ID NLGN2_HUMAN Reviewed; 835 AA. AC Q8NFZ4; Q9P2I1; DT 23-MAY-2003, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2002, sequence version 1. DT 24-JAN-2024, entry version 168. DE RecName: Full=Neuroligin-2; DE Flags: Precursor; GN Name=NLGN2; Synonyms=KIAA1366; 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 [MRNA]. RX PubMed=12669065; DOI=10.1038/ng1136; RA Jamain S., Quach H., Betancur C., Rastam M., Colineaux C., Gillberg I.C., RA Soderstrom H., Giros B., Leboyer M., Gillberg C., Bourgeron T., Nyden A., RA Philippe A., Cohen D., Chabane N., Mouren-Simeoni M.C., Brice A., RA Sponheim E., Spurkland I., Skjeldal O.H., Coleman M., Pearl P.L., RA Cohen I.L., Tsiouris J., Zappella M., Menchetti G., Pompella A., RA Aschauer H., Van Maldergem L.; RT "Mutations of the X-linked genes encoding neuroligins NLGN3 and NLGN4 are RT associated with autism."; RL Nat. Genet. 34:27-29(2003). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 286-835. RC TISSUE=Brain; RX PubMed=10718198; DOI=10.1093/dnares/7.1.65; RA Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.; RT "Prediction of the coding sequences of unidentified human genes. XVI. The RT complete sequences of 150 new cDNA clones from brain which code for large RT proteins in vitro."; RL DNA Res. 7:65-73(2000). RN [3] RP INTERACTION WITH DLG4. RX PubMed=9278515; DOI=10.1126/science.277.5331.1511; RA Irie M., Hata Y., Takeuchi M., Ichtchenko K., Toyoda A., Hirao K., RA Takai Y., Rosahl T.W., Suedhof T.C.; RT "Binding of neuroligins to PSD-95."; RL Science 277:1511-1515(1997). RN [4] 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 [5] RP TISSUE SPECIFICITY. RX PubMed=19926856; DOI=10.1073/pnas.0809510106; RA Bottos A., Destro E., Rissone A., Graziano S., Cordara G., Assenzio B., RA Cera M.R., Mascia L., Bussolino F., Arese M.; RT "The synaptic proteins neurexins and neuroligins are widely expressed in RT the vascular system and contribute to its functions."; RL Proc. Natl. Acad. Sci. U.S.A. 106:20782-20787(2009). RN [6] 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). 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 (By similarity). CC {ECO:0000250, ECO:0000250|UniProtKB:Q69ZK9}. CC -!- SUBUNIT: Interacts with neurexins NRXN1, NRXN2 and NRXN3 (By CC similarity). Interaction with neurexins is mediated by heparan sulfate CC glycan modification on neurexin (By similarity). Interacts (via its C- CC terminus) with DLG4/PSD-95 (via PDZ domain 3) (PubMed:9278515). CC Interacts with PATJ (By similarity). Interacts with GPHN (By CC similarity). Interacts with MDGA1 and MDGA2 (By similarity). Found in a CC complex with MAGI2 and IGSF9B, where it interacts with MAGI2 (via WW 1, CC WW 2 and PDZ 2 domains) (PubMed:23751499). Identified in a complex of CC 720 kDa composed of LHFPL4, NLGN2, GABRA1, GABRB2, GABRG2 and GABRB3 CC (By similarity). Interacts with LHFPL4; leading to mutual regulation