ID   GRIK3_HUMAN             Reviewed;         919 AA.
AC   Q13003; A9Z1Z8; B1AMS6; Q13004; Q16136;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   04-NOV-2008, sequence version 3.
DT   27-MAR-2024, entry version 204.
DE   RecName: Full=Glutamate receptor ionotropic, kainate 3;
DE            Short=GluK3;
DE   AltName: Full=Excitatory amino acid receptor 5;
DE            Short=EAA5;
DE   AltName: Full=Glutamate receptor 7;
DE            Short=GluR-7;
DE            Short=GluR7;
DE   Flags: Precursor;
GN   Name=GRIK3; Synonyms=GLUR7;
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 [GENOMIC DNA / MRNA] (ISOFORM 1), VARIANT ALA-310, AND
RP   RNA EDITING OF POSITION 352.
RC   TISSUE=Fetal brain;
RX   PubMed=7719709;
RA   Nutt S.L., Hoo K.H., Rampersad V., Deverill R.M., Elliott C.E.,
RA   Fletcher E.J., Adams S.-L., Korczak B., Foldes R.L., Kamboj R.K.;
RT   "Molecular characterization of the human EAA5 (GluR7) receptor: a high-
RT   affinity kainate receptor with novel potential RNA editing sites.";
RL   Recept. Channels 2:315-326(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC   TISSUE=Erythroleukemia;
RA   Langer A., Xu D., Kuehcke K., Fehse B., Abdallah S., Lother H.;
RT   "Myeloid progenitor cell growth and apoptosis involves known and cell-
RT   specific ionotropic glutamate receptors.";
RL   Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16710414; DOI=10.1038/nature04727;
RA   Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA   Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA   Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA   Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA   Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA   Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA   Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA   Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA   Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA   Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA   Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA   Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA   Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA   Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA   Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA   Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA   Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA   Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA   McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA   Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA   Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA   Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA   Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA   Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA   White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA   Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA   Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA   Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT   "The DNA sequence and biological annotation of human chromosome 1.";
RL   Nature 441:315-321(2006).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 268-320.
RC   TISSUE=Placenta;
RX   PubMed=8128318; DOI=10.1007/bf01233385;
RA   Puranam R.S., Eubanks J.H., Heinemann S.F., McNamara J.O.;
RT   "Chromosomal localization of gene for human glutamate receptor subunit-7.";
RL   Somat. Cell Mol. Genet. 19:581-588(1993).
RN   [6]
RP   VARIANT ALA-310.
RX   PubMed=11124978; DOI=10.1523/jneurosci.20-24-09025.2000;
RA   Schiffer H.H., Swanson G.T., Masliah E., Heinemann S.F.;
RT   "Unequal expression of allelic kainate receptor GluR7 mRNAs in human
RT   brains.";
RL   J. Neurosci. 20:9025-9033(2000).
RN   [7]
RP   VARIANTS [LARGE SCALE ANALYSIS] HIS-215 AND HIS-391.
RX   PubMed=16959974; DOI=10.1126/science.1133427;
RA   Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA   Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA   Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA   Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA   Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA   Velculescu V.E.;
RT   "The consensus coding sequences of human breast and colorectal cancers.";
RL   Science 314:268-274(2006).
CC   -!- FUNCTION: Receptor for glutamate that functions as a 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   -!- SUBUNIT: Homotetramer, and heterotetramer with either GRIK4 or GRIK5.
CC       Interacts with PRKCABP (By similarity). Interacts with NETO2 (By
CC       similarity). {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=1;
CC         IsoId=Q13003-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q13003-2; Sequence=VSP_056588;
CC   -!- RNA EDITING: Modified_positions=352 {ECO:0000269|PubMed:7719709};
CC       Note=Partially edited.;
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; U16127; AAB60407.1; -; mRNA.
DR   EMBL; U16128; AAC50421.1; -; Genomic_DNA.
DR   EMBL; AJ249210; CAC80548.1; -; mRNA.
