DORS_DROME
ID DORS_DROME Reviewed; 999 AA.
AC P15330; O77088; Q0E8P9; Q6AWP3; Q9VJD9; Q9VJE0;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 2.
DT 03-AUG-2022, entry version 231.
DE RecName: Full=Embryonic polarity protein dorsal;
GN Name=dl; ORFNames=CG6667;
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] (ISOFORM A).
RX PubMed=3118464; DOI=10.1126/science.3118464;
RA Steward R.;
RT "Dorsal, an embryonic polarity gene in Drosophila, is homologous to the
RT vertebrate proto-oncogene, c-rel.";
RL Science 238:692-694(1987).
RN [2]
RP SEQUENCE REVISION, FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=2598266; DOI=10.1016/0092-8674(89)90773-3;
RA Steward R.;
RT "Relocalization of the dorsal protein from the cytoplasm to the nucleus
RT correlates with its function.";
RL Cell 59:1179-1188(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), FUNCTION, TISSUE SPECIFICITY,
RP DEVELOPMENTAL STAGE, AND ALTERNATIVE SPLICING.
RC STRAIN=Oregon-R;
RX PubMed=10072776; DOI=10.1016/s0378-1119(98)00595-2;
RA Gross I., Georgel P., Oertel-Buchheit P., Schnarr M., Reichhart J.-M.;
RT "Dorsal-B, a splice variant of the Drosophila factor Dorsal, is a novel
RT Rel/NF-kappaB transcriptional activator.";
RL Gene 228:233-242(1999).
RN [4]
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 [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
RC STRAIN=Berkeley; TISSUE=Embryo;
RA Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M.,
RA Park S., Wan K.H., Yu C., Rubin G.M., Celniker S.E.;
RL Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP INTERACTION WITH TAMO, AND SUBCELLULAR LOCATION.
RX PubMed=12653959; DOI=10.1046/j.1365-2443.2002.00634.x;
RA Minakhina S., Yang J., Steward R.;
RT "Tamo selectively modulates nuclear import in Drosophila.";
RL Genes Cells 8:299-310(2003).
RN [8]
RP INTERACTION WITH EMB, AND SUBCELLULAR LOCATION.
RX PubMed=14638854; DOI=10.1083/jcb.200304046;
RA Roth P., Xylourgidis N., Sabri N., Uv A.E., Fornerod M., Samakovlis C.;
RT "The Drosophila nucleoporin DNup88 localizes DNup214 and CRM1 on the
RT nuclear envelope and attenuates NES-mediated nuclear export.";
RL J. Cell Biol. 163:701-706(2003).
RN [9]
RP INTERACTION WITH EMB, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=17032737; DOI=10.1242/jcs.03201;
RA Xylourgidis N., Roth P., Sabri N., Tsarouhas V., Samakovlis C.;
RT "The nucleoporin Nup214 sequesters CRM1 at the nuclear rim and modulates
RT NFkappaB activation in Drosophila.";
RL J. Cell Sci. 119:4409-4419(2006).
RN [10]
RP FUNCTION.
RX PubMed=18000549; DOI=10.1371/journal.pone.0001178;
RA Ayyar S., Pistillo D., Calleja M., Brookfield A., Gittins K., Goldstone C.,
RA Simpson P.;
RT "NF-kappaB/Rel-mediated regulation of the neural fate in Drosophila.";
RL PLoS ONE 2:E1178-E1178(2007).
RN [11]
RP FUNCTION.
RX PubMed=25477468; DOI=10.1126/science.1258236;
RA Meyer S.N., Amoyel M., Bergantinos C., de la Cova C., Schertel C.,
RA Basler K., Johnston L.A.;
RT "An ancient defense system eliminates unfit cells from developing tissues
RT during cell competition.";
RL Science 346:1258236-1258236(2014).
CC -!- FUNCTION: Embryonic developmental protein (PubMed:2598266,
CC PubMed:10072776). The lateral or ventral identity of a cell depends
CC upon the concentration of this protein in its nucleus during the
CC blastoderm stage (PubMed:2598266). A morphogenetic protein that
CC specifically binds to the kappa B-related consensus sequence 5'-
CC GRGAAAANCC-3', located in the enhancer region of zygotic genes such as
CC Zen, Twist, Snail and Decapentaplegic. Mediates an immune response in
CC larvae (PubMed:10072776). Part of a signaling pathway involving NF-
CC kappa-B and Toll-related receptors, that functions in the apoptosis of
CC unfit cells during cell competition (PubMed:25477468). May be part of a
CC NF-kappa-B and Tollo signaling cascade that regulates development of
CC the peripheral nervous system (PubMed:18000549).