of CC the protein level and synaptic clustering (By similarity). Interacts CC with NLGN2 (By similarity). {ECO:0000250|UniProtKB:Q62888, CC ECO:0000250|UniProtKB:Q69ZK9, ECO:0000269|PubMed:23751499, CC ECO:0000269|PubMed:9278515}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I CC membrane protein {ECO:0000250}. Postsynaptic cell membrane CC {ECO:0000250}. Presynaptic cell membrane {ECO:0000250}. Note=Detected CC at postsynaptic membranes in brain. Detected at dendritic spines in CC cultured neurons. Colocalizes with GPHN and ARHGEF9 at neuronal cell CC membranes (By similarity). Localized at presynaptic membranes in CC retina. Colocalizes with GABRG2 at inhibitory synapses in the retina CC (By similarity). {ECO:0000250}. CC -!- TISSUE SPECIFICITY: Expressed in the blood vessel walls. Detected in CC colon, brain and pancreas islets of Langerhans (at protein level). CC Detected in brain, and at lower levels in pancreas islet beta cells. CC {ECO:0000269|PubMed:18755801, ECO:0000269|PubMed:19926856}. CC -!- SIMILARITY: Belongs to the type-B carboxylesterase/lipase family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF376802; AAM46111.1; -; mRNA. DR EMBL; AB037787; BAA92604.1; -; mRNA. DR CCDS; CCDS11103.1; -. DR RefSeq; NP_065846.1; NM_020795.3. DR PDB; 5XEQ; X-ray; 3.14 A; A=42-611. DR PDB; 8GS4; EM; 3.50 A; A/B=1-835. DR PDBsum; 5XEQ; -. DR PDBsum; 8GS4; -. DR AlphaFoldDB; Q8NFZ4; -. DR EMDB; EMD-34220; -. DR SMR; Q8NFZ4; -. DR BioGRID; 121611; 109. DR IntAct; Q8NFZ4; 10. DR STRING; 9606.ENSP00000305288; -. DR ESTHER; human-NLGN2; Neuroligin. DR MEROPS; S09.995; -. DR TCDB; 8.A.117.1.1; the neuroligin (nlg) family. DR GlyCosmos; Q8NFZ4; 4 sites, 1 glycan. DR GlyGen; Q8NFZ4; 4 sites, 1 O-linked glycan (1 site). DR iPTMnet; Q8NFZ4; -. DR PhosphoSitePlus; Q8NFZ4; -. DR BioMuta; NLGN2; -. DR DMDM; 31076824; -. DR jPOST; Q8NFZ4; -. DR MassIVE; Q8NFZ4; -. DR PaxDb; 9606-ENSP00000305288; -. DR PeptideAtlas; Q8NFZ4; -. DR ProteomicsDB; 73397; -. DR Pumba; Q8NFZ4; -. DR ABCD; Q8NFZ4; 1 sequenced antibody. DR Antibodypedia; 24107; 149 antibodies from 32 providers. DR DNASU; 57555; -. DR Ensembl; ENST00000302926.7; ENSP00000305288.2; ENSG00000169992.10. DR Ensembl; ENST00000575301.5; ENSP00000461168.1; ENSG00000169992.10. DR Ensembl; ENST00000639647.1; ENSP00000492323.1; ENSG00000283859.2. DR Ensembl; ENST00000640620.2; ENSP00000492198.1; ENSG00000283859.2. DR GeneID; 57555; -. DR KEGG; hsa:57555; -. DR MANE-Select; ENST00000302926.7; ENSP00000305288.2; NM_020795.4; NP_065846.1. DR UCSC; uc002ggt.3; human. DR AGR; HGNC:14290; -. DR CTD; 57555; -. DR DisGeNET; 57555; -. DR GeneCards; NLGN2; -. DR HGNC; HGNC:14290; NLGN2. DR HPA; ENSG00000169992; Tissue enhanced (brain). DR MIM; 606479; gene. DR neXtProt; NX_Q8NFZ4; -. DR OpenTargets; ENSG00000169992; -. DR PharmGKB; PA31648; -. DR VEuPathDB; HostDB:ENSG00000169992; -. DR eggNOG; KOG1516; Eukaryota. DR