GABR2_RAT
ID GABR2_RAT Reviewed; 940 AA.
AC O88871; Q9JK36; Q9QWU2;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2001, sequence version 2.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Gamma-aminobutyric acid type B receptor subunit 2;
DE Short=GABA-B receptor 2;
DE Short=GABA-B-R2;
DE Short=GABA-BR2;
DE Short=GABABR2;
DE Short=Gb2;
DE AltName: Full=G-protein coupled receptor 51;
DE Flags: Precursor;
GN Name=Gabbr2; Synonyms=Gpr51;
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], FUNCTION, INTERACTION WITH GABBR1, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Hypothalamus {ECO:0000303|PubMed:9872315};
RX PubMed=9872315; DOI=10.1038/25348;
RA Jones K.A., Borowsky B., Tamm J.A., Craig D.A., Durkin M.M., Dai M.,
RA Yao W.-J., Johnson M., Gunwaldsen C.A., Huang L.-Y., Tang C., Shen Q.,
RA Salon J.A., Morse K., Laz T., Smith K.E., Nagarathnam D., Noble S.A.,
RA Branchek T.A., Gerald C.;
RT "GABA(B) receptors function as a heteromeric assembly of the subunits
RT GABA(B)R1 and GABA(B)R2.";
RL Nature 396:674-679(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, INTERACTION WITH GABBR1,
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC TISSUE=Brain cortex, and Cerebellum {ECO:0000303|PubMed:9872317};
RX PubMed=9872317; DOI=10.1038/25360;
RA Kaupmann K., Malitschek B., Schuler V., Heid J., Froestl W., Beck P.,
RA Mosbacher J., Bischoff S., Kulik A., Shigemoto R., Karschin A., Bettler B.;
RT "GABA-B receptor subtypes assemble into functional heteromeric complexes.";
RL Nature 396:683-687(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Brain cortex {ECO:0000303|PubMed:10727622};
RX PubMed=10727622; DOI=10.1016/s0006-8993(00)01958-2;
RA Clark J.A., Mezey E., Lam A.S., Bonner T.I.;
RT "Distribution of the GABA(B) receptor subunit gb2 in rat CNS.";
RL Brain Res. 860:41-52(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Hypothalamus {ECO:0000303|Ref.4};
RA Borowsky B., Laz T., Gerald C.;
RL Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION.
RX PubMed=10658574; DOI=10.1016/s0968-0896(99)00214-x;
RA Belley M., Sullivan R., Reeves A., Evans J.F., O'Neill G.P., Ng G.Y.K.;
RT "Synthesis of the nanomolar photoaffinity GABA(B) receptor ligand CGP 71872
RT reveals diversity in the tissue distribution of GABA(B) receptor forms.";
RL Bioorg. Med. Chem. 7:2697-2704(1999).
RN [6]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=Wistar; TISSUE=Hippocampus;
RX PubMed=10457184; DOI=10.1046/j.1460-9568.1999.00704.x;
RA Pfaff T., Malitschek B., Kaupmann K., Prezeau L., Pin J.-P., Bettler B.,
RA Karschin A.;
RT "Alternative splicing generates a novel isoform of the rat metabotropic
RT GABA(B)R1 receptor.";
RL Eur. J. Neurosci. 11:2874-2882(1999).
RN [7]
RP FUNCTION.
RX PubMed=10075644; DOI=10.1074/jbc.274.12.7607;
RA Ng G.Y.K., Clark J., Coulombe N., Ethier N., Hebert T.E., Sullivan R.,
RA Kargman S., Chateauneuf A., Tsukamoto N., McDonald T., Whiting P.,
RA Mezey E., Johnson M.P., Liu Q., Kolakowski L.F. Jr., Evans J.F.,
RA Bonner T.I., O'Neill G.P.;
RT "Identification of a GABAB receptor subunit, gb2, required for functional
RT GABAB receptor activity.";
RL J. Biol. Chem. 274:7607-7610(1999).
RN [8]
RP FUNCTION, INTERACTION WITH GABBR1, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP AND VARIANTS PRO-19 INS AND TYR-337.
RC TISSUE=Hippocampus {ECO:0000303|PubMed:9872744};
RX PubMed=9872744; DOI=10.1126/science.283.5398.74;
RA Kuner R., Koehr G., Gruenewald S., Eisenhardt G., Bach A., Kornau H.-C.;
RT "Role of heteromer formation in GABAB receptor function.";
RL Science 283:74-77(1999).
RN [9]
RP FUNCTION, AND INTERACTION WITH ATF4.
RX PubMed=10924501; DOI=10.1074/jbc.m002727200;
RA Nehring R.B., Horikawa H.P.M., El Far O., Kneussel M., Brandstatter J.H.,
RA Stamm S., Wischmeyer E., Betz H., Karschin A.;
RT "The metabotropic GABAB receptor directly interacts with the activating
RT transcription factor 4.";
RL J. Biol. Chem. 275:35185-35191(2000).