CC {ECO:0000269|PubMed:10072776, ECO:0000269|PubMed:18000549,
CC ECO:0000269|PubMed:25477468, ECO:0000269|PubMed:2598266}.
CC -!- SUBUNIT: Interacts with tamo via the nuclear localization signal
CC (PubMed:12653959). Interacts with emb, a component of the nuclear
CC export complex (PubMed:14638854, PubMed:17032737).
CC {ECO:0000269|PubMed:12653959, ECO:0000269|PubMed:14638854,
CC ECO:0000269|PubMed:17032737}.
CC -!- INTERACTION:
CC P15330; Q03017: cact; NbExp=4; IntAct=EBI-198375, EBI-200600;
CC P15330; P98149: Dif; NbExp=2; IntAct=EBI-198375, EBI-188843;
CC P15330; P15330: dl; NbExp=2; IntAct=EBI-198375, EBI-198375;
CC P15330; Q94527-1: Rel; NbExp=2; IntAct=EBI-198375, EBI-15786027;
CC P15330; Q9W1A4: tamo; NbExp=4; IntAct=EBI-198375, EBI-91385;
CC P15330; P22812: tub; NbExp=3; IntAct=EBI-198375, EBI-93181;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14638854,
CC ECO:0000269|PubMed:17032737, ECO:0000269|PubMed:2598266}. Nucleus
CC {ECO:0000269|PubMed:14638854, ECO:0000269|PubMed:17032737,
CC ECO:0000269|PubMed:2598266}. Note=In ventral regions it is first
CC cytoplasmic, then the protein is relocalized in the nucleus
CC (PubMed:2598266). Its nuclear localization is essential to its function
CC as a morphogen (PubMed:2598266). In dorsal regions it remains
CC cytoplasmic (PubMed:2598266). Tamo negatively regulates nuclear import
CC of dl (PubMed:12653959). Emb is responsible for export of dl from the
CC nucleus (PubMed:14638854). Nuclear localization is enhanced upon
CC microbial infection (PubMed:17032737). {ECO:0000269|PubMed:12653959,
CC ECO:0000269|PubMed:14638854, ECO:0000269|PubMed:17032737,
CC ECO:0000269|PubMed:2598266}.
CC -!- SUBCELLULAR LOCATION: [Isoform A]: Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=C;
CC IsoId=P15330-1; Sequence=Displayed;
CC Name=A; Synonyms=B;
CC IsoId=P15330-2; Sequence=VSP_005581, VSP_005582;
CC -!- TISSUE SPECIFICITY: In unchallenged larvae, expression of both isoforms
CC is seen in fat body and gut (isoform A is more abundant). After immune
CC challenge levels of both isoforms are enhanced.
CC {ECO:0000269|PubMed:10072776, ECO:0000269|PubMed:17032737}.
CC -!- DEVELOPMENTAL STAGE: Isoform A is expressed maternally and both
CC isoforms are expressed zygotically from 6-9 hours embryos through to
CC adulthood. {ECO:0000269|PubMed:10072776}.
CC -!- MISCELLANEOUS: [Isoform A]: Nuclear localization signal at positions
CC 335-340. {ECO:0000305}.
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DR EMBL; M23702; AAA28479.1; -; mRNA.
DR EMBL; AF053614; AAC35296.1; -; mRNA.
DR EMBL; AE014134; AAF53611.1; -; Genomic_DNA.
DR EMBL; AE014134; AAF53612.1; -; Genomic_DNA.
DR EMBL; BT015205; AAT94434.1; -; mRNA.
DR PIR; A30350; A30350.
DR RefSeq; NP_001163000.1; NM_001169529.1. [P15330-2]
DR RefSeq; NP_001163001.1; NM_001169530.1. [P15330-2]
DR RefSeq; NP_001286014.1; NM_001299085.1. [P15330-1]
DR RefSeq; NP_724052.1; NM_165217.3. [P15330-2]
DR RefSeq; NP_724053.1; NM_165218.3. [P15330-2]
DR RefSeq; NP_724054.1; NM_165219.2. [P15330-1]
DR AlphaFoldDB; P15330; -.
DR SMR; P15330; -.
DR BioGRID; 61043; 74.
