GBRG2_MOUSE
ID GBRG2_MOUSE Reviewed; 474 AA.
AC P22723; Q91V50; Q91VA8;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 27-MAR-2002, sequence version 3.
DT 03-AUG-2022, entry version 196.
DE RecName: Full=Gamma-aminobutyric acid receptor subunit gamma-2;
DE AltName: Full=GABA(A) receptor subunit gamma-2;
DE Flags: Precursor;
GN Name=Gabrg2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2L AND 2S).
RX PubMed=1846404; DOI=10.1111/j.1471-4159.1991.tb08209.x;
RA Kofuji P., Wang J.B., Moss S.J., Huganir R.L., Burt D.R.;
RT "Generation of two forms of the gamma-aminobutyric acidA receptor gamma 2-
RT subunit in mice by alternative splicing.";
RL J. Neurochem. 56:713-715(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2L).
RA Sikela J.M., Shaw W.D., Khan A.S., Lin L.-H., Leidenheimer G., Siegel R.E.;
RL Submitted (APR-1991) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2L).
RC STRAIN=C57BL/6J, DBA/2J, and Various BXD strains; TISSUE=Brain;
RX PubMed=11003197; DOI=10.1111/j.1530-0277.2000.tb02100.x;
RA Hood H.M., Buck K.J.;
RT "Allelic variation in the GABA A receptor gamma2 subunit is associated with
RT genetic susceptibility to ethanol-induced motor incoordination and
RT hypothermia, conditioned taste aversion, and withdrawal in BXD/Ty
RT recombinant inbred mice.";
RL Alcohol. Clin. Exp. Res. 24:1327-1334(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2L).
RC TISSUE=Retina;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP PALMITOYLATION.
RX PubMed=15229235; DOI=10.1523/jneurosci.1037-04.2004;
RA Keller C.A., Yuan X., Panzanelli P., Martin M.L., Alldred M.,
RA Sassoe-Pognetto M., Luescher B.;
RT "The gamma2 subunit of GABA(A) receptors is a substrate for palmitoylation
RT by GODZ.";
RL J. Neurosci. 24:5881-5891(2004).
RN [6]
RP PALMITOYLATION.
RX PubMed=15207850; DOI=10.1016/j.mcn.2004.01.012;
RA Rathenberg J., Kittler J.T., Moss S.J.;
RT "Palmitoylation regulates the clustering and cell surface stability of
RT GABAA receptors.";
RL Mol. Cell. Neurosci. 26:251-257(2004).
RN [7]
RP PALMITOYLATION BY ZDHHC3, AND SUBCELLULAR LOCATION.
RX PubMed=17151279; DOI=10.1523/jneurosci.4214-06.2006;
RA Fang C., Deng L., Keller C.A., Fukata M., Fukata Y., Chen G., Luescher B.;
RT "GODZ-mediated palmitoylation of GABA(A) receptors is required for normal
RT assembly and function of GABAergic inhibitory synapses.";
RL J. Neurosci. 26:12758-12768(2006).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, AND SUBUNIT.
RX PubMed=18281286; DOI=10.1074/jbc.m709993200;
RA Saras A., Gisselmann G., Vogt-Eisele A.K., Erlkamp K.S., Kletke O.,
RA Pusch H., Hatt H.;
RT "Histamine action on vertebrate GABAA receptors: direct channel gating and
RT potentiation of GABA responses.";
RL J. Biol. Chem. 283:10470-10475(2008).
RN [9]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=25172774; DOI=10.1016/j.ejcb.2014.07.007;
RA Labonte D., Thies E., Kneussel M.;
RT "The kinesin KIF21B participates in the cell surface delivery of gamma2
RT subunit-containing GABAA receptors.";
RL Eur. J. Cell Biol. 93:338-346(2014).
RN [10]
RP FUNCTION, GLYCOSYLATION, AND DOMAIN EXTRACELLULAR.
