NLGN2_RAT
ID NLGN2_RAT Reviewed; 836 AA.
AC Q62888;
DT 23-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Neuroligin-2;
DE Flags: Precursor;
GN Name=Nlgn2;
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] (ISOFORMS 1 AND 2), PROTEIN SEQUENCE OF
RP N-TERMINUS, TISSUE SPECIFICITY, AND INTERACTION WITH NEUREXIN 1-BETA;
RP NEUREXIN 2-BETA AND NEUREXIN 3-BETA.
RC TISSUE=Forebrain;
RX PubMed=8576240; DOI=10.1074/jbc.271.5.2676;
RA Ichtchenko K., Nguyen T., Suedhof T.C.;
RT "Structures, alternative splicing, and neurexin binding of multiple
RT neuroligins.";
RL J. Biol. Chem. 271:2676-2682(1996).
RN [2]
RP INTERACTION WITH PATJ.
RX PubMed=9647694; DOI=10.1006/mcne.1998.0679;
RA Kurschner C., Mermelstein P.G., Holden W.T., Surmeier D.J.;
RT "CIPP, a novel multivalent PDZ domain protein, selectively interacts with
RT Kir4.0 family members, NMDA receptor subunits, neurexins, and
RT neuroligins.";
RL Mol. Cell. Neurosci. 11:161-172(1998).
RN [3]
RP TISSUE SPECIFICITY.
RX PubMed=11329178; DOI=10.1002/glia.1050;
RA Gilbert M., Smith J., Roskams A.J., Auld V.J.;
RT "Neuroligin 3 is a vertebrate gliotactin expressed in the olfactory
RT ensheathing glia, a growth-promoting class of macroglia.";
RL Glia 34:151-164(2001).
RN [4]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=15620359; DOI=10.1016/j.cell.2004.11.035;
RA Graf E.R., Zhang X., Jin S.X., Linhoff M.W., Craig A.M.;
RT "Neurexins induce differentiation of GABA and glutamate postsynaptic
RT specializations via neuroligins.";
RL Cell 119:1013-1026(2004).
RN [5]
RP TISSUE SPECIFICITY, AND ALTERNATIVE SPLICING.
RX PubMed=18755801; DOI=10.1210/en.2008-0274;
RA Suckow A.T., Comoletti D., Waldrop M.A., Mosedale M., Egodage S.,
RA Taylor P., Chessler S.D.;
RT "Expression of neurexin, neuroligin, and their cytoplasmic binding partners
RT in the pancreatic beta-cells and the involvement of neuroligin in insulin
RT secretion.";
RL Endocrinology 149:6006-6017(2008).
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=18434543; DOI=10.1073/pnas.0801383105;
RA Bolliger M.F., Pei J., Maxeiner S., Boucard A.A., Grishin N.V.,
RA Sudhof T.C.;
RT "Unusually rapid evolution of neuroligin-4 in mice.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:6421-6426(2008).
RN [7]
RP INTERACTION WITH NRXN1.
RX PubMed=18334216; DOI=10.1016/j.str.2007.12.024;
RA Koehnke J., Jin X., Trbovic N., Katsamba P.S., Brasch J., Ahlsen G.,
RA Scheiffele P., Honig B., Palmer A.G. III, Shapiro L.;
RT "Crystal structures of beta-neurexin 1 and beta-neurexin 2 ectodomains and
RT dynamics of splice insertion sequence 4.";
RL Structure 16:410-421(2008).
RN [8]
RP FUNCTION, INTERACTION WITH GPHN, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP AND MUTAGENESIS OF TYR-770.
RX PubMed=19755106; DOI=10.1016/j.neuron.2009.08.023;
RA Poulopoulos A., Aramuni G., Meyer G., Soykan T., Hoon M., Papadopoulos T.,
RA Zhang M., Paarmann I., Fuchs C., Harvey K., Jedlicka P., Schwarzacher S.W.,
RA Betz H., Harvey R.J., Brose N., Zhang W., Varoqueaux F.;
RT "Neuroligin 2 drives postsynaptic assembly at perisomatic inhibitory
RT synapses through gephyrin and collybistin.";
RL Neuron 63:628-642(2009).
RN [9]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=19859968; DOI=10.1002/jnr.22258;
RA Lui L., Levinson J.N., Noel G., Handrigan G.R., Richman J.M.,
RA El-Husseini A., Moukhles H.;
RT "Synaptic localization of neuroligin 2 in the rodent retina: comparative
RT study with the dystroglycan-containing complex.";
RL J. Neurosci. Res. 88:837-849(2010).
