ANR11_MOUSE
ID ANR11_MOUSE Reviewed; 2643 AA.
AC E9Q4F7; B2RY01; Q6PB57;
DT 08-JUN-2016, integrated into UniProtKB/Swiss-Prot.
DT 05-APR-2011, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Ankyrin repeat domain-containing protein 11 {ECO:0000312|MGI:MGI:1924337};
GN Name=Ankrd11 {ECO:0000312|MGI:MGI:1924337};
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 {ECO:0000312|Proteomes:UP000000589};
RN [1] {ECO:0000312|Proteomes:UP000000589}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J {ECO:0000312|Proteomes:UP000000589};
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] {ECO:0000312|EMBL:AAH59876.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:AAH59876.1};
RC TISSUE=Brain {ECO:0000312|EMBL:AAH59876.1};
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 [3] {ECO:0000305}
RP FUNCTION, AND MUTAGENESIS OF GLU-2502.
RX PubMed=17986521; DOI=10.1152/physiolgenomics.00116.2007;
RA Barbaric I., Perry M.J., Dear T.N., Rodrigues Da Costa A., Salopek D.,
RA Marusic A., Hough T., Wells S., Hunter A.J., Cheeseman M., Brown S.D.;
RT "An ENU-induced mutation in the Ankrd11 gene results in an osteopenia-like
RT phenotype in the mouse mutant Yoda.";
RL Physiol. Genomics 32:311-321(2008).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-276; SER-1070; THR-1111;
RP SER-1114; SER-1676; SER-1832; TYR-1835; TYR-1836; SER-1837; SER-1844 AND
RP SER-2139, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Liver, Lung, 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 [5] {ECO:0000305}
RP FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=25556659; DOI=10.1016/j.devcel.2014.11.031;
RA Gallagher D., Voronova A., Zander M.A., Cancino G.I., Bramall A.,
RA Krause M.P., Abad C., Tekin M., Neilsen P.M., Callen D.F., Scherer S.W.,
RA Keller G.M., Kaplan D.R., Walz K., Miller F.D.;
RT "Ankrd11 is a chromatin regulator involved in autism that is essential for
RT neural development.";
RL Dev. Cell 32:31-42(2015).
RN [6] {ECO:0000305}
RP SUBCELLULAR LOCATION, PROTEASOMAL DEGRADATION, AND MUTAGENESIS OF GLU-2502.
RX PubMed=25413698; DOI=10.1007/s00439-014-1509-2;
RA Walz K., Cohen D., Neilsen P.M., Foster J. II, Brancati F., Demir K.,
RA Fisher R., Moffat M., Verbeek N.E., Bjoergo K., Lo Castro A., Curatolo P.,
RA Novelli G., Abad C., Lei C., Zhang L., Diaz-Horta O., Young J.I.,
RA Callen D.F., Tekin M.;
RT "Characterization of ANKRD11 mutations in humans and mice related to KBG
RT syndrome.";
RL Hum. Genet. 134:181-190(2015).
CC -!- FUNCTION: Chromatin regulator which modulates histone acetylation and
CC gene expression in neural precursor cells (PubMed:25556659). May
CC recruit histone deacetylases (HDACs) to the p160 coactivators/nuclear
CC receptor complex to inhibit ligand-dependent transactivation (By
CC similarity). Has a role in proliferation and development of cortical
CC neural precursors (PubMed:25556659). May also regulate bone homeostasis
CC (PubMed:17986521). {ECO:0000250|UniProtKB:Q6UB99,
CC ECO:0000269|PubMed:17986521, ECO:0000269|PubMed:25556659}.
CC -!- SUBUNIT: Interacts with the PAS region of the p160 coactivators.
CC {ECO:0000250|UniProtKB:Q6UB99}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:25413698}.
CC Note=Localizes to chromatin during prometaphase (By similarity).
CC {ECO:0000250|UniProtKB:Q6UB99}.
CC -!- DEVELOPMENTAL STAGE: Detected in the cerebral cortex from embryonic
CC stage 11 dpc through to postnatal stage P3, where it is primarily
CC expressed in neural precursors. {ECO:0000269|PubMed:25556659}.