DR   EMBL; AC117945; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL355386; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL591883; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471059; EAX07350.1; -; Genomic_DNA.
DR   EMBL; CH471059; EAX07351.1; -; Genomic_DNA.
DR   EMBL; S69349; AAB30157.1; -; Genomic_DNA.
DR   CCDS; CCDS416.1; -. [Q13003-1]
DR   PIR; I59604; I59604.
DR   RefSeq; NP_000822.2; NM_000831.3. [Q13003-1]
DR   AlphaFoldDB; Q13003; -.
DR   EMDB; EMD-15985; -.
DR   EMDB; EMD-15986; -.
DR   SMR; Q13003; -.
DR   BioGRID; 109156; 6.
DR   IntAct; Q13003; 1.
DR   STRING; 9606.ENSP00000362183; -.
DR   BindingDB; Q13003; -.
DR   ChEMBL; CHEMBL3684; -.
DR   DrugBank; DB00237; Butabarbital.
DR   DrugBank; DB00142; Glutamic acid.
DR   DrugBank; DB00273; Topiramate.
DR   DrugCentral; Q13003; -.
DR   GuidetoPHARMACOLOGY; 452; -.
DR   GlyCosmos; Q13003; 10 sites, No reported glycans.
DR   GlyGen; Q13003; 10 sites.
DR   iPTMnet; Q13003; -.
DR   PhosphoSitePlus; Q13003; -.
DR   BioMuta; GRIK3; -.
DR   DMDM; 212276502; -.
DR   EPD; Q13003; -.
DR   jPOST; Q13003; -.
DR   MassIVE; Q13003; -.
DR   PaxDb; 9606-ENSP00000362183; -.
DR   PeptideAtlas; Q13003; -.
DR   ProteomicsDB; 2530; -.
DR   ProteomicsDB; 59094; -. [Q13003-1]
DR   Antibodypedia; 3095; 229 antibodies from 28 providers.
DR   DNASU; 2899; -.
DR   Ensembl; ENST00000373091.8; ENSP00000362183.3; ENSG00000163873.10. [Q13003-1]
DR   Ensembl; ENST00000373093.4; ENSP00000362185.4; ENSG00000163873.10. [Q13003-2]
DR   GeneID; 2899; -.
DR   KEGG; hsa:2899; -.
DR   MANE-Select; ENST00000373091.8; ENSP00000362183.3; NM_000831.4; NP_000822.2.
DR   UCSC; uc001caz.3; human. [Q13003-1]
DR   AGR; HGNC:4581; -.
DR   CTD; 2899; -.
DR   DisGeNET; 2899; -.
DR   GeneCards; GRIK3; -.
DR   HGNC; HGNC:4581; GRIK3.
DR   HPA; ENSG00000163873; Tissue enhanced (brain, intestine, pituitary gland).
DR   MIM; 138243; gene.
DR   neXtProt; NX_Q13003; -.
DR   OpenTargets; ENSG00000163873; -.
DR   PharmGKB; PA28975; -.
DR   VEuPathDB; HostDB:ENSG00000163873; -.
DR   eggNOG; KOG1052; Eukaryota.
DR   GeneTree; ENSGT00940000159465; -.
DR   HOGENOM; CLU_007257_1_1_1; -.
DR   InParanoid; Q13003; -.
DR   OMA; FMQCEIN; -.
DR   OrthoDB; 511851at2759; -.
DR   PhylomeDB; Q13003; -.
DR   TreeFam; TF334668; -.
DR   PathwayCommons; Q13003; -.
DR   Reactome; R-HSA-451308; Activation of Ca-permeable Kainate Receptor.
DR   Reactome; R-HSA-500657; Presynaptic function of Kainate receptors.
DR   SignaLink; Q13003; -.
DR   SIGNOR; Q13003; -.
DR   BioGRID-ORCS; 2899; 15 hits in 1153 CRISPR screens.
DR   ChiTaRS; GRIK3; human.
DR   GeneWiki; GRIK3; -.
