NEB2_MOUSE
ID NEB2_MOUSE Reviewed; 817 AA.
AC Q6R891; Q8K0X7;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Neurabin-2;
DE AltName: Full=Neurabin-II;
DE AltName: Full=Protein phosphatase 1 regulatory subunit 9B;
DE AltName: Full=Spinophilin;
GN Name=Ppp1r9b;
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] (ISOFORM 1).
RC STRAIN=C57BL/6J;
RA Allen P.B.;
RT "Mouse spinophilin cDNA.";
RL Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Eye;
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 [4]
RP PHOSPHORYLATION BY PKA, PHOSPHORYLATION AT SER-94, AND DEPHOSPHORYLATION BY
RP PP1 AND PP2A.
RX PubMed=16300646; DOI=10.1111/j.1471-4159.2005.03491.x;
RA Uematsu K., Futter M., Hsieh-Wilson L.C., Higashi H., Maeda H., Nairn A.C.,
RA Greengard P., Nishi A.;
RT "Regulation of spinophilin Ser94 phosphorylation in neostriatal neurons
RT involves both DARPP-32-dependent and independent pathways.";
RL J. Neurochem. 95:1642-1652(2005).
RN [5]
RP PHOSPHORYLATION BY MAPK1 AND CDK5, PHOSPHORYLATION AT SER-15; SER-17 AND
RP SER-205, AND MUTAGENESIS OF SER-15.
RX PubMed=15728359; DOI=10.1073/pnas.0409802102;
RA Futter M., Uematsu K., Bullock S.A., Kim Y., Hemmings H.C. Jr., Nishi A.,
RA Greengard P., Nairn A.C.;
RT "Phosphorylation of spinophilin by ERK and cyclin-dependent PK 5 (Cdk5).";
RL Proc. Natl. Acad. Sci. U.S.A. 102:3489-3494(2005).
RN [6]
RP INTERACTION WITH DCLK2.
RX PubMed=16628014; DOI=10.4161/cc.5.9.2715;
RA Coquelle F.M., Levy T., Bergmann S., Wolf S.G., Bar-El D., Sapir T.,
RA Brody Y., Orr I., Barkai N., Eichele G., Reiner O.;
RT "Common and divergent roles for members of the mouse DCX superfamily.";
RL Cell Cycle 5:976-983(2006).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Lung, Pancreas, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Seems to act as a scaffold protein in multiple signaling
CC pathways. Modulates excitatory synaptic transmission and dendritic
CC spine morphology. Binds to actin filaments (F-actin) and shows cross-
CC linking activity. Binds along the sides of the F-actin. May play an
CC important role in linking the actin cytoskeleton to the plasma membrane
CC at the synaptic junction. Believed to target protein phosphatase 1/PP1
CC to dendritic spines, which are rich in F-actin, and regulates its
CC specificity toward ion channels and other substrates, such as AMPA-type
CC and NMDA-type glutamate receptors. Plays a role in regulation of G-
CC protein coupled receptor signaling, including dopamine D2 receptors and
CC alpha-adrenergic receptors. May establish a signaling complex for
CC dopaminergic neurotransmission through D2 receptors by linking
CC receptors downstream signaling molecules and the actin cytoskeleton.
CC Binds to ADRA1B and RGS2 and mediates regulation of ADRA1B signaling.
CC May confer to Rac signaling specificity by binding to both, RacGEFs and
CC Rac effector proteins. Probably regulates p70 S6 kinase activity by
CC forming a complex with TIAM1. Required for hepatocyte growth factor
CC (HGF)-induced cell migration (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Possibly exists as a homodimer, homotrimer or a homotetramer.
CC Interacts with F-actin, PPP1CA, neurabin-1, TGN38 and D(2) dopamine
CC receptor. Interacts with RGS1, RGS2, RGS4, RGS19 and ADRA1B, ADRA2A,
CC ADRA2B, ADRA2C, CDKN2A, PPP1R2, RASGFR1 and TIAM1. Interacts (via C-
CC terminus) with SPATA13 (via C-terminal tail) (By similarity). Interacts
CC with DCLK2. Interacts with ADRA2B (By similarity).