DR DIP; DIP-17423N; -.
DR IntAct; P15330; 7.
DR STRING; 7227.FBpp0080560; -.
DR iPTMnet; P15330; -.
DR PaxDb; P15330; -.
DR PRIDE; P15330; -.
DR EnsemblMetazoa; FBtr0081005; FBpp0080558; FBgn0260632. [P15330-2]
DR EnsemblMetazoa; FBtr0081006; FBpp0080559; FBgn0260632. [P15330-2]
DR EnsemblMetazoa; FBtr0081007; FBpp0080560; FBgn0260632. [P15330-1]
DR EnsemblMetazoa; FBtr0301383; FBpp0290597; FBgn0260632. [P15330-2]
DR EnsemblMetazoa; FBtr0301384; FBpp0290598; FBgn0260632. [P15330-2]
DR EnsemblMetazoa; FBtr0340250; FBpp0309222; FBgn0260632. [P15330-1]
DR GeneID; 35047; -.
DR KEGG; dme:Dmel_CG6667; -.
DR UCSC; CG6667-RA; d. melanogaster. [P15330-1]
DR CTD; 35047; -.
DR FlyBase; FBgn0260632; dl.
DR VEuPathDB; VectorBase:FBgn0260632; -.
DR eggNOG; ENOG502QQS6; Eukaryota.
DR GeneTree; ENSGT00940000171058; -.
DR HOGENOM; CLU_016080_0_0_1; -.
DR InParanoid; P15330; -.
DR OMA; IPMEDIM; -.
DR PhylomeDB; P15330; -.
DR Reactome; R-DME-1169091; Activation of NF-kappaB in B cells.
DR Reactome; R-DME-1810476; RIP-mediated NFkB activation via ZBP1.
DR Reactome; R-DME-202424; Downstream TCR signaling.
DR Reactome; R-DME-209400; Transcriptional activtion by phosphorylated DL/DIF dimer.
DR Reactome; R-DME-209406; Degradation of NF-kappa-B inhibitor, CACT.
DR Reactome; R-DME-209560; NF-kB is activated and signals survival.
DR Reactome; R-DME-214842; DL and DIF homodimers bind to TUB and phosphorylated PLL in the TL receptor 'signalling complex'.
DR Reactome; R-DME-214844; DL and DIF homodimers complexed with CACT are all phosphorylated in the TL receptor 'signalling complex'.
DR Reactome; R-DME-214869; Phosphorylated CACT, DL and DIF homodimers dissociate from the TL receptor 'signalling complex'.
DR Reactome; R-DME-2871837; FCERI mediated NF-kB activation.
DR Reactome; R-DME-3134963; DEx/H-box helicases activate type I IFN and inflammatory cytokines production.
DR Reactome; R-DME-445989; TAK1-dependent IKK and NF-kappa-B activation.
DR Reactome; R-DME-4755510; SUMOylation of immune response proteins.
DR Reactome; R-DME-5607761; Dectin-1 mediated noncanonical NF-kB signaling.
DR Reactome; R-DME-5607764; CLEC7A (Dectin-1) signaling.
DR Reactome; R-DME-5621575; CD209 (DC-SIGN) signaling.
DR Reactome; R-DME-5676590; NIK-->noncanonical NF-kB signaling.
DR Reactome; R-DME-6798695; Neutrophil degranulation.
DR Reactome; R-DME-9020702; Interleukin-1 signaling.
DR Reactome; R-DME-933542; TRAF6 mediated NF-kB activation.
DR SignaLink; P15330; -.
DR ChiTaRS; Dl; fly.
DR GenomeRNAi; 35047; -.
DR PRO; PR:P15330; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0260632; Expressed in crop (Drosophila) and 24 other tissues.
DR ExpressionAtlas; P15330; baseline and differential.
DR Genevisible; P15330; DM.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:FlyBase.
DR GO; GO:0031594; C:neuromuscular junction; IDA:FlyBase.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0071212; C:subsynaptic reticulum; IDA:FlyBase.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:FlyBase.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IDA:FlyBase.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; IPI:FlyBase.
DR GO; GO:0070379; F:high mobility group box 1 binding; IPI:FlyBase.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IDA:FlyBase.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:FlyBase.
DR GO; GO:0009950; P:dorsal/ventral axis specification; IGI:FlyBase.
DR GO; GO:0009953; P:dorsal/ventral pattern formation; IMP:FlyBase.
