BSN_RAT
ID BSN_RAT Reviewed; 3938 AA.
AC O88778;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Protein bassoon {ECO:0000303|PubMed:9679147, ECO:0000305};
GN Name=Bsn {ECO:0000312|RGD:2223};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND SUBCELLULAR LOCATION.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RX PubMed=9679147; DOI=10.1083/jcb.142.2.499;
RA tom Dieck S., Sanmarti-Vila L., Langnaese K., Richter K., Kindler S.,
RA Soyke A., Wex H., Smalla K.-H., Kaempf U., Fraenzer J.-T., Stumm M.,
RA Garner C.C., Gundelfinger E.D.;
RT "Bassoon, a novel zinc-finger CAG/Glutamine-repeat protein selectively
RT localized at the active zone of presynaptic nerve terminals.";
RL J. Cell Biol. 142:499-509(1998).
RN [2]
RP SUBCELLULAR LOCATION.
RX PubMed=10564375; DOI=10.1046/j.1460-9568.1999.00793.x;
RA Brandstatter J.H., Fletcher E.L., Garner C.C., Gundelfinger E.D.,
RA Wassle H.;
RT "Differential expression of the presynaptic cytomatrix protein bassoon
RT among ribbon synapses in the mammalian retina.";
RL Eur. J. Neurosci. 11:3683-3693(1999).
RN [3]
RP SUBCELLULAR LOCATION, MYRISTOYLATION AT GLY-2, AND MUTAGENESIS OF GLY-2.
RX PubMed=12812759; DOI=10.1016/s1044-7431(03)00015-0;
RA Dresbach T., Hempelmann A., Spilker C., tom Dieck S., Altrock W.D.,
RA Zuschratter W., Garner C.C., Gundelfinger E.D.;
RT "Functional regions of the presynaptic cytomatrix protein bassoon:
RT significance for synaptic targeting and cytomatrix anchoring.";
RL Mol. Cell. Neurosci. 23:279-291(2003).
RN [4]
RP INTERACTION WITH ERC2; RIMS1 AND UNC13A, DEVELOPMENTAL STAGE, AND FUNCTION.
RX PubMed=12163476; DOI=10.1083/jcb.200202083;
RA Ohtsuka T., Takao-Rikitsu E., Inoue E., Inoue M., Takeuchi M.,
RA Matsubara K., Deguchi-Tawarada M., Satoh K., Morimoto K., Nakanishi H.,
RA Takai Y.;
RT "Cast: a novel protein of the cytomatrix at the active zone of synapses
RT that forms a ternary complex with RIM1 and Munc13-1.";
RL J. Cell Biol. 158:577-590(2002).
RN [5]
RP FUNCTION, INTERACTION WITH ERC2; RIMS1 AND UNC13A, AND IDENTIFICATION IN A
RP COMPLEX WITH RIMS1 AND ERC2.
RX PubMed=14734538; DOI=10.1083/jcb.200307101;
RA Takao-Rikitsu E., Mochida S., Inoue E., Deguchi-Tawarada M., Inoue M.,
RA Ohtsuka T., Takai Y.;
RT "Physical and functional interaction of the active zone proteins, CAST,
RT RIM1, and Bassoon, in neurotransmitter release.";
RL J. Cell Biol. 164:301-311(2004).
RN [6]
RP GLYCOSYLATION AT THR-1339.
RC TISSUE=Brain;
RX PubMed=15340146; DOI=10.1073/pnas.0403471101;
RA Khidekel N., Ficarro S.B., Peters E.C., Hsieh-Wilson L.C.;
RT "Exploring the O-GlcNAc proteome: direct identification of O-GlcNAc-
RT modified proteins from the brain.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:13132-13137(2004).
RN [7]
RP FUNCTION.
RX PubMed=22875941; DOI=10.1523/jneurosci.0195-12.2012;
RA Maas C., Torres V.I., Altrock W.D., Leal-Ortiz S., Wagh D.,
RA Terry-Lorenzo R.T., Fejtova A., Gundelfinger E.D., Ziv N.E., Garner C.C.;
RT "Formation of Golgi-derived active zone precursor vesicles.";
RL J. Neurosci. 32:11095-11108(2012).
RN [8]
RP FUNCTION, INTERACTION WITH SIAH1, AND DISRUPTION PHENOTYPE.