CC {ECO:0000250|UniProtKB:O35274, ECO:0000250|UniProtKB:Q96SB3,
CC ECO:0000269|PubMed:16628014}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:O35274}. Nucleus {ECO:0000250}. Postsynaptic
CC density {ECO:0000250|UniProtKB:O35274}. Cell junction, adherens
CC junction {ECO:0000250}. Cell projection, dendritic spine
CC {ECO:0000250|UniProtKB:O35274}. Cytoplasm {ECO:0000250}. Cell membrane
CC {ECO:0000250}. Cell projection, lamellipodium {ECO:0000250}. Cell
CC projection, filopodium {ECO:0000250}. Cell projection, ruffle membrane
CC {ECO:0000250}. Note=Enriched at synapse and cadherin-based cell-cell
CC adhesion sites. In neurons, both cytosolic and membrane-associated, and
CC highly enriched in the postsynaptic density apposed to exitatory
CC synapses (By similarity). Colocalizes with PPP1R2 at actin-rich
CC adherens junctions in epithelial cells and in dendritic spines.
CC Accumulates in the lamellipodium, filopodium and ruffle membrane in
CC response to hepatocyte growth factor (HGF) treatment (By similarity).
CC {ECO:0000250, ECO:0000250|UniProtKB:O35274}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6R891-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6R891-2; Sequence=VSP_017674, VSP_017675;
CC -!- DOMAIN: The PP1 binding region is natively unstructured, upon PP1
CC binding, it acquires structure, blocks a substrate-binding site, and
CC restricts PP1 phosphatase specificity to a subset of substrates.
CC {ECO:0000250}.
CC -!- PTM: Stimulation of D1 (but not D2) dopamine receptors induces Ser-94
CC phosphorylation. Dephosphorylation of Ser-94 is mediated mainly by PP1
CC and to a lesser extent by PP2A. Phosphorylation of spinophilin disrupts
CC its association with F-actin, but does not affect its binding to PP1
CC (By similarity). {ECO:0000250}.
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DR EMBL; AY508450; AAR91608.1; -; mRNA.
DR EMBL; AL606480; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC029672; AAH29672.1; -; mRNA.
DR CCDS; CCDS25268.1; -. [Q6R891-1]
DR RefSeq; NP_758465.2; NM_172261.3. [Q6R891-1]
DR AlphaFoldDB; Q6R891; -.
DR BMRB; Q6R891; -.
DR SMR; Q6R891; -.
DR BioGRID; 229847; 482.
DR IntAct; Q6R891; 16.
DR MINT; Q6R891; -.
DR STRING; 10090.ENSMUSP00000041732; -.
DR iPTMnet; Q6R891; -.
DR PhosphoSitePlus; Q6R891; -.
DR EPD; Q6R891; -.
DR jPOST; Q6R891; -.
DR MaxQB; Q6R891; -.
DR PaxDb; Q6R891; -.
DR PeptideAtlas; Q6R891; -.
DR PRIDE; Q6R891; -.
DR ProteomicsDB; 252873; -. [Q6R891-1]
DR ProteomicsDB; 252874; -. [Q6R891-2]
DR Antibodypedia; 30484; 149 antibodies from 28 providers.
DR DNASU; 217124; -.
DR Ensembl; ENSMUST00000038696; ENSMUSP00000041732; ENSMUSG00000038976. [Q6R891-1]
DR Ensembl; ENSMUST00000107748; ENSMUSP00000103377; ENSMUSG00000038976. [Q6R891-2]
DR GeneID; 217124; -.
DR KEGG; mmu:217124; -.
DR UCSC; uc007kzr.2; mouse. [Q6R891-1]
DR UCSC; uc007kzs.2; mouse. [Q6R891-2]
DR CTD; 84687; -.
