DAB_DROME
ID DAB_DROME Reviewed; 2224 AA.
AC P98081; Q9VV93;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 2.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Protein disabled;
GN Name=Dab; ORFNames=CG9695;
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] (ISOFORMS 1 AND 2), FUNCTION, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND PHOSPHORYLATION AT
RP TYR-112; TYR-483; TYR-1604; TYR-1609; TYR-1643; TYR-1646; TYR-1655;
RP TYR-1681; TYR-1768 AND TYR-1905.
RC TISSUE=Embryo;
RX PubMed=7680635; DOI=10.1101/gad.7.3.441;
RA Gertler F.B., Hill K.K., Clark M.J., Hoffmann F.M.;
RT "Dosage-sensitive modifiers of Drosophila abl tyrosine kinase function:
RT prospero, a regulator of axonal outgrowth, and disabled, a novel tyrosine
RT kinase substrate.";
RL Genes Dev. 7:441-453(1993).
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 FUNCTION, TISSUE SPECIFICITY, PHOSPHORYLATION, INTERACTION WITH DRK AND
RP SEV, AND MUTAGENESIS OF SER-120.
RX PubMed=9671493; DOI=10.1128/mcb.18.8.4844;
RA Le N., Simon M.A.;
RT "Disabled is a putative adaptor protein that functions during signaling by
RT the sevenless receptor tyrosine kinase.";
RL Mol. Cell. Biol. 18:4844-4854(1998).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-998; SER-1336; SER-1339;
RP SER-1344; SER-1348; SER-1700; SER-1713; SER-1716; SER-1811; SER-1812;
RP SER-1814; SER-1815 AND SER-2074, AND IDENTIFICATION BY 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).
CC -!- FUNCTION: Together with Abl, involved in embryonic neural development.
CC May have a role in eye development. Acts as an adapter protein for SH2-
CC domain containing proteins during sevenless (sev) signaling.
CC {ECO:0000269|PubMed:7680635, ECO:0000269|PubMed:9671493}.
CC -!- SUBUNIT: Binds the SH3 domains of drk via the Pro-rich domain. When
CC phosphorylated, can interact with the SH2 domains of drk. Binds sev via
CC the phosphotyrosine interaction domain (PID).
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:7680635}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P98081-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P98081-2; Sequence=VSP_004185;
CC -!- TISSUE SPECIFICITY: Uniformly expressed in the embryo from blastoderm
CC through gastrulation. Highly expressed in the mesoderm and CNS during
CC germ-band retraction. CNS expression is later localized to axon
CC bundles. Detected in the embryonic PNS and body wall muscles. Expressed
CC in the eye at the morphogenetic furrow and in developing photoreceptor
CC cells posterior to the furrow. {ECO:0000269|PubMed:7680635,
CC ECO:0000269|PubMed:9671493}.
CC -!- DEVELOPMENTAL STAGE: Embryonic axonogenesis.
CC {ECO:0000269|PubMed:7680635}.
CC -!- PTM: Probably phosphorylated by the Abl tyrosine kinase. Phosphorylated
CC on tyrosine residues in response to sevenless activation.
CC {ECO:0000269|PubMed:18327897, ECO:0000269|PubMed:9671493}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB08527.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAB08527.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
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DR EMBL; L08845; AAB08527.1; ALT_SEQ; mRNA.
DR EMBL; AE014296; AAF49424.2; -; Genomic_DNA.
DR PIR; A46299; A46299.
DR RefSeq; NP_524119.2; NM_079395.4. [P98081-1]
DR AlphaFoldDB; P98081; -.
DR SMR; P98081; -.
DR BioGRID; 65165; 11.
DR IntAct; P98081; 4.
DR STRING; 7227.FBpp0075077; -.
DR iPTMnet; P98081; -.
DR PaxDb; P98081; -.
DR PRIDE; P98081; -.
DR EnsemblMetazoa; FBtr0075318; FBpp0075077; FBgn0000414. [P98081-1]
DR GeneID; 39866; -.
DR KEGG; dme:Dmel_CG9695; -.
DR CTD; 39866; -.
DR FlyBase; FBgn0000414; Dab.
DR VEuPathDB; VectorBase:FBgn0000414; -.
DR eggNOG; KOG3535; Eukaryota.