RX PubMed=27129275; DOI=10.1074/jbc.m116.714790;
RA Brown L.E., Nicholson M.W., Arama J.E., Mercer A., Thomson A.M.,
RA Jovanovic J.N.;
RT "Gamma-aminobutyric acid type A (GABAA) receptor subunits play a direct
RT structural role in synaptic contact formation via their N-terminal
RT extracellular domains.";
RL J. Biol. Chem. 291:13926-13942(2016).
RN [11]
RP INTERACTION WITH LHFPL4.
RX PubMed=28978485; DOI=10.1016/j.celrep.2017.09.025;
RA Davenport E.C., Pendolino V., Kontou G., McGee T.P., Sheehan D.F.,
RA Lopez-Domenech G., Farrant M., Kittler J.T.;
RT "An essential role for the tetraspanin LHFPL4 in the cell-type-specific
RT targeting and clustering of synaptic GABAA ceceptors.";
RL Cell Rep. 21:70-83(2017).
RN [12]
RP SUBCELLULAR LOCATION.
RX PubMed=28279354; DOI=10.1016/j.neuron.2017.02.023;
RA Yamasaki T., Hoyos-Ramirez E., Martenson J.S., Morimoto-Tomita M.,
RA Tomita S.;
RT "GARLH family proteins stabilize GABAA receptors at synapses.";
RL Neuron 93:1138-1152(2017).
RN [13]
RP INTERACTION WITH LHFLP4.
RX PubMed=29742426; DOI=10.1016/j.celrep.2018.04.015;
RA Wu M., Tian H.L., Liu X., Lai J.H.C., Du S., Xia J.;
RT "Impairment of inhibitory synapse formation and motor behavior in mice
RT lacking the NL2 binding partner LHFPL4/GARLH4.";
RL Cell Rep. 23:1691-1705(2018).
RN [14]
RP INTERACTION WITH SHISA7.
RX PubMed=31601770; DOI=10.1126/science.aax5719;
RA Han W., Li J., Pelkey K.A., Pandey S., Chen X., Wang Y.X., Wu K., Ge L.,
RA Li T., Castellano D., Liu C., Wu L.G., Petralia R.S., Lynch J.W.,
RA McBain C.J., Lu W.;
RT "Shisa7 is a GABAA receptor auxiliary subunit controlling benzodiazepine
RT actions.";
RL Science 366:246-250(2019).
CC -!- FUNCTION: Ligand-gated chloride channel which is a component of the
CC heteropentameric receptor for GABA, the major inhibitory
CC neurotransmitter in the brain (PubMed:27129275). Plays an important
CC role in the formation of functional inhibitory GABAergic synapses in
CC addition to mediating synaptic inhibition as a GABA-gated ion channel
CC (PubMed:27129275). The gamma2 subunit is necessary but not sufficient
CC for a rapid formation of active synaptic contacts and the synaptogenic
CC effect of this subunit is influenced by the type of alpha and beta
CC subunits present in the receptor pentamer (PubMed:27129275). The
CC alpha1/beta2/gamma2 receptor, alpha2/beta2/gamma2 receptor and the
CC alpha1/beta3/gamma2 receptor exhibit synaptogenic activity whereas the
CC alpha2/beta3/gamma2 receptor shows very little or no synaptogenic
CC activity (PubMed:27129275). Functions also as histamine receptor and
CC mediates cellular responses to histamine (PubMed:18281286).
CC {ECO:0000269|PubMed:18281286, ECO:0000269|PubMed:27129275}.
CC -!- ACTIVITY REGULATION: Allosterically activated by benzodiazepines (By
CC similarity). Activated by pentobarbitol (By similarity). Inhibited by
CC the antagonist bicuculline (By similarity). Inhibited by zinc ions (By
CC similarity). {ECO:0000250|UniProtKB:P18507,
CC ECO:0000250|UniProtKB:P18508}.