GeneTree; ENSGT00940000160598; -. DR HOGENOM; CLU_006586_5_1_1; -. DR InParanoid; Q8NFZ4; -. DR OMA; WADRDNT; -. DR OrthoDB; 4386at2759; -. DR PhylomeDB; Q8NFZ4; -. DR TreeFam; TF326187; -. DR PathwayCommons; Q8NFZ4; -. DR Reactome; R-HSA-6794361; Neurexins and neuroligins. DR SignaLink; Q8NFZ4; -. DR SIGNOR; Q8NFZ4; -. DR BioGRID-ORCS; 57555; 10 hits in 1155 CRISPR screens. DR ChiTaRS; NLGN2; human. DR GeneWiki; NLGN2; -. DR GenomeRNAi; 57555; -. DR Pharos; Q8NFZ4; Tbio. DR PRO; PR:Q8NFZ4; -. DR Proteomes; UP000005640; Chromosome 17. DR RNAct; Q8NFZ4; Protein. DR Bgee; ENSG00000169992; Expressed in cortical plate and 96 other cell types or tissues. DR ExpressionAtlas; Q8NFZ4; baseline and differential. DR GO; GO:0009986; C:cell surface; ISS:BHF-UCL. DR GO; GO:0043198; C:dendritic shaft; IEA:Ensembl. DR GO; GO:0098691; C:dopaminergic synapse; IEA:Ensembl. DR GO; GO:0060076; C:excitatory synapse; IEA:Ensembl. DR GO; GO:0098690; C:glycinergic synapse; IEA:Ensembl. DR GO; GO:0060077; C:inhibitory synapse; ISS:BHF-UCL. DR GO; GO:0016020; C:membrane; TAS:ARUK-UCL. DR GO; GO:0005886; C:plasma membrane; TAS:Reactome. DR GO; GO:0045211; C:postsynaptic membrane; ISS:BHF-UCL. DR GO; GO:0099634; C:postsynaptic specialization membrane; IEA:Ensembl. DR GO; GO:0042734; C:presynaptic membrane; IEA:UniProtKB-SubCell. DR GO; GO:0097470; C:ribbon synapse; IEA:Ensembl. DR GO; GO:0098983; C:symmetric, GABA-ergic, inhibitory synapse; TAS:ARUK-UCL. 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; IEA:Ensembl. 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:0098609; P:cell-cell adhesion; NAS:UniProtKB. DR GO; GO:0045217; P:cell-cell junction maintenance; NAS:UniProtKB. 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; IEA:Ensembl. DR GO; GO:1901142; P:insulin metabolic process; IEA:Ensembl. DR GO; GO:0007630; P:jump response; IEA:Ensembl. DR GO; GO:0035641; P:locomotory exploration behavior; IEA:Ensembl. DR GO; GO:0050804; P:modulation of chemical synaptic transmission; ISS:BHF-UCL. DR GO; GO:0050885; P:neuromuscular process controlling balance; IEA:Ensembl. DR GO; GO:0007158; P:neuron cell-cell adhesion; ISS:BHF-UCL. DR GO; GO:0072578; P:neurotransmitter-gated ion channel clustering; IEA:Ensembl. DR GO; GO:0008284; P:positive regulation of cell population proliferation; IEA:Ensembl. DR GO; GO:0060999; P:positive regulation of dendritic spine development; IEA:Ensembl. 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; ISS:BHF-UCL. DR GO; GO:0032024; P:positive regulation of insulin secretion; IMP:CACAO. DR GO; GO:1902474; P:positive regulation of protein localization to synapse; IDA:MGI. DR GO; GO:0051965; P:positive regulation of synapse assembly; ISS: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; IEA:Ensembl. DR GO; GO:1904034; P:positive regulation of t-SNARE clustering; IEA:Ensembl. 