AFFL_DROME
ID AFFL_DROME Reviewed; 1673 AA.
AC Q9VQI9; B7YZZ6; C9QPD1; Q95RP2; Q9BH66;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 2.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=AF4/FMR2 family member lilli {ECO:0000305};
DE AltName: Full=Protein lilliputian {ECO:0000303|PubMed:11171403};
DE AltName: Full=Suppressor of Raf at 2A {ECO:0000303|PubMed:8770593};
DE AltName: Full=Suppressor of sina 2-1 {ECO:0000303|PubMed:9475739};
GN Name=lilli {ECO:0000312|EMBL:AAF51180.2, ECO:0000312|FlyBase:FBgn0041111};
GN Synonyms=l(2)00632 {ECO:0000303|PubMed:8978055},
GN SS2-1 {ECO:0000303|PubMed:9475739}, Su(Raf)2A {ECO:0000303|PubMed:8770593};
GN ORFNames=CG8817;
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] {ECO:0000305, ECO:0000312|EMBL:AAG53639.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), FUNCTION, SUBCELLULAR LOCATION,
RP DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=11171403; DOI=10.1242/dev.128.5.791;
RA Wittwer F., van der Straten A., Keleman K., Dickson B.J., Hafen E.;
RT "Lilliputian: an AF4/FMR2-related protein that controls cell identity and
RT cell growth.";
RL Development 128:791-800(2001).
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAK18163.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), FUNCTION, DEVELOPMENTAL STAGE, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=11171404; DOI=10.1242/dev.128.5.801;
RA Tang A.H., Neufeld T.P., Rubin G.M., Muller H.A.;
RT "Transcriptional regulation of cytoskeletal functions and segmentation by a
RT novel maternal pair-rule gene, lilliputian.";
RL Development 128:801-813(2001).
RN [3] {ECO:0000312|EMBL:AAF51180.2}
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 [4] {ECO:0000305, ECO:0000312|EMBL:AAF51180.2}
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 [5] {ECO:0000305, ECO:0000312|EMBL:ACX54921.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM D).
RC STRAIN=Berkeley; TISSUE=Testis;
RA Carlson J.W., Booth B., Frise E., Park S., Wan K.H., Yu C., Celniker S.E.;
RL Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
RN [6] {ECO:0000305, ECO:0000312|EMBL:AAL28786.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1374-1673 (ISOFORMS A/D).
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAL28786.1};
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 [7] {ECO:0000305}
RP FUNCTION.
RX PubMed=8770593; DOI=10.1093/genetics/142.1.163;
RA Dickson B.J., van der Straten A., Dominguez M., Hafen E.;
RT "Mutations Modulating Raf signaling in Drosophila eye development.";
RL Genetics 142:163-171(1996).
RN [8] {ECO:0000305}
RP FUNCTION.
RX PubMed=8978055; DOI=10.1093/genetics/144.4.1681;
RA Perrimon N., Lanjuin A., Arnold C., Noll E.;
RT "Zygotic lethal mutations with maternal effect phenotypes in Drosophila
RT melanogaster. II. Loci on the second and third chromosomes identified by P-
RT element-induced mutations.";
RL Genetics 144:1681-1692(1996).
RN [9] {ECO:0000305}
RP FUNCTION.
RX PubMed=9475739; DOI=10.1093/genetics/148.1.277;
RA Neufeld T.P., Tang A.H., Rubin G.M.;
RT "A genetic screen to identify components of the sina signaling pathway in
RT Drosophila eye development.";
RL Genetics 148:277-286(1998).
RN [10] {ECO:0000305}
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-420; SER-450; SER-452;
RP SER-821; SER-822; SER-871; SER-873; SER-1362 AND THR-1364, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Embryo {ECO:0000269|PubMed:18327897};
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 [11]
RP IDENTIFICATION IN THE SEC COMPLEX, AND SUBCELLULAR LOCATION.
RX PubMed=22195968; DOI=10.1016/j.molcel.2011.12.008;
RA Smith E.R., Lin C., Garrett A.S., Thornton J., Mohaghegh N., Hu D.,
RA Jackson J., Saraf A., Swanson S.K., Seidel C., Florens L., Washburn M.P.,
RA Eissenberg J.C., Shilatifard A.;
RT "The little elongation complex regulates small nuclear RNA transcription.";
RL Mol. Cell 44:954-965(2011).
