ID   FRY_DROME               Reviewed;        3479 AA.
AC   Q9VT28; Q0E8G4; Q8T9A1; Q9BIR5; Q9GPT8;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 2.
DT   02-SEP-2026, entry version 149.
DE   RecName: Full=Protein furry;
GN   Name=fry {ECO:0000312|EMBL:AAF50228.2}; ORFNames=CG32045;
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Altocrustacea; Allotriocarida;
OC   Hexapoda; Insecta; Pterygota; Neoptera; Eumetabola; Endopterygota;
OC   Aparaglossata; Panorpida; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:AAG41424.1}
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS B AND D), FUNCTION, DEVELOPMENTAL
RP   STAGE, AND DISRUPTION PHENOTYPE.
RC   TISSUE=Imaginal disk {ECO:0000269|PubMed:11526084};
RX   PubMed=11526084; DOI=10.1242/dev.128.14.2793;
RA   Cong J., Geng W., He B., Liu J., Charlton J., Adler P.N.;
RT   "The furry gene of Drosophila is important for maintaining the integrity of
RT   cellular extensions during morphogenesis.";
RL   Development 128:2793-2802(2001).
RN   [2] {ECO:0000312|EMBL:AAF50228.2}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Berkeley {ECO:0000269|PubMed:10731132};
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] {ECO:0000305, ECO:0000312|EMBL:AAF50228.2}
RP   GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
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] {ECO:0000305, ECO:0000312|EMBL:AAL40005.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2555-3479.
RC   STRAIN=Berkeley {ECO:0000269|PubMed:12537569};
RC   TISSUE=Embryo {ECO:0000269|PubMed:12537569};
RX   PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA   Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA   Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA   Celniker S.E.;
RT   "A Drosophila full-length cDNA resource.";
RL   Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN   [5] {ECO:0000305}
RP   FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=15479641; DOI=10.1016/j.cell.2004.09.036;
RA   Emoto K., He Y., Ye B., Grueber W.B., Adler P.N., Jan L.Y., Jan Y.-N.;
RT   "Control of dendritic branching and tiling by the Tricornered-kinase/Furry
RT   signaling pathway in Drosophila sensory neurons.";
RL   Cell 119:245-256(2004).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-129; SER-1838; SER-1841;
RP   SER-2357; THR-2842; SER-2845; SER-2851; SER-2853; SER-2999; SER-3001;
RP   THR-3004; SER-3018; SER-3019; SER-3025 AND SER-3027, 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   FUNCTION.
RX   PubMed=32022690; DOI=10.7554/elife.52009;
RA   Norkett R., Del Castillo U., Lu W., Gelfand V.I.;
RT   "Ser/Thr kinase Trc controls neurite outgrowth in Drosophila by modulating
RT   microtubule-microtubule sliding.";
RL   Elife 9:0-0(2020).
CC   -!- FUNCTION: Plays a role in the Trc/fry signaling pathway by promoting
CC       trc kinase activity (PubMed:11526084, PubMed:15479641,
CC       PubMed:32022690). Plays a key role in maintaining the integrity of
CC       polarized cell extensions (arista) during morphogenesis, regulates the
CC       actin cytoskeleton (PubMed:11526084). Plays a key role in patterning
CC       sensory neuron dendritic fields by promoting avoidance between
CC       homologous dendrites as well as by limiting dendritic branching
CC       (PubMed:15479641). Together with trc, has a role in regulating
CC       microtubule-sliding during neurite outgrowth (PubMed:32022690).
CC       {ECO:0000269|PubMed:11526084, ECO:0000269|PubMed:15479641,
CC       ECO:0000269|PubMed:32022690}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=B {ECO:0000269|PubMed:11526084}; Synonyms=Long
CC       {ECO:0000269|PubMed:11526084};
CC         IsoId=Q9VT28-1; Sequence=Displayed;
CC       Name=D {ECO:0000269|PubMed:11526084}; Synonyms=Short
CC       {ECO:0000269|PubMed:11526084};
CC         IsoId=Q9VT28-2; Sequence=VSP_052372, VSP_052373;
CC   -!- TISSUE SPECIFICITY: Co-expressed with trc in all da neurons in third
CC       instar wild-type larvae; axons and dendritic branches.