DR   GenomeRNAi; 2899; -.
DR   Pharos; Q13003; Tclin.
DR   PRO; PR:Q13003; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   RNAct; Q13003; Protein.
DR   Bgee; ENSG00000163873; Expressed in cortical plate and 120 other cell types or tissues.
DR   GO; GO:0030424; C:axon; ISS:UniProtKB.
DR   GO; GO:0030425; C:dendrite; ISS:UniProtKB.
DR   GO; GO:0032839; C:dendrite cytoplasm; ISS:UniProtKB.
DR   GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR   GO; GO:0032983; C:kainate selective glutamate receptor complex; IBA:GO_Central.
DR   GO; GO:0043204; C:perikaryon; ISS:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR   GO; GO:0098839; C:postsynaptic density membrane; IBA:GO_Central.
DR   GO; GO:0042734; C:presynaptic membrane; IBA:GO_Central.
DR   GO; GO:0043195; C:terminal bouton; ISS:UniProtKB.
DR   GO; GO:0001640; F:adenylate cyclase inhibiting G protein-coupled glutamate receptor activity; IDA:UniProtKB.
DR   GO; GO:0008066; F:glutamate receptor activity; TAS:UniProtKB.
DR   GO; GO:0004970; F:glutamate-gated receptor activity; IDA:MGI.
DR   GO; GO:0015277; F:kainate selective glutamate receptor activity; IDA:UniProtKB.
DR   GO; GO:0099507; F:ligand-gated monoatomic ion channel activity involved in regulation of presynaptic membrane potential; IEA:Ensembl.
DR   GO; GO:1904315; F:transmitter-gated monoatomic ion channel activity involved in regulation of postsynaptic membrane potential; IBA:GO_Central.
DR   GO; GO:0007216; P:G protein-coupled glutamate receptor signaling pathway; IDA:UniProtKB.
DR   GO; GO:0007215; P:glutamate receptor signaling pathway; IDA:UniProtKB.
DR   GO; GO:0050804; P:modulation of chemical synaptic transmission; IBA:GO_Central.
DR   GO; GO:0051967; P:negative regulation of synaptic transmission, glutamatergic; ISS:UniProtKB.
DR   GO; GO:0042391; P:regulation of membrane potential; IDA:MGI.
DR   GO; GO:0035249; P:synaptic transmission, glutamatergic; IBA:GO_Central.
DR   CDD; cd06382; PBP1_iGluR_Kainate; 1.
DR   CDD; cd13723; PBP2_iGluR_Kainate_GluR7; 1.
DR   Gene3D; 1.10.287.70; -; 1.
DR   Gene3D; 3.40.50.2300; -; 2.
DR   Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 1.
DR   InterPro; IPR001828; ANF_lig-bd_rcpt.
DR   InterPro; IPR019594; Glu/Gly-bd.
DR   InterPro; IPR001508; Iono_Glu_rcpt_met.
DR   InterPro; IPR015683; Ionotropic_Glu_rcpt.
DR   InterPro; IPR001320; Iontro_rcpt_C.
DR   InterPro; IPR028082; Peripla_BP_I.
DR   PANTHER; PTHR18966:SF174; GLUTAMATE RECEPTOR IONOTROPIC, KAINATE 3; 1.
DR   PANTHER; PTHR18966; IONOTROPIC GLUTAMATE RECEPTOR; 1.
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; Periplasmic binding protein-like I; 1.
DR   SUPFAM; SSF53850; Periplasmic binding protein-like II; 1.
DR   Genevisible; Q13003; HS.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Cell membrane; Disulfide bond; Glycoprotein;
KW   Ion channel; Ion transport; Isopeptide bond; Ligand-gated ion channel;
KW   Membrane; Phosphoprotein; Postsynaptic cell membrane; Receptor;
KW   Reference proteome; RNA editing; Signal; Synapse; Transmembrane;
KW   Transmembrane helix; Transport; Ubl conjugation.
