SPTCB_DROME
ID SPTCB_DROME Reviewed; 2291 AA.
AC Q00963; Q6NNX2; Q9VX30;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 2.
DT 03-AUG-2022, entry version 203.
DE RecName: Full=Spectrin beta chain;
GN Name=beta-Spec; Synonyms=Spec-b; ORFNames=CG5870;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1631106; DOI=10.1073/pnas.89.13.6187;
RA Byers T.J., Brandin E., Lue R., Winograd E., Branton D.;
RT "The complete sequence of Drosophila beta-spectrin reveals supra-motifs
RT comprising eight 106-residue segments.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:6187-6191(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1404.
RC STRAIN=Berkeley; TISSUE=Testis;
RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Champe M.,
RA Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A.,
RA Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., Miranda A.,
RA Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., Patel S.,
RA Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E.;
RL Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION.
RX PubMed=3680372; DOI=10.1083/jcb.105.5.2095;
RA Dubreuil R., Byers T.J., Branton D., Goldstein L.S.B., Kiehart D.P.;
RT "Drosophilia spectrin. I. Characterization of the purified protein.";
RL J. Cell Biol. 105:2095-2102(1987).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2195, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
RN [7]
RP STRUCTURE BY NMR OF 2145-2262.
RX PubMed=8591029; DOI=10.1016/s0969-2126(01)00254-4;
RA Zhang P., Talluri S., Deng H., Branton D., Wagner G.;
RT "Solution structure of the pleckstrin homology domain of Drosophila beta-
RT spectrin.";
RL Structure 3:1185-1195(1995).
CC -!- FUNCTION: Spectrin is the major constituent of the cytoskeletal network
CC underlying the erythrocyte plasma membrane. It associates with band 4.1
CC and actin to form the cytoskeletal superstructure of the erythrocyte
CC plasma membrane. Interacts with calmodulin in a calcium-dependent
CC manner. {ECO:0000269|PubMed:3680372}.
CC -!- SUBUNIT: Native spectrin molecule is a tetramer composed of two
CC antiparallel heterodimers joined head to head so that each end of the
CC native molecule includes the C-terminus of the alpha subunit and the N-
CC terminus of the beta subunit.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cytoplasm, cell cortex.
CC -!- SIMILARITY: Belongs to the spectrin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAR82828.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={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; M92288; AAA28399.1; -; mRNA.
DR EMBL; AE014298; AAF48751.1; -; Genomic_DNA.
DR EMBL; BT011160; AAR82828.1; ALT_SEQ; mRNA.
DR PIR; A46147; A46147.
DR RefSeq; NP_523388.1; NM_078664.3.
DR PDB; 1DRO; NMR; -; A=2142-2262.
DR PDBsum; 1DRO; -.
DR AlphaFoldDB; Q00963; -.
DR SMR; Q00963; -.
DR BioGRID; 59071; 17.
DR DIP; DIP-18565N; -.
DR IntAct; Q00963; 3.
DR STRING; 7227.FBpp0074228; -.
DR iPTMnet; Q00963; -.
DR PaxDb; Q00963; -.
DR PRIDE; Q00963; -.
DR EnsemblMetazoa; FBtr0074454; FBpp0074228; FBgn0250788.
DR GeneID; 32746; -.
DR KEGG; dme:Dmel_CG5870; -.
DR CTD; 32746; -.
DR FlyBase; FBgn0250788; beta-Spec.
DR VEuPathDB; VectorBase:FBgn0250788; -.
DR eggNOG; KOG0517; Eukaryota.
DR InParanoid; Q00963; -.
DR PhylomeDB; Q00963; -.
DR Reactome; R-DME-375165; NCAM signaling for neurite out-growth.
DR Reactome; R-DME-5673001; RAF/MAP kinase cascade.
DR Reactome; R-DME-6807878; COPI-mediated anterograde transport.
DR Reactome; R-DME-9013420; RHOU GTPase cycle.
DR Reactome; R-DME-9013424; RHOV GTPase cycle.
DR SignaLink; Q00963; -.
DR BioGRID-ORCS; 32746; 0 hits in 3 CRISPR screens.
DR ChiTaRS; beta-Spec; fly.
DR EvolutionaryTrace; Q00963; -.
DR GenomeRNAi; 32746; -.