CC       {ECO:0000269|PubMed:15479641}.
CC   -!- DEVELOPMENTAL STAGE: Expression is very low in embryonic and early
CC       larval stages, increases to be high from third larval instar to adults.
CC       {ECO:0000269|PubMed:11526084}.
CC   -!- DISRUPTION PHENOTYPE: Flies exhibit branched arista laterals, branched
CC       bristles and a strong multiple hair cell phenotype that consists of
CC       clusters of epidermal hairs and branched hairs. Dendrites of fry and
CC       trc mutants display excessive terminal branching. Branched laterals in
CC       mutant pupae arista are due to the splitting of individual laterals
CC       during elongation and abnormally shaped actin bundles.
CC       {ECO:0000269|PubMed:11526084}.
CC   -!- SIMILARITY: Belongs to the furry protein family. {ECO:0000255}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAL40005.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AF310159; AAG41424.1; -; mRNA.
DR   EMBL; AF351187; AAK37558.1; -; mRNA.
DR   EMBL; AE014296; AAF50228.2; -; Genomic_DNA.
DR   EMBL; AE014296; ABI31247.1; -; Genomic_DNA.
DR   EMBL; AY069860; AAL40005.1; ALT_INIT; mRNA.
DR   RefSeq; NP_729520.1; NM_168357.3. [Q9VT28-1]
DR   AlphaFoldDB; Q9VT28; -.
DR   BioGRID; 64513; 19.
DR   FunCoup; Q9VT28; 1225.
DR   IntAct; Q9VT28; 20.
DR   STRING; 7227.FBpp0297352; -.
DR   GlyGen; Q9VT28; 3 sites.
DR   iPTMnet; Q9VT28; -.
DR   PaxDb; 7227-FBpp0297352; -.
DR   PeptideAtlas; Q9VT28; -.
DR   EnsemblMetazoa; FBtr0076417; FBpp0076146; FBgn0016081.
DR   GeneID; 39122; -.
DR   KEGG; dme:Dmel_CG32045; -.
DR   AGR; FB:FBgn0016081; -.
DR   CTD; 10129; -.
DR   FlyBase; FBgn0016081; fry.
DR   VEuPathDB; VectorBase:FBgn0016081; -.
DR   eggNOG; KOG1825; Eukaryota.
DR   HOGENOM; CLU_000483_0_0_1; -.
DR   InParanoid; Q9VT28; -.
DR   OrthoDB; 6287725at2759; -.
DR   PhylomeDB; Q9VT28; -.
DR   SignaLink; Q9VT28; -.
DR   BioGRID-ORCS; 39122; 0 hits in 3 CRISPR screens.
DR   GenomeRNAi; 39122; -.
DR   PRO; PR:Q9VT28; -.
DR   Proteomes; UP000000803; Chromosome 3L.
DR   Bgee; FBgn0016081; Expressed in midgut large flat cell (Drosophila) in digestive tract and 193 other cell types or tissues.
DR   ExpressionAtlas; Q9VT28; baseline and differential.
DR   GO; GO:0045177; C:apical part of cell; IDA:FlyBase.
DR   GO; GO:0030424; C:axon; IDA:FlyBase.
DR   GO; GO:0044297; C:cell body; IDA:FlyBase.
DR   GO; GO:0005938; C:cell cortex; IDA:FlyBase.
DR   GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
DR   GO; GO:0030425; C:dendrite; IDA:FlyBase.
DR   GO; GO:0030427; C:site of polarized growth; IBA:GO_Central.
DR   GO; GO:0048800; P:antennal morphogenesis; IMP:FlyBase.
DR   GO; GO:0000902; P:cell morphogenesis; IBA:GO_Central.
DR   GO; GO:0008407; P:chaeta morphogenesis; IMP:FlyBase.
DR   GO; GO:0070593; P:dendrite self-avoidance; IGI:FlyBase.
DR   GO; GO:0035317; P:imaginal disc-derived wing hair organization; IGI:FlyBase.
DR   GO; GO:0007476; P:imaginal disc-derived wing morphogenesis; IMP:FlyBase.
DR   GO; GO:0051012; P:microtubule sliding; IMP:UniProtKB.