CC -!- SUBUNIT: Heteropentamer, formed by a combination of alpha, beta, gamma,
CC delta and rho chains (PubMed:18281286). Interacts with GABARAP (By
CC similarity). Interacts with KIF21B (By similarity). Identified in a
CC complex of 720 kDa composed of LHFPL4, NLGN2, GABRA1, GABRB2, GABRG2
CC and GABRB3 (By similarity). Interacts with LHFPL4 (PubMed:28978485,
CC PubMed:29742426). Interacts with SHISA7; interaction leads to the
CC regulation of GABA(A) receptor trafficking, channel deactivation
CC kinetics and pharmacology (PubMed:31601770).
CC {ECO:0000250|UniProtKB:P18507, ECO:0000250|UniProtKB:P18508,
CC ECO:0000269|PubMed:18281286, ECO:0000269|PubMed:28978485,
CC ECO:0000269|PubMed:29742426, ECO:0000269|PubMed:31601770}.
CC -!- SUBCELLULAR LOCATION: Postsynaptic cell membrane
CC {ECO:0000269|PubMed:17151279, ECO:0000269|PubMed:18281286}; Multi-pass
CC membrane protein {ECO:0000255}. Cell membrane
CC {ECO:0000269|PubMed:18281286, ECO:0000269|PubMed:25172774,
CC ECO:0000269|PubMed:28279354}; Multi-pass membrane protein
CC {ECO:0000255}. Cell projection, dendrite {ECO:0000269|PubMed:25172774}.
CC Cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:P18508}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=2L;
CC IsoId=P22723-1; Sequence=Displayed;
CC Name=2S;
CC IsoId=P22723-2; Sequence=VSP_000091;
CC -!- TISSUE SPECIFICITY: Expressed in brain neurons (at protein level).
CC {ECO:0000269|PubMed:25172774}.
CC -!- DOMAIN: The extracellular domain contributes to synaptic contact
CC formation. {ECO:0000269|PubMed:27129275}.
CC -!- PTM: Glycosylated. {ECO:0000269|PubMed:27129275}.
CC -!- PTM: Palmitoylated by ZDHHC3/GODZ; required for the accumulation of
CC GABA(A) receptors at the postsynaptic membrane of inhibitory GABAergic
CC synapses. {ECO:0000269|PubMed:15207850, ECO:0000269|PubMed:15229235,
CC ECO:0000269|PubMed:17151279}.
CC -!- MISCELLANEOUS: This subunit carries the benzodiazepine binding site.
CC -!- SIMILARITY: Belongs to the ligand-gated ion channel (TC 1.A.9) family.
CC Gamma-aminobutyric acid receptor (TC 1.A.9.5) subfamily. GABRG2 sub-
CC subfamily. {ECO:0000305}.
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DR EMBL; M86572; AAB59635.1; -; mRNA.
DR EMBL; M62374; AAA37653.1; -; mRNA.
DR EMBL; AF233775; AAK71573.1; -; mRNA.
DR EMBL; AF233776; AAK71574.1; -; mRNA.
DR EMBL; AF233777; AAK71575.1; -; mRNA.
DR EMBL; AF233778; AAK71576.1; -; mRNA.
DR EMBL; AF233779; AAK71577.1; -; mRNA.
DR EMBL; AF233780; AAK71578.1; -; mRNA.
DR EMBL; AF233781; AAK71579.1; -; mRNA.
DR EMBL; AF233782; AAK71580.1; -; mRNA.
DR EMBL; AF233783; AAK71581.1; -; mRNA.
DR EMBL; AF233784; AAK71582.1; -; mRNA.
DR EMBL; AF233785; AAK71583.1; -; mRNA.
DR EMBL; AF233786; AAK71584.1; -; mRNA.
DR EMBL; AF233787; AAK71585.1; -; mRNA.
DR EMBL; AF233788; AAK71586.1; -; mRNA.
DR EMBL; AF233789; AAK71587.1; -; mRNA.