DR MGI; MGI:2387581; Ppp1r9b.
DR VEuPathDB; HostDB:ENSMUSG00000038976; -.
DR eggNOG; KOG1945; Eukaryota.
DR GeneTree; ENSGT00940000158833; -.
DR HOGENOM; CLU_007401_1_0_1; -.
DR InParanoid; Q6R891; -.
DR OMA; AHKEEVD; -.
DR OrthoDB; 128743at2759; -.
DR PhylomeDB; Q6R891; -.
DR TreeFam; TF105540; -.
DR BioGRID-ORCS; 217124; 4 hits in 73 CRISPR screens.
DR ChiTaRS; Ppp1r9b; mouse.
DR PRO; PR:Q6R891; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q6R891; protein.
DR Bgee; ENSMUSG00000038976; Expressed in dentate gyrus of hippocampal formation granule cell and 85 other tissues.
DR Genevisible; Q6R891; MM.
DR GO; GO:0015629; C:actin cytoskeleton; ISO:MGI.
DR GO; GO:0005912; C:adherens junction; IEA:UniProtKB-SubCell.
DR GO; GO:0030864; C:cortical actin cytoskeleton; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:1990780; C:cytoplasmic side of dendritic spine plasma membrane; ISO:MGI.
DR GO; GO:0030425; C:dendrite; IBA:GO_Central.
DR GO; GO:0043197; C:dendritic spine; ISO:MGI.
DR GO; GO:0044327; C:dendritic spine head; ISO:MGI.
DR GO; GO:0032591; C:dendritic spine membrane; ISO:MGI.
DR GO; GO:0044326; C:dendritic spine neck; ISO:MGI.
DR GO; GO:0030175; C:filopodium; IDA:MGI.
DR GO; GO:0030426; C:growth cone; ISO:MGI.
DR GO; GO:0030027; C:lamellipodium; ISS:UniProtKB.
DR GO; GO:0043005; C:neuron projection; ISO:MGI.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0014069; C:postsynaptic density; ISO:MGI.
DR GO; GO:0032587; C:ruffle membrane; ISS:UniProtKB.
DR GO; GO:0003779; F:actin binding; ISO:MGI.
DR GO; GO:0051015; F:actin filament binding; ISO:MGI.
DR GO; GO:0031749; F:D2 dopamine receptor binding; ISO:MGI.
DR GO; GO:0019900; F:kinase binding; ISO:MGI.
DR GO; GO:0008022; F:protein C-terminus binding; ISO:MGI.
DR GO; GO:0004672; F:protein kinase activity; ISO:MGI.
DR GO; GO:0008157; F:protein phosphatase 1 binding; ISO:MGI.
DR GO; GO:0004864; F:protein phosphatase inhibitor activity; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0044325; F:transmembrane transporter binding; ISO:MGI.
DR GO; GO:0030036; P:actin cytoskeleton organization; TAS:MGI.
DR GO; GO:0030042; P:actin filament depolymerization; IEA:Ensembl.
DR GO; GO:0007015; P:actin filament organization; IPI:MGI.
DR GO; GO:0007568; P:aging; IEA:Ensembl.
DR GO; GO:0019722; P:calcium-mediated signaling; IMP:MGI.
DR GO; GO:0016477; P:cell migration; ISS:UniProtKB.
DR GO; GO:0071364; P:cellular response to epidermal growth factor stimulus; IEA:Ensembl.
DR GO; GO:0071392; P:cellular response to estradiol stimulus; IEA:Ensembl.
DR GO; GO:0071315; P:cellular response to morphine; IMP:UniProtKB.
DR GO; GO:1901653; P:cellular response to peptide; IEA:Ensembl.
DR GO; GO:0071466; P:cellular response to xenobiotic stimulus; IEA:Ensembl.
DR GO; GO:0021987; P:cerebral cortex development; IEA:Ensembl.
DR GO; GO:0016358; P:dendrite development; IMP:MGI.