CC -!- PTM: Subject to proteasomal degradation which is probably essential to
CC regulate its activity. {ECO:0000269|PubMed:25413698}.
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DR EMBL; AC132287; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC059876; AAH59876.1; -; mRNA.
DR EMBL; BC158043; AAI58044.1; -; mRNA.
DR CCDS; CCDS40507.2; -.
DR RefSeq; NP_001074848.2; NM_001081379.2.
DR AlphaFoldDB; E9Q4F7; -.
DR SMR; E9Q4F7; -.
DR IntAct; E9Q4F7; 1.
DR MINT; E9Q4F7; -.
DR STRING; 10090.ENSMUSP00000095938; -.
DR iPTMnet; E9Q4F7; -.
DR PhosphoSitePlus; E9Q4F7; -.
DR EPD; E9Q4F7; -.
DR jPOST; E9Q4F7; -.
DR MaxQB; E9Q4F7; -.
DR PaxDb; E9Q4F7; -.
DR PRIDE; E9Q4F7; -.
DR ProteomicsDB; 296048; -.
DR Antibodypedia; 4516; 137 antibodies from 22 providers.
DR Ensembl; ENSMUST00000098334; ENSMUSP00000095939; ENSMUSG00000035569.
DR GeneID; 77087; -.
DR KEGG; mmu:77087; -.
DR UCSC; uc009ntz.2; mouse.
DR CTD; 29123; -.
DR MGI; MGI:1924337; Ankrd11.
DR VEuPathDB; HostDB:ENSMUSG00000035569; -.
DR eggNOG; ENOG502QQG5; Eukaryota.
DR GeneTree; ENSGT00940000155966; -.
DR HOGENOM; CLU_229338_0_0_1; -.
DR OMA; LNDGESC; -.
DR OrthoDB; 854133at2759; -.
DR BioGRID-ORCS; 77087; 20 hits in 71 CRISPR screens.
DR ChiTaRS; Ankrd11; mouse.
DR PRO; PR:E9Q4F7; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; E9Q4F7; protein.
DR Bgee; ENSMUSG00000035569; Expressed in rostral migratory stream and 227 other tissues.
DR ExpressionAtlas; E9Q4F7; baseline and differential.
DR Genevisible; E9Q4F7; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0009653; P:anatomical structure morphogenesis; IBA:GO_Central.
DR GO; GO:0060348; P:bone development; IMP:MGI.
DR GO; GO:0060325; P:face morphogenesis; ISO:MGI.
DR GO; GO:0060323; P:head morphogenesis; IMP:MGI.
DR GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR GO; GO:0035264; P:multicellular organism growth; IMP:MGI.
DR GO; GO:0042475; P:odontogenesis of dentin-containing tooth; ISO:MGI.
DR GO; GO:0048705; P:skeletal system morphogenesis; IMP:MGI.
DR GO; GO:0001894; P:tissue homeostasis; IMP:MGI.
DR Gene3D; 1.25.40.20; -; 1.
DR InterPro; IPR042636; ANKRD11.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR PANTHER; PTHR24145; PTHR24145; 1.
DR Pfam; PF00023; Ank; 1.
DR Pfam; PF12796; Ank_2; 1.
DR SMART; SM00248; ANK; 3.
DR SUPFAM; SSF48403; SSF48403; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 3.