RX PubMed=23403927; DOI=10.1038/emboj.2013.27;
RA Waites C.L., Leal-Ortiz S.A., Okerlund N., Dalke H., Fejtova A.,
RA Altrock W.D., Gundelfinger E.D., Garner C.C.;
RT "Bassoon and Piccolo maintain synapse integrity by regulating protein
RT ubiquitination and degradation.";
RL EMBO J. 32:954-969(2013).
RN [9]
RP SUBCELLULAR LOCATION.
RX PubMed=26212709; DOI=10.1016/j.neuron.2015.07.001;
RA Koerber C., Horstmann H., Venkataramani V., Herrmannsdoerfer F., Kremer T.,
RA Kaiser M., Schwenger D.B., Ahmed S., Dean C., Dresbach T., Kuner T.;
RT "Modulation of Presynaptic Release Probability by the Vertebrate-Specific
RT Protein Mover.";
RL Neuron 87:521-533(2015).
RN [10]
RP FUNCTION, AND INTERACTION WITH CTBP1.
RX PubMed=25652077; DOI=10.15252/embj.201488796;
RA Ivanova D., Dirks A., Montenegro-Venegas C., Schoene C., Altrock W.D.,
RA Marini C., Frischknecht R., Schanze D., Zenker M., Gundelfinger E.D.,
RA Fejtova A.;
RT "Synaptic activity controls localization and function of CtBP1 via binding
RT to Bassoon and Piccolo.";
RL EMBO J. 34:1056-1077(2015).
RN [11]
RP FUNCTION, AND INTERACTION WITH TRIO.
RX PubMed=27907191; DOI=10.1371/journal.pone.0167535;
RA Terry-Lorenzo R.T., Torres V.I., Wagh D., Galaz J., Swanson S.K.,
RA Florens L., Washburn M.P., Waites C.L., Gundelfinger E.D., Reimer R.J.,
RA Garner C.C.;
RT "Trio, a Rho Family GEF, Interacts with the Presynaptic Active Zone
RT Proteins Piccolo and Bassoon.";
RL PLoS ONE 11:E0167535-E0167535(2016).
RN [12]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=29150638; DOI=10.1038/s41598-017-16004-1;
RA Riemann D., Wallrafen R., Dresbach T.;
RT "The Kohlschuetter-Toenz syndrome associated gene Rogdi encodes a novel
RT presynaptic protein.";
RL Sci. Rep. 7:15791-15791(2017).
CC -!- FUNCTION: Scaffold protein of the presynaptic cytomatrix at the active
CC zone (CAZ) which is the place in the synapse where neurotransmitter is
CC released (PubMed:22875941). After synthesis, participates in the
CC formation of Golgi-derived membranous organelles termed Piccolo-Bassoon
CC transport vesicles (PTVs) that are transported along axons to sites of
CC nascent synaptic contacts (PubMed:22875941). At the presynaptic active
CC zone, regulates the spatial organization of synaptic vesicle cluster,
CC the protein complexes that execute membrane fusion and compensatory
CC endocytosis (PubMed:27907191). Functions also in processes other than
CC assembly such as the regulation of specific presynaptic protein
CC ubiquitination by interacting with SIAH1 or the regulation of
CC presynaptic autophagy by associating with ATG5 (PubMed:23403927,
CC PubMed:27907191). Mediates also synapse to nucleus communication
CC leading to reconfiguration of gene expression by associating with the
CC transcriptional corepressor CTBP1 and by subsequently reducing the size
CC of its pool available for nuclear import (PubMed:25652077).
CC {ECO:0000269|PubMed:22875941, ECO:0000269|PubMed:23403927,
CC ECO:0000269|PubMed:25652077, ECO:0000269|PubMed:27907191}.
CC -!- SUBUNIT: Interacts with PCLO, ERC2/CAST1, RIMS1 and UNC13A
CC (PubMed:12163476, PubMed:14734538). Interacts with TPRG1L (By
CC similarity). Interacts with DYNLL1 and DYNLL2; these interactions
CC potentially link PTVs to dynein and myosin V motor complexes (By
CC similarity). Interacts with ATG5; this interaction is important for the
CC regulation of presynaptic autophagy (By similarity). Interacts (via C-
CC terminus) with TRIO (via N-terminus) (PubMed:27907191). Interacts with
CC CTBP1 (PubMed:25652077). Interacts with SIAH1; this interaction
CC negatively regulates SIAH1 E3 ligase activity (PubMed:23403927).
