SHAN1_MOUSE
ID SHAN1_MOUSE Reviewed; 2167 AA.
AC D3YZU1;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=SH3 and multiple ankyrin repeat domains protein 1;
DE Short=Shank1;
GN Name=Shank1;
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 [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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 854-939.
RX PubMed=15033168; DOI=10.1016/j.mcn.2003.11.004;
RA Thuret S., Bhatt L., O'Leary D.D., Simon H.H.;
RT "Identification and developmental analysis of genes expressed by
RT dopaminergic neurons of the substantia nigra pars compacta.";
RL Mol. Cell. Neurosci. 25:394-405(2004).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT "Comprehensive identification of phosphorylation sites in postsynaptic
RT density preparations.";
RL Mol. Cell. Proteomics 5:914-922(2006).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-186, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=18034455; DOI=10.1021/pr0701254;
RA Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT "Large-scale identification and evolution indexing of tyrosine
RT phosphorylation sites from murine brain.";
RL J. Proteome Res. 7:311-318(2008).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-540; SER-671; SER-791;
RP SER-898 AND SER-1291, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Brain;
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).
RN [6]
RP TISSUE SPECIFICITY.
RX PubMed=21423165; DOI=10.1038/nature09965;
RA Peca J., Feliciano C., Ting J.T., Wang W., Wells M.F., Venkatraman T.N.,
RA Lascola C.D., Fu Z., Feng G.;
RT "Shank3 mutant mice display autistic-like behaviours and striatal
RT dysfunction.";
RL Nature 472:437-442(2011).
RN [7]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-43; ARG-544; ARG-958; ARG-1059;
RP ARG-1098; ARG-1109; ARG-1257; ARG-1429; ARG-1901; ARG-2022; ARG-2042 AND
RP ARG-2080, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Embryo;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
CC -!- FUNCTION: Seems to be an adapter protein in the postsynaptic density
CC (PSD) of excitatory synapses that interconnects receptors of the
CC postsynaptic membrane including NMDA-type and metabotropic glutamate
CC receptors, and the actin-based cytoskeleton. Plays a role in the
CC structural and functional organization of the dendritic spine and
CC synaptic junction. Overexpression promotes maturation of dendritic
CC spines and the enlargement of spine heads via its ability to recruit
CC Homer to postsynaptic sites, and enhances presynaptic function (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: May homomultimerize via its SAM domain. Interacts with the C-
CC terminus of SSTR2 via the PDZ domain. Interacts with SHARPIN, SPTAN1,
CC HOMER1 and DLGAP1/GKAP. Part of a complex with DLG4/PSD-95 and
CC DLGAP1/GKAP. Interacts with BAIAP2. Interacts with IGSF9 (By
CC similarity). Interacts with HOMER1 and HOMER3 (By similarity).
CC {ECO:0000250, ECO:0000250|UniProtKB:Q9WV48}.
CC -!- INTERACTION:
CC D3YZU1; Q9EP53: Tsc1; NbExp=2; IntAct=EBI-2314988, EBI-1202690;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Synapse {ECO:0000250}.
CC Postsynaptic density {ECO:0000250}. Note=Colocalizes with alpha-
CC latrotoxin receptor 1. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: In brain, highly expressed in cortex, hippocampus
CC and cerebellum. {ECO:0000269|PubMed:21423165}.
CC -!- SIMILARITY: Belongs to the SHANK family. {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; AC152939; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CO436178; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS52229.1; -.
DR RefSeq; NP_001029287.1; NM_001034115.1.
DR RefSeq; XP_006540927.1; XM_006540864.3.
DR AlphaFoldDB; D3YZU1; -.
DR SMR; D3YZU1; -.
DR BioGRID; 232591; 15.
DR CORUM; D3YZU1; -.
DR IntAct; D3YZU1; 13.
DR MINT; D3YZU1; -.
DR STRING; 10090.ENSMUSP00000103571; -.
DR iPTMnet; D3YZU1; -.
DR PhosphoSitePlus; D3YZU1; -.
DR MaxQB; D3YZU1; -.
DR PaxDb; D3YZU1; -.
DR PeptideAtlas; D3YZU1; -.
DR PRIDE; D3YZU1; -.
DR ProteomicsDB; 257149; -.