PE 1: Evidence at protein level;
KW ANK repeat; Nucleus; Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..2643
FT /note="Ankyrin repeat domain-containing protein 11"
FT /id="PRO_0000436376"
FT REPEAT 167..196
FT /note="ANK 1"
FT /evidence="ECO:0000255"
FT REPEAT 200..229
FT /note="ANK 2"
FT /evidence="ECO:0000255"
FT REPEAT 233..262
FT /note="ANK 3"
FT /evidence="ECO:0000255"
FT REPEAT 266..292
FT /note="ANK 4"
FT /evidence="ECO:0000255"
FT REGION 1..90
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 128..170
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 289..365
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 423..504
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 517..651
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 727..805
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 918..962
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 977..1037
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1051..1074
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1114..1388
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1420..1711
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1863..1900
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1981..2027
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2111..2386
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2349..2643
FT /note="Important for protein degradation"
FT /evidence="ECO:0000250|UniProtKB:Q6UB99"
FT COMPBIAS 23..59
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 70..90
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 128..156
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 302..320
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 450..465
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 517..536
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 553..587
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 632..647
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1136..1301
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1302..1319
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1324..1388
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1420..1444
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1453..1538
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1547..1564
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1578..1592
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1599..1637
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1678..1698
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2173..2188
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2303..2317
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2350..2365
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2371..2386
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 276
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 408
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6UB99"
FT MOD_RES 410
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q6UB99"
FT MOD_RES 411
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6UB99"
FT MOD_RES 838
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6UB99"
FT MOD_RES 1070
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1111
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1114
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1676
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1777
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6UB99"
FT MOD_RES 1832
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1835
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1836
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1837
