OSA_DROME
ID OSA_DROME Reviewed; 2716 AA.
AC Q8IN94; O61603; Q9VEG7;
DT 25-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Trithorax group protein osa;
DE AltName: Full=Protein eyelid;
GN Name=osa; Synonyms=eld; ORFNames=CG7467;
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], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=9271118; DOI=10.1101/gad.11.15.1949;
RA Treisman J.E., Luk A., Rubin G.M., Heberlein U.;
RT "Eyelid antagonizes wingless signaling during Drosophila development and
RT has homology to the Bright family of DNA-binding proteins.";
RL Genes Dev. 11:1949-1962(1997).
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, AND DEVELOPMENTAL STAGE.
RX PubMed=9895321; DOI=10.1242/dev.126.4.733;
RA Vazquez M., Moore L., Kennison J.A.;
RT "The trithorax group gene osa encodes an ARID-domain protein that
RT genetically interacts with the brahma chromatin-remodeling factor to
RT regulate transcription.";
RL Development 126:733-742(1999).
RN [5]
RP DNA-BINDING, AND IDENTIFICATION IN A BRAHMA COMPLEX WITH BRM AND SNR1.
RX PubMed=10601025; DOI=10.1093/emboj/18.24.7029;
RA Collins R.T., Furukawa T., Tanese N., Treisman J.E.;
RT "Osa associates with the Brahma chromatin remodeling complex and promotes
RT the activation of some target genes.";
RL EMBO J. 18:7029-7040(1999).
RN [6]
RP FUNCTION.
RX PubMed=10471712; DOI=10.1093/genetics/153.1.275;
RA Staehling-Hampton K., Ciampa P.J., Brook A., Dyson N.;
RT "A genetic screen for modifiers of E2F in Drosophila melanogaster.";
RL Genetics 153:275-287(1999).
RN [7]
RP IDENTIFICATION IN A BRAHMA COMPLEX WITH BRM; OSA; MOR; SNR1; DALAO; BAP55;
RP BAP60 AND BAP47, AND FUNCTION AS A COACTIVATOR.
RX PubMed=10809665;
RA Kal A.J., Mahmoudi T., Zak N.B., Verrijzer C.P.;
RT "The Drosophila brahma complex is an essential coactivator for the
RT trithorax group protein zeste.";
RL Genes Dev. 14:1058-1071(2000).
RN [8]
RP FUNCTION AS A COREPRESSOR.
RX PubMed=11124806; DOI=10.1101/gad.854300;
RA Collins R.T., Treisman J.E.;
RT "Osa-containing Brahma chromatin remodeling complexes are required for the
RT repression of wingless target genes.";
RL Genes Dev. 14:3140-3152(2000).
RN [9]
RP FUNCTION AS A COREPRESSOR, AND INTERACTION WITH PNR AND CHI.
RX PubMed=12629041; DOI=10.1101/gad.255703;
RA Heitzler P., Vanolst L., Biryukova I., Ramain P.;
RT "Enhancer-promoter communication mediated by Chip during Pannier-driven
RT proneural patterning is regulated by Osa.";
RL Genes Dev. 17:591-596(2003).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-384; THR-747; SER-1930;
RP SER-1932; SER-2081; SER-2168; SER-2169; THR-2176 AND SER-2181, AND
RP 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: Trithorax group (trxG) protein required for embryonic
CC segmentation, development of the notum and wing margin, and
CC photoreceptor differentiation. Required for the activation of genes
CC such as Antp, Ubx and Eve. Binds to DNA without specific affinity,
CC suggesting that it is recruited to promoters by promoter-specific
CC proteins. Essential component of the Brahma complex, a multiprotein
CC complex which is the equivalent of the yeast SWI/SNF complex and acts
CC by remodeling the chromatin by catalyzing an ATP-dependent alteration
CC in the structure of nucleosomal DNA. This complex can both serve as a
CC transcriptional coactivator or corepressor, depending on the context.
CC Acts as an essential coactivator for Zeste, which recruits the whole
CC complex to specific genes. In contrast, it acts as a corepressor for Wg
CC target genes, possibly via an interaction with Pan and Gro. It also
CC acts as a negative regulator for proneural achaete-scute, when it is
CC directly recruited by Pan and Chi. Also represses E2f activation.
CC {ECO:0000269|PubMed:10471712, ECO:0000269|PubMed:10809665,
CC ECO:0000269|PubMed:11124806, ECO:0000269|PubMed:12629041,
CC ECO:0000269|PubMed:9271118, ECO:0000269|PubMed:9895321}.