CC {ECO:0000250|UniProtKB:O88737, ECO:0000250|UniProtKB:Q9UPA5,
CC ECO:0000269|PubMed:12163476, ECO:0000269|PubMed:14734538,
CC ECO:0000269|PubMed:23403927, ECO:0000269|PubMed:25652077,
CC ECO:0000269|PubMed:27907191}.
CC -!- INTERACTION:
CC O88778; Q920M9: Siah1; NbExp=3; IntAct=EBI-2271660, EBI-957514;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10564375}.
CC Presynaptic active zone {ECO:0000269|PubMed:10564375,
CC ECO:0000269|PubMed:12812759, ECO:0000269|PubMed:26212709}. Cytoplasm,
CC cytoskeleton {ECO:0000269|PubMed:10564375}. Cytoplasmic vesicle,
CC secretory vesicle, synaptic vesicle membrane
CC {ECO:0000269|PubMed:26212709, ECO:0000269|PubMed:29150638}; Peripheral
CC membrane protein {ECO:0000269|PubMed:26212709,
CC ECO:0000269|PubMed:29150638}. Note=In retina, is localized in the outer
CC plexiform layer at ribbon synapses formed by rods and cones but was
CC absent from basal synaptic contacts formed by cones. In the retinal
CC inner plexiform layer localized to conventional inhibitory GABAergic
CC synapses, made by amacrine cells, but absent from the bipolar cell
CC ribbon synapses (PubMed:10564375). {ECO:0000269|PubMed:10564375,
CC ECO:0000269|PubMed:12812759, ECO:0000269|PubMed:26212709}.
CC -!- TISSUE SPECIFICITY: Detected at synapses in the stratum lucidum in the
CC hippocampus CA3 region (at protein level).
CC {ECO:0000269|PubMed:29150638}.
CC -!- DEVELOPMENTAL STAGE: Detected at embryonic day E18 and at later stages.
CC The expression does not significantly change during the developmental
CC stages tested. {ECO:0000269|PubMed:12163476}.
CC -!- PTM: Myristoylated. The N-terminal myristoylation is not sufficient for
CC presynaptic localization. {ECO:0000269|PubMed:12812759}.
CC -!- DISRUPTION PHENOTYPE: Loss of both Bassoon/BSN and Piccolo/PCLO leads
CC to the aberrant degradation of multiple presynaptic proteins,
CC culminating in synapse degeneration. {ECO:0000269|PubMed:23403927}.
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DR EMBL; Y16563; CAA76287.1; -; mRNA.
DR PIR; T42761; T42761.
DR IntAct; O88778; 8.
DR MINT; O88778; -.
DR STRING; 10116.ENSRNOP00000039162; -.
DR GlyGen; O88778; 7 sites.
DR iPTMnet; O88778; -.
DR PhosphoSitePlus; O88778; -.
DR PaxDb; O88778; -.
DR PRIDE; O88778; -.
DR ABCD; O88778; 1 sequenced antibody.
DR UCSC; RGD:2223; rat.
DR RGD; 2223; Bsn.
DR eggNOG; ENOG502QSYS; Eukaryota.
DR InParanoid; O88778; -.
DR PhylomeDB; O88778; -.
DR PRO; PR:O88778; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030424; C:axon; ISO:RGD.
DR GO; GO:1904115; C:axon cytoplasm; IDA:SynGO-UCL.
DR GO; GO:0009986; C:cell surface; ISO:RGD.
DR GO; GO:0048788; C:cytoskeleton of presynaptic active zone; IDA:SynGO-UCL.
DR GO; GO:0030425; C:dendrite; ISO:RGD.
DR GO; GO:0060076; C:excitatory synapse; IDA:BHF-UCL.
DR GO; GO:0019898; C:extrinsic component of membrane; IDA:SynGO-UCL.
DR GO; GO:0098982; C:GABA-ergic synapse; IDA:SynGO.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0005798; C:Golgi-associated vesicle; IDA:UniProtKB.
DR GO; GO:0098686; C:hippocampal mossy fiber to CA3 synapse; IDA:SynGO.
DR GO; GO:0060077; C:inhibitory synapse; IDA:RGD.
DR GO; GO:0044306; C:neuron projection terminus; ISO:RGD.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:1990257; C:piccolo-bassoon transport vesicle; IDA:SynGO-UCL.