DR ABCD; D3YZU1; 3 sequenced antibodies.
DR Antibodypedia; 18886; 232 antibodies from 27 providers.
DR Ensembl; ENSMUST00000107938; ENSMUSP00000103571; ENSMUSG00000038738.
DR GeneID; 243961; -.
DR KEGG; mmu:243961; -.
DR UCSC; uc012fjo.1; mouse.
DR CTD; 50944; -.
DR MGI; MGI:3613677; Shank1.
DR VEuPathDB; HostDB:ENSMUSG00000038738; -.
DR eggNOG; KOG0504; Eukaryota.
DR eggNOG; KOG4375; Eukaryota.
DR GeneTree; ENSGT00940000153561; -.
DR InParanoid; D3YZU1; -.
DR OMA; DYEPAMG; -.
DR OrthoDB; 468249at2759; -.
DR PhylomeDB; D3YZU1; -.
DR TreeFam; TF324593; -.
DR Reactome; R-MMU-6794361; Neurexins and neuroligins.
DR BioGRID-ORCS; 243961; 3 hits in 72 CRISPR screens.
DR PRO; PR:D3YZU1; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; D3YZU1; protein.
DR Bgee; ENSMUSG00000038738; Expressed in prefrontal cortex and 140 other tissues.
DR ExpressionAtlas; D3YZU1; baseline and differential.
DR Genevisible; D3YZU1; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0030425; C:dendrite; IDA:BHF-UCL.
DR GO; GO:0043197; C:dendritic spine; IDA:BHF-UCL.
DR GO; GO:0060076; C:excitatory synapse; IDA:BHF-UCL.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0043005; C:neuron projection; IDA:BHF-UCL.
DR GO; GO:0005886; C:plasma membrane; IDA:BHF-UCL.
DR GO; GO:0014069; C:postsynaptic density; IDA:BHF-UCL.
DR GO; GO:0045211; C:postsynaptic membrane; IDA:MGI.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IDA:SynGO.
DR GO; GO:0045202; C:synapse; ISO:MGI.
DR GO; GO:0071532; F:ankyrin repeat binding; ISS:BHF-UCL.
DR GO; GO:0042802; F:identical protein binding; ISS:BHF-UCL.
DR GO; GO:0035255; F:ionotropic glutamate receptor binding; IPI:BHF-UCL.
DR GO; GO:0008022; F:protein C-terminus binding; ISS:BHF-UCL.
DR GO; GO:0044877; F:protein-containing complex binding; ISS:BHF-UCL.
DR GO; GO:0097110; F:scaffold protein binding; ISS:BHF-UCL.
DR GO; GO:0017124; F:SH3 domain binding; ISS:BHF-UCL.
DR GO; GO:0030159; F:signaling receptor complex adaptor activity; ISO:MGI.
DR GO; GO:0031877; F:somatostatin receptor binding; ISS:BHF-UCL.
DR GO; GO:0098919; F:structural constituent of postsynaptic density; IC:SynGO.
DR GO; GO:0030160; F:synaptic receptor adaptor activity; IMP:BHF-UCL.
DR GO; GO:0030534; P:adult behavior; ISO:MGI.
DR GO; GO:0008306; P:associative learning; IMP:BHF-UCL.
DR GO; GO:0060997; P:dendritic spine morphogenesis; IMP:BHF-UCL.
DR GO; GO:0050894; P:determination of affect; ISO:MGI.
DR GO; GO:0046959; P:habituation; IMP:BHF-UCL.
DR GO; GO:0007616; P:long-term memory; IMP:BHF-UCL.
DR GO; GO:0032232; P:negative regulation of actin filament bundle assembly; IDA:MGI.
DR GO; GO:0050885; P:neuromuscular process controlling balance; IMP:BHF-UCL.
DR GO; GO:0042048; P:olfactory behavior; IMP:BHF-UCL.
DR GO; GO:0060999; P:positive regulation of dendritic spine development; ISS:BHF-UCL.
DR GO; GO:2000463; P:positive regulation of excitatory postsynaptic potential; IMP:BHF-UCL.
DR GO; GO:0099173; P:postsynapse organization; IDA:SynGO.
DR GO; GO:0035418; P:protein localization to synapse; IMP:BHF-UCL.
