NACAM_MOUSE
ID NACAM_MOUSE Reviewed; 2187 AA.
AC P70670; E9QMB1;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Nascent polypeptide-associated complex subunit alpha, muscle-specific form;
DE AltName: Full=Alpha-NAC, muscle-specific form;
DE Short=skNAC;
GN Name=Naca; Synonyms=Gm1878;
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 [GENOMIC DNA / MRNA] (ISOFORM 2), FUNCTION, ALTERNATIVE
RP SPLICING, AND TISSUE SPECIFICITY.
RX PubMed=8698236; DOI=10.1101/gad.10.14.1763;
RA Yotov W.V., St Arnaud R.;
RT "Differential splicing-in of a proline-rich exon converts alphaNAC into a
RT muscle-specific transcription factor.";
RL Genes Dev. 10:1763-1772(1996).
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 INTERACTION WITH SMYD1, MUTAGENESIS OF LEU-1952, AND SUBCELLULAR LOCATION.
RX PubMed=12011100; DOI=10.1074/jbc.m204121200;
RA Sims R.J. III, Weihe E.K., Zhu L., O'Malley S., Harriss J.V.,
RA Gottlieb P.D.;
RT "m-Bop, a repressor protein essential for cardiogenesis, interacts with
RT skNAC, a heart- and muscle-specific transcription factor.";
RL J. Biol. Chem. 277:26524-26529(2002).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2138, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic brain;
RX PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT "Phosphoproteomic analysis of the developing mouse brain.";
RL Mol. Cell. Proteomics 3:1093-1101(2004).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2138, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2138, AND IDENTIFICATION BY
RP 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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-590; SER-822; SER-1174;
RP SER-1177; THR-1364; SER-1368; SER-1392; THR-1398; SER-1400; SER-1423;
RP SER-1492; THR-2131 AND SER-2138, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
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 [8]
RP FUNCTION, INTERACTION WITH SMYD1, AND DISRUPTION PHENOTYPE.
RX PubMed=21071677; DOI=10.1073/pnas.1013493107;
RA Park C.Y., Pierce S.A., von Drehle M., Ivey K.N., Morgan J.A., Blau H.M.,
RA Srivastava D.;
RT "skNAC, a Smyd1-interacting transcription factor, is involved in cardiac
RT development and skeletal muscle growth and regeneration.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:20750-20755(2010).
RN [9]
RP FUNCTION.
RX PubMed=23662692; DOI=10.1042/bj20130195;
RA Berkholz J., Zakrzewicz A., Munz B.;
RT "skNAC depletion stimulates myoblast migration and perturbs
RT sarcomerogenesis by enhancing calpain 1 and 3 activity.";
RL Biochem. J. 453:303-310(2013).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-2114, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [11]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-247, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
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: Cardiac- and muscle-specific transcription factor. May act to
CC regulate the expression of genes involved in the development of
CC myotubes. Plays a critical role in ventricular cardiomyocyte expansion
CC and regulates postnatal skeletal muscle growth and regeneration.
CC Involved in the organized assembly of thick and thin filaments of
CC myofibril sarcomeres. {ECO:0000269|PubMed:21071677,
CC ECO:0000269|PubMed:23662692, ECO:0000269|PubMed:8698236}.
CC -!- SUBUNIT: Interacts (via PXLXP motif) with the muscle-restricted histone
CC methyltransferase SMYD1 (via MYND-type zinc finger).
CC {ECO:0000269|PubMed:12011100, ECO:0000269|PubMed:21071677}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12011100}. Nucleus
CC {ECO:0000269|PubMed:12011100}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=2; Synonyms=Gp220, skNAC;
CC IsoId=P70670-1; Sequence=Displayed;
CC Name=1;
CC IsoId=Q60817-1; Sequence=External;
CC -!- TISSUE SPECIFICITY: Specifically expressed in heart and skeletal
CC muscle: it is present in differentiated myotubes but not in myoblasts.
CC {ECO:0000269|PubMed:8698236}.
CC -!- DEVELOPMENTAL STAGE: Expressed concomitant with the onset of
CC mineralization in ossification centers of developing bone.