DR GO; GO:0014069; C:postsynaptic density; ISO:RGD.
DR GO; GO:0098793; C:presynapse; ISO:RGD.
DR GO; GO:0048786; C:presynaptic active zone; IDA:UniProtKB.
DR GO; GO:0098831; C:presynaptic active zone cytoplasmic component; IDA:SynGO.
DR GO; GO:0097470; C:ribbon synapse; IDA:RGD.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; ISO:RGD.
DR GO; GO:0045202; C:synapse; IDA:RGD.
DR GO; GO:0008021; C:synaptic vesicle; IDA:UniProtKB.
DR GO; GO:0030672; C:synaptic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005802; C:trans-Golgi network; IDA:RGD.
DR GO; GO:0045503; F:dynein light chain binding; IPI:SynGO-UCL.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0098882; F:structural constituent of presynaptic active zone; ISO:RGD.
DR GO; GO:0001222; F:transcription corepressor binding; IPI:ParkinsonsUK-UCL.
DR GO; GO:0008088; P:axo-dendritic transport; IDA:SynGO-UCL.
DR GO; GO:0007010; P:cytoskeleton organization; NAS:RGD.
DR GO; GO:0099526; P:presynapse to nucleus signaling pathway; ISO:RGD.
DR GO; GO:1904071; P:presynaptic active zone assembly; IDA:UniProtKB.
DR GO; GO:0035418; P:protein localization to synapse; ISO:RGD.
DR GO; GO:0098693; P:regulation of synaptic vesicle cycle; ISO:RGD.
DR GO; GO:1904666; P:regulation of ubiquitin protein ligase activity; IDA:UniProtKB.
DR GO; GO:0008090; P:retrograde axonal transport; IDA:SynGO-UCL.
DR GO; GO:0050808; P:synapse organization; IDA:UniProtKB.
DR Gene3D; 3.30.40.10; -; 2.
DR InterPro; IPR030627; Bsn.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR008899; Znf_piccolo.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR14113:SF1; PTHR14113:SF1; 1.
DR Pfam; PF05715; zf-piccolo; 2.
DR SUPFAM; SSF57903; SSF57903; 2.
PE 1: Evidence at protein level;
KW Cell projection; Coiled coil; Cytoplasm; Cytoplasmic vesicle; Cytoskeleton;
KW Glycoprotein; Lipoprotein; Membrane; Metal-binding; Methylation; Myristate;
KW Phosphoprotein; Reference proteome; Repeat; Synapse; Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..3938
FT /note="Protein bassoon"
FT /id="PRO_0000065004"
FT REPEAT 568..574
FT /note="1"
FT REPEAT 575..581
FT /note="2"
FT REPEAT 582..588
FT /note="3"
FT ZN_FING 167..190
FT /note="C4-type"
FT /evidence="ECO:0000255"
FT ZN_FING 195..217
FT /note="C4-type"
FT /evidence="ECO:0000255"
FT ZN_FING 462..485
FT /note="C4-type"
FT /evidence="ECO:0000255"
FT ZN_FING 490..512
FT /note="C4-type"
FT /evidence="ECO:0000255"
FT REGION 1..158
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 62..70
FT /note="4 X 2 AA tandem repeats of P-G"
FT REGION 228..346
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 361..456
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 523..921
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 568..588
FT /note="3 X 7 AA tandem repeats of K-A-S-P-Q-A-[AK]"
FT REGION 934..1247
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1294..1541
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1561..1611
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1914..1964
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2280..2305
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2318..2343
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2461..2486
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2513..2648
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2839..2859
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2934..2996
FT /note="Sufficient for binding to ERC2"
FT REGION 3055..3148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3162..3399
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3414..3546
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3569..3910
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1032..1087
FT /evidence="ECO:0000255"
FT COILED 1176..1203
FT /evidence="ECO:0000255"
FT COILED 2345..2470
FT /evidence="ECO:0000255"
FT COILED 2933..2975
FT /evidence="ECO:0000255"
FT COILED 3772..3803
FT /evidence="ECO:0000255"
FT COMPBIAS 85..99
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 126..158
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 229..244
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 263..289
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 324..338
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 361..377
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 396..412
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 591..605
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 613..627
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 668..706
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 782..815
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 833..848
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 949..974
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 975..1000
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1001..1019
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1046..1087
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1102..1116
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1151..1175