DR PRO; PR:Q00963; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0250788; Expressed in oviduct (Drosophila) and 35 other tissues.
DR ExpressionAtlas; Q00963; baseline and differential.
DR Genevisible; Q00963; DM.
DR GO; GO:0030424; C:axon; IDA:FlyBase.
DR GO; GO:0030054; C:cell junction; IBA:GO_Central.
DR GO; GO:0042995; C:cell projection; IBA:GO_Central.
DR GO; GO:0030864; C:cortical actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0045169; C:fusome; IDA:FlyBase.
DR GO; GO:0016328; C:lateral plasma membrane; IDA:FlyBase.
DR GO; GO:0031594; C:neuromuscular junction; IDA:FlyBase.
DR GO; GO:0005886; C:plasma membrane; IDA:FlyBase.
DR GO; GO:0008091; C:spectrin; IEA:InterPro.
DR GO; GO:0045170; C:spectrosome; IDA:FlyBase.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0030506; F:ankyrin binding; IDA:FlyBase.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0008017; F:microtubule binding; IDA:FlyBase.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IDA:FlyBase.
DR GO; GO:0005200; F:structural constituent of cytoskeleton; IEA:InterPro.
DR GO; GO:0030036; P:actin cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0051693; P:actin filament capping; IEA:UniProtKB-KW.
DR GO; GO:0007411; P:axon guidance; IMP:FlyBase.
DR GO; GO:0016199; P:axon midline choice point recognition; IMP:FlyBase.
DR GO; GO:0007409; P:axonogenesis; IMP:FlyBase.
DR GO; GO:0042062; P:long-term strengthening of neuromuscular junction; IMP:FlyBase.
DR GO; GO:0048790; P:maintenance of presynaptic active zone structure; IDA:FlyBase.
DR GO; GO:0007026; P:negative regulation of microtubule depolymerization; IMP:FlyBase.
DR GO; GO:0007399; P:nervous system development; IMP:FlyBase.
DR GO; GO:0007274; P:neuromuscular synaptic transmission; IMP:FlyBase.
DR GO; GO:0048666; P:neuron development; IBA:GO_Central.
DR GO; GO:0072499; P:photoreceptor cell axon guidance; IMP:FlyBase.
DR GO; GO:1903729; P:regulation of plasma membrane organization; IMP:UniProtKB.
DR GO; GO:0050807; P:regulation of synapse organization; IMP:FlyBase.
DR CDD; cd00014; CH; 2.
DR CDD; cd00176; SPEC; 9.
DR Gene3D; 1.10.418.10; -; 2.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR001589; Actinin_actin-bd_CS.
DR InterPro; IPR001715; CH-domain.
DR InterPro; IPR036872; CH_dom_sf.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR041681; PH_9.
DR InterPro; IPR001605; PH_dom-spectrin-type.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR018159; Spectrin/alpha-actinin.
DR InterPro; IPR016343; Spectrin_bsu.
DR InterPro; IPR002017; Spectrin_repeat.
DR Pfam; PF00307; CH; 2.
DR Pfam; PF15410; PH_9; 1.
DR Pfam; PF00435; Spectrin; 17.
DR PIRSF; PIRSF002297; Spectrin_beta_subunit; 1.
DR PRINTS; PR00683; SPECTRINPH.
DR SMART; SM00033; CH; 2.
DR SMART; SM00233; PH; 1.
DR SMART; SM00150; SPEC; 17.
DR SUPFAM; SSF47576; SSF47576; 1.
DR PROSITE; PS00019; ACTININ_1; 1.
DR PROSITE; PS00020; ACTININ_2; 1.
DR PROSITE; PS50021; CH; 2.