DR GO; GO:0007249; P:I-kappaB kinase/NF-kappaB signaling; IBA:GO_Central.
DR GO; GO:0006955; P:immune response; IMP:UniProtKB.
DR GO; GO:0045087; P:innate immune response; IBA:GO_Central.
DR GO; GO:0035006; P:melanization defense response; IMP:FlyBase.
DR GO; GO:0038061; P:NIK/NF-kappaB signaling; IBA:GO_Central.
DR GO; GO:0048935; P:peripheral nervous system neuron development; IMP:FlyBase.
DR GO; GO:0002225; P:positive regulation of antimicrobial peptide production; IMP:FlyBase.
DR GO; GO:0045612; P:positive regulation of hemocyte differentiation; IMP:FlyBase.
DR GO; GO:0035208; P:positive regulation of hemocyte proliferation; IMP:FlyBase.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:FlyBase.
DR GO; GO:0035206; P:regulation of hemocyte proliferation; IDA:FlyBase.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0034097; P:response to cytokine; IBA:GO_Central.
DR GO; GO:0008063; P:Toll signaling pathway; IMP:FlyBase.
DR CDD; cd01177; IPT_NFkappaB; 1.
DR Gene3D; 2.60.40.10; -; 1.
DR Gene3D; 2.60.40.340; -; 1.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR002909; IPT_dom.
DR InterPro; IPR033926; IPT_NFkappaB.
DR InterPro; IPR000451; NFkB/Dor.
DR InterPro; IPR008967; p53-like_TF_DNA-bd.
DR InterPro; IPR030492; RHD_CS.
DR InterPro; IPR032397; RHD_dimer.
DR InterPro; IPR011539; RHD_DNA_bind_dom.
DR InterPro; IPR037059; RHD_DNA_bind_dom_sf.
DR PANTHER; PTHR24169; PTHR24169; 1.
DR Pfam; PF16179; RHD_dimer; 1.
DR Pfam; PF00554; RHD_DNA_bind; 1.
DR PRINTS; PR00057; NFKBTNSCPFCT.
DR SMART; SM00429; IPT; 1.
DR SUPFAM; SSF49417; SSF49417; 1.
DR SUPFAM; SSF81296; SSF81296; 1.
DR PROSITE; PS01204; REL_1; 1.
DR PROSITE; PS50254; REL_2; 1.
PE 1: Evidence at protein level;
KW Activator; Alternative splicing; Cytoplasm; Developmental protein;
KW DNA-binding; Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..999
FT /note="Embryonic polarity protein dorsal"
FT /id="PRO_0000205164"
FT DOMAIN 47..342
FT /note="RHD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00265"
FT REGION 1..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 389..424
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 670..851
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 668..677
FT /note="Nuclear export signal"
FT /evidence="ECO:0000269|PubMed:17032737"
FT MOTIF 756..773
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 1..42
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 399..424
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 676..690
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 700..716
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 717..734
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 775..796
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 312
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000255"
FT VAR_SEQ 330..677
FT /note="GKHTFWNLHRHLKRKPDEDLFQQILRLDAKREVQPPTIEVIDLDTPKIDVQR