DR GO; GO:0065003; P:protein-containing complex assembly; ISS:BHF-UCL.
DR GO; GO:2000311; P:regulation of AMPA receptor activity; IMP:BHF-UCL.
DR GO; GO:0060013; P:righting reflex; IMP:BHF-UCL.
DR GO; GO:0035176; P:social behavior; IMP:BHF-UCL.
DR GO; GO:0060074; P:synapse maturation; ISS:BHF-UCL.
DR GO; GO:0071625; P:vocalization behavior; IMP:BHF-UCL.
DR Gene3D; 1.10.150.50; -; 1.
DR Gene3D; 1.25.40.20; -; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR041489; PDZ_6.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR001660; SAM.
DR InterPro; IPR013761; SAM/pointed_sf.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR Pfam; PF12796; Ank_2; 2.
DR Pfam; PF17820; PDZ_6; 1.
DR Pfam; PF00536; SAM_1; 1.
DR Pfam; PF07653; SH3_2; 1.
DR SMART; SM00248; ANK; 6.
DR SMART; SM00228; PDZ; 1.
DR SMART; SM00454; SAM; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF47769; SSF47769; 1.
DR SUPFAM; SSF48403; SSF48403; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR SUPFAM; SSF50156; SSF50156; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 3.
DR PROSITE; PS50106; PDZ; 1.
DR PROSITE; PS50105; SAM_DOMAIN; 1.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW ANK repeat; Cytoplasm; Differentiation; Methylation; Neurogenesis;
KW Phosphoprotein; Reference proteome; Repeat; SH3 domain; Synapse.
FT CHAIN 1..2167
FT /note="SH3 and multiple ankyrin repeat domains protein 1"
FT /id="PRO_0000411019"
FT REPEAT 212..242
FT /note="ANK 1"
FT REPEAT 246..275
FT /note="ANK 2"
FT REPEAT 279..309
FT /note="ANK 3"
FT REPEAT 313..342
FT /note="ANK 4"
FT REPEAT 346..375
FT /note="ANK 5"
FT REPEAT 379..407
FT /note="ANK 6"
FT DOMAIN 554..613
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 663..757
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 2104..2167
FT /note="SAM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
FT REGION 1..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 413..432
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 454..546
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 841..894
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 917..1233
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1245..1290
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1308..1331
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1361..1417
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1429..1458
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1500..1725
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1740..1790
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1828..1866
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1898..1988
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2002..2029
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..20
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 454..495
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 500..514
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 925..946
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1004..1025
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1033..1050
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1066..1084
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1138..1157
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1165..1189
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1205..1224
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1377..1400
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1588..1619
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1622..1639
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1647..1676
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1691..1711
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1846..1862
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1917..1948