DR GO; GO:0003006; P:developmental process involved in reproduction; IEA:Ensembl.
DR GO; GO:0046847; P:filopodium assembly; ISS:UniProtKB.
DR GO; GO:0021766; P:hippocampus development; IEA:Ensembl.
DR GO; GO:0007612; P:learning; IEA:Ensembl.
DR GO; GO:0060179; P:male mating behavior; IEA:Ensembl.
DR GO; GO:0050804; P:modulation of chemical synaptic transmission; IEA:InterPro.
DR GO; GO:0030308; P:negative regulation of cell growth; ISO:MGI.
DR GO; GO:0032515; P:negative regulation of phosphoprotein phosphatase activity; ISO:MGI.
DR GO; GO:0031175; P:neuron projection development; IBA:GO_Central.
DR GO; GO:1903829; P:positive regulation of protein localization; ISO:MGI.
DR GO; GO:1904372; P:positive regulation of protein localization to actin cortical patch; ISO:MGI.
DR GO; GO:1903078; P:positive regulation of protein localization to plasma membrane; ISO:MGI.
DR GO; GO:1903119; P:protein localization to actin cytoskeleton; ISO:MGI.
DR GO; GO:1990778; P:protein localization to cell periphery; ISO:MGI.
DR GO; GO:0042127; P:regulation of cell population proliferation; IEA:InterPro.
DR GO; GO:2000474; P:regulation of opioid receptor signaling pathway; IMP:UniProtKB.
DR GO; GO:0001932; P:regulation of protein phosphorylation; IMP:MGI.
DR GO; GO:0061458; P:reproductive system development; IEA:Ensembl.
DR GO; GO:0001975; P:response to amphetamine; IEA:Ensembl.
DR GO; GO:0097338; P:response to clozapine; IEA:Ensembl.
DR GO; GO:0035902; P:response to immobilization stress; IEA:Ensembl.
DR GO; GO:1904373; P:response to kainic acid; IEA:Ensembl.
DR GO; GO:1904386; P:response to L-phenylalanine derivative; IEA:Ensembl.
DR GO; GO:0035094; P:response to nicotine; IEA:Ensembl.
DR GO; GO:0034695; P:response to prostaglandin E; IEA:Ensembl.
DR GO; GO:0048545; P:response to steroid hormone; IEA:Ensembl.
DR Gene3D; 2.30.42.10; -; 1.
DR InterPro; IPR029921; NEB2.
DR InterPro; IPR040645; Neurabin-1/2_PDZ.
DR InterPro; IPR043446; Neurabin-like.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR PANTHER; PTHR16154; PTHR16154; 1.
DR PANTHER; PTHR16154:SF24; PTHR16154:SF24; 1.
DR Pfam; PF00595; PDZ; 1.
DR Pfam; PF17817; PDZ_5; 1.
DR SMART; SM00228; PDZ; 1.
DR SUPFAM; SSF50156; SSF50156; 1.
DR PROSITE; PS50106; PDZ; 1.
PE 1: Evidence at protein level;
KW Actin-binding; Alternative splicing; Cell junction; Cell membrane;
KW Cell projection; Coiled coil; Cytoplasm; Cytoskeleton;
KW Developmental protein; Differentiation; Membrane; Neurogenesis; Nucleus;
KW Phosphoprotein; Reference proteome; Synapse.