CC -!- SUBUNIT: Component of the Brahma complex, which is composed of Brm,
CC Osa, Mor, Snr1/Bap45, Bap111/Dalao, Bap55, Bap60 and Bap47. Interacts
CC with Pnr and Chi via its EHD domain. {ECO:0000269|PubMed:10601025,
CC ECO:0000269|PubMed:10809665, ECO:0000269|PubMed:12629041}.
CC -!- INTERACTION:
CC Q8IN94; P25439: brm; NbExp=4; IntAct=EBI-115993, EBI-868480;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00355,
CC ECO:0000269|PubMed:9271118}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed in early embryo. In third
CC instar larvae, it is ubiquitously expressed in wing and eye-antenna
CC imaginal disks, with a stronger expression in a band just anterior to
CC the morphogenetic furrow. {ECO:0000269|PubMed:9271118}.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
CC {ECO:0000269|PubMed:9271118, ECO:0000269|PubMed:9895321}.
CC -!- DOMAIN: The ARID domains mediates the binding to DNA.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF55457.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF053091; AAC06254.1; -; mRNA.
DR EMBL; AE014297; AAF55457.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AE014297; AAN13750.1; -; Genomic_DNA.
DR PIR; T13049; T13049.
DR RefSeq; NP_001163639.1; NM_001170168.2.
DR RefSeq; NP_524392.2; NM_079668.3.
DR RefSeq; NP_732263.1; NM_169775.2.
DR SMR; Q8IN94; -.
DR BioGRID; 67162; 62.
DR DIP; DIP-20699N; -.
DR IntAct; Q8IN94; 6.
DR MINT; Q8IN94; -.
DR STRING; 7227.FBpp0088543; -.
DR iPTMnet; Q8IN94; -.
DR PaxDb; Q8IN94; -.
DR EnsemblMetazoa; FBtr0089581; FBpp0088543; FBgn0261885.
DR EnsemblMetazoa; FBtr0301487; FBpp0290702; FBgn0261885.
DR GeneID; 42130; -.
DR KEGG; dme:Dmel_CG7467; -.
DR CTD; 42130; -.
DR FlyBase; FBgn0261885; osa.
DR VEuPathDB; VectorBase:FBgn0261885; -.
DR eggNOG; KOG2510; Eukaryota.
DR GeneTree; ENSGT00940000169092; -.
DR InParanoid; Q8IN94; -.
DR OMA; CRPIDMD; -.
DR OrthoDB; 256110at2759; -.
DR PhylomeDB; Q8IN94; -.
DR Reactome; R-DME-3214858; RMTs methylate histone arginines.
DR Reactome; R-DME-8939243; RUNX1 interacts with co-factors whose precise effect on RUNX1 targets is not known.
DR BioGRID-ORCS; 42130; 1 hit in 3 CRISPR screens.
DR ChiTaRS; osa; fly.
DR GenomeRNAi; 42130; -.
DR PRO; PR:Q8IN94; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0261885; Expressed in eye disc (Drosophila) and 26 other tissues.
DR ExpressionAtlas; Q8IN94; baseline and differential.
DR Genevisible; Q8IN94; DM.
DR GO; GO:0035060; C:brahma complex; IDA:FlyBase.
DR GO; GO:0071565; C:nBAF complex; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; HDA:FlyBase.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005700; C:polytene chromosome; IDA:FlyBase.
DR GO; GO:0016514; C:SWI/SNF complex; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR GO; GO:0006338; P:chromatin remodeling; IEA:InterPro.
DR GO; GO:0007480; P:imaginal disc-derived leg morphogenesis; IMP:FlyBase.
DR GO; GO:0008587; P:imaginal disc-derived wing margin morphogenesis; IMP:UniProtKB.
DR GO; GO:0007476; P:imaginal disc-derived wing morphogenesis; IMP:FlyBase.
DR GO; GO:0008586; P:imaginal disc-derived wing vein morphogenesis; IMP:FlyBase.
DR GO; GO:0007406; P:negative regulation of neuroblast proliferation; IGI:FlyBase.
DR GO; GO:0014017; P:neuroblast fate commitment; IMP:FlyBase.
DR GO; GO:0046530; P:photoreceptor cell differentiation; IMP:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:FlyBase.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IMP:FlyBase.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0007379; P:segment specification; IMP:UniProtKB.
DR GO; GO:0048190; P:wing disc dorsal/ventral pattern formation; IGI:FlyBase.
DR GO; GO:0016055; P:Wnt signaling pathway; IMP:UniProtKB.
DR Gene3D; 1.10.150.60; -; 1.