DR PROSITE; PS50003; PH_DOMAIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Actin capping; Actin-binding; Calmodulin-binding; Cytoplasm;
KW Cytoskeleton; Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..2291
FT /note="Spectrin beta chain"
FT /id="PRO_0000073468"
FT DOMAIN 50..154
FT /note="Calponin-homology (CH) 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT DOMAIN 169..274
FT /note="Calponin-homology (CH) 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT REPEAT 300..408
FT /note="Spectrin 1"
FT /evidence="ECO:0000255"
FT REPEAT 420..521
FT /note="Spectrin 2"
FT /evidence="ECO:0000255"
FT REPEAT 525..633
FT /note="Spectrin 3"
FT /evidence="ECO:0000255"
FT REPEAT 636..739
FT /note="Spectrin 4"
FT /evidence="ECO:0000255"
FT REPEAT 743..843
FT /note="Spectrin 5"
FT /evidence="ECO:0000255"
FT REPEAT 848..948
FT /note="Spectrin 6"
FT /evidence="ECO:0000255"
FT REPEAT 954..1057
FT /note="Spectrin 7"
FT /evidence="ECO:0000255"
FT REPEAT 1060..1166
FT /note="Spectrin 8"
FT /evidence="ECO:0000255"
FT REPEAT 1170..1272
FT /note="Spectrin 9"
FT /evidence="ECO:0000255"
FT REPEAT 1276..1376
FT /note="Spectrin 10"
FT /evidence="ECO:0000255"
FT REPEAT 1386..1484
FT /note="Spectrin 11"
FT /evidence="ECO:0000255"
FT REPEAT 1488..1591
FT /note="Spectrin 12"
FT /evidence="ECO:0000255"
FT REPEAT 1594..1697
FT /note="Spectrin 13"
FT /evidence="ECO:0000255"
FT REPEAT 1701..1802
FT /note="Spectrin 14"
FT /evidence="ECO:0000255"
FT REPEAT 1807..1909
FT /note="Spectrin 15"
FT /evidence="ECO:0000255"
FT REPEAT 1913..2015
FT /note="Spectrin 16"
FT /evidence="ECO:0000255"
FT REPEAT 2020..2089
FT /note="Spectrin 17"
FT /evidence="ECO:0000255"
FT DOMAIN 2147..2259
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT REGION 1..271
FT /note="Actin-binding"
FT REGION 2097..2152
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2262..2291
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2097..2144
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2195
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT CONFLICT 2278
FT /note="D -> Y (in Ref. 1; AAA28399)"
FT /evidence="ECO:0000305"
FT STRAND 2146..2157
FT /evidence="ECO:0007829|PDB:1DRO"
FT STRAND 2173..2182
FT /evidence="ECO:0007829|PDB:1DRO"
FT STRAND 2185..2191
FT /evidence="ECO:0007829|PDB:1DRO"
FT HELIX 2192..2195
FT /evidence="ECO:0007829|PDB:1DRO"
FT STRAND 2219..2223
FT /evidence="ECO:0007829|PDB:1DRO"
FT STRAND 2226..2230
FT /evidence="ECO:0007829|PDB:1DRO"
FT STRAND 2232..2234
FT /evidence="ECO:0007829|PDB:1DRO"
FT STRAND 2236..2240
FT /evidence="ECO:0007829|PDB:1DRO"
FT STRAND 2242..2244
FT /evidence="ECO:0007829|PDB:1DRO"