DR EMBL; AF233790; AAK71588.1; -; mRNA.
DR EMBL; AF233791; AAK71589.1; -; mRNA.
DR EMBL; AF233792; AAK71590.1; -; mRNA.
DR EMBL; AF233793; AAK71591.1; -; mRNA.
DR EMBL; AF233794; AAK71592.1; -; mRNA.
DR EMBL; AF233795; AAK71593.1; -; mRNA.
DR EMBL; AF233796; AAK71594.1; -; mRNA.
DR EMBL; AF233797; AAK71595.1; -; mRNA.
DR EMBL; AF233798; AAK71596.1; -; mRNA.
DR EMBL; AF233799; AAK71597.1; -; mRNA.
DR EMBL; AF233800; AAK71598.1; -; mRNA.
DR EMBL; AF233801; AAK71599.1; -; mRNA.
DR EMBL; AF233802; AAK71600.1; -; mRNA.
DR EMBL; BC031762; AAH31762.1; -; mRNA.
DR CCDS; CCDS24551.1; -. [P22723-1]
DR CCDS; CCDS24552.2; -. [P22723-2]
DR PIR; JH0316; JH0316.
DR PIR; JH0317; JH0317.
DR RefSeq; NP_032099.1; NM_008073.3. [P22723-1]
DR RefSeq; NP_803127.3; NM_177408.6. [P22723-2]
DR PDB; 7CDB; X-ray; 1.95 A; C=406-423.
DR PDBsum; 7CDB; -.
DR AlphaFoldDB; P22723; -.
DR SMR; P22723; -.
DR BioGRID; 199808; 4.
DR ComplexPortal; CPX-2979; GABA-A receptor, alpha-1/beta-2/gamma-2.
DR ComplexPortal; CPX-2981; GABA-A receptor, alpha-6/beta-3/gamma-2.
DR ComplexPortal; CPX-2982; GABA-A receptor, alpha-3/beta-3/gamma-2.
DR ComplexPortal; CPX-2983; GABA-A receptor, alpha-1/beta-3/gamma-2.
DR ComplexPortal; CPX-2984; GABA-A receptor, alpha-5/beta-3/gamma-2.
DR ComplexPortal; CPX-2985; GABA-A receptor, alpha-2/beta-3/gamma-2.
DR DIP; DIP-48995N; -.
DR IntAct; P22723; 2.
DR MINT; P22723; -.
DR STRING; 10090.ENSMUSP00000063812; -.
DR BindingDB; P22723; -.
DR ChEMBL; CHEMBL4296058; -.
DR ChEMBL; CHEMBL4296059; -.
DR DrugCentral; P22723; -.
DR GlyConnect; 2327; 8 N-Linked glycans (2 sites).
DR GlyGen; P22723; 3 sites, 8 N-linked glycans (2 sites).
DR iPTMnet; P22723; -.
DR PhosphoSitePlus; P22723; -.
DR SwissPalm; P22723; -.
DR MaxQB; P22723; -.
DR PaxDb; P22723; -.
DR PeptideAtlas; P22723; -.
DR PRIDE; P22723; -.
DR ProteomicsDB; 268851; -. [P22723-1]
DR ProteomicsDB; 268852; -. [P22723-2]
DR ABCD; P22723; 3 sequenced antibodies.
DR Antibodypedia; 28585; 397 antibodies from 38 providers.
DR DNASU; 14406; -.
DR Ensembl; ENSMUST00000070725; ENSMUSP00000064739; ENSMUSG00000020436. [P22723-2]
DR Ensembl; ENSMUST00000070735; ENSMUSP00000063812; ENSMUSG00000020436. [P22723-1]
DR GeneID; 14406; -.
DR KEGG; mmu:14406; -.
DR UCSC; uc007imb.2; mouse. [P22723-1]
DR UCSC; uc007imc.3; mouse. [P22723-2]
DR CTD; 2566; -.
DR MGI; MGI:95623; Gabrg2.