CC -!- FUNCTION: Has a role in transcriptional regulation. Acts in parallel
CC with the Ras/MAPK and the PI3K/PKB pathways in the control of cell
CC identity and cellular growth. Essential for regulation of the
CC cytoskeleton and cell growth but not for cell proliferation or growth
CC rate. Required specifically for the microtubule-based basal transport
CC of lipid droplets. Plays a partially redundant function downstream of
CC Raf in cell fate specification in the developing eye. Pair-rule protein
CC that regulates embryonic cellularization, gastrulation and
CC segmentation. {ECO:0000269|PubMed:11171403,
CC ECO:0000269|PubMed:11171404, ECO:0000269|PubMed:8770593,
CC ECO:0000269|PubMed:8978055, ECO:0000269|PubMed:9475739}.
CC -!- SUBUNIT: Component of the super elongation complex (SEC), at least
CC composed of Ell, Cdk9, cyclin-T (CycT), lilli and ear.
CC {ECO:0000269|PubMed:22195968}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11171403,
CC ECO:0000269|PubMed:22195968}. Note=Associates to transcriptionally
CC active chromatin.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=A {ECO:0000269|PubMed:10731132}; Synonyms=B
CC {ECO:0000269|PubMed:10731132}, C {ECO:0000269|PubMed:10731132}, G
CC {ECO:0000269|PubMed:10731132};
CC IsoId=Q9VQI9-1; Sequence=Displayed;
CC Name=D {ECO:0000269|PubMed:10731132}; Synonyms=E
CC {ECO:0000269|PubMed:10731132}, F {ECO:0000269|PubMed:10731132};
CC IsoId=Q9VQI9-2; Sequence=VSP_039294;
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
CC {ECO:0000269|PubMed:11171403, ECO:0000269|PubMed:11171404}.
CC -!- DISRUPTION PHENOTYPE: Embryos lacking maternal lilli show specific
CC defects in the establishment of a functional cytoskeleton during
CC cellularization, and exhibit a pair-rule segmentation phenotype. Adults
CC lacking lilli exhibit reduction in cell and organ size and partial
CC suppression of the increased growth associated with loss of PTEN
CC function. {ECO:0000269|PubMed:11171403, ECO:0000269|PubMed:11171404}.
CC -!- SIMILARITY: Belongs to the AF4 family. {ECO:0000255}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL28786.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=ACX54921.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF293971; AAG53639.1; -; mRNA.
DR EMBL; AF289034; AAK18163.1; -; mRNA.
DR EMBL; AE014134; AAF51180.2; -; Genomic_DNA.
DR EMBL; AE014134; AAN10399.1; -; Genomic_DNA.
DR EMBL; AE014134; AAN10400.1; -; Genomic_DNA.
DR EMBL; AE014134; ACL82979.1; -; Genomic_DNA.
DR EMBL; AE014134; ACL82980.1; -; Genomic_DNA.
DR EMBL; AE014134; ACL82981.1; -; Genomic_DNA.
DR EMBL; AE014134; ACL82982.1; -; Genomic_DNA.
DR EMBL; BT100013; ACX54921.1; ALT_FRAME; mRNA.
DR EMBL; AY061238; AAL28786.1; ALT_INIT; mRNA.
DR RefSeq; NP_001137772.1; NM_001144300.2. [Q9VQI9-2]
DR RefSeq; NP_001137773.1; NM_001144301.1. [Q9VQI9-2]
DR RefSeq; NP_001137774.1; NM_001144302.2. [Q9VQI9-2]
DR RefSeq; NP_001137775.1; NM_001144303.1. [Q9VQI9-1]
DR RefSeq; NP_001259973.1; NM_001273044.1. [Q9VQI9-2]
DR RefSeq; NP_523464.1; NM_078740.3. [Q9VQI9-1]
DR RefSeq; NP_722863.1; NM_164516.2. [Q9VQI9-1]
DR RefSeq; NP_722864.1; NM_164517.1. [Q9VQI9-1]
DR AlphaFoldDB; Q9VQI9; -.
DR SMR; Q9VQI9; -.
DR BioGRID; 59717; 38.
DR IntAct; Q9VQI9; 5.
DR STRING; 7227.FBpp0077318; -.
DR iPTMnet; Q9VQI9; -.
DR PaxDb; Q9VQI9; -.
DR PRIDE; Q9VQI9; -.
