO; GO:0001640; F:adenylate cyclase inhibiting G protein-coupled glutamate receptor activity; ISO:RGD.
DR GO; GO:0008066; F:glutamate receptor activity; IDA:RGD.
DR GO; GO:0004970; F:ionotropic glutamate receptor activity; IDA:MGI.
DR GO; GO:0015277; F:kainate selective glutamate receptor activity; ISO:RGD.
DR GO; GO:0015276; F:ligand-gated ion channel activity; IBA:GO_Central.
DR GO; GO:0099507; F:ligand-gated ion channel activity involved in regulation of presynaptic membrane potential; ISO:RGD.
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:0007268; P:chemical synaptic transmission; NAS:RGD.
DR GO; GO:0007216; P:G protein-coupled glutamate receptor signaling pathway; ISO:RGD.
DR GO; GO:0007215; P:glutamate receptor signaling pathway; ISO:RGD.
DR GO; GO:0050804; P:modulation of chemical synaptic transmission; IBA:GO_Central.
DR GO; GO:0051967; P:negative regulation of synaptic transmission, glutamatergic; IDA:UniProtKB.
DR GO; GO:0042391; P:regulation of membrane potential; IDA:MGI.
DR GO; GO:0035249; P:synaptic transmission, glutamatergic; IBA:GO_Central.
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;
KW Direct protein sequencing; Disulfide bond; Glycoprotein; Ion channel;
KW Ion transport; Isopeptide bond; Ligand-gated ion channel; Membrane;
KW Phosphoprotein; Postsynaptic cell membrane; Receptor; Reference proteome;
KW Signal; Synapse; Transmembrane; Transmembrane helix; Transport;
KW Ubl conjugation.
FT SIGNAL 1..31
FT /evidence="ECO:0000269|PubMed:20951142"
FT CHAIN 32..919
FT /note="Glutamate receptor ionotropic, kainate 3"
FT /id="PRO_0000011548"
FT TOPO_DOM 32..563
FT /note="Extracellular"
FT TRANSMEM 564..584
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 585..636
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 637..657
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 658..820
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 821..841
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 842..919
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT BINDING 520
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000269|PubMed:21907808"
FT BINDING 525
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000269|PubMed:21907808"
FT BINDING 690..692
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT BINDING 739
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000269|PubMed:21907808"
FT MOD_RES 869
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13002"
FT CARBOHYD 70
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:20951142"
FT CARBOHYD 76
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 278
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:20951142,
FT ECO:0007744|PubMed:24090084"
FT CARBOHYD 381
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:20951142"