RN [10]
RP INTERACTION WITH NRXN1.
RX PubMed=20624592; DOI=10.1016/j.neuron.2010.06.001;
RA Koehnke J., Katsamba P.S., Ahlsen G., Bahna F., Vendome J., Honig B.,
RA Shapiro L., Jin X.;
RT "Splice form dependence of beta-neurexin/neuroligin binding interactions.";
RL Neuron 67:61-74(2010).
RN [11]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=19914352; DOI=10.1016/j.neuroscience.2009.11.016;
RA Levinson J.N., Li R., Kang R., Moukhles H., El-Husseini A., Bamji S.X.;
RT "Postsynaptic scaffolding molecules modulate the localization of
RT neuroligins.";
RL Neuroscience 165:782-793(2010).
RN [12]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=22528485; DOI=10.1074/jbc.m111.280537;
RA Suckow A.T., Zhang C., Egodage S., Comoletti D., Taylor P., Miller M.T.,
RA Sweet I.R., Chessler S.D.;
RT "Transcellular neuroligin-2 interactions enhance insulin secretion and are
RT integral to pancreatic beta-cell function.";
RL J. Biol. Chem. 287:19816-19826(2012).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-714, AND IDENTIFICATION BY
RP 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 [14] {ECO:0000305}
RP IDENTIFICATION IN A COMPLEX WITH MAGI2 AND IGSF9B.
RX PubMed=23751499; DOI=10.1083/jcb.201209132;
RA Woo J., Kwon S.K., Nam J., Choi S., Takahashi H., Krueger D., Park J.,
RA Lee Y., Bae J.Y., Lee D., Ko J., Kim H., Kim M.H., Bae Y.C., Chang S.,
RA Craig A.M., Kim E.;
RT "The adhesion protein IgSF9b is coupled to neuroligin 2 via S-SCAM to
RT promote inhibitory synapse development.";
RL J. Cell Biol. 201:929-944(2013).
RN [15]
RP INTERACTION WITH MDGA1 AND MDGA2.
RX PubMed=23248271; DOI=10.1073/pnas.1219987110;
RA Lee K., Kim Y., Lee S.-J., Qiang Y., Lee D., Lee H.W., Kim H., Je H.S.,
RA Suedhof T.C., Ko J.;
RT "MDGAs interact selectively with neuroligin-2 but not other neuroligins to
RT regulate inhibitory synapse development.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:336-341(2013).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN A COMPLEX WITH
RP LHFPL4; GABRA1; GABRB2; GABRG2 AND GABRB3, AND INTERACTION WITH LHFPL4 AND
RP GABRA1.
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 [17]
RP SUBCELLULAR LOCATION.
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).
CC -!- FUNCTION: Transmembrane scaffolding protein involved in cell-cell
CC interactions via its interactions with neurexin family members.
CC Mediates cell-cell interactions both in neurons and in other types of
CC cells, such as Langerhans beta cells. Plays a role in synapse function
CC and synaptic signal transmission, especially via gamma-aminobutyric
CC acid receptors (GABA(A) receptors). Functions by recruiting and
CC clustering synaptic proteins. Promotes clustering of postsynaptic
CC GABRG2 and GPHN. Promotes clustering of postsynaptic LHFPL4 (By
CC similarity). Modulates signaling by inhibitory synapses, and thereby
CC plays a role in controlling the ratio of signaling by excitatory and
CC inhibitory synapses and information processing. Required for normal
CC signal amplitude from inhibitory synapses, but is not essential for
CC normal signal frequency. May promote the initial formation of synapses,
CC but is not essential for this. In vitro, triggers the de novo formation
CC of presynaptic structures. Mediates cell-cell interactions between
CC Langerhans beta cells and modulates insulin secretion.
CC {ECO:0000250|UniProtKB:Q69ZK9, ECO:0000269|PubMed:19755106,
CC ECO:0000269|PubMed:22528485}.