FT EIPSEMEFNHEESQQSEPALEQEQSVQQEQYTQEQSLQQEQYTQEQSLQQEQYLQQLEQ
FT QQSFQLEEPMQQDQELPAQQSFDQAIDHLPDHTSDHIPEDMEAADAHAEAEAHRLRSEQ
FT EKEIDTIIDEKVRELEQLDLGQQLEPRPLTANDKITEWMKSSEIEQQVHEPSPTAEADV
FT LDSALEISKADKTLDELLETVAELDEIYTDFKVQRDTYKNTIQNELAGLQGRAPLQVED
FT SFDDAATYTSLQIAFKNPVLIPMDDIMPPTPPMSQCAPEDAHQHYDPVEVNSQARKPET
FT P -> DPAHLRRKRQKTGGDPMHLLLQQQQKQQLQNDHQDGRQTNMNCWNTQNIPPIKT
FT EPRDTSPQPFGLSYRAPPELTPSPQPLSPSSNYNHNSTPSPYNMASAVTPTNGQQQLMS
FT PNHPQQQQQQQQYGATDLGSNYNPFAQQVLAQQQQHQQQQQQHQHQHQQQHQQQQQQQQ
FT QQQQQSLQFHANPFGNPGGNSWESKFSAAAVAAAAATATGAAPANGNSNNLSNLNNPFT
FT MHNLLTSGGGPGNANNLQWNLTTNHLHNQHTLHQQQQLQQQQQQQYDNTAPTNNNANLN
FT NNNNNNNTAGNQADNNGPTLSNLLSFDSGQLVHINSEDQQILRLNSEDLQISNLSIST
FT (in isoform A)"
FT /evidence="ECO:0000303|PubMed:10072776,
FT ECO:0000303|PubMed:3118464, ECO:0000303|Ref.6"
FT /id="VSP_005581"
FT VAR_SEQ 678..999
FT /note="Missing (in isoform A)"
FT /evidence="ECO:0000303|PubMed:10072776,
FT ECO:0000303|PubMed:3118464, ECO:0000303|Ref.6"
FT /id="VSP_005582"
FT CONFLICT 236
FT /note="T -> S (in Ref. 6; AAT94434)"
FT /evidence="ECO:0000305"
FT CONFLICT 391
FT /note="H -> Q (in Ref. 3; AAC35296)"
FT /evidence="ECO:0000305"
FT CONFLICT 401
FT /note="L -> F (in Ref. 3; AAC35296)"
FT /evidence="ECO:0000305"
FT CONFLICT 407
FT /note="V -> SQQEQYTQEQSL (in Ref. 3; AAC35296)"
FT /evidence="ECO:0000305"
FT CONFLICT 698..699
FT /note="DK -> EQ (in Ref. 3; AAC35296)"
FT /evidence="ECO:0000305"
FT CONFLICT 965..999
FT /note="ASEFDETSAYYAPVDAGEILTPDEVAKRLAAANGI -> PVNLTRPPPTMLP
FT WMLARF (in Ref. 3; AAC35296)"
FT /evidence="ECO:0000305"
FT CONFLICT P15330-2:506
FT /note="Q -> QQ (in Ref. 1; AAA28479)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 999 AA; 111551 MW; E29C6594AC07D662 CRC64;
MFPNQNNGAA PGQGPAVDGQ QSLNYNGLPA QQQQQLAQST KNVRKKPYVK ITEQPAGKAL
RFRYECEGRS AGSIPGVNST PENKTYPTIE IVGYKGRAVV VVSCVTKDTP YRPHPHNLVG
KEGCKKGVCT LEINSETMRA VFSNLGIQCV KKKDIEAALK AREEIRVDPF KTGFSHRFQP
SSIDLNSVRL CFQVFMESEQ KGRFTSPLPP VVSEPIFDKK AMSDLVICRL CSCSATVFGN
TQIILLCEKV AKEDISVRFF EEKNGQSVWE AFGDFQHTDV HKQTAITFKT PRYHTLDITE
PAKVFIQLRR PSDGVTSEAL PFEYVPMDSG KHTFWNLHRH LKRKPDEDLF QQILRLDAKR
EVQPPTIEVI DLDTPKIDVQ REIPSEMEFN HEESQQSEPA LEQEQSVQQE QYTQEQSLQQ
EQYTQEQSLQ QEQYLQQLEQ QQSFQLEEPM QQDQELPAQQ SFDQAIDHLP DHTSDHIPED
MEAADAHAEA EAHRLRSEQE KEIDTIIDEK VRELEQLDLG QQLEPRPLTA NDKITEWMKS
SEIEQQVHEP SPTAEADVLD SALEISKADK TLDELLETVA ELDEIYTDFK VQRDTYKNTI
QNELAGLQGR APLQVEDSFD DAATYTSLQI AFKNPVLIPM DDIMPPTPPM SQCAPEDAHQ
HYDPVEVNSQ ARKPETPMRP VPPVPPAILT IQYPPEEDKL PPLPPKRIRK QDSNAENRSI
EANTVQTKPS TGESPLNKRL PPAPKNPNFN TLPRQKKPGF FSKLFSRRKS KPDLAQGQEN
SSILDSKANS REPSIGHFNM QDPMRASLRS SKSAAPFISN PAPAKSSPVK AKKPGSKLTK
PVGRSVSSVS GKRPAYLNAD VVHIPLKGDS VNSLPQQQRT EGYSQSSTIS VGAGLDRRTA
SALQLADIPI SEGGMELVAI ADRQSLHNLV SSIEGHFNVQ LDPNLDLTEA EHFALYTSIP
PLAAASEFDE TSAYYAPVDA GEILTPDEVA KRLAAANGI