RN [10]
RP SUBCELLULAR LOCATION.
RX PubMed=14718537; DOI=10.1074/jbc.m311737200;
RA Couve A., Restituito S., Brandon J.M., Charles K.J., Bawagan H.,
RA Freeman K.B., Pangalos M.N., Calver A.R., Moss S.J.;
RT "Marlin-1, a novel RNA-binding protein associates with GABA receptors.";
RL J. Biol. Chem. 279:13934-13943(2004).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-818 AND SER-883, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [12]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-388, 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).
CC -!- FUNCTION: Component of a heterodimeric G-protein coupled receptor for
CC GABA, formed by GABBR1 and GABBR2 (PubMed:9872315, PubMed:9872317,
CC PubMed:9872744). Within the heterodimeric GABA receptor, only GABBR1
CC seems to bind agonists, while GABBR2 mediates coupling to G proteins
CC (PubMed:9872317, PubMed:10658574). Ligand binding causes a conformation
CC change that triggers signaling via guanine nucleotide-binding proteins
CC (G proteins) and modulates the activity of down-stream effectors, such
CC as adenylate cyclase (PubMed:9872315, PubMed:9872317, Ref.4,
CC PubMed:10075644, PubMed:9872744, PubMed:10924501). Signaling inhibits
CC adenylate cyclase, stimulates phospholipase A2, activates potassium
CC channels, inactivates voltage-dependent calcium-channels and modulates
CC inositol phospholipid hydrolysis (PubMed:9872315, PubMed:9872317,
CC PubMed:10457184, PubMed:9872744, PubMed:10924501). Plays a critical
CC role in the fine-tuning of inhibitory synaptic transmission
CC (PubMed:9872317, PubMed:10457184, PubMed:9872744). Pre-synaptic GABA
CC receptor inhibits neurotransmitter release by down-regulating high-
CC voltage activated calcium channels, whereas postsynaptic GABA receptor
CC decreases neuronal excitability by activating a prominent inwardly
CC rectifying potassium (Kir) conductance that underlies the late
CC inhibitory postsynaptic potentials (PubMed:9872744, PubMed:10924501).
CC Not only implicated in synaptic inhibition but also in hippocampal
CC long-term potentiation, slow wave sleep, muscle relaxation and
CC antinociception (By similarity). {ECO:0000250|UniProtKB:O75899,
CC ECO:0000269|PubMed:10075644, ECO:0000269|PubMed:10457184,
CC ECO:0000269|PubMed:10658574, ECO:0000269|PubMed:10924501,
CC ECO:0000269|PubMed:9872315, ECO:0000269|PubMed:9872317,
CC ECO:0000269|PubMed:9872744, ECO:0000269|Ref.4}.
CC -!- SUBUNIT: Heterodimer of GABBR1 and GABBR2 (PubMed:9872315,
CC PubMed:9872317, PubMed:9872744). Homodimers may form, but are inactive
CC (PubMed:9872317). Interacts (via C-terminus) with ATF4 (via leucine
CC zipper domain) (PubMed:10924501). {ECO:0000269|PubMed:10924501,
CC ECO:0000269|PubMed:9872317, ECO:0000269|PubMed:9872744}.
CC -!- INTERACTION:
CC O88871; P27732: Cacna1d; NbExp=6; IntAct=EBI-7090239, EBI-8072674;
CC O88871; Q9Z0U4: Gabbr1; NbExp=8; IntAct=EBI-7090239, EBI-7090268;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:9872315,
CC ECO:0000269|PubMed:9872317, ECO:0000305|PubMed:10457184}; Multi-pass
CC membrane protein {ECO:0000269|PubMed:9872317}. Postsynaptic cell
CC membrane {ECO:0000269|PubMed:9872317}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:9872317}. Perikaryon {ECO:0000269|PubMed:14718537}.
CC Cell projection, dendrite {ECO:0000269|PubMed:10457184}.
CC Note=Coexpression of GABBR1 and GABBR2 is required for GABBR1
CC maturation and transport to the plasma membrane (PubMed:10457184). In
CC contrast, GABBR2 does not depend on GABBR1 for transport to the cell
CC membrane. {ECO:0000305|PubMed:10457184}.
CC -!- TISSUE SPECIFICITY: Highly expressed in areas of the brain including
CC thalamic nuclei, the hippocampus, cerebellar Purkinje cells and the
CC medial habenula, and moderately expressed in the cerebral cortex,
CC certain anterioventral thalamic nuclei, dorsal medial hypothalamic
CC nucleus and suprachiasmatic nuclei (PubMed:9872315, PubMed:9872317,
CC PubMed:10727622, PubMed:9872744). Also weakly expressed in the testis
CC (PubMed:9872744). {ECO:0000269|PubMed:10727622,
CC ECO:0000269|PubMed:9872315, ECO:0000269|PubMed:9872317,
CC ECO:0000269|PubMed:9872744}.