CC -!- SUBUNIT: Interacts with NRXN1, NRXN2 and NRXN3 (PubMed:8576240,
CC PubMed:18334216, PubMed:20624592). Interacts (via its C-terminus) with
CC DLG4/PSD-95 (via PDZ domain 3) (By similarity). Interacts with PATJ
CC (PubMed:9647694). Interacts with GPHN (PubMed:19755106). Interacts with
CC MDGA1 and MDGA2 (PubMed:23248271). Found in a complex with MAGI2 and
CC IGSF9B, where it interacts with MAGI2 (via WW 1, WW 2 and PDZ 2
CC domains) (PubMed:23751499). Identified in a complex of 720 kDa composed
CC of LHFPL4, NLGN2, GABRA1, GABRB2, GABRG2 and GABRB3 (PubMed:28279354).
CC Interacts with LHFPL4; leading to mutual regulation of the protein
CC level and synaptic clustering (PubMed:29742426, PubMed:28279354).
CC Interacts with GABRA1 (PubMed:28279354). {ECO:0000250|UniProtKB:Q8NFZ4,
CC ECO:0000269|PubMed:18334216, ECO:0000269|PubMed:19755106,
CC ECO:0000269|PubMed:20624592, ECO:0000269|PubMed:23248271,
CC ECO:0000269|PubMed:23751499, ECO:0000269|PubMed:28279354,
CC ECO:0000269|PubMed:29742426, ECO:0000269|PubMed:8576240,
CC ECO:0000269|PubMed:9647694}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC protein. Postsynaptic cell membrane {ECO:0000269|PubMed:29742426}.
CC Presynaptic cell membrane. Note=Detected at presynaptic membranes in
CC retina, and at postsynaptic membranes in brain. Detected at dendritic
CC spines in cultured neurons. Colocalizes with GPHN and ARHGEF9 at
CC neuronal cell membranes.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q62888-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q62888-2; Sequence=VSP_007533;
CC -!- TISSUE SPECIFICITY: Detected on hippocampus neurons, especially at
CC inhibitory synapses. Detected in retina, in the outer and inner
CC plexiform layer. Detected in pancreas, in islet of Langerhans beta
CC cells (at protein level). Expressed in brain, spinal cord and dorsal
CC root ganglion. Detected in brain, and at lower levels in pancreas islet
CC beta cells. {ECO:0000269|PubMed:11329178, ECO:0000269|PubMed:15620359,
CC ECO:0000269|PubMed:18755801, ECO:0000269|PubMed:19755106,
CC ECO:0000269|PubMed:19859968, ECO:0000269|PubMed:19914352,
CC ECO:0000269|PubMed:8576240}.
CC -!- SIMILARITY: Belongs to the type-B carboxylesterase/lipase family.
CC {ECO:0000305}.
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DR EMBL; U41662; AAA97870.1; -; mRNA.
DR RefSeq; NP_446444.1; NM_053992.1. [Q62888-1]
DR PDB; 5V5V; X-ray; 4.11 A; A/B/C/D/E/F=42-612.
DR PDBsum; 5V5V; -.
DR AlphaFoldDB; Q62888; -.
DR SMR; Q62888; -.
DR BioGRID; 250669; 13.
DR CORUM; Q62888; -.
DR IntAct; Q62888; 5.
DR MINT; Q62888; -.
DR STRING; 10116.ENSRNOP00000053713; -.
DR ESTHER; ratno-2neur; Neuroligin.
DR MEROPS; S09.995; -.
DR GlyGen; Q62888; 3 sites.
DR iPTMnet; Q62888; -.
DR PhosphoSitePlus; Q62888; -.
DR PaxDb; Q62888; -.
DR PRIDE; Q62888; -.
DR ABCD; Q62888; 1 sequenced antibody.
DR Ensembl; ENSRNOT00000056872; ENSRNOP00000053713; ENSRNOG00000015430. [Q62888-1]
DR Ensembl; ENSRNOT00000092662; ENSRNOP00000075845; ENSRNOG00000015430. [Q62888-2]
DR GeneID; 117096; -.
DR KEGG; rno:117096; -.
DR UCSC; RGD:621118; rat. [Q62888-1]
DR CTD; 57555; -.
DR RGD; 621118; Nlgn2.
DR eggNOG; KOG1516; Eukaryota.
DR GeneTree; ENSGT00940000160598; -.
DR InParanoid; Q62888; -.
DR OrthoDB; 754103at2759; -.
DR PhylomeDB; Q62888; -.
DR Reactome; R-RNO-6794361; Neurexins and neuroligins.
DR PRO; PR:Q62888; -.
DR Proteomes; UP000002494; Chromosome 10.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0009986; C:cell surface; IDA:BHF-UCL.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0043198; C:dendritic shaft; IDA:RGD.