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1302..1330
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1353..1378
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1399..1427
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1462..1541
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1561..1595
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2542..2562
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2577..2607
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3055..3081
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3082..3097
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3162..3179
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3196..3222
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3281..3303
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3383..3399
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3453..3472
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3570..3595
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3606..3634
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3648..3675
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3694..3709
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3720..3827
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3832..3846
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 142
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O88737"
FT MOD_RES 145
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:O88737"
FT MOD_RES 241
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O88737"
FT MOD_RES 245
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O88737"
FT MOD_RES 863
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:O88737"
FT MOD_RES 965
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O88737"
FT MOD_RES 1035
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O88737"
FT MOD_RES 1036
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O88737"
FT MOD_RES 1085
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O88737"
FT MOD_RES 1087
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O88737"
FT MOD_RES 1093
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O88737"
FT MOD_RES 1099
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O88737"
FT MOD_RES 1221
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O88737"
FT MOD_RES 1470
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O88737"
FT MOD_RES 1479
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O88737"
FT MOD_RES 1481
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O88737"
FT MOD_RES 1780
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:O88737"
FT MOD_RES 1784
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:O88737"
FT MOD_RES 1794
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:O88737"
FT MOD_RES 1794
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:O88737"
FT MOD_RES 1806
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:O88737"
FT MOD_RES 1978
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O88737"
FT MOD_RES 2034
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O88737"
FT MOD_RES 2039
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:O88737"
FT MOD_RES 2069
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:O88737"
FT MOD_RES 2243
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:O88737"
FT MOD_RES 2253
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:O88737"
FT MOD_RES 2259
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:O88737"
FT MOD_RES 2564
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O88737"
FT MOD_RES 2581
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O88737"
FT MOD_RES 2608
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O88737"
FT MOD_RES 2796
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O88737"
FT MOD_RES 2845
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O88737"
FT MOD_RES 2851
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O88737"
FT MOD_RES 3007
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O88737"
FT MOD_RES 3286
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O88737"
FT MOD_RES 3368
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O88737"
FT MOD_RES 3488
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:O88737"
FT MOD_RES 3822
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:O88737"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000269|PubMed:12812759"
FT CARBOHYD 1339
FT /note="O-linked (GlcNAc) threonine"
FT /evidence="ECO:0000269|PubMed:15340146"
FT CARBOHYD 1380
FT /note="O-linked (GlcNAc) threonine"
FT /evidence="ECO:0000250"
FT CARBOHYD 1922
FT /note="O-linked (GlcNAc) threonine"
FT /evidence="ECO:0000250"
FT CARBOHYD 2307
FT /note="O-linked (GlcNAc) threonine"
FT /evidence="ECO:0000250"
FT CARBOHYD 2510
FT /note="O-linked (GlcNAc) threonine"
FT /evidence="ECO:0000250"
FT CARBOHYD 2685
FT /note="O-linked (GlcNAc) threonine"
FT /evidence="ECO:0000250"
FT CARBOHYD 2930
FT /note="O-linked (GlcNAc) threonine"
FT /evidence="ECO:0000250"
FT MUTAGEN 2
FT /note="G->A: Loss of myristoylation."