FT   SIGNAL          1..31
FT                   /evidence="ECO:0000255"
FT   CHAIN           32..919
FT                   /note="Glutamate receptor ionotropic, kainate 3"
FT                   /id="PRO_0000011547"
FT   TOPO_DOM        32..563
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
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:0000250"
FT   BINDING         525
FT                   /ligand="L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:29985"
FT                   /evidence="ECO:0000250"
FT   BINDING         690..692
FT                   /ligand="L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:29985"
FT                   /evidence="ECO:0000250"
FT   BINDING         739
FT                   /ligand="L-glutamate"
FT                   /ligand_id="ChEBI:CHEBI:29985"
FT                   /evidence="ECO:0000250"
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:0000255"
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:0000255"
FT   CARBOHYD        381
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
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:0000250"
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="RSFCSTVADEIRFSLTCQRRVKHKPQPPMMVKTDAVINMHTFNDRRLPGKDS
FT                   MACSTSLAPVFP -> VSLRAWSLHRMGNGDSR (in isoform 2)"
FT                   /evidence="ECO:0000303|Ref.2"
FT                   /id="VSP_056588"
FT   VARIANT         215
FT                   /note="R -> H (in a colorectal cancer sample; somatic
FT                   mutation; dbSNP:rs755366301)"
FT                   /evidence="ECO:0000269|PubMed:16959974"
FT                   /id="VAR_035695"
FT   VARIANT         310
FT                   /note="S -> A (in dbSNP:rs6691840)"
FT                   /evidence="ECO:0000269|PubMed:11124978,
FT                   ECO:0000269|PubMed:7719709"
FT                   /id="VAR_000308"
FT   VARIANT         352
FT                   /note="R -> Q (in RNA edited version)"
FT                   /id="VAR_000309"
FT   VARIANT         391
FT                   /note="D -> H (in a breast cancer sample; somatic
FT                   mutation)"
FT                   /evidence="ECO:0000269|PubMed:16959974"
FT                   /id="VAR_035696"
FT   CONFLICT        303
FT                   /note="R -> L (in Ref. 3; AAB30157)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        627
FT                   /note="E -> V (in Ref. 1; AAB60407)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        713
FT                   /note="S -> R (in Ref. 1; AAB60407)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   919 AA;  104037 MW;  0F68F6CF33E4CE71 CRC64;
     MTAPWRRLRS LVWEYWAGLL VCAFWIPDSR GMPHVIRIGG IFEYADGPNA QVMNAEEHAF
     RFSANIINRN RTLLPNTTLT YDIQRIHFHD SFEATKKACD QLALGVVAIF GPSQGSCTNA
     VQSICNALEV PHIQLRWKHH PLDNKDTFYV NLYPDYASLS HAILDLVQYL KWRSATVVYD
     DSTGLIRLQE LIMAPSRYNI RLKIRQLPID SDDSRPLLKE MKRGREFRII FDCSHTMAAQ
     ILKQAMAMGM MTEYYHFIFT TLDLYALDLE PYRYSGVNLT GFRILNVDNP HVSAIVEKWS
     MERLQAAPRS ESGLLDGVMM TDAALLYDAV HIVSVCYQRA PQMTVNSLQC HRHKAWRFGG
     RFMNFIKEAQ WEGLTGRIVF NKTSGLRTDF DLDIISLKED GLEKVGVWSP ADGLNITEVA
     KGRGPNVTDS LTNRSLIVTT VLEEPFVMFR 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
     NNEEGIQRAL TADYALLMES TTIEYVTQRN CNLTQIGGLI DSKGYGIGTP MGSPYRDKIT
     IAILQLQEED KLHIMKEKWW RGSGCPEEEN KEASALGIQK IGGIFIVLAA GLVLSVLVAV
     GEFVYKLRKT AEREQRSFCS TVADEIRFSL TCQRRVKHKP QPPMMVKTDA VINMHTFNDR
     RLPGKDSMAC STSLAPVFP
//