FT CHAIN 1..817
FT /note="Neurabin-2"
FT /id="PRO_0000228615"
FT DOMAIN 496..584
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT REGION 1..154
FT /note="Actin-binding"
FT /evidence="ECO:0000250"
FT REGION 1..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 64..163
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 100..371
FT /note="Interaction with D(2) dopamine receptor"
FT /evidence="ECO:0000250"
FT REGION 164..282
FT /note="Actin-binding"
FT /evidence="ECO:0000250"
FT REGION 169..255
FT /note="Interaction with ADRA2A, ADRA2B and ADRA2C"
FT /evidence="ECO:0000250"
FT REGION 216..451
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 417..494
FT /note="Interaction with protein phosphatase 1"
FT /evidence="ECO:0000250"
FT REGION 480..525
FT /note="Interaction with RGS2"
FT /evidence="ECO:0000250"
FT REGION 595..816
FT /note="Interaction with TGN38"
FT /evidence="ECO:0000250"
FT COILED 595..616
FT /evidence="ECO:0000255"
FT COILED 665..816
FT /evidence="ECO:0000255"
FT MOTIF 447..451
FT /note="PP1-binding motif"
FT /evidence="ECO:0000250|UniProtKB:O35274"
FT COMPBIAS 97..111
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 286..305
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 370..391
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 407..426
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 15
FT /note="Phosphoserine; by MAPK1"
FT /evidence="ECO:0000269|PubMed:15728359"
FT MOD_RES 17
FT /note="Phosphoserine; by CDK5"
FT /evidence="ECO:0000269|PubMed:15728359"
FT MOD_RES 94
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000269|PubMed:16300646"
FT MOD_RES 100
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O35274"
FT MOD_RES 116
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O35274"
FT MOD_RES 192
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96SB3"
FT MOD_RES 193
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q96SB3"
FT MOD_RES 205
FT /note="Phosphoserine; by MAPK1"
FT /evidence="ECO:0000269|PubMed:15728359"
FT MOD_RES 207
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q96SB3"
FT MOD_RES 438
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96SB3"
FT MOD_RES 658
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96SB3"
FT VAR_SEQ 1..424
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_017674"
FT VAR_SEQ 425..456
FT /note="YEPESGCVEIPGLSEEEDPAPSRKIHFSTAPI -> MDTGLHATQLAQGPSP
FT ANVLLPSYGPLRTAPP (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_017675"
FT MUTAGEN 15
FT /note="S->E: Increases filopodial density."
FT /evidence="ECO:0000269|PubMed:15728359"
SQ SEQUENCE 817 AA; 89520 MW; 1654037C196F2F6B CRC64;
MMKTEPRGPG GPLRSASPHR SAYEAGIQAL KPPDAPGPDE APKAAHHKKY GSNVHRIKSM
FLQMGTTAGP PGEAGGGAGM AEAPRASDRG VRLSLPRASS LNENVDHSAL LKLGTSVSER
VSRFDSKPAP SAQPAPPPHP PSRLQETRKL FERSVPAASG GDKEAVARRL LRQERAGLQD
RKLDVVVRFN GSTEALDKLD ADAVSPTVSQ LSAVFEKADS RTGLHRAPGP PRAAGAPQVN
SKLVTKRSRV FQPPPPPPAP SGDGATEKER GPGGQQPPQH RVAPARPPPK PREVRKIKPV
EVEESGESEA ESAPGEVIQA EVTVHAALEN GSTPATTASP APEEPKAEAV PEEEAAASVA
TLERGVDNGR APDMAPEEVD ESKKEDFSEA DLVDVSAYSG LGEDSGGSAL EEDDEEDEED
GEPPYEPESG CVEIPGLSEE EDPAPSRKIH FSTAPIQVFS TYSNEDYDRR NEDVDPMAAS
AEYELEKRVE RLELFPVELE KDSEGLGISI IGMGAGADMG LEKLGIFVKT VTEGGAAHRD
GRIQVNDLLV EVDGTSLVGV TQSFAASVLR NTKGRVRFMI GRERPGEQSE VAQLIQQTLE
QERWQREMME QRYAQYGEDD EETGEYATDE DEELSPTFPG GEMAIEVFEL AENEDALSPV
EMEPEKLVHK FKELQIKHAV TEAEIQQLKR KLQSLEQEKG RWRVEKAQLE QSVEENKERM
EKLEGYWGEA QSLCQAVDEH LRETQAQYQA LERKYSKAKR LIKDYQQKEI EFLKKETAQR
RVLEESELAR KEEMDKLLDK ISELEGNLQT LRNSNST