FT /evidence="ECO:0000269|PubMed:12812759"
SQ SEQUENCE 3938 AA; 418424 MW; 5BF3C230E2C71AE2 CRC64;
MGNEASLEGG AGEGPLPPGG SGLGPGPGAG KPPSALAGGG QLPVAGAARA AGPPTPGLGL
VPGPGPGPGP GSVSRRLDPK EPLGSQRATS PTPKQASATA PGRESPRETR AQGLSGQEAE
GPRRTLQVDS RTQRSGRSPS VSPDRGSTPT SPYSVPQIAP LPSSTLCPIC KTSDLTSTSS
QPNFNTCTQC HNKVCNQCGF NPNPHLTQVK EWLCLNCQMQ RALGMDMTTA PRSKSQQQLH
SPALSPAHSP AKQPLGKPEQ ERSRSPGATQ SGPRQAEAAR ATSVPGPTQA TAPPEVGRVS
PQPPLSTKPS TAEPRPPAGE AQGKSATTVP SGLGAAEQTQ GGLTGKLFGL GASLLTQAST
LMSVQPEADT QGQPSPSKGP PKIVFSDASK EAGPRPPGSG PGPGPTPGAK TEPGPRTGPG
SGPGALAKTG GTPSPKHGRA DHQAASKAAA KPKTMPKERA ACPLCQAELN VGSRGPANYN
TCTACKLRVC TLCGFNPTPH LVEKTEWLCL NCQTKRLLEG SLGEPAPLPL PTPQEPPAGV
PQRAAGASPL KQKGPQGPGQ PSGSLPPKAS PQAAKASPQA AKASPQAKPL RASEPSKTSS
SAPEKKTGIP VKAEPVPKPP PETAVPPGTP KAKSGVKRTD PATPVVKPVP EAPKSGEAEE
PVPKPYSQDL SRSPQSLSDT GYSSDGVSSS QSEITGVVQQ EVEQLDSAGV TGPRPPSPSE
LHKVGSSMRP SLEAQAVAPS GEWSKPPSGS AVEDQKRRPH SLSIMPEAFD SDEELGDILE
EDDSLAMGRQ REQQDTAESS DDFGSQLRHD YVEDSSEGGL SPLPPQPPAR ADMTDEEFMR
RQILEMSAEE DNLEEDDTAV SGRGLAKHGA QKASARPRPE SSQESVALPK RRLPHNATTG
YEELLSEEGP AEPTDGALQG GLRRFKTIGL NSTGRLWSTS LDLGQGSDPN LDREPELEME
SLTGSPEDRS RGEHSSTLPA STPSYTSGTS PTSLSSLEED SDSSPSRRQR LEEAKQQRKA
RHRSHGPLLP TIEDSSEEEE LREEEELLRE QEKMREVEQQ RIRSTARKTR RDKEELRAQR
RRERSKTPPS NLSPIEDASP TEELRQAAEM EELHRSSCSE YSPSPSLDSE AETLDGGPTR
LYKSGSEYNL PAFMSLCSPT ETPSGSSTTP SSGRPLKSAE EAYEDMMRKA ELLQRQQGQA
AGARGPHGGP SQPTGPRSQG SFEYQDTLDH DYGGRASQPA ADGTPAGLGA TVYEEILQTS
QSIARMRQAS SRDLAFTEDK KKEKQFLNAE SAYMDPMKQN GGPLTPGTSP TQLAAPVSFP
TSTSSDSSGG RVIPDVRVTQ HFAKEPQEPL KLHSSPASPS LASKEVGMTF SQGPGTPATT
AMAPCPASLP RGYMTPAGPE RSPSTSSTIH SYGQPPTTAN YGSQTEELPH APSGPAGSGR
ASREKPLSGG DGEVGPPQPS RGYSYFTGSS PPLSPSTPSE SPTFSPSKLG PRATAEFSTQ
TPSLTPSSDI PRSVGTPSPM VAQGTQTPHR PSTPRLVWQQ SSQEAPVMVI TLASDASSQT
RMVHASASTS PLCSPTDSQP ASHSYSQTTP PSASQMPSEP AGPPGFPRAP SAGVDGPLAL
YGWGALPAEN ISLCRISSVP GTSRVEPGPR PPGTAVVDLR TAVKPTPIIL TDQGMDLTSL
AVEARKYGLA LDPVPGRQST AVQPLVINLN AQEQTHTFLA TATTVSITMA SSVLMAQQKQ
PVVYGDPFQS RLDFGQGSGS PVCLAQVKQV EQAVQTAPYR GGPRGRPREA KFARYNLPNQ
VTPLARRDIL ITQMGTAQSV SLKPGPVPEP GAEPHRATPA ELRAHALPGT RKPHTVVVQM
GEGAAGTVTT LLPEEPAGAL DLTGMRPESR LACCDMAYKF PFGSSCTGTF HPAPSAPDKS