CC -!- INDUCTION: Induced in muscle by wounding.
CC -!- PTM: Phosphorylation of Ser-2015 by ILK during cell adhesion may
CC promote nuclear localization. Phosphorylation of Thr-2131 by GSK3B may
CC promote proteasome mediated degradation.
CC -!- DISRUPTION PHENOTYPE: Partial embryonic lethality by embryonic day
CC 12.5, with ventricular hypoplasia and decreased cardiomyocyte
CC proliferation. Viable skNAC(-/-) adult mice have reduced postnatal
CC skeletal muscle growth and impaired regenerative capacity after
CC cardiotoxin-induced injury. Satellite cells have impaired survival
CC compared with wild-type. {ECO:0000269|PubMed:21071677}.
CC -!- SIMILARITY: Belongs to the NAC-alpha family. {ECO:0000305}.
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DR EMBL; U48364; AAB18734.1; -; mRNA.
DR EMBL; U48363; AAB18732.1; -; Genomic_DNA.
DR EMBL; AC131120; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS48723.1; -. [P70670-1]
DR PIR; T30826; T30826.
DR RefSeq; NP_001106670.1; NM_001113199.1. [P70670-1]
DR RefSeq; NP_038636.2; NM_013608.3.
DR AlphaFoldDB; P70670; -.
DR SMR; P70670; -.
DR BioGRID; 201682; 16.
DR ELM; P70670; -.
DR IntAct; P70670; 6.
DR MINT; P70670; -.
DR STRING; 10090.ENSMUSP00000089680; -.
DR iPTMnet; P70670; -.
DR PhosphoSitePlus; P70670; -.
DR SwissPalm; P70670; -.
DR EPD; P70670; -.
DR jPOST; P70670; -.
DR PaxDb; P70670; -.
DR PeptideAtlas; P70670; -.
DR PRIDE; P70670; -.
DR ProteomicsDB; 252644; -. [P70670-1]
DR Antibodypedia; 28384; 97 antibodies from 17 providers.
DR DNASU; 17938; -.
DR Ensembl; ENSMUST00000092048; ENSMUSP00000089680; ENSMUSG00000061315. [P70670-1]
DR GeneID; 17938; -.
DR KEGG; mmu:17938; -.
DR UCSC; uc007hlc.2; mouse. [P70670-1]
DR CTD; 4666; -.
DR MGI; MGI:106095; Naca.
DR VEuPathDB; HostDB:ENSMUSG00000061315; -.
DR eggNOG; KOG2239; Eukaryota.
DR GeneTree; ENSGT00440000033468; -.
DR HOGENOM; CLU_237256_0_0_1; -.
DR InParanoid; P70670; -.
DR OMA; PHKGAPT; -.
DR OrthoDB; 1331328at2759; -.
DR PhylomeDB; P70670; -.
DR TreeFam; TF313348; -.
DR BioGRID-ORCS; 17938; 27 hits in 73 CRISPR screens.
DR ChiTaRS; Naca; mouse.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; P70670; protein.
DR Bgee; ENSMUSG00000061315; Expressed in ventricular zone and 67 other tissues.
DR ExpressionAtlas; P70670; baseline and differential.
DR Genevisible; P70670; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005854; C:nascent polypeptide-associated complex; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0017025; F:TBP-class protein binding; IDA:MGI.
DR GO; GO:0003713; F:transcription coactivator activity; IDA:MGI.
DR GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR GO; GO:0051451; P:myoblast migration; IMP:MGI.
DR GO; GO:1905551; P:negative regulation of protein localization to endoplasmic reticulum; ISO:MGI.
DR GO; GO:0006612; P:protein targeting to membrane; IBA:GO_Central.
DR Gene3D; 2.20.70.30; -; 1.
DR InterPro; IPR016641; EGD2/NACA.
DR InterPro; IPR044034; NAC-like_UBA.
DR InterPro; IPR038187; NAC_A/B_dom_sf.
DR InterPro; IPR002715; Nas_poly-pep-assoc_cplx_dom.
DR PANTHER; PTHR21713; PTHR21713; 2.