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:0099054; P:presynapse assembly; TAS:ARUK-UCL. DR GO; GO:0097105; P:presynaptic membrane assembly; ISS:BHF-UCL. DR GO; GO:0034394; P:protein localization to cell surface; IEA:Ensembl. 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; IEA:Ensembl. 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; IEA:Ensembl. DR GO; GO:0035176; P:social behavior; IEA:Ensembl. DR GO; GO:0007416; P:synapse assembly; ISS:BHF-UCL. DR GO; GO:0050808; P:synapse organization; ISS:BHF-UCL. DR GO; GO:0051932; P:synaptic transmission, GABAergic; IEA:Ensembl. DR GO; GO:0048488; P:synaptic vesicle endocytosis; IBA:GO_Central. DR GO; GO:0072553; P:terminal button organization; ISS:BHF-UCL. DR GO; GO:0001966; P:thigmotaxis; IEA:Ensembl. DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1. DR InterPro; IPR029058; AB_hydrolase. DR InterPro; IPR002018; CarbesteraseB. DR InterPro; IPR019819; Carboxylesterase_B_CS. DR InterPro; IPR000460; Nlgn. DR PANTHER; PTHR43903; NEUROLIGIN; 1. DR PANTHER; PTHR43903:SF3; NEUROLIGIN-2; 1. DR Pfam; PF00135; COesterase; 1. DR PRINTS; PR01090; NEUROLIGIN. DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1. DR PROSITE; PS00941; CARBOXYLESTERASE_B_2; 1. DR Genevisible; Q8NFZ4; HS. PE 1: Evidence at protein level; KW 3D-structure; Cell adhesion; Cell membrane; Cell projection; KW Disulfide bond; Glycoprotein; Membrane; Phosphoprotein; KW Postsynaptic cell membrane; Reference proteome; Signal; Synapse; KW Transmembrane; Transmembrane helix. FT SIGNAL 1..14 FT /evidence="ECO:0000255" FT CHAIN 15..835 FT /note="Neuroligin-2" FT /id="PRO_0000008643" FT TOPO_DOM 15..677 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 678..698 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 699..835 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT REGION 623..668 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 678..698 FT /note="Required for interaction with LHFPL4" FT /evidence="ECO:0000250|UniProtKB:Q69ZK9" FT REGION 790..835 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 626..656 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 792..822 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 713 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q69ZK9" FT MOD_RES 718 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 STRAND 43..45 FT /evidence="ECO:0007829|PDB:5XEQ" FT STRAND 50..52 FT /evidence="ECO:0007829|PDB:5XEQ" FT STRAND 54..57 FT /evidence="ECO:0007829|PDB:5XEQ" FT STRAND 61..63 FT /evidence="ECO:0007829|PDB:5XEQ" FT STRAND 65..73 FT /evidence="ECO:0007829|PDB:5XEQ" FT TURN 81..84 FT /evidence="ECO:0007829|PDB:5XEQ" FT STRAND 94..98 FT /evidence="ECO:0007829|PDB:5XEQ" FT TURN 116..118 FT /evidence="ECO:0007829|PDB:5XEQ" FT HELIX 121..125 FT /evidence="ECO:0007829|PDB:5XEQ" FT HELIX 127..131 FT /evidence="ECO:0007829|PDB:5XEQ" FT HELIX 132..134 FT /evidence="ECO:0007829|PDB:5XEQ" FT STRAND 135..137 FT /evidence="ECO:0007829|PDB:5XEQ" FT STRAND 143..148 FT /evidence="ECO:0007829|PDB:5XEQ" FT STRAND 177..183 FT /evidence="ECO:0007829|PDB:5XEQ" FT STRAND 186..190 FT /evidence="ECO:0007829|PDB:5XEQ" FT HELIX 193..195 FT /evidence="ECO:0007829|PDB:5XEQ" FT HELIX 199..205 FT /evidence="ECO:0007829|PDB:5XEQ" FT STRAND 208..212 FT /evidence="ECO:0007829|PDB:5XEQ" FT HELIX 217..221 FT /evidence="ECO:0007829|PDB:5XEQ" FT STRAND 225..228 FT /evidence="ECO:0007829|PDB:5XEQ" FT HELIX 233..246 FT /evidence="ECO:0007829|PDB:5XEQ" FT HELIX 249..252 FT /evidence="ECO:0007829|PDB:5XEQ" FT STRAND 254..264 FT /evidence="ECO:0007829|PDB:5XEQ" FT HELIX 266..276 FT /evidence="ECO:0007829|PDB:5XEQ" FT TURN 279..283 FT /evidence="ECO:0007829|PDB:5XEQ" FT STRAND 285..291 FT /evidence="ECO:0007829|PDB:5XEQ" FT STRAND 294..296 FT /evidence="ECO:0007829|PDB:5XEQ" FT TURN 297..299 FT /evidence="ECO:0007829|PDB:5XEQ" FT STRAND 300..302 FT /evidence="ECO:0007829|PDB:5XEQ" FT HELIX 304..314 FT /evidence="ECO:0007829|PDB:5XEQ" FT HELIX 322..329 FT /evidence="ECO:0007829|PDB:5XEQ" FT HELIX 334..338 FT /evidence="ECO:0007829|PDB:5XEQ" FT STRAND 350..352 FT /evidence="ECO:0007829|PDB:5XEQ" FT STRAND 357..360 FT /evidence="ECO:0007829|PDB:5XEQ" FT HELIX 364..369 FT /evidence="ECO:0007829|PDB:5XEQ" FT STRAND 377..383 FT /evidence="ECO:0007829|PDB:5XEQ" FT HELIX 388..391 FT /evidence="ECO:0007829|PDB:5XEQ" FT HELIX 403..417 FT /evidence="ECO:0007829|PDB:5XEQ" FT HELIX 424..434 FT /evidence="ECO:0007829|PDB:5XEQ" FT HELIX 444..459 FT /evidence="ECO:0007829|PDB:5XEQ" FT HELIX 461..473 FT /evidence="ECO:0007829|PDB:5XEQ" FT STRAND 478..483 FT /evidence="ECO:0007829|PDB:5XEQ" FT TURN 500..503 FT /evidence="ECO:0007829|PDB:5XEQ" FT HELIX 504..507 FT /evidence="ECO:0007829|PDB:5XEQ" FT HELIX 510..512 FT /evidence="ECO:0007829|PDB:5XEQ" FT STRAND 517..519 FT /evidence="ECO:0007829|PDB:5XEQ" FT HELIX 525..544 FT /evidence="ECO:0007829|PDB:5XEQ" FT TURN 575..577 FT /evidence="ECO:0007829|PDB:5XEQ" FT STRAND 580..586 FT /evidence="ECO:0007829|PDB:5XEQ" FT STRAND 588..591 FT /evidence="ECO:0007829|PDB:5XEQ" FT HELIX 595..603 FT /evidence="ECO:0007829|PDB:5XEQ" FT TURN 604..607 FT /evidence="ECO:0007829|PDB:5XEQ" SQ SEQUENCE 835 AA; 90820 MW; 359938630193EF87 CRC64; MWLLALCLVG LAGAQRGGGG PGGGAPGGPG LGLGSLGEER FPVVNTAYGR VRGVRRELNN EILGPVVQFL GVPYATPPLG ARRFQPPEAP ASWPGVRNAT TLPPACPQNL HGALPAIMLP VWFTDNLEAA ATYVQNQSED CLYLNLYVPT EDGPLTKKRD EATLNPPDTD IRDPGKKPVM LFLHGGSYME GTGNMFDGSV LAAYGNVIVA TLNYRLGVLG FLSTGDQAAK GNYGLLDQIQ ALRWLSENIA HFGGDPERIT IFGSGAGASC VNLLILSHHS EGLFQKAIAQ SGTAISSWSV NYQPLKYTRL LAAKVGCDRE DSAEAVECLR RKPSRELVDQ 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 PRPPAGAPGT RRPPPPATLP PEPEPEPGPR AYDRFPGDSR DYSTELSVTV AVGASLLFLN ILAFAALYYK RDRRQELRCR RLSPPGGSGS GVPGGGPLLP AAGRELPPEE ELVSLQLKRG GGVGADPAEA LRPACPPDYT LALRRAPDDV PLLAPGALTL LPSGLGPPPP PPPPSLHPFG PFPPPPPTAT SHNNTLPHPH STTRV //