DR   GO; GO:0150013; P:negative regulation of neuron projection arborization; IMP:UniProtKB.
DR   GO; GO:0031175; P:neuron projection development; IBA:GO_Central.
DR   GO; GO:0035316; P:non-sensory hair organization; IMP:FlyBase.
DR   GO; GO:0048601; P:oocyte morphogenesis; IDA:FlyBase.
DR   GO; GO:0045893; P:positive regulation of DNA-templated transcription; IMP:UniProtKB.
DR   GO; GO:0045860; P:positive regulation of protein kinase activity; IMP:UniProtKB.
DR   GO; GO:0071902; P:positive regulation of protein serine/threonine kinase activity; IMP:UniProtKB.
DR   GO; GO:0050773; P:regulation of dendrite development; IMP:UniProtKB.
DR   GO; GO:0048814; P:regulation of dendrite morphogenesis; IMP:FlyBase.
DR   GO; GO:0042052; P:rhabdomere development; IMP:FlyBase.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR025614; Cell_morpho_N.
DR   InterPro; IPR025481; Cell_Morphogen_C.
DR   InterPro; IPR045842; Fry_C.
DR   InterPro; IPR039867; Furry/Tao3/Mor2.
DR   InterPro; IPR029473; MOR2-PAG1_mid.
DR   PANTHER; PTHR12295; FURRY-RELATED; 1.
DR   PANTHER; PTHR12295:SF30; PROTEIN FURRY; 1.
DR   Pfam; PF19421; Fry_C; 2.
DR   Pfam; PF14225; MOR2-PAG1_C; 1.
DR   Pfam; PF14228; MOR2-PAG1_mid; 5.
DR   Pfam; PF14222; MOR2-PAG1_N; 1.
DR   SUPFAM; SSF48371; ARM repeat; 3.
PE   1: Evidence at protein level;
KW   Alternative splicing; Phosphoprotein; Reference proteome; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..3479
FT                   /note="Protein furry"
FT                   /id="PRO_0000282939"
FT   REGION          1..49
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          104..165
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1133..1155
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1263..1282
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2125..2185
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2337..2375
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2829..2859
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2901..2936
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2982..3079
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          3460..3479
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        33..49
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        123..157
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1263..1272
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2127..2157
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2359..2375
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2839..2854
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2909..2919
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        3017..3029
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         129
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18327897"
FT   MOD_RES         1838
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18327897"
FT   MOD_RES         1841
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18327897"
FT   MOD_RES         2357
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18327897"
FT   MOD_RES         2842