DR GO; GO:0098691; C:dopaminergic synapse; ISO:RGD.
DR GO; GO:0060076; C:excitatory synapse; IDA:RGD.
DR GO; GO:0098982; C:GABA-ergic synapse; IDA:SynGO.
DR GO; GO:0098690; C:glycinergic synapse; ISO:RGD.
DR GO; GO:0060077; C:inhibitory synapse; IDA:BHF-UCL.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0099055; C:integral component of postsynaptic membrane; IDA:BHF-UCL.
DR GO; GO:0099060; C:integral component of postsynaptic specialization membrane; IDA:SynGO.
DR GO; GO:0005886; C:plasma membrane; IDA:BHF-UCL.
DR GO; GO:0045211; C:postsynaptic membrane; IDA:RGD.
DR GO; GO:0042734; C:presynaptic membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0097470; C:ribbon synapse; IDA:RGD.
DR GO; GO:0045202; C:synapse; ISS:BHF-UCL.
DR GO; GO:0050839; F:cell adhesion molecule binding; ISS:BHF-UCL.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0042043; F:neurexin family protein binding; ISS:BHF-UCL.
DR GO; GO:0038023; F:signaling receptor activity; IBA:GO_Central.
DR GO; GO:0007420; P:brain development; IEP:RGD.
DR GO; GO:0007268; P:chemical synaptic transmission; IBA:GO_Central.
DR GO; GO:0097116; P:gephyrin clustering involved in postsynaptic density assembly; ISS:BHF-UCL.
DR GO; GO:1904862; P:inhibitory synapse assembly; ISO:RGD.
DR GO; GO:1901142; P:insulin metabolic process; IDA:RGD.
DR GO; GO:0007630; P:jump response; IMP:BHF-UCL.
DR GO; GO:0035641; P:locomotory exploration behavior; ISS:BHF-UCL.
DR GO; GO:0050804; P:modulation of chemical synaptic transmission; ISS:BHF-UCL.
DR GO; GO:0050885; P:neuromuscular process controlling balance; ISS:BHF-UCL.
DR GO; GO:0007158; P:neuron cell-cell adhesion; IDA:BHF-UCL.
DR GO; GO:0072578; P:neurotransmitter-gated ion channel clustering; ISO:RGD.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IDA:RGD.
DR GO; GO:0060999; P:positive regulation of dendritic spine development; IMP:RGD.
DR GO; GO:2000463; P:positive regulation of excitatory postsynaptic potential; ISS:BHF-UCL.
DR GO; GO:0097151; P:positive regulation of inhibitory postsynaptic potential; IMP:BHF-UCL.
DR GO; GO:0032024; P:positive regulation of insulin secretion; IDA:RGD.
DR GO; GO:1902474; P:positive regulation of protein localization to synapse; IMP:RGD.
DR GO; GO:0051965; P:positive regulation of synapse assembly; IDA:BHF-UCL.
DR GO; GO:0032230; P:positive regulation of synaptic transmission, GABAergic; ISS:BHF-UCL.
DR GO; GO:0051968; P:positive regulation of synaptic transmission, glutamatergic; ISS:BHF-UCL.
DR GO; GO:2000809; P:positive regulation of synaptic vesicle clustering; ISO:RGD.
DR GO; GO:1904034; P:positive regulation of t-SNARE clustering; IDA:RGD.
DR GO; GO:0097119; P:postsynaptic density protein 95 clustering; ISS:BHF-UCL.
DR GO; GO:0097104; P:postsynaptic membrane assembly; ISS:BHF-UCL.
DR GO; GO:0098698; P:postsynaptic specialization assembly; ISO:RGD.
DR GO; GO:0097105; P:presynaptic membrane assembly; IDA:BHF-UCL.
DR GO; GO:0034394; P:protein localization to cell surface; ISO:RGD.
DR GO; GO:0035418; P:protein localization to synapse; ISS:BHF-UCL.
DR GO; GO:2000311; P:regulation of AMPA receptor activity; ISS:BHF-UCL.
DR GO; GO:1905606; P:regulation of presynapse assembly; IDA:SynGO.
DR GO; GO:0002087; P:regulation of respiratory gaseous exchange by nervous system process; ISS:BHF-UCL.
DR GO; GO:0019233; P:sensory perception of pain; ISS:BHF-UCL.
DR GO; GO:0035176; P:social behavior; IMP:BHF-UCL.