DR EnsemblMetazoa; FBtr0077632; FBpp0077317; FBgn0041111. [Q9VQI9-1]
DR EnsemblMetazoa; FBtr0077633; FBpp0077318; FBgn0041111. [Q9VQI9-1]
DR EnsemblMetazoa; FBtr0077634; FBpp0077319; FBgn0041111. [Q9VQI9-1]
DR EnsemblMetazoa; FBtr0290038; FBpp0288477; FBgn0041111. [Q9VQI9-2]
DR EnsemblMetazoa; FBtr0290039; FBpp0288478; FBgn0041111. [Q9VQI9-2]
DR EnsemblMetazoa; FBtr0290040; FBpp0288479; FBgn0041111. [Q9VQI9-2]
DR EnsemblMetazoa; FBtr0290041; FBpp0288480; FBgn0041111. [Q9VQI9-1]
DR EnsemblMetazoa; FBtr0332458; FBpp0304731; FBgn0041111. [Q9VQI9-2]
DR GeneID; 33496; -.
DR KEGG; dme:Dmel_CG8817; -.
DR UCSC; CG8817-RA; d. melanogaster. [Q9VQI9-1]
DR CTD; 33496; -.
DR FlyBase; FBgn0041111; lilli.
DR VEuPathDB; VectorBase:FBgn0041111; -.
DR eggNOG; ENOG502QR32; Eukaryota.
DR GeneTree; ENSGT00950000182974; -.
DR InParanoid; Q9VQI9; -.
DR PhylomeDB; Q9VQI9; -.
DR Reactome; R-DME-112382; Formation of RNA Pol II elongation complex.
DR Reactome; R-DME-674695; RNA Polymerase II Pre-transcription Events.
DR Reactome; R-DME-75955; RNA Polymerase II Transcription Elongation.
DR BioGRID-ORCS; 33496; 0 hits in 3 CRISPR screens.
DR ChiTaRS; lilli; fly.
DR GenomeRNAi; 33496; -.
DR PRO; PR:Q9VQI9; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0041111; Expressed in saliva-secreting gland and 18 other tissues.
DR ExpressionAtlas; Q9VQI9; baseline and differential.
DR Genevisible; Q9VQI9; DM.
DR GO; GO:0000791; C:euchromatin; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:FlyBase.
DR GO; GO:0032783; C:super elongation complex; IPI:FlyBase.
DR GO; GO:0008023; C:transcription elongation factor complex; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IPI:FlyBase.
DR GO; GO:0003712; F:transcription coregulator activity; IMP:UniProtKB.
DR GO; GO:0007611; P:learning or memory; IMP:FlyBase.
DR GO; GO:0097150; P:neuronal stem cell population maintenance; IMP:FlyBase.
DR GO; GO:0007366; P:periodic partitioning by pair rule gene; IMP:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:FlyBase.
DR GO; GO:0051493; P:regulation of cytoskeleton organization; IMP:UniProtKB.
DR GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR GO; GO:0032368; P:regulation of lipid transport; IMP:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IMP:UniProtKB.
DR GO; GO:0007379; P:segment specification; HMP:FlyBase.
DR GO; GO:0048190; P:wing disc dorsal/ventral pattern formation; IGI:FlyBase.
DR InterPro; IPR007797; AF4/FMR2.
DR InterPro; IPR043640; AF4/FMR2_CHD.
DR PANTHER; PTHR10528; PTHR10528; 1.
DR Pfam; PF18876; AF-4_C; 1.