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000269|PubMed:18327897"
FT   MOD_RES         2845
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18327897"
FT   MOD_RES         2851
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18327897"
FT   MOD_RES         2853
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18327897"
FT   MOD_RES         2999
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18327897"
FT   MOD_RES         3001
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18327897"
FT   MOD_RES         3004
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000269|PubMed:18327897"
FT   MOD_RES         3018
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18327897"
FT   MOD_RES         3019
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18327897"
FT   MOD_RES         3025
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18327897"
FT   MOD_RES         3027
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18327897"
FT   VAR_SEQ         1624..1629
FT                   /note="EDDKVG -> GMRFSY (in isoform D)"
FT                   /evidence="ECO:0000303|PubMed:11526084"
FT                   /id="VSP_052372"
FT   VAR_SEQ         1630..3479
FT                   /note="Missing (in isoform D)"
FT                   /evidence="ECO:0000303|PubMed:11526084"
FT                   /id="VSP_052373"
FT   CONFLICT        170
FT                   /note="E -> V (in Ref. 1; AAG41424/AAK37558)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1876
FT                   /note="M -> I (in Ref. 1; AAG41424)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1933
FT                   /note="I -> L (in Ref. 1; AAG41424)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        2530
FT                   /note="T -> I (in Ref. 1; AAG41424)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        3375
FT                   /note="I -> V (in Ref. 4; AAL40005)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        3403
FT                   /note="I -> M (in Ref. 4; AAL40005)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   3479 AA;  384352 MW;  281389C02117A0CF CRC64;
     MDQLELQDDL FGLEAGVAGT NQNPNEQHLS DPAASPSTSS PANNNATAGA ATTSTATVIT
     AVGGAGGGVA AAGVGVVTPT KSPQRNAFQE DAYQANLAGG DSVDNIESAQ LDGGNPSGGS
     PGQRHSINSA EYTSTPKTTR SGPNGSTTAS GTTSPINYQL PGDDYPYGIE YESQQLLYQQ
     QQQQQQQQSQ QQQQQQQQQQ QQLPVGDVEQ SSAVTYQSLP VSRQSYASPP ALIIPQRQSL
     LPWGAHSRSS IINVLPSYTQ AEMHALAARV ASVETSAPRP GEIVMRNLFS DFTAQAEKKI
     ELVMLESADK NLSKLLQRGE DQQFDQLLSA LGSVAEHCLP SLLHTLLAWH RRQLSDMEIK
     NDLKKPAPSG SSSQAATNKP TVDLDFQLQR REAAVEFIFC LALIEILKQL PYHPGHEDLV
     RSIENLAFKH FKYKDGLQNN PNALNIHMIA DLYAEVIGVL AQSRFASVRK RFMSELKELR
     GKEVSPTTTQ SIISLLMGMK FFRVKMVPIE EFEASFQFMH ECGQYFLEVK DKDIKHALAG
     LFVEILVPVA AAVKNEVNVP CVKNFVELLY VQTLDASTKS KHRLALFPLV TCLLCVSQKT
     FFLTNWHYFL AMCLSNLKNR DAKMSRVALE SLFRLLWVYM IRIKCESNSA THSRLQSIVN
     SLFPKGSKGV VPRDTPLNIF VKIIQFIAQE RLDFAMREIV YDLLCVGRSI KLILNPERMS
     IGLRAFLVVA DSLQQKAGEP PMPRTVPVLP SGNTLRVKKT FNKMYVLLTD DTARSIGMST
     YFPHVRRVFV DILRALDVHY GRPLMMTNTQ NQNKEPDEML SGERKPRIDL FRTCVAAVPR