DR InterPro; IPR001606; ARID_dom.
DR InterPro; IPR036431; ARID_dom_sf.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR021906; BAF250/Osa.
DR InterPro; IPR033388; BAF250_C.
DR PANTHER; PTHR12656; PTHR12656; 2.
DR Pfam; PF01388; ARID; 1.
DR Pfam; PF12031; BAF250_C; 1.
DR SMART; SM00501; BRIGHT; 1.
DR SUPFAM; SSF46774; SSF46774; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR PROSITE; PS51011; ARID; 1.
PE 1: Evidence at protein level;
KW Activator; Chromatin regulator; Developmental protein; DNA-binding;
KW Nucleus; Phosphoprotein; Reference proteome; Repressor; Transcription;
KW Transcription regulation.
FT CHAIN 1..2716
FT /note="Trithorax group protein osa"
FT /id="PRO_0000200593"
FT DOMAIN 1000..1091
FT /note="ARID"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00355"
FT DOMAIN 1769..2517
FT /note="EHD"
FT REGION 1..969
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1108..1766
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1914..1936
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2045..2124
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2520..2617
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2684..2716
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..20
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 45..66
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 67..86
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 95..109
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 171..211
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 233..251
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 259..293
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 294..348
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 350..386
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 410..470
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 471..503
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 511..549
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 552..570
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 571..593
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 594..623
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 651..684
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 749..764
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 803..826
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 827..846
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 857..872
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 881..932
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1126..1146
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1269..1285
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1286..1301
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1308..1325
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1343..1359
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1360..1383
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1425..1442
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1504..1524
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1531..1546
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1590..1604
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1635..1656
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1914..1930
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2045..2076
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2077..2093
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2540..2617
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 384
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 747
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 1930
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 1932
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 2081