DR GeneTree; ENSGT00940000168807; -.
DR InParanoid; P98081; -.
DR Reactome; R-DME-190873; Gap junction degradation.
DR Reactome; R-DME-196025; Formation of annular gap junctions.
DR Reactome; R-DME-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Reactome; R-DME-8856828; Clathrin-mediated endocytosis.
DR Reactome; R-DME-8866376; Reelin signalling pathway.
DR SignaLink; P98081; -.
DR BioGRID-ORCS; 39866; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 39866; -.
DR PRO; PR:P98081; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0000414; Expressed in second segment of antenna (Drosophila) and 21 other tissues.
DR ExpressionAtlas; P98081; baseline and differential.
DR Genevisible; P98081; DM.
DR GO; GO:0030424; C:axon; IDA:FlyBase.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:FlyBase.
DR GO; GO:0098793; C:presynapse; IEA:GOC.
DR GO; GO:0005118; F:sevenless binding; IPI:UniProtKB.
DR GO; GO:0017124; F:SH3 domain binding; IEA:UniProtKB-KW.
DR GO; GO:0007349; P:cellularization; IMP:FlyBase.
DR GO; GO:0072583; P:clathrin-dependent endocytosis; IDA:FlyBase.
DR GO; GO:0042051; P:compound eye photoreceptor development; IMP:FlyBase.
DR GO; GO:0007391; P:dorsal closure; IMP:FlyBase.
DR GO; GO:0008045; P:motor neuron axon guidance; IMP:FlyBase.
DR GO; GO:0045874; P:positive regulation of sevenless signaling pathway; IGI:FlyBase.
DR GO; GO:0048488; P:synaptic vesicle endocytosis; IDA:FlyBase.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR028761; Dab.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR006020; PTB/PI_dom.
DR PANTHER; PTHR11232:SF47; PTHR11232:SF47; 1.
DR Pfam; PF00640; PID; 1.
DR SMART; SM00462; PTB; 1.
DR PROSITE; PS01179; PID; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Developmental protein; Differentiation;
KW Neurogenesis; Phosphoprotein; Reference proteome; Repeat; SH3-binding.
FT CHAIN 1..2224
FT /note="Protein disabled"
FT /id="PRO_0000079773"
FT DOMAIN 45..197
FT /note="PID"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00148"
FT REPEAT 1631..1642
FT /note="Alternate Arg and acidic residues"
FT REPEAT 1682..1692
FT /note="Alternate Arg and acidic residues"
FT REPEAT 1733..1743
FT /note="Alternate Arg and acidic residues"
FT REGION 281..377
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 607..654
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 704..724
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 766..906
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1212..1321
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1334..1519
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1545..1566
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1603..2100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1631..1743
FT /note="Repeat-rich region"
FT REGION 2134..2164
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2177..2224
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 281..304
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 357..373
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 640..654
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 704..722
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 779..801
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 808..837
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1253..1267
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1269..1283
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1290..1305
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1337..1351
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1359..1373
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1386..1400
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1402..1416
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1457..1475
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1620..1661
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1677..1709
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1724..1749
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1880..1895
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1911..1928
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1929..1960
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1984..2073
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2074..2088
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2177..2209
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 112
FT /note="Phosphotyrosine; by ABL"
FT /evidence="ECO:0000305|PubMed:7680635"
FT MOD_RES 483
FT /note="Phosphotyrosine; by ABL"
FT /evidence="ECO:0000305|PubMed:7680635"
FT MOD_RES 998
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 1336
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 1339
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 1344
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 1348
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 1604
FT /note="Phosphotyrosine; by ABL"
FT /evidence="ECO:0000305|PubMed:7680635"
FT MOD_RES 1609
FT /note="Phosphotyrosine; by ABL"
FT /evidence="ECO:0000305|PubMed:7680635"
FT MOD_RES 1643
FT /note="Phosphotyrosine; by ABL"
FT /evidence="ECO:0000305|PubMed:7680635"
FT MOD_RES 1646
FT /note="Phosphotyrosine; by ABL"
FT /evidence="ECO:0000305|PubMed:7680635"
FT MOD_RES 1655
FT /note="Phosphotyrosine; by ABL"
FT /evidence="ECO:0000305|PubMed:7680635"
FT MOD_RES 1681
FT /note="Phosphotyrosine; by ABL"
FT /evidence="ECO:0000305|PubMed:7680635"
FT MOD_RES 1700
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 1713
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 1716
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 1768
FT /note="Phosphotyrosine; by ABL"
FT /evidence="ECO:0000305|PubMed:7680635"
FT MOD_RES 1811
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 1812
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 1814
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 1815
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 1905
FT /note="Phosphotyrosine; by ABL"
FT /evidence="ECO:0000305|PubMed:7680635"
FT MOD_RES 2074
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT VAR_SEQ 463..614
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:7680635"
FT /id="VSP_004185"
FT MUTAGEN 120
FT /note="S->A: Greatly reduces sev binding and sev
FT signaling."