DR VEuPathDB; HostDB:ENSMUSG00000020436; -.
DR eggNOG; KOG3642; Eukaryota.
DR GeneTree; ENSGT00940000156685; -.
DR HOGENOM; CLU_010920_2_0_1; -.
DR InParanoid; P22723; -.
DR OMA; PMDVHSC; -.
DR OrthoDB; 1057372at2759; -.
DR PhylomeDB; P22723; -.
DR TreeFam; TF315453; -.
DR Reactome; R-MMU-977443; GABA receptor activation.
DR BioGRID-ORCS; 14406; 4 hits in 75 CRISPR screens.
DR ChiTaRS; Gabrg2; mouse.
DR PRO; PR:P22723; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; P22723; protein.
DR Bgee; ENSMUSG00000020436; Expressed in visual cortex and 89 other tissues.
DR ExpressionAtlas; P22723; baseline and differential.
DR Genevisible; P22723; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030424; C:axon; IDA:MGI.
DR GO; GO:0034707; C:chloride channel complex; IEA:UniProtKB-KW.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0032590; C:dendrite membrane; ISO:MGI.
DR GO; GO:1902710; C:GABA receptor complex; ISO:MGI.
DR GO; GO:1902711; C:GABA-A receptor complex; IMP:UniProtKB.
DR GO; GO:0098982; C:GABA-ergic synapse; IDA:SynGO.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:MGI.
DR GO; GO:0060077; C:inhibitory synapse; ISO:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; IMP:UniProtKB.
DR GO; GO:0099060; C:integral component of postsynaptic specialization membrane; ISO:MGI.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0098794; C:postsynapse; IBA:GO_Central.
DR GO; GO:0045202; C:synapse; IBA:GO_Central.
DR GO; GO:0005254; F:chloride channel activity; IMP:UniProtKB.
DR GO; GO:0005231; F:excitatory extracellular ligand-gated ion channel activity; IBA:GO_Central.
DR GO; GO:0016917; F:GABA receptor activity; ISO:MGI.
DR GO; GO:0004890; F:GABA-A receptor activity; IDA:MGI.
DR GO; GO:0022851; F:GABA-gated chloride ion channel activity; ISO:MGI.
DR GO; GO:0005237; F:inhibitory extracellular ligand-gated ion channel activity; IBA:GO_Central.
DR GO; GO:0030594; F:neurotransmitter receptor activity; IBA:GO_Central.
DR GO; GO:1904315; F:transmitter-gated ion channel activity involved in regulation of postsynaptic membrane potential; IDA:SynGO.
DR GO; GO:0030534; P:adult behavior; IMP:MGI.
DR GO; GO:0071420; P:cellular response to histamine; IDA:UniProtKB.
DR GO; GO:0007268; P:chemical synaptic transmission; IDA:MGI.
DR GO; GO:1902476; P:chloride transmembrane transport; IMP:UniProtKB.
DR GO; GO:0007214; P:gamma-aminobutyric acid signaling pathway; IDA:MGI.
DR GO; GO:1904862; P:inhibitory synapse assembly; IDA:UniProtKB.
DR GO; GO:0034220; P:ion transmembrane transport; IBA:GO_Central.
DR GO; GO:0050877; P:nervous system process; IBA:GO_Central.
DR GO; GO:0009791; P:post-embryonic development; IMP:MGI.
DR GO; GO:0042391; P:regulation of membrane potential; IBA:GO_Central.
DR GO; GO:0060078; P:regulation of postsynaptic membrane potential; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR GO; GO:0051932; P:synaptic transmission, GABAergic; ISO:MGI.
DR Gene3D; 1.20.58.390; -; 1.
DR Gene3D; 2.70.170.10; -; 1.
DR InterPro; IPR006028; GABAA/Glycine_rcpt.
DR InterPro; IPR005439; GABBAg2_rcpt.
DR InterPro; IPR005437; GABRG-1/4.