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1844
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1981
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6UB99"
FT MOD_RES 2139
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MUTAGEN 2502
FT /note="E->K: In Yoda; protein degradation is impaired.
FT Homozygotes are embryonic lethal. Heterozygotes have
FT reduced body size, craniofacial abnormalities, and reduced
FT bone mineral density."
FT /evidence="ECO:0000269|PubMed:17986521,
FT ECO:0000269|PubMed:25413698"
FT CONFLICT 239
FT /note="H -> R (in Ref. 2; AAI58044)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2643 AA; 296186 MW; 9442C1C4500DC15A CRC64;
MPKGGCSKTP QQEDFALSND MVEKQTGKKD KDKVSLTKTP KLDRSDGGKE VRERATKRKL
PFTVGANGEQ KDSDTEKQGP ERKRIKKEPV ARKSGLLFGM GLSGIRAGYP LSERQQVALL
MQMTAEESAN SPVDTTPKHP SQSTVCQKGT PNSASKTKDK VNKRNERGET RLHRAAIRGD
ARRIKELISE GADVNVKDFA GWTALHEACN RGYYDIAKQL LAAGAEVNTK GLDDDTPLHD
AANNGHYKVV KLLLRYGGNP QQSNRKGETP LKVANSPTMV NLLLGKGTYT SSEESSTESS
EEEDAPSFAP SSSVDGNNTD SEFEKGLKLK AKNPEPQKTV TPVKDEYEFD EDDEQDRVPP
VDDKHLLKKD YRKEAKANSF ISIPKMEVKS YSKNNTLAPK KAAHRILSDT SDEEDVSVSI
GAGEKLRLSA HTMLPGSKAR ESSSSRQQKE KNKLKKKRKK ETKGKEVRFG KRSDKFCSSG
SESESSESEE DDGDSVGSSG CLKGSPLVLK DPSLFSSLSA SSTSSHGSAV AQKHGSGHTD
QHTKHWRTDN WKAISSPAWS EVSSLSDSSR TGLTSESDCS SEGSSVESLK PTRRKQEHRK
RGVLQSAPSE KRSSFHPCTD GAVPKLDKEG KVVKKHKTKH KHKHKEKGQC SVSQELKLKS
FTYEYEDSKQ KSDKAILLES DLSTENKLKV LKHDREHLKK EDKLGRMKPE DKDWLFKDEK
VLKRIKDANK DMSRAFREDK DRASKAERER ATKDKSPKEE KLRLYKEERK KKSKDRASRL
ERKNDMKEDK LSKEKEKAFK EDKEKLKKEK LYREDAAFDD YCNKSQFLDH EDTKFSLSDD
QQERWFSDLS DSSFDFKGED SWDSVTDYRD IKNDSVAKLI LETVKEDSKE KKRDNKIREK
RDFKDSFFRK RDRDCLDKNS EKRRDQTEKH KSIPSYLSEK DKKRRESAEG GRDRRDGRIR
SEEVHREDLK ECGFESSFKD KSDCDFPKNL EPWERPHAAR EKEKKDALEK ERKEKGRADK
YKEKSSERER SDKSTLDKCQ KDKEFEKCFK EKKDGKEKHK DIHSKDRKAS FDQLREKKEK
VFSSIISEDF SERKDDRKGK EKSWYIADIF TDESEDEKDD CVAGSFKATE ASDTQRVDGL
PEKEEGREHP SDRHRKSSSD RQHTEKPRDK EPKEKKKDRG ASEGGKDKKE KMEKIFEKHK
EKKDKECAER YKDRKERASA DSAPEKKNKQ KLPEKVEKKH FAEDKVKSKH KEKPEKEHSR
ERERKPSRGP DVEKSLLEKL EEEALHDYRE DSNDKISEVS SDSFADHGQE PSLSTLLEVS
FSEPPAEDKA RDSACLSEKL REKERHRHSS SSSKKSHERE RAKKEKAEKK EKSEDYKDSI
SSVRKDASQF EKDFLDAETY GVSYPTKADV EEELDKAIEL FSSEKKDRSD PEREPAKRIE
KELKPYGSSA ISILKEKKKR EKHRERWREE KERHRDKHVD GFLRHHKDEP KPAAKDKDNP
PNSFKEKSRE ESLKLSETKL KEKFKENTER EKGDSIKMSN GNDKLVPSRD SGKKDSRPRE
KLLGDGDLMM TSFERMLSQK DLEIEERHKR HKERMKQMEK MRHRSGDPKL KEKKPTEDGR
KKSLDFPSKK ALGLDKKVKE PAPTLTTGES KPHSGPGTES KDWLSGQPLK EVLPASPRTE
QSRPTGVPTP TSVVSCPSYE EVMHTPRTPS CSADDYPDLV FDCTDSQHSM PVSTASTSAC
SPPFFDRFSV ASSVVSENAA GQTPTRPIST NLYRSISVDI RRTPEEEFSA GDKLFRQQSV
PAPSSFDSPV QHLLEEKAPL PPVPAEKFAC LSPGYYSPDY GIPSPKVDTL HCPPTAVVSA
TPPPDSVFSN LPPKSSPSPR GELLSPAIEG TLPPDLGLPL DATEDQQATA AILPQEPSYL
EPLDEGPFTT VITEEPVEWT HTAAEQGLSS SSLIASASEN PVSWPVGSEL MLKSPQRFAE
SPKHFCPGES LHSTTPGPYS AAEPTYPVSP GSYPLPAPEP ALEEVKDGGT GAIPVAISAA
EGAAPYAAPA RLESFFSNCK SHPDAPLDTA PEPTGVTAVA QVEALGPLES SFLDSNPSIS
TLSQVEPVSW HEAFTSPEDD LDLGPFSLPE LPLQAKDASD VEAEAAKASP VPPAESPPGP
TGVLGGGDVP APAAEEPPAP PPQEASPQLS TEPEPSEEPK LDVVLEATVE TEVLADDSAP
EASISNSVPA PSPPQQQPPG GGDEEAETED PSATPCCAPD GPTTDGLAQA HNSAEASCVV
AAAEGPPGNV QAEATDPEPK PTSEVPKAPK VEEVPQRMTR NRAQMLASQS KQGIPAAEKD
PMPTPASRAK GRASEEEDAQ AQHPRKRRFQ RSSQQLQQQL NTSTQQTREV IQQTLAAIVD
AIKLDAIEPY HSDRSNPYFE YLQIRKKIEE KRKILCCITP QAPQCYAEYV TYTGSYLLDG
KPLSKLHIPV IAPPPSLAEP LKELFKQQEA VRGKLRLQHS IEREKLIVSC EQEILRVHCR
AARTIANQAV PFSACTMLLD SEVYNMPLES QGDENKSVRD RFNARQFISW LQDVDDKYDR
MKTCLLMRQQ HEAAALNAVQ RMEWQLKAQE LDPAGHKSLC VNEVPSFYVP MVDVNDDFVL
LPA