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1961..1988
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 43
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 186
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:18034455"
FT MOD_RES 540
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 544
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 671
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 791
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 898
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 958
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 1059
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 1098
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 1109
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 1257
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 1291
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1429
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 1442
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9WV48"
FT MOD_RES 1901
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 2022
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 2042
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 2080
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT CONFLICT 939
FT /note="P -> R (in Ref. 2; CO436178)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2167 AA; 226317 MW; A732912793A975AE CRC64;
MTHSPATSED EERHSASECP EGGSESDSSP DGPGRGPQGT RGRGSGAPGN LASTRGLQGR
SMSVPDDAHF SMMVFRIGIP DLHQTKCLRF NPDATIWTAK QQVLCALSES LQDVLNYGLF
QPATSGRDAN FLEEERLLRE YPQSFEKGVP YLEFRYKTRV YKQTNLDEKQ LAKLHTKTGL
KKFLEYVQLG TSDKVARLLD KGLDPNYHDS DSGETPLTLA AQTEGSVEVI RTLCLGGAHI
DFRARDGMTA LHKAACARHC LALTALLDLG GSPNYKDRRG LTPLFHTAMV GGDPRCCELL
LYNRAQLGIA DENGWQEIHQ ACQRGHSQHL EHLLFYGAEP GAQNASGNTA LHICALYNKE
TCARILLYRG ANKDVKNNNG QTPFQVAVIA GNFELGELIR NHREQDVVPF QESPKYAARR
RGPPGAGLTV PPALLRANSD TSMALPDWMV FSAPGASSSG TPGPTSGSQG QSQPSAPSTK
LSSGTLRSAS SPRGARARSP SRGRHPEDAK RQPRGRPSSS GTPRDGPAGG TGGSGGPGGS
LGSRGRRRKL YSAVPGRSFM AVKSYQAQGE GEISLSKGEK IKVLSIGEGG FWEGQVKGRV
GWFPSDCLEE VANRSQEGRQ ESRSDKAKRL FRHYTVGSYD SFDAPSLIDG IDSGSDYIIK
EKTVLLQKKD SEGFGFVLRG AKAQTPIEEF TPTPAFPALQ YLESVDEGGV AWRAGLRMGD
FLIEVNGQNV VKVGHRQVVN MIRQGGNTLM VKVVMVTRHP DMDEAVHKKA SQQAKRLPPP
AISLRSKSMT SELEEMVSPW KKKIEYEQQP AAVPSMEKKR TVYQMALNKL DEILAAAQQT
ISASESPGPG GLASLGKHRP KGFFATESSF DPHHRSQPSY DRPSFLPPGP GLMLRQKSIG
AAEDDRPYLA PPAMKFSRSL SVPGSEDIPP PPTTSPPEPP YSTPPAPSSS GRLTPSPRGG
PFNPGSGGPL PASSPSSFDG PSPPDPRSGG REKSLYHSGA LPPAHHHPPH HHHHHAPPPQ
PHHHHAHPPH PPEMETGGSP DDPPPRLALG PQPSLRGWRG GGPSPTSGAP SPSHHSSSGG
SSGPAQAPAL RYFQLPPRAA SAAMYVPARS GRGRKGPLVK QTKVEGEPQK GSLPPASSPT
SPALPRSEPP PAGPSEKNSI PIPTIIIKAP STSSSGRSSQ GSSTEAEPPT QPDGAGGGGS
SPSPAPATSP VPPSPSPVPT PASPSGPATL DFTSQFGAAL VGAARREGGW QNEARRRSTL
FLSTDAGDED GGDSGLGPGA PPGPRLRHSK SIDEGMFSAE PYLRLESGGS SGGYGAYAAG
SRAYGGSGSS SAFTSFLPPR PLVHPLTGKA LDPASPLGLA LAARERALKE SSEGGVTPQP
PPRPPSPRYD APPPTLHHHS PHSPHSPHAR HEPVLRLWGD PARRELGYRA GLGSQEKALT
ASPPAARRSL LHRLPPTAPG VGPLLLQLGP EPPTPHPGVS KAWRTAAPEE PERLPLHVRF
LENCQARPPP AGTRGSSTED GPGVPPPSPR RVLPTSPTSP RGNEENGLPL LVLPPPAPSV
DVDDGEFLFA EPLPPPLEFS NSFEKPESPL TPGPPHPLPD PPSPATPLPA APPPAVAAAP
PTLDSTASSL TSYDSEVATL TQGAPAAPGD PPAPGPPAPA APAPPAPQPG PDPPPGTDSG
IEEVDSRSSS DHPLETISSA STLSSLSAEG GGNTGGVAGG GAGVASGTEL LDTYVAYLDG
QAFGGSGTPG PPYPPQLMTP SKLRGRALGT SGNLRPGPSG GLRDPVTPTS PTVSVTGAGT
DGLLALSACS GPSTAGVAGG PVAVEPEVPP VPLPTASSLP RKLLPWEEGP GPPPPPLPGP
LSQPQASALA TVKASIISEL SSKLQQFGGA STAGGALPWA RGGSGGSTDS HHGGASYIPE
RTSSLQRQRL SEDSQTSLLS KPSSSIFQNW PKPPLPPLPT GSGVSSSTAA APGATSPSAS
SASASTRHLQ GVEFEMRPPL LRRAPSPSLL PASDHKVSPA PRPSSLPILP SGPLYPGLFD
IRSSPTGGAG GSADPFAPVF VPPHPGISGG LGGALSGASR SLSPTRLLSL PPDKPFGAKP
LGFWTKFDVA DWLEWLGLSE HRAQFLDHEI DGSHLPALTK EDYVDLGVTR VGHRMNIDRA
LKFFLER