CC -!- DEVELOPMENTAL STAGE: On the day of birth, expressed in the regions of
CC the brain including hippocampus, thalamic nuclei and cortex
CC (PubMed:9872744). Abundant in brain cortex and cerebellum throughout
CC postnatal development whereas its expression in spinal cord gradually
CC decreases (PubMed:9872317). {ECO:0000269|PubMed:9872317,
CC ECO:0000269|PubMed:9872744}.
CC -!- DOMAIN: Alpha-helical parts of the C-terminal intracellular region
CC mediate heterodimeric interaction with GABA-B receptor 1.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 3 family. GABA-B
CC receptor subfamily. {ECO:0000305}.
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DR EMBL; AF074482; AAD03335.1; -; mRNA.
DR EMBL; AJ011318; CAA09592.1; -; Genomic_DNA.
DR EMBL; AF058795; AAC63994.1; -; mRNA.
DR EMBL; AF109405; AAD03338.1; -; mRNA.
DR RefSeq; NP_113990.1; NM_031802.1.
DR AlphaFoldDB; O88871; -.
DR SMR; O88871; -.
DR BioGRID; 249797; 6.
DR ComplexPortal; CPX-404; GABA-B receptor complex.
DR CORUM; O88871; -.
DR IntAct; O88871; 4.
DR MINT; O88871; -.
DR STRING; 10116.ENSRNOP00000011573; -.
DR BindingDB; O88871; -.
DR ChEMBL; CHEMBL2111474; -.
DR DrugCentral; O88871; -.
DR GuidetoPHARMACOLOGY; 241; -.
DR GlyGen; O88871; 5 sites, 2 N-linked glycans (1 site).
DR iPTMnet; O88871; -.
DR PhosphoSitePlus; O88871; -.
DR PaxDb; O88871; -.
DR PRIDE; O88871; -.
DR ABCD; O88871; 2 sequenced antibodies.
DR GeneID; 83633; -.
DR KEGG; rno:83633; -.
DR UCSC; RGD:619864; rat.
DR CTD; 9568; -.
DR RGD; 619864; Gabbr2.
DR eggNOG; KOG1055; Eukaryota.
DR InParanoid; O88871; -.
DR OrthoDB; 590810at2759; -.
DR PhylomeDB; O88871; -.
DR TreeFam; TF313965; -.
DR Reactome; R-RNO-1296041; Activation of G protein gated Potassium channels.
DR Reactome; R-RNO-418594; G alpha (i) signalling events.
DR Reactome; R-RNO-420499; Class C/3 (Metabotropic glutamate/pheromone receptors).
DR Reactome; R-RNO-977444; GABA B receptor activation.
DR Reactome; R-RNO-997272; Inhibition of voltage gated Ca2+ channels via Gbeta/gamma subunits.
DR PRO; PR:O88871; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR GO; GO:1902712; C:G protein-coupled GABA receptor complex; IPI:ComplexPortal.
DR GO; GO:0038039; C:G protein-coupled receptor heterodimeric complex; ISS:UniProtKB.
DR GO; GO:1902710; C:GABA receptor complex; ISO:RGD.
DR GO; GO:0098982; C:GABA-ergic synapse; IDA:SynGO.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0016021; C:integral component of membrane; TAS:RGD.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0099055; C:integral component of postsynaptic membrane; IDA:SynGO.
DR GO; GO:0099056; C:integral component of presynaptic membrane; IDA:SynGO.
DR GO; GO:0043005; C:neuron projection; ISO:RGD.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR GO; GO:0004965; F:G protein-coupled GABA receptor activity; IDA:RGD.
DR GO; GO:0046982; F:protein heterodimerization activity; ISO:RGD.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; IBA:GO_Central.
DR GO; GO:0007193; P:adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway; IDA:ComplexPortal.
DR GO; GO:0007214; P:gamma-aminobutyric acid signaling pathway; IDA:RGD.
DR GO; GO:0150099; P:neuron-glial cell signaling; IGI:ARUK-UCL.
DR GO; GO:0051932; P:synaptic transmission, GABAergic; IC:ComplexPortal.
DR InterPro; IPR001828; ANF_lig-bd_rcpt.
DR InterPro; IPR041689; GBR2_CC.
DR InterPro; IPR002455; GPCR3_GABA-B.
DR InterPro; IPR000337; GPCR_3.
DR InterPro; IPR017978; GPCR_3_C.
DR InterPro; IPR017979; GPCR_3_CS.
DR InterPro; IPR002457; GPCR_3_GABA_rcpt_B2.
DR InterPro; IPR028082; Peripla_BP_I.