     LIPDTMTPHE LVDMLSRLSV HMDEELRILT HQSLTTLVID FPDWRQDVVH GYTQFLVRDV
     TDTYPQLLEN CTRILFTFLN IWRCATNVNG NNTTSAPSGA TNVVNTSQAK MTTATTTTTV
     VQATVVQVTS APAKDTASSQ LSKQQHLNTA SSAASSITTS SGMSSITQHT VLNMASDVGK
     KNEIPLATTL HFVEGFALVL LCNYRTYLRK LAALILKEVK NLMRALGIPE TEPPLIDVMD
     RCVPGIIEKC LPQLPQTEKT AILNANCIDL QWIAERSSGV WLAGLTDDNS KSSTSTLNLS
     QSSSTPNASA TAASSPQLPF DPWATCLFGL LERQNVLQQC PSAVAQAWPI CFTRLNALYS
     VIDPTPVSDN RASLLRSSAP TKKVPTESQK DSYLRLWRNQ VACAMRLVPQ IPSVAVRCAS
     PDLSLSSSPD SLNADRSDKS AMGSASPQAL YKLVVPLLRC EVVDVRDAAV NALGLINHDA
     LKDLMEELVV YIREAVDCKQ ENMRRRRRRD ALRLQVVRVL EKIAENGTFG VSTCVLERDT
     MSLHPTFVLY ISGAMGYLTS ETDKDNLSIR EVKAHFCNFI RKMIKNFPLE ACATLLSRVL
     KRNLFNLFAA WCGSFSKPLG YTMQSDHTLE EEKLQFSALQ AMSALLCCGQ IFNPSYLQDD
     SIIYKWLDML LTSKNEKIYQ LARDTVVLLL ESNPDIGQLL EWVIDRCYTS TPREADACFL
     ALASIFSAKE YPCDHYTSVI TVTLLMTGCP RVEVHATALQ LLQILDKRFF GSVVGTLHSD
     SDKEDDKVGT LDVLLSSAYC RSQRFLSKQL AQLRPELTMS IFSEITHRFQ SAREDVRALL
     LQCLLPWLQN MELVATSVPP ATPLSYIMYF PDSGTRGRRE GTGSTEATEM ILNNLFYITA
     KFSDAHPRDI EELWGTLCQF WPNNLKVILR YLVIMSGMAP TELLPYAKRV ALYLVRSCPD
     RLLDELMAEL QTVETLNCLI ERTETPPFYR LTSMRKASSH SADGQAAGGI NDSRIQDLAV
     EKGTIHTKRH SGEDPMKIGT CKSDSGIRAY TQAAAAAAAA AVTPGSSGNR PPRGADKIRA
     ASGPSILPRP EDILINDPEL RQEENVELRG TSDAAPNGHP HPLPMPEYGG YFAPLTEFLP
     DVSLPISGFH RCNVAVMLLT DIVVDGIPGI DWTLHLPLML HILFLGLDHT RIIVREHCKQ
     LCVNLLIVLA EHNDHLTVAR ILLNSETSKL DLGLTVPALP VIDNNFTELH QQFDSYLLHV
     SPQAAAYALQ HNLSSSTIIA AHHQNLSQTP QSQQQTGSQN GQTTTPPGLT ATPAALQINP
     NNSENSEVPL IHPDEHAPPQ PGPSMPIAHV IKSLLKFLAQ DTCQPLWNYE DITAKVWAVK
     SAEQLSCFLK HMVKVFADSY PQARIAERWA QTALQLGLSC SSRHYAGRCL QIFRALNVPI
     NSRMLSDILS RLVETVAEQG EDMQGYVTEL LLTLEAAVDS LDSDFRPLDV MKDIFKSTPN
     LNNKDGGPNS ILPGKKSPSG MTPQSSNYSI PSHGRSTSYS VSYCGRKANN SPCDKQVELR
     NRSSGIDLER SVVCKFGVGG GGAGSALSRS RSAQSLKMLG DTATQDDKMT ILAQLFWLSV
     SLLESDYEHE FMLALRLLTR VLHRLPLDRP DARDKVEKLQ QQLKWTAYPG VHALLLKGCT
     HSATYEPTIT LLSQFAPLLT LPVCDPTQSC AFPMNVIALL PYMLLHYEDA NEICIRSAEN
     IAQVSTELGA KLENLGTVMT LYSRKTFCKE SFQWTKCVVK YLHDTYAHMG LHMVAFLIEV
     LEKGPQQVQV PVLNVIHCML HYVDLSAPQA QSINADLLRA IGKYLDTAYW KDSLKILKLI
     VTRSSSLQVV PPSDGSSAGL SFSFYGAYPD SDMFCKKELA GRTMEFTFDV SQTPLIGRRI
     LLKTEEPVAG GAVSTTGSSS LNSTLTNATT VTVAPSAAQQ QTNVQMQQQR ANTNVAALAA
     AAAAQHQQQQ HAIGAGSSVV GTPNSPRRSA SLSPADTVPL SGWKRPWMSQ CRVRECLVNL
     LTTCGQRVGL PKSPSVIFSQ SSDLMERQSS AASSTEETSG PQGDLSSGSR RDDGQPDFTV
     FKDFDFLEYE DSIAGESTDN FNWGVRRHQL FEGDEDRLNC GSGIGGSIKG GHSSAFEDSF
     SDKTPILSKR KRQIADDSSD EEAESESPLD EDHRQSFLKS GYSAVPPTSL SLRERRRRNS
     VSRSDTSGSS AGDLGDLTPC NASPHLPGII RFSAAIHDEA EENWRRQVQA LLVNQPSAHT
     SELLQQLYRL IKELTFKTVN ISKEAKKFFT GIGSQLGNRI SLFTDLLSSR ADPPQVWCSE
     LQATSPKLFE TLRFNVLEVQ EHLETFFDRK DQVLECLDAV KTSCKLSLFN EADVAASGLE
     LPSTSSIVYM PFDPASTEVV LDLGRSLYKL MFQLLLLIES NHKISSNVVN HFRMNEDMHD
     ISDLYALVRD ALVRYISEAE LDCLESSTST EGEHTPTPSP GLPMTPEEFE AVLTEHIDLQ
     RWPSAIAHVR QYRRISTLNA SGYQNVTIFS YNSADNRQKW DEISVILNAY AHGIMKDRTE
     AFIVSKSDSE VFEIYAILSE NLYQVSSALT NMEISMKSYS AGSASGNSHR SEQDIVTNL
//