FT HELIX 2245..2258
FT /evidence="ECO:0007829|PDB:1DRO"
SQ SEQUENCE 2291 AA; 265739 MW; 5CDFB0C548BBC39B CRC64;
MTTDISIVRW DPSQGPGNEY IDEYEYDGGN SSSRLFERSR IKALAEERES VQKKTFTKWV
NSHLCRVNCR IADLYVDMRD GKHLIKLLEV LSGERLPKPT KGKMRIHCLE NVDKALQFLR
EQRVHLENIG SHDIVDGNAS LNLGLIWTII LRFQIQDITI EEVDNKETKS AKDALLLWCQ
MKTAGYHNVN VRNFTTSWRD GLAFNAIIHK HRPDLVQFEK LSKTNAIHNL NNAFDVAEDK
LGLAKLLDAE DVFVEHPDEK SIITYVVTYY HYFSKLKQET VQGKRIGKVV GIAMENDKMV
HDYENFTSDL LKWIETTIQS LGEREFENSL AGVQGQLAQF SNYRTIEKPP KFVEKGNLEV
LLFTLQSKMR ANNQKPYTPK EGKMISDINK AWERLEKAEH ERELALREEL IRQEKLEQLA
ARFDRKASMR ETWLSENQRL VSQDNFGFDL AAVEAAAKKH EAIETDIFAY EERVQAVVAV
CDELESERYH DVKRILLRKD NVMRLWTYLL ELLRARRMRL EISLQLQQNF QEMLYILDNM
EEIKQLLMTD DYGKHLMGVE DLLQKHSLVE ADINILGERV KVVVQNSQKF LSDDPESYKP
CDPEIIVSRV QQLEDAYAEL VRLAVERRSR LEESRKLWQF YWDTADEENW IKEKEQIVST
DEVGHDLTTV NLMLSKHKAL ESEITSHDPQ LQNVAKVGSE LITEGHFGAD RIKDRLKEIL
NKWDHLLDLT KYRRQRLENA VEYFQLFADA DDVDNWMLDT LRIVSSEDVG RDEANVQSLL
KKHKDVADEL KNYAEVIDAL HKQAESLKLN EAEKANVDKR LEAIDNRYKE LTELAKLRKQ
RLLDALSLYK LMSEADGVEQ WIKEKTKMLD TMTPGKDIED VEIMKHRFEG FDKEMNANAS
RVAVVNQLAR QLLHVEHPNS DEILERQNHL NQEWSTLREK AEAKMDDLKS AHGVQTFYIE
CRETISWIED KKRILTETDS LEMDLTGVMT LQRRLSGMDR DLAAIQAKLS SLEREANSIE
DEHPEEAKII RERIAQIELI WEQLTQMLKE RDSKLEEAGD LHRFLRDLDH FQTWLTKTQT
DVASEDTPTS LPEAEKLLNQ HQSIREEIDN YTEDYKNMME YGERLTSEGS TSDDPQYMFL
RERLNALKDG WEELHQMWEN RQVLLSQSLD QQLFNRDARQ TEVLLSQQEH FLSKDDTPVN
LEQAENQLKR HEAFLTTMEA NDDKINTLLQ VADTLVEKDH FDADKIGKRA ENITGRRDDN
RQRALDQHEK LKNQVKLHEF LQDLEELAEW VQEKYATSQD ESYRSAKTIH SKWTRHQAFE
AEIAANKERL FEAEKSAQEL SKEKPEFKDV IEPKLKELAK QFDDLEVHTK EKGAMLFDAN
REVLVQQTCD DIDSYITDLE KQIVSGDTAN DLTSVNILMQ KQQVIQTQMA VKARQVEEID
KQTEYLQKTV PEEKIEPIVV KKTAVLERFE KIKAPLLERQ KALEKKKEAF QFCRDVEDEK
LWIDEKLPVA NSPDYGNSLF NVHVLKKKNQ SLATEIDNHE PRINAICNNG RKLIDEGHED
AKKFEALISD LTQKWQELKD AIENRRKHLL ESEKVQQYFF DAQEAESWMS EQELYMMVED
RGKDEISAQN LMKKHENLEQ SVEDYANTIR QLGEVARQFS GDDISSGDAV AVKQSQLDKL
YAGLKDLAGE RRARLNEALQ LFMLSREVDD LEQWITDREV VAGSQELGQD FDHVTLLSER
FNEFARDTEA VGGERVAKVN GIADNLIQAG HSDSATIAEW KDNLNESWQD LLELIETRTQ
MLAASRELHK FFHDCKDVLG RILEKQHGVS DELGRDAGSV STLQRKHYNF LQDLITLYSQ
VQQIQEESAK LQDAYAGDKA KEITNREQEV LHAWDNLQAM CDARKQKLAD TGDLFRFFNM
VRILMIWMED LVRQMNTSEK PRDVSGVELL MNNHQSLKAE IDTREDNFGA CISLGKELLT
RNHYASADIK DRLMTLSNSR NALLRRWEER WENLQLILEV YQFARDAAVA EAWLIAQEPY
LLSSELGHTI DEVENLIKKH EAFEKSAAAQ EERFSALERL TTFELKEMKR RQELAEEAER
QRIKEEQEAK AASEAAEQAK REAERRDDVD VGASHDDSER GGTPGAGEGH EGYVTRKHEW
DSTTKKASNR SWDKVYMAAK AGRISFYKDQ KGYKSNPELT FRGEPSYDLQ NAAIEIASDY
TKKKHVLRVK LANGALFLLQ AHDDTEMSQW VTSLKAQSDS TAVAASRSQT LPATSQKDEP
KRRSFFTLKK K