FT CARBOHYD 415
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 426
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 433
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 548
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 551
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 752
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 99..350
FT /evidence="ECO:0000269|PubMed:20951142"
FT CROSSLNK 887
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1)"
FT /evidence="ECO:0000250|UniProtKB:Q13002"
FT VAR_SEQ 856..919
FT /note="RSFCSTVADEIRFSLTCQRRLKHKPQPPMMVKTDAVINMHTFNDRRLPGKDS
FT MSCSTSLAPVFP -> VRPWRRLRWTGKEALFLQHSGRRDPLLPHLPAASQAQATASYD
FT GQDRCGYQHAHL (in isoform GluR7B)"
FT /evidence="ECO:0000303|PubMed:9390526"
FT /id="VSP_000135"
FT CONFLICT 118
FT /note="T -> I (in Ref. 4)"
FT /evidence="ECO:0000305"
FT CONFLICT 290
FT /note="A -> P (in Ref. 4; AAC80577)"
FT /evidence="ECO:0000305"
FT CONFLICT 341
FT /note="S -> P (in Ref. 4; AAC80577)"
FT /evidence="ECO:0000305"
FT CONFLICT 355
FT /note="P -> A (in Ref. 4; AAC80577)"
FT /evidence="ECO:0000305"
FT STRAND 35..43
FT /evidence="ECO:0007829|PDB:3OLZ"
FT HELIX 47..49
FT /evidence="ECO:0007829|PDB:3OLZ"
FT HELIX 55..69
FT /evidence="ECO:0007829|PDB:3OLZ"
FT STRAND 71..74
FT /evidence="ECO:0007829|PDB:3OLZ"
FT STRAND 78..86
FT /evidence="ECO:0007829|PDB:3OLZ"
FT HELIX 91..104
FT /evidence="ECO:0007829|PDB:3OLZ"
FT STRAND 113..115
FT /evidence="ECO:0007829|PDB:3OLZ"
FT HELIX 118..128
FT /evidence="ECO:0007829|PDB:3OLZ"
FT STRAND 132..134
FT /evidence="ECO:0007829|PDB:3OLZ"
FT STRAND 148..154
FT /evidence="ECO:0007829|PDB:3OLZ"
FT HELIX 156..169
FT /evidence="ECO:0007829|PDB:3OLZ"
FT STRAND 173..181
FT /evidence="ECO:0007829|PDB:3OLZ"
FT HELIX 184..187
FT /evidence="ECO:0007829|PDB:3OLZ"
FT HELIX 189..192
FT /evidence="ECO:0007829|PDB:3OLZ"
FT TURN 195..197
FT /evidence="ECO:0007829|PDB:3OLZ"
FT STRAND 201..206
FT /evidence="ECO:0007829|PDB:3OLZ"
FT HELIX 215..223
FT /evidence="ECO:0007829|PDB:3OLZ"
FT STRAND 228..233
FT /evidence="ECO:0007829|PDB:3OLZ"
FT HELIX 235..247
FT /evidence="ECO:0007829|PDB:3OLZ"
FT STRAND 256..259
FT /evidence="ECO:0007829|PDB:3OLZ"
FT HELIX 264..266
FT /evidence="ECO:0007829|PDB:3OLZ"
FT TURN 270..275
FT /evidence="ECO:0007829|PDB:3OLZ"
FT STRAND 278..283
FT /evidence="ECO:0007829|PDB:3OLZ"
FT HELIX 290..302
FT /evidence="ECO:0007829|PDB:3OLZ"
FT HELIX 321..339
FT /evidence="ECO:0007829|PDB:3OLZ"
FT STRAND 350..352
FT /evidence="ECO:0007829|PDB:3OLZ"
FT HELIX 359..368
FT /evidence="ECO:0007829|PDB:3OLZ"
FT STRAND 370..373
FT /evidence="ECO:0007829|PDB:3OLZ"
FT STRAND 376..379
FT /evidence="ECO:0007829|PDB:3OLZ"
FT TURN 382..384
FT /evidence="ECO:0007829|PDB:3OLZ"