DR GO; GO:0007416; P:synapse assembly; IDA:BHF-UCL.
DR GO; GO:0050808; P:synapse organization; IDA:MGI.
DR GO; GO:0051932; P:synaptic transmission, GABAergic; ISO:RGD.
DR GO; GO:0048488; P:synaptic vesicle endocytosis; IBA:GO_Central.
DR GO; GO:0072553; P:terminal button organization; IMP:BHF-UCL.
DR GO; GO:0001966; P:thigmotaxis; IMP:BHF-UCL.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR002018; CarbesteraseB.
DR InterPro; IPR019819; Carboxylesterase_B_CS.
DR InterPro; IPR000460; Nlgn.
DR InterPro; IPR030023; NLGN2.
DR PANTHER; PTHR43903:SF3; PTHR43903:SF3; 1.
DR Pfam; PF00135; COesterase; 1.
DR PRINTS; PR01090; NEUROLIGIN.
DR SUPFAM; SSF53474; SSF53474; 1.
DR PROSITE; PS00941; CARBOXYLESTERASE_B_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell adhesion; Cell membrane;
KW Cell projection; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Membrane; Phosphoprotein; Postsynaptic cell membrane; Reference proteome;
KW Signal; Synapse; Transmembrane; Transmembrane helix.
FT SIGNAL 1..14
FT /evidence="ECO:0000305|PubMed:8576240"
FT CHAIN 15..836
FT /note="Neuroligin-2"
FT /id="PRO_0000008644"
FT TOPO_DOM 15..678
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 679..699
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 700..836
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 623..661
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 679..699
FT /note="Required for interaction with LHFPL4"
FT /evidence="ECO:0000250|UniProtKB:Q69ZK9"
FT REGION 711..735
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 791..836
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 627..653
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 793..823
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 714
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 719
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q69ZK9"
FT CARBOHYD 98
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 136
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 522
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 106..141
FT /evidence="ECO:0000250"
FT DISULFID 317..328
FT /evidence="ECO:0000250"
FT DISULFID 487..521
FT /evidence="ECO:0000250"
FT VAR_SEQ 153..169
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:8576240"
FT /id="VSP_007533"
FT MUTAGEN 770
FT /note="Y->A: Abolishes interaction with GPHN."
FT /evidence="ECO:0000269|PubMed:19755106"
SQ SEQUENCE 836 AA; 90961 MW; 1AD51CB1BE4BF9CF CRC64;
MWLLALCLVG LAGAQRGGGG PGGGAPGGPG LGLGSLGEER FPVVNTAYGR VRGVRRELNN
EILGPVVQFL GVPYATPPLG ARRFQPPEAP ASWPGVRNAT TLPPACPQNL HGALPAIMLP
VWFTDNLEAA ATYVQNQSED CLYLNLYVPT EDGPLTKKRD EATLNPPDTD IRDSGKKPVM
LFLHGGSYME GTGNMFDGSV LAAYGNVIVA TLNYRLGVLG FLSTGDQAAK GNYGLLDQIQ
ALRWLSENIA HFGGDPERIT IFGSGAGASC VNLLILSHHS EGLFQKAIAQ SGTAISSWSV
NYQPLKYTRL LAAKVGCDRE DSTEAVECLR RKSSRELVDQ DVQPARYHIA FGPVVDGDVV
PDDPEILMQQ GEFLNYDMLI GVNQGEGLKF VEDSAESEDG VSASAFDFTV SNFVDNLYGY
PEGKDVLRET IKFMYTDWAD RDNGEMRRKT LLALFTDHQW VAPAVATAKL HADYQSPVYF
YTFYHHCQAE GRPEWADAAH GDELPYVFGV PMVGATDLFP CNFSKNDVML SAVVMTYWTN
FAKTGDPNQP VPQDTKFIHT KPNRFEEVVW SKFNSKEKQY LHIGLKPRVR DNYRANKVAF
WLELVPHLHN LHTELFTTTT RLPPYATRWP PRTPGPGTSG TRRPPPPATL PPESDIDLGP
RAYDRFPGDS RDYSTELSVT VAVGASLLFL NILAFAALYY KRDRRQELRC RRLSPPGGSG
SGVPGGGPLL PTAGRELPPE EELVSLQLKR GGGVGADPAE ALRPACPPDY TLALRRAPDD
VPLLAPGALT LLPSGLGPPP PPPPPSLHPF GPFPPPPPTA TSHNNTLPHP HSTTRV