DR PANTHER; PTHR10519; PTHR10519; 1.
DR Pfam; PF00003; 7tm_3; 1.
DR Pfam; PF01094; ANF_receptor; 1.
DR Pfam; PF18455; GBR2_CC; 1.
DR PRINTS; PR01178; GABAB2RECPTR.
DR PRINTS; PR00248; GPCRMGR.
DR SUPFAM; SSF53822; SSF53822; 1.
DR PROSITE; PS00981; G_PROTEIN_RECEP_F3_3; 1.
DR PROSITE; PS50259; G_PROTEIN_RECEP_F3_4; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cell projection; Coiled coil; Disulfide bond;
KW G-protein coupled receptor; Glycoprotein; Membrane; Phosphoprotein;
KW Postsynaptic cell membrane; Receptor; Reference proteome; Signal; Synapse;
KW Transducer; Transmembrane; Transmembrane helix.
FT SIGNAL 1..40
FT /evidence="ECO:0000255"
FT CHAIN 41..940
FT /note="Gamma-aminobutyric acid type B receptor subunit 2"
FT /id="PRO_0000012953"
FT TOPO_DOM 41..482
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 483..503
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 504..521
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 522..542
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 543..550
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 551..571
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 572..596
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 597..617
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 618..653
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 654..674
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 675..690
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 691..711
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 712..719
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 720..740
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 741..940
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 762..789
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 780..818
FT /evidence="ECO:0000255"
FT MOD_RES 775
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q80T41"
FT MOD_RES 778
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q80T41"
FT MOD_RES 818
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 883
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 892
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q80T41"
FT MOD_RES 912
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q80T41"
FT MOD_RES 915
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q80T41"
FT MOD_RES 919
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q80T41"
FT MOD_RES 923
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q80T41"
FT CARBOHYD 89
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 297
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 388
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0007744|PubMed:24090084"
FT CARBOHYD 403
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 452
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 107..134
FT /evidence="ECO:0000250"
FT DISULFID 236..265
FT /evidence="ECO:0000250"
FT DISULFID 264..301
FT /evidence="ECO:0000250"
FT VARIANT 19
FT /note="P -> PP"
FT /evidence="ECO:0000269|PubMed:9872744"
FT VARIANT 19
FT /note="P -> R"
FT VARIANT 337
FT /note="F -> Y"
FT /evidence="ECO:0000269|PubMed:9872744"
FT CONFLICT 343
FT /note="S -> T (in Ref. 2; CAA09592)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 940 AA; 105751 MW; 77BB42D833C7505D CRC64;
MASPPSSGQP RPPPPPPPPA RLLLPLLLSL LLWLAPGAWG WTRGAPRPPP SSPPLSIMGL
MPLTKEVAKG SIGRGVLPAV ELAIEQIRNE SLLRPYFLDL RLYDTECDNA KGLKAFYDAI
KYGPNHLMVF GGVCPSVTSI IAESLQGWNL VQLSFAATTP VLADKKKYPY FFRTVPSDNA
VNPAILKLLK HFRWRRVGTL TQDVQRFSEV RNDLTGVLYG EDIEISDTES FSNDPCTSVK
KLKGNDVRII LGQFDQNMAA KVFCCAFEES MFGSKYQWII PGWYEPAWWE QVHVEANSSR
CLRRSLLAAM EGYIGVDFEP LSSKQIKTIS GKTPQQFERE YNSKRSGVGP SKFHGYAYDG
IWVIAKTLQR AMETLHASSR HQRIQDFNYT DHTLGKIILN AMNETNFFGV TGQVVFRNGE
RMGTIKFTQF QDSREVKVGE YNAVADTLEI INDTIRFQGS EPPKDKTIIL EQLRKISLPL
YSILSALTIL GMIMASAFLF FNIKNRNQKL IKMSSPYMNN LIILGGMLSY ASIFLFGLDG
SFVSEKTFET LCTVRTWILT VGYTTAFGAM FAKTWRVHAI FKNVKMKKKI IKDQKLLVIV
GGMLLIDLCI LICWQAVDPL RRTVERYSME PDPAGRDISI RPLLEHCENT HMTIWLGIVY
AYKGLLMLFG CFLAWETRNV SIPALNDSKY IGMSVYNVGI MCIIGAAVSF LTRDQPNVQF
CIVALVIIFC STITLCLVFV PKLITLRTNP DAATQNRRFQ FTQNQKKEDS KTSTSVTSVN
QASTSRLEGL QSENHRLRMK ITELDKDLEE VTMQLQDTPE KTTYIKQNHY QELNDILSLG
NFTESTDGGK AILKNHLDQN PQLQWNTTEP SRTCKDPIED INSPEHIQRR LSLQLPILHH
AYLPSIGGVD ASCVSPCVSP TASPRHRHVP PSFRVMVSGL