FT /evidence="ECO:0000269|PubMed:9671493"
FT CONFLICT 620
FT /note="N -> T (in Ref. 1; AAB08527)"
FT /evidence="ECO:0000305"
FT CONFLICT 885..886
FT /note="LL -> SW (in Ref. 1; AAB08527)"
FT /evidence="ECO:0000305"
FT CONFLICT 1061
FT /note="V -> M (in Ref. 1; AAB08527)"
FT /evidence="ECO:0000305"
FT CONFLICT 1126..1127
FT /note="EL -> DV (in Ref. 1; AAB08527)"
FT /evidence="ECO:0000305"
FT CONFLICT 1158..1159
FT /note="LR -> RG (in Ref. 1; AAB08527)"
FT /evidence="ECO:0000305"
FT CONFLICT 1241
FT /note="Y -> D (in Ref. 1; AAB08527)"
FT /evidence="ECO:0000305"
FT CONFLICT 1294
FT /note="L -> Q (in Ref. 1; AAB08527)"
FT /evidence="ECO:0000305"
FT CONFLICT 1297
FT /note="Q -> QQ (in Ref. 1; AAB08527)"
FT /evidence="ECO:0000305"
FT CONFLICT 1594
FT /note="V -> A (in Ref. 1; AAB08527)"
FT /evidence="ECO:0000305"
FT CONFLICT 1693
FT /note="R -> P (in Ref. 1; AAB08527)"
FT /evidence="ECO:0000305"
FT CONFLICT 1787
FT /note="R -> L (in Ref. 1; AAB08527)"
FT /evidence="ECO:0000305"
FT CONFLICT 1803
FT /note="V -> A (in Ref. 1; AAB08527)"
FT /evidence="ECO:0000305"
FT CONFLICT 1808..1809
FT /note="LR -> FA (in Ref. 1; AAB08527)"
FT /evidence="ECO:0000305"
FT CONFLICT 1978
FT /note="A -> V (in Ref. 1; AAB08527)"
FT /evidence="ECO:0000305"
FT CONFLICT 2039
FT /note="Missing (in Ref. 1; AAB08527)"
FT /evidence="ECO:0000305"
FT CONFLICT 2089
FT /note="D -> E (in Ref. 1; AAB08527)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2224 AA; 243072 MW; F91939C029292B38 CRC64;
MVKSLVAKLS TASSNLSLAS TFGGGSGAAE ETNYAKHRND PGRFFGDGVQ FKAKLIGILE
VGEARGDRMC QEALQDLKMA IRAAGEHKQR ITIHVTIDGL RLRDEKTGDS LYHHPVHKIS
FIAQDMTDSR AFGYIFGSPD SGHRFFGIKT DKAASQVVLA MRDLFQVVFE LKKKEIEMAR
QQIQGKSLHD HSSQLASLSS LKSSGLGGMG LGHSDLASGG ISSGHALTLL GSSLSTTNGT
SRLGVSLDVA KASGSAAKEV SPESVADLVD LEQELTSLQR GISQMERITP NEPTTSSTGG
AGHPSLAKSA SEDDPFGDSF IYVPSYSILP PPPDSGRNRH KPPNKTPDAV TSLDAMLSPP
PGTSSSHGSA SAGLQAADND DDNWLQELDQ QNDVFDTSKV VSSSGLGSVL AMAPLASSES