DR Pfam; PF19026; HYPK_UBA; 1.
DR Pfam; PF01849; NAC; 1.
DR SMART; SM01407; NAC; 1.
DR PROSITE; PS51151; NAC_AB; 1.
PE 1: Evidence at protein level;
KW Acetylation; Activator; Alternative splicing; Cytoplasm; DNA-binding;
KW Isopeptide bond; Methylation; Nucleus; Phosphoprotein; Reference proteome;
KW Transcription; Transcription regulation; Transport; Ubl conjugation.
FT CHAIN 1..2187
FT /note="Nascent polypeptide-associated complex subunit
FT alpha, muscle-specific form"
FT /id="PRO_0000135578"
FT DOMAIN 2042..2107
FT /note="NAC-A/B"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00507"
FT DOMAIN 2148..2185
FT /note="UBA"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 32..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 172..196
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 335..370
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 579..611
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 738..835
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 884..1847
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1892..2053
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2041..2052
FT /note="Required for DNA-binding"
FT MOTIF 1950..1954
FT /note="PXLXP"
FT COMPBIAS 50..73
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 174..193
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 343..370
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 751..770
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 772..805
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 819..835
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 888..905
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 937..951
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1021..1035
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1059..1080
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1104..1128
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1206..1220
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1236..1253
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1416..1445
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1478..1492
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1606..1630
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1659..1673
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1684..1776
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1805..1822
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1969..1983
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2033..2052
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 247
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 590
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 822
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1174
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1177
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1364
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1368
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1392
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1398
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1400
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1423
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1492
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 2015
FT /note="Phosphoserine; by ILK1"
FT /evidence="ECO:0000305"
FT MOD_RES 2104
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:E9PAV3"
FT MOD_RES 2114
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 2131