DR PROSITE; PS00354; HMGI_Y; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Developmental protein; DNA-binding; Nucleus;
KW Pair-rule protein; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..1673
FT /note="AF4/FMR2 family member lilli"
FT /id="PRO_0000394675"
FT DNA_BIND 851..863
FT /note="A.T hook"
FT /evidence="ECO:0000255"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 54..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 125..302
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 407..534
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 575..604
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 722..1086
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1114..1133
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1141..1160
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1187..1315
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1564..1588
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 60..80
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 139..186
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 219..262
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 430..462
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 463..486
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 498..534
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 722..745
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 771..798
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 859..885
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 909..923
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 930..980
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 990..1060
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1061..1082
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1191..1205
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1220..1239
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1251..1311
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1564..1585
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 420
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 450
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 452
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 821
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 822
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 871
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 873
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 1362
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 1364
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT VAR_SEQ 1..59
FT /note="Missing (in isoform D)"
FT /evidence="ECO:0000303|PubMed:10731132, ECO:0000303|Ref.5"
FT /id="VSP_039294"
FT CONFLICT 235
FT /note="V -> A (in Ref. 5; ACX54921)"
FT /evidence="ECO:0000305"
FT CONFLICT 254
FT /note="L -> M (in Ref. 5; ACX54921)"
FT /evidence="ECO:0000305"
FT CONFLICT 614
FT /note="A -> T (in Ref. 5; ACX54921)"
FT /evidence="ECO:0000305"
FT CONFLICT 1201
FT /note="D -> I (in Ref. 5; ACX54921)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1673 AA; 180089 MW; 7D32A4E81C55B752 CRC64;
MAQQQQQQMQ QQQQHHTSSI NNNNSSSIVL LQQQQPQQQQ QQLDQLQQYN NNLYSQNYNM
EEYERRKRRE REKIERQQGI QIDDRETSLF GEPRRLTEGD AEITAALGEF FEAREYINNQ
TVGISRSAPG AGNPRLQPNL APQAKSLGHS PSSASSAAGP TAASATTSLP GQQQHYQQQQ
RPPTYVKQAD NKPPYNGRGG YPGQPMKNDI PSSSGMAPPR GPPRTSSSNS NSSSVTNNAS
SGGVPASTPL GPPLSTQMPN GREKSFLGPP APALHNGTGG RFVPPAASKR PGVGQQPPPP
EKDVNKIISD IANIFTVQPL TLIAATPHAP TRENYNLLAP NRQKYAMDIP SSPPSAEPSS
LMTPLFAPIT SPIAPLVTTP PQASQMPLGG ATSGTILAGE ALAPLHQLPP TMPKAASGVT
SPGPVKPLKT EKNHSLEKQD SCLENDLELS ESEDEQRKKE GRSGGNSSNS SESDSSESGS
ESSSKNDLQH HPNHQQHHHQ LQQQQQQQQA TMQQQQVLQQ QHRSQPLTSN GAQNKKFRHE
IIARGSNTIT GLLSSSGFGS GGNVGPAGVN SNAVVGTGSG SGGTLSSGGS SSNKTPSPTE
SNKWNLSRFF HKPANQTNSE SVSPGNVSMK VPGILPGGAQ IIPESIDVTT AIVKNEKNDM
AMEEGEEEDD DEEQQLRYGG GLSVTPVAVK KEAIDAVSEM ALGAIPKTQI KRESAETLLS
ARLSDSGTSA SGSSSSSSSS SDSAMGGEVV PMPGPGETLQ LPGVPAAITT VMRVQPTQSQ
KAPPSNSVTL TPILPLPTSP KQRQKKPRKK KAITSAPILD SSDDDEPPPK HPGLDHTAVS
VQTQPATDTV KKGRGRPRKQ QQSGGSGNLS SASAGSSSQT KGPTLTAAKK PLAKTPLAMS
RARKREHSSQ SSSNGNTPTK KVATPQLVAA PLKPTSNTAG SSSSDEDSSS SAESSSKSSS
SSSSSDDTET QNTNCRIVKL NKTGAVQKKA LLGSGSSSPS SSGSEAEDQT TRSQVGSGQA
LAQQLPPYKQ LPISQHSQHL SSSDCSSSSG GCTAVCSSSS GEEDEGRREK ERERKPKSDK
NKINTLTRIF NPKEGGAKKQ GQVVIVDLQE EQQQGKLDAA AQPSAPQAPP AAPAAIMAKP
RMTPTQQQQL GAGLASPART TTPHLTSLIC KIDLSKLSRE RIMRLKKLTP AQQNGHLTPK
DQATNAVHVP NGYAGDTNPA AKVKHEHPVK PEPELDAGYE AKFKPGNVKQ EFQLKQERDR
DRERERERER ERERDREREQ PPGRRRKRSS SSSSSPYKEK KRKKEKADQL QMGKELLPVP
VLLPSNNHER MPNHDRLSYD KLQLLHEDAA AVIGDVSAPN GSPTKKLLAM SPLPPPPTVT
VAPATCNEAV QTTPPSATAT SAIAPPVPAT RLIYRSYFDR DVEHPSDDPR KNNQFLQEAI
NRKHAADLER DSFNQVTLYL EAVVYFLLTA DAMERCSSEQ ATNTMYKDTL SLIKFISTKF
RPYQQQSTTN IQHETHNKVA ILSLRCQSLI SLKLYKLRRK DCRAIINSLT DFFRVGRGDI
ANGNTPSSIS PSNSVGSQGS GSNTPPGRIV PPDIHNMLCK QNEFLSYLNS AHELWDQADR
LVRTGNHIDF IRELDHENGP LTLHSTMHEV FRYVQAGLKT LRDAVSHPTH QSQ