TATPTQQLTE VAAGSGPLAD LDIGLSTALG NEEQTSTILS LDAFTDLDPL GTGRTRPYVD
KKYFFQELKN PPKKLLKELS SGSQAGLGLG LSLGQLDGLF PEDSTTISTT TTTATNITAG
NPQQNSANTL TSTASTAASL GQLLSTVALN PDPLPAPISI PTSISHSITP SAELKLLLGH
VTNPPNPTGH YYTTEPPTLN SLENPHPPAD PVLLPRDTDP FSPTRKKSDP DPFQESDLFA
KLDAFEFEAP PAVPAPSIPN LATETKANVF NGPLQVQLPP EKELQLQQPP STVRNRPTAS
VSALPSGGAL DVISSISNKK MPHLFGQARS FGKSGSDIGS SVNMRRLQES DSLSETEAAP
EPPPRPDSTP YSEPPPLPPK KQFSDLVIRP SPANTTQPPT SGRYEYLNSN VTARRTASSV
DAPPIPLPSR RVGRSDGCFP GPGRPRKPGH TEDDYLAPLG APPPLLPPPS QGSSARARPQ
RQASLGRPQD IYENKAEILQ AQAQAQAQAP EVAPSSNTLA PDITLTQLLT LGMDDLAIKL
NVPASKLSTM TLVQLTAYLS EYLSSEKSQV HSQERRSSPA NTAPAPASTA AVFKVNFDQQ
TSFVAKFDDT FGEDEPVMPS GSSDSTFVAN FANFNDAPTP VPTVSPVVAT VPSADRYAVF
REIIDQELQQ QQQETDLMGD LTPPPVDETQ AKEISEGLEV NNVGAELPID ALDVKPAPKI
DTKITEVVAQ AKDRYAALRD IILVENLFDK PAIATDTQPE KEKDLLQDFP EFSDEFNEDH
DLRQIMDHQN VQTHARDRHG LVDSRGFPTE PSSSALTVGD YDEDEDADAG GESSLDSNEK
DAEPVSGQDQ YEKLSTSTQQ LDAAAPALED VQQLQQQSLP PKQDQKFLSI LTAPGGGTKD
DIEIDELMHR AISNLSLDSR DRVSPATSSA APSRGAPGLH TPSQFNDVST SPIPLQKPGM
GPSPVPSQLS AVSQLIDTAT KQMMGDKDRE KQSWATFDSP KAKGKARLTL PPPPPPASNT
SQPDTVESPC SSDPRDDGWS KQQRRWAKKE RQQTSSSSRD LSPWDDETPE YLKRRQLAAA
QMAHPHQPPM QAPPQHTDRH GYYMRHARRM NSCDEDYDYD GEFVARRDQP QHQQQQRKFK
HGLSRSRDNF ELESPSWYHH PAHHTWSPQE IEQVRVRSFD RTAYERSSYG PPPPIYDKRG
QLRGKYRGDH RDRERERDRD REYRDYARPS YDFDYENVYE ERGGRSPLAY KPGRGGGDYL
YDRERDRDRE RDRKSFDRES LESYESATRR RRSFGSGNDV YGSLDSRDDY RGDRERDRER
DREQMKTRSL RKPTTTSGKL RISGDIDYEQ DSEQDFQQRS GVRSLQRPNQ LGGDVVLPSN
AVVGPQRLRK SSGSSPWDGE EPALPGQKSW KRPASAAETE RRLAESRRAV ALGQTPSDGE
KERRFRKKTR ARSAKDLATV GAPSASTSAP SRSSYGRGIR DNYDYICPGQ RNDDDDDDDE
DYVDDEPPTD EDKFERLNRR RHEMHQRMLE SERRQMERHQ PPSLAKLPGQ NRTRGVVANS
DYGFVDSYEQ TPTPTPRSNA SSTGPGGLMM SGGESSAGVT SSKFNFDDGF ESDFNQSSPP
PAPAGTASSC NSTPAGPVSA NANNGGSKSL FRFSNDFSDR EKREQFEMDT PPTSTPPITQ
KLRFDDNVKV SQFDDAAFED DFAKASFDFE KEQAGSATAG AGGSGAMSRK QNMRTSKLQQ
RQELIKKSES VNIFAKKQED PFEDDEFFKS PDQEQAMDQH NDDTEGGKFQ WSEDANFAKF
DENM