DR InterPro; IPR006202; Neur_chan_lig-bd.
DR InterPro; IPR036734; Neur_chan_lig-bd_sf.
DR InterPro; IPR006201; Neur_channel.
DR InterPro; IPR036719; Neuro-gated_channel_TM_sf.
DR InterPro; IPR038050; Neuro_actylchol_rec.
DR InterPro; IPR006029; Neurotrans-gated_channel_TM.
DR InterPro; IPR018000; Neurotransmitter_ion_chnl_CS.
DR PANTHER; PTHR18945; PTHR18945; 1.
DR Pfam; PF02931; Neur_chan_LBD; 1.
DR Pfam; PF02932; Neur_chan_memb; 1.
DR PRINTS; PR00253; GABAARECEPTR.
DR PRINTS; PR01620; GABAARGAMMA.
DR PRINTS; PR01622; GABAARGAMMA2.
DR PRINTS; PR00252; NRIONCHANNEL.
DR SUPFAM; SSF63712; SSF63712; 1.
DR SUPFAM; SSF90112; SSF90112; 1.
DR TIGRFAMs; TIGR00860; LIC; 1.
DR PROSITE; PS00236; NEUROTR_ION_CHANNEL; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane; Cell projection;
KW Chloride; Chloride channel; Cytoplasmic vesicle; Disulfide bond;
KW Glycoprotein; Ion channel; Ion transport; Lipoprotein; Membrane; Palmitate;
KW Phosphoprotein; Postsynaptic cell membrane; Reference proteome; Signal;
KW Synapse; Transmembrane; Transmembrane helix; Transport.
FT SIGNAL 1..38
FT /evidence="ECO:0000255"
FT CHAIN 39..474
FT /note="Gamma-aminobutyric acid receptor subunit gamma-2"
FT /id="PRO_0000000478"
FT TOPO_DOM 39..272
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 273..295
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TRANSMEM 299..321
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TRANSMEM 333..355
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 356..450
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 451..474
FT /note="Helical"
FT /evidence="ECO:0000305"
FT MOD_RES 381
FT /note="Phosphoserine; by PKC"
FT /evidence="ECO:0000305"
FT CARBOHYD 51
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 128
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 246
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 189..203
FT /evidence="ECO:0000250"
FT VAR_SEQ 376..383
FT /note="Missing (in isoform 2S)"
FT /evidence="ECO:0000303|PubMed:1846404"
FT /id="VSP_000091"
FT VARIANT 49
FT /note="A -> T (in strain: DBA/2J)"
FT HELIX 418..421
FT /evidence="ECO:0007829|PDB:7CDB"
SQ SEQUENCE 474 AA; 55099 MW; 45BD61649C296EA9 CRC64;
MSSPNTWSIG SSVYSPVFSQ KMTLWILLLL SLYPGFTSQK SDDDYEDYAS NKTWVLTPKV
PEGDVTVILN NLLEGYDNKL RPDIGVKPTL IHTDMYVNSI GPVNAINMEY TIDIFFAQTW
YDRRLKFNST IKVLRLNSNM VGKIWIPDTF FRNSKKADAH WITTPNRMLR IWNDGRVLYT
LRLTIDAECQ LQLHNFPMDE HSCPLEFSSY GYPREEIVYQ WKRSSVEVGD TRSWRLYQFS
FVGLRNTTEV VKTTSGDYVV MSVYFDLSRR MGYFTIQTYI PCTLIVVLSW VSFWINKDAV
PARTSLGITT VLTMTTLSTI ARKSLPKVSY VTAMDLFVSV CFIFVFSALV EYGTLHYFVS
NRKPSKDKDK KKKNPLLRMF SFKAPTIDIR PRSATIQMNN ATHLQERDEE YGYECLDGKD
CASFFCCFED CRTGAWRHGR IHIRIAKMDS YARIFFPTAF CLFNLVYWVS YLYL