VTDAALPGQS SGPFYSPRDP EPPEPLTFRA QGVVGPGPHE EQRPYPQGLP GRLYSSMSDT
NLAEAGLNYH AQRIGQLFQG PGRDSAVDLS SLKHSYSLGF ADGRYLGQGL QYGSFTDLRH
PTDLLSHPLP MRPYSSVSNI YSDHRYGPRG DAVGFQEASL AQYSATTARE ISRMCAALNS
MDQYGGRHGG GSGGPDLVPY QPQHGPGLNA PQGLASLRSG LLGNPTYPEG QPSPGNLAQY
GPAASQGTAV RQLLPSTATV RAADGMIYST INTPIAATLP ITTQPASVLR PMVRGGMYRP
YGSGGVTAVP LTSLTRVPMI APRVPLGPAG LYRYPAPSRF PIASTIPPAE GPVYLGKPAA
AKASGAGGPP RPELPAGGAR EEPLSTTAPP AVIKEAPVAQ APAPPPGQKP AGDAAAGSGS
GVLGRPVMEK EEASQEDRQR KQQEQLLQLE RERVELEKLR QLRLQEELER ERVELQRHRE
EEQLLVQREL QELQTIKHHV LQQQQEERQA QFALQREQLA QQRLQLEQIQ QLQQQLQQQL
EEQKQRQKAP FPATCEAPSR GPPPAATELA QNGQYWPPLT HTAFIAVAGT EGPGQAREPV
LHRGLPSSAS DMSLQTEEQW EAGRSGIKKR HSMPRLRDAC EPESGPDPST VRRIADSSVQ
TDDEEGEGRY LLTRRRRTRR SADCSVQTDD EDNAEWEQPV RRRRSRLSRH SDSGSDSKHE
ASASSSAAAA AARAMSSVGI QTISDCSVQT EPEQLPRVSP AIHITAATDP KVEIVRYISA
PEKTGRGESL ACQTEPDGQA QGVAGPQLIG PTAISPYLPG IQIVTPGALG RFEKKKPDPL
EIGYQAHLPP ESLSQLVSRQ PPKSPQVLYS PVSPLSPHRL LDTSFASSER LNKAHVSPQK
QFIADSTLRQ QTLPRPMKTL QRSLSDPKPL SPTAEESAKE RFSLYQHQGG LGSQVSALPP
NGLVRKVKRT LPSPPPEEAH LPLAGQVPSQ LYAASLLQRG LAGPTTVPAT KASLLRELDR
DLRLVEHEST KLRKKQAELD EEEKEIDAKL KYLELGITQR KESLAKDRVG RDYPPLRGLG
EHRDYLSDSE LNQLRLQGCT TPAGQYVDYP ASAAVPATPS GPTAFQQPRF PPAATQYTAG
SSGPTQNGFL AHQAPTYTGP STYPAPTYPP GTSYPAEPGL PSQPAFHPTG HYAAPTPMPT
TQSAPFPVQA DSHAAHQKPR QTSLADLEQK VPTNYEVISS PAVTVSSTPS ETGYSGPAVS
SSYEHGKAPE HPRGGDRSSV SQSPAPTYPS DSHYTSLEQN VPRNYVMIDD ISELTKDSTP
TASDSQRPEP LGPGGVSGRP GKDPGEPAVL EGPTLPCCYG RGEEESEEDS YDPRGKSGHH
RSMESNGRPA STHYYSDSDY RHGARADKYG PGPMGPKHPS KNLAPAAISS KRSKHRKQGM
EQKISKFSPI EEAKDVESDL ASYPPPTVSS SLTSRSRKFQ DEITYGLKKN VYEQQRYYGV
SSRDTAEEDD RMYGGSSRSR VASAYSGEKL SSHDFSSRSK GYERERETAQ RLQKAGPKPS
SLSMAHGRAR PPMRSQASEE ESPVSPLGRP RPAGGALPPG DTCPQFCSSH SMPDVQEHVK
DGPRAHAYKR EEGYILDDSH CVVSDSEAYH LGQEETDWFD KPRDARSDRF RHHGGHTVSS
SQKRGPARHS YHDYDEPPEE GLWPHDEGGP GRHTSAKEHR HHGDHGRHSG RHAGEEPGRR
AARPHARDMG RHETRPHPQA SPAPAMQKKG QPGYPSSADY SQPSRAPSAY HHASDSKKGS
RQAHSGPTVL QPKPEAQAQP QMQGRQAVPG PQQSQPPSSR QTPSGTASRQ PQTQQQQQQQ
QQQQQQQQQQ QQQQQQQGLG QQAPQQAPSQ ARLQQQSQPT TRSTAPAASH PAGKPQPGPT
TAPGPQPAGL PRAEQAGSSK PAAKAPQQGR APQAQSAPGP AGAKTGARPG GTPGAPAGQP
AAEGESVFSK ILPGGAAEQA GKLTEAVSAF GKKFSSFW