FT /note="Phosphothreonine; by GSK3-beta"
FT /evidence="ECO:0000305, ECO:0007744|PubMed:21183079"
FT MOD_RES 2133
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:E9PAV3"
FT MOD_RES 2138
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15345747,
FT ECO:0007744|PubMed:17242355, ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 2158
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:E9PAV3"
FT MOD_RES 2163
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:E9PAV3"
FT MOD_RES 2175
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:E9PAV3"
FT CROSSLNK 2114
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:E9PAV3"
FT MUTAGEN 1952
FT /note="L->A: Loss of interaction with SMYD1."
FT /evidence="ECO:0000269|PubMed:12011100"
FT CONFLICT 941
FT /note="P -> Q (in Ref. 1; AAB18734/AAB18732)"
FT /evidence="ECO:0000305"
FT CONFLICT 1523
FT /note="A -> G (in Ref. 1; AAB18734/AAB18732)"
FT /evidence="ECO:0000305"
FT CONFLICT 1653
FT /note="A -> R (in Ref. 1; AAB18734/AAB18732)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2187 AA; 220499 MW; 7BB6EDE3538F0954 CRC64;
MPGEATETVP ATEQELPQPQ AETAVLPMSS ALKVAAVGQP GPTPPSSLGP QQSPIVTAHQ
PSPLPSSVSS TPFEVPFAQP ITAETALPSG TAPPTPTFLP HLIGPPISPA ALALASPMIG
LAQKGARSSS APLSLVALAP HSVQKSSVCP PHPLTSPPSA AGAELGALTA SIPPLEPKTS
TSQVPSQGTL NLKGTAPCPP DVVRAFPSHL ENPLASVQPG LMSCPQTLSN TSPVKGVPIS
SALTQSRLSL NLKGPVSPPA RNTAAPSIPL APSTSLGCHL PLLHHSSVDS PIQPPGQSGL
AVSNPTSVGH SGIAASCPPE RCVVPALPSR LLAVDSGAAP SDDKGSSAVT NELCSPPGSS
NVAGTSLSPK ASLVPKGSNV ALQPLVTQVP ASQKTGLKEI PVSCIGATHH ALDNPSAISV
APATHVPPPT SSGLVSSKDP ASPVTSLVVP AAHKQFPAPP ASATLGVPVS PLPATEGLKN
LPISALVNVG APVSPAQAGL PTRKDTTLQP LAPIALKESP SSQSASSLEV LSEDTVTKKT
TGGPAPVVRP AIAGVATTTS LRADSPPAVI RADSCVSPNT VSQPLKRSVT DPAMAPRTAK
NTAPSTTSPL VPLASEGCPV ASSMALSPQN ASVSETALAL SPEIPKSVPF PDPPLAEISF
SNARKVDAVS HMESSGSSRQ GHPDASVTAK GTVVCLADSS LDTSVSASKG SALSGASSPL
YPLEVSFLPE AGLAVQGPKG SLNKLSPTPP SSKGAPVPST GAPPSPKGAP IVPTESSISS
KQVPAEILPS PQKTPEVTAS RLISAVQSPK VDPIMSDVTP TSPKKTSATA VPKDTSATLS
LKSVPAVTSL SPPKAPVAPS NEATIVPTEI PTSLKNALAA ATPKETLATS IPKVTSPSPQ
KTPKSVSLKG APAMTSKKAT EIAASKDVSP SQFPKEVPLL PHVPPTSPPK SPVSDTLSGA
LTSPPPKGPP ATLAETPTYP KKSPKPAASK KTPATPSPEG VTAVPLEIPP CSKKAPKTAA
PKESSATSSS KRAPKTAVSK EIPSKGVTAV PLEISLPLKE TSKSATPGEK SASSPKRSPK
TAGPKETPPG GVTAVPPEIS LPPKETPQNA TPNESLAASS QKRSPKTSVP KETPPGGVTA
MPLEIPSAPQ KAPKTAVPKQ IPTPEDAVTI LAGSPLSPKK ASKTAAPKEA PATPSVGVIA
VSGEISPSPK KTSKTAAPKE NSATLPPKRS PKTAAPKETP ATSSEGVTAV PSEISPSPPT
PASKGVPVTL TPKGAPNALA ESPASPKKVP KTAAPEETST TPSPQKIPKV AGPKEASATP
PSKKTPKTAV PKETSAPSEG VTAVPLEIPP SPRKAPKTAA PKETPAPSPE GATTAPVQIP
PSPRKGSKKA GSKETPTTPS PEGVTAAPLE IPISSKKTSK MASPKETLVT PSSKKLSQTV
GPKETSLEGA TAVPLEIPPS HKKAPKTVDP KQVPLTPSPK DAPTTLAESP SSPKKAPKTA
APPSERVTTV PPEKPATPQK ASATTASKVP VPAETQEVAV SSRETPVTPA VPPVKNPSSH
KKTSKTIELK EAPATLPPSP TKSPKIPSSK KAPRTSAPKE FPASPSIKPV TTSLAQTAPP
SLQKAPSTTI PKENLAAPAV LPVSSKSPAA PAAASASLSP ATAAPQTAPK EATTIPSCKK
AAATETPIET STAPSLEGAP KETSETSVSK VLMSSPPKKA SSSKRASTLP ATTLPSLKEA
SVLSPTATSS GKDSHISPVS DACSTGTTTP QASEKLPSKK GPTAFTEMLA APAPESALAI
TAPIQKSPGA NSNSASSPKC PDPSSKKDTK GLPSAVALAP QTVPVEKDTS KAIETLLVSP
AKGSDCLHSP KGPVGSQVAT PLAAFTSDKV PPEAVSASVA PKPAPAASLT LAPSPVAPLP
PKQPLLESAP GSVLESPSKL PVPAEEDELP PLIPPEAVSG GEPFQPILVN MPAPKPAGTP
APAPSAKQPV LKNNKGSGTE SDSDESVPEL EEQDSTQTAT QQAQLAAAAE IDEEPVSKAK
QSRSEKKARK AMSKLGLRQV TGVTRVTIRK SKNILFVITK PDVYKSPASD TYIVFGEAKI
EDLSQQAQLA AAEKFKVQGE AVSNIQENTQ TPTVQEESEE EEVDETGVEV KDIELVMSQA
NVSRAKAVRA LKNNSNDIVN AIMELTM