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 2168
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 2169
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 2176
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 2181
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT CONFLICT 61
FT /note="Missing (in Ref. 1; AAC06254)"
FT /evidence="ECO:0000305"
FT CONFLICT 1169
FT /note="V -> G (in Ref. 1; AAC06254)"
FT /evidence="ECO:0000305"
FT CONFLICT 1795
FT /note="M -> T (in Ref. 1; AAC06254)"
FT /evidence="ECO:0000305"
FT CONFLICT 2637
FT /note="G -> E (in Ref. 1; AAC06254)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2716 AA; 284064 MW; EFAE76CB51C7C675 CRC64;
MNEKIKSPQT QQQQQGGAPA PAATPPSAGA APGAATPPTS GPPTPNNNSN NGSDPSIQQQ
QQNVAPHPYG APPPPGSGPG GPPGPDPAAV MHYHHLHQQQ QQHPPPPHMQ QQQHHGGPAP
PPPGGAPEHA PGVKEEYTHL PPPHPHPAYG RYHADPNMDP YRYGQPLPGG KPPQQQQPHP
QQQPPQQPGP GGSPNRPPQQ RYIPGQPPQG PTPTLNSLLQ SSNPPPPPQH RYANTYDPQQ
AAASAAAAAA AQQQQAGGPP PPGHGPPPPQ HQPSPYGGQQ GGWAPPPRPY SPQLGPSQQY
RTPPPTNTSR GQSPYPPAHG QNSGSYPSSP QQQQQQQQQQ QQQAGQQPGG PVPGGPPPGT
GQQPPQQNTP PTSQYSPYPQ RYPTPPGLPA GGSNHRTAYS THQYPEPNRP WPGGSSPSPG
SGHPLPPASP HHVPPLQQQP PPPPHVSAGG PPPSSSPGHA PSPSPQPSQA SPSPHQELIG
QNSNDSSSGG AHSGMGSGPP GTPNPQQVMR PTPSPTGSSG SRSMSPAVAQ NHPISRPASN
QSSSGGPMQQ PPVGAGGPPP MPPHPGMPGG PPQQQQSQQQ QASNSASSAS NSPQQTPPPA
PPPNQGMNNM ATPPPPPQGA AGGGYPMPPH MHGGYKMGGP GQSPGAQGYP PQQPQQYPPG
NYPPRPQYPP GAYATGPPPP PTSQAGAGGA NSMPSGAQAG GYPGRGMPNH TGQYPPYQWV
PPSPQQTVPG GAPGGAMVGN HVQGKGTPPP PVVGGPPPPQ GSGSPRPLNY LKQHLQHKGG
YGGSPTPPQG PQGYGNGPTG MHPGMPMGPP HHMGPPHGPT NMGPPTSTPP QSQMLQGGQP
QGQGASGGPE SGGPEHISQD NGISSSGPTG AAGMHAVTSV VTTGPDGTSM DEVSQQSTLS
NASAASGEDP QCTTPKSRKN DPYSQSHLAP PSTSPHPVVM HPGGGPGEEY DMSSPPNWPR
PAGSPQVFNH VPVPQEPFRS TITTTKKSDS LCKLYEMDDN PDRRGWLDKL RAFMEERRTP
ITACPTISKQ PLDLYRLYIY VKERGGFVEV TKSKTWKDIA GLLGIGASSS AAYTLRKHYT
KNLLTFECHF DRGDIDPLPI IQQVEAGSKK KTAKAASVPS PGGGHLDAGT TNSTGSSNSQ
DSFPAPPGSA PNAAIDGYPG YPGGSPYPVA SGPQPDYATA GQMQRPPSQN NPQTPHPGAA
AAVAAGDNIS VSNPFEDPIA AGGGPGSGTG PGPGQGPGPG AASGGAGAVG AVGGGPQPHP
PPPHSPHTAA QQAAGQHQQQ HPQHQHPGLP GPPPPQQQQG QQGQQPPPSV GGGPPPAPQQ
HGPGQVPPSP QQHVRPAAGA PYPPGGSGYP TPVSRTPGSP YPSQPGAYGQ YGSSDQYNAT
GPPGQPFGQG PGQYPPQNRN MYPPYGPEGE APPTGANQYG PYGSRPYSQP PPGGPQPPTQ
TVAGGPPAGG APGAPPSSAY PTGRPSQQDY YQPPPDQSPQ PRRHPDFIKD SQPYPGYNAR
PQIYGAWQSG TQQYRPQYPS SPAPQNWGGA PPRGAAPPPG APHGPPIQQP AGVAQWDQHR
YPPQQGPPPP PQQQQQPQQQ QQQPPYQQVA GPPGQQPPQA PPQWAQMNPG QTAQSGIAPP
GSPLRPPSGP GQQNRMPGMP AQQQQSQQQG GVPQPPPQQA SHGGVPSPGL PQVGPGGMVK
PPYAMPPPPS QGVGQQVGQG PPGGMMSQKP PPMPGQAMQQ QPLQQQPPSH QHPHPHQHPQ
HQHPHQMPPN QTAPGGYGPP GMPGGGAQLV KKELIFPHDS VESTTPVLYR RKRLMKADVC
PVDPWRIFMA MRSGLLTECT WALDVLNVLL FDDSTVQFFG ISNLPGLLTL LLEHFQKNLA
EMFDERENEE QSALLAEDAD DDADSGTVMC EKLRTSGRQP RCVRSISSYN RRRHYENMDR
SGKDGAGNGS DSEDADEGID LGQVRVQPNP EERSLLLSFT PNYTMVTRKG VPVRIQPAEN
DIFVDERQKA WDIDTNRLYE QLEPVGSDAW TYGFTEPDPL DGIIDVFKSE IVNIPFARYI
RSDKKGRKRT ELASSSRKPE IKTEENSTEE QTFNKKRRLV SGGSSSSGAH AEGKKSKLTS
EEFAQPNAEV KKEPGTADSD CRPVDMDIEA PQQRLTNGVA PCSSTPAIFD PRTTAKDEAR
VLQRRRDSSF EDECYTRDEA SLHLVSESQD SLARRCIALS NIFRNLTFVP GNETVLAKST
RFLAVLGRLL LLNHEHLRRT PKTRNYDREE DTDFSDSCSS LQGEREWWWD YLITIRENML
VAMANIAGHL ELSRYDELIA RPLIDGLLHW AVCPSAHGQD PFPSCGPNSV LSPQRLALEA
LCKLCVTDAN VDLVIATPPF SRLEKLCAVL TRHLCRNEDQ VLREFSVNLL HYLAAADSAM
ARTVALQSPC ISYLVAFIEQ AEQTALGVAN QHGINYLREN PDSMGTSLDM LRRAAGTLLH
LAKHPDNRSL FMQQEQRLLG LVMSHILDQQ VALIISRVLY QVSRGTGPIH SVEFRLLQQR
QQQQLRPGPA GKQAASAGGS ATVKAETAST ETSSTEAKPA PAATTAVVND ENSNSSQQLP
PAATFNDVSN SSTNSNSCGT ASSNQTNNST TNSSHSSSAI SSQSAITVAA PSAAATGAGS
ATAAAIASDQ QQVSKVAAAA AAAAALSNAS AAAAAAAAAA AASVGPPTSS SVSAGAAVAQ
PAAPPPTNAG TTTAVA