FT STRAND 392..398
FT /evidence="ECO:0007829|PDB:3OLZ"
FT STRAND 401..409
FT /evidence="ECO:0007829|PDB:3OLZ"
FT TURN 410..412
FT /evidence="ECO:0007829|PDB:3OLZ"
FT STRAND 413..415
FT /evidence="ECO:0007829|PDB:3OLZ"
FT STRAND 436..440
FT /evidence="ECO:0007829|PDB:3S9E"
FT TURN 444..446
FT /evidence="ECO:0007829|PDB:3S9E"
FT STRAND 447..449
FT /evidence="ECO:0007829|PDB:3S9E"
FT HELIX 458..461
FT /evidence="ECO:0007829|PDB:3S9E"
FT STRAND 462..464
FT /evidence="ECO:0007829|PDB:3S9E"
FT HELIX 465..477
FT /evidence="ECO:0007829|PDB:3S9E"
FT STRAND 481..485
FT /evidence="ECO:0007829|PDB:3S9E"
FT STRAND 496..498
FT /evidence="ECO:0007829|PDB:3U94"
FT HELIX 502..508
FT /evidence="ECO:0007829|PDB:3S9E"
FT STRAND 513..520
FT /evidence="ECO:0007829|PDB:3S9E"
FT HELIX 523..526
FT /evidence="ECO:0007829|PDB:3S9E"
FT STRAND 529..531
FT /evidence="ECO:0007829|PDB:3S9E"
FT STRAND 535..538
FT /evidence="ECO:0007829|PDB:3S9E"
FT STRAND 540..546
FT /evidence="ECO:0007829|PDB:3S9E"
FT HELIX 673..677
FT /evidence="ECO:0007829|PDB:3S9E"
FT STRAND 680..685
FT /evidence="ECO:0007829|PDB:3S9E"
FT HELIX 691..698
FT /evidence="ECO:0007829|PDB:3S9E"
FT HELIX 702..711
FT /evidence="ECO:0007829|PDB:3S9E"
FT TURN 715..717
FT /evidence="ECO:0007829|PDB:3S9E"
FT STRAND 718..721
FT /evidence="ECO:0007829|PDB:3S9E"
FT HELIX 722..731
FT /evidence="ECO:0007829|PDB:3S9E"
FT STRAND 732..739
FT /evidence="ECO:0007829|PDB:3S9E"
FT HELIX 740..749
FT /evidence="ECO:0007829|PDB:3S9E"
FT STRAND 753..757
FT /evidence="ECO:0007829|PDB:3S9E"
FT STRAND 763..770
FT /evidence="ECO:0007829|PDB:3S9E"
FT HELIX 776..788
FT /evidence="ECO:0007829|PDB:3S9E"
FT HELIX 791..800
FT /evidence="ECO:0007829|PDB:3S9E"
SQ SEQUENCE 919 AA; 104071 MW; C0739129ACF60258 CRC64;
MTAPWRRLRS LVWEYWAGFL VCAFWIPDSR GMPHVIRIGG IFEYADGPNA QVMNAEEHAF
RFSANIINRN RTLLPNTTLT YDIQRIHFHD SFEATKKACD QLALGVVAIF GPSQGSCTNA
VQSICNALEV PHIQLRWKHH PLDNKDTFYV NLYPDYASLS HAILDLVQSL KWRSATVVYD
DSTGLIRLQE LIMAPSRYNI RLKIRQLPID SDDSRPLLKE MKRGREFRII FDCSHTMAAQ
ILKQAMAMGM MTEYYHFIFT TLDLYALDLE PYRYSGVNLT GFRILNVDNA HVSAIVEKWS
MERLQAAPRA ESGLLDGVMM TDAALLYDAV HIVSVCYQRA SQMTVNSLQC HRHKPWRFGG
RFMNFIKEAQ WEGLTGRIVF NKTSGLRTDF DLDIISLKED GLEKVGVWSP ADGLNITEVA
KGRGPNVTDS LTNRSLIVTT LLEEPFVMFR KSDRTLYGND RFEGYCIDLL KELAHILGFS
YEIRLVEDGK YGAQDDKGQW NGMVKELIDH KADLAVAPLT ITHVREKAID FSKPFMTLGV
SILYRKPNGT NPSVFSFLNP LSPDIWMYVL LAYLGVSCVL FVIARFSPYE WYDAHPCNPG
SEVVENNFTL LNSFWFGMGS LMQQGSELMP KALSTRIIGG IWWFFTLIII SSYTANLAAF
LTVERMESPI DSADDLAKQT KIEYGAVKDG ATMTFFKKSK ISTFEKMWAF MSSKPSALVK
NNEEGIQRTL TADYALLMES TTIEYITQRN CNLTQIGGLI DSKGYGIGTP MGSPYRDKIT
IAILQLQEED KLHIMKEKWW RGSGCPEEEN KEASALGIQK IGGIFIVLAA GLVLSVLVAV
GEFIYKLRKT AEREQRSFCS TVADEIRFSL TCQRRLKHKP QPPMMVKTDA VINMHTFNDR
RLPGKDSMSC STSLAPVFP
