BSN_MOUSE
ID BSN_MOUSE Reviewed; 3942 AA.
AC O88737; E9QMZ3; Q6ZQB5;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 4.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Protein bassoon {ECO:0000303|PubMed:9679147, ECO:0000305};
GN Name=Bsn {ECO:0000312|MGI:MGI:1277955}; Synonyms=Kiaa0434;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
RC STRAIN=129/SvJ;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2714-3942 (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:167-180(2003).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=12628168; DOI=10.1016/s0896-6273(03)00086-2;
RA Dick O., tom Dieck S., Altrock W.D., Ammermueller J., Weiler R.,
RA Garner C.C., Gundelfinger E.D., Brandstaetter J.H.;
RT "The presynaptic active zone protein bassoon is essential for photoreceptor
RT ribbon synapse formation in the retina.";
RL Neuron 37:775-786(2003).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=12628169; DOI=10.1016/s0896-6273(03)00088-6;
RA Altrock W.D., tom Dieck S., Sokolov M., Meyer A.C., Sigler A.,
RA Brakebusch C., Faessler R., Richter K., Boeckers T.M., Potschka H.,
RA Brandt C., Loescher W., Grimberg D., Dresbach T., Hempelmann A., Hassan H.,
RA Balschun D., Frey J.U., Brandstaetter J.H., Garner C.C., Rosenmund C.,
RA Gundelfinger E.D.;
RT "Functional inactivation of a fraction of excitatory synapses in mice
RT deficient for the active zone protein bassoon.";
RL Neuron 37:787-800(2003).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1108; SER-1236; SER-2578;
RP THR-2595; THR-2622 AND SER-3382, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT "Comprehensive identification of phosphorylation sites in postsynaptic
RT density preparations.";
RL Mol. Cell. Proteomics 5:914-922(2006).
RN [7]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT THR-1395; SER-1707; THR-1934;
RP THR-2318; THR-2524; THR-2700 AND THR-2945.
RC TISSUE=Brain;
RX PubMed=16452088; DOI=10.1074/mcp.t500040-mcp200;
RA Vosseller K., Trinidad J.C., Chalkley R.J., Specht C.G., Thalhammer A.,
RA Lynn A.J., Snedecor J.O., Guan S., Medzihradszky K.F., Maltby D.A.,
RA Schoepfer R., Burlingame A.L.;
RT "O-linked N-acetylglucosamine proteomics of postsynaptic density
RT preparations using lectin weak affinity chromatography and mass
RT spectrometry.";
RL Mol. Cell. Proteomics 5:923-934(2006).
RN [8]
RP INTERACTION WITH TPRG1L.
RC TISSUE=Brain;
RX PubMed=17869247; DOI=10.1016/j.febslet.2007.08.070;
RA Kremer T., Kempf C., Wittenmayer N., Nawrotzki R., Kuner T., Kirsch J.,
RA Dresbach T.;
RT "Mover is a novel vertebrate-specific presynaptic protein with differential
RT distribution at subsets of CNS synapses.";
RL FEBS Lett. 581:4727-4733(2007).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain cortex;
RX PubMed=17114649; DOI=10.1074/mcp.m600046-mcp200;
RA Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B.,
RA Panse C., Schlapbach R., Mansuy I.M.;
RT "Qualitative and quantitative analyses of protein phosphorylation in naive
RT and stimulated mouse synaptosomal preparations.";
RL Mol. Cell. Proteomics 6:283-293(2007).
RN [10]
RP FUNCTION, INTERACTION WITH PCLO, ERC2/CAST1, RIMS1 AND UNC13A, AND TISSUE
RP SPECIFICITY.
RX PubMed=19812333; DOI=10.1523/jneurosci.1255-09.2009;
RA Wang X., Hu B., Zieba A., Neumann N.G., Kasper-Sonnenberg M., Honsbein A.,
RA Hultqvist G., Conze T., Witt W., Limbach C., Geitmann M., Danielson H.,
RA Kolarow R., Niemann G., Lessmann V., Kilimann M.W.;
RT "A protein interaction node at the neurotransmitter release site: domains
RT of Aczonin/Piccolo, Bassoon, CAST, and rim converge on the N-terminal
RT domain of Munc13-1.";
RL J. Neurosci. 29:12584-12596(2009).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-142; SER-241; SER-245;
RP SER-980; SER-1050; SER-1051; SER-1100; THR-1102; SER-1108; SER-1114;
RP SER-1236; SER-1482; SER-1491; SER-1493; SER-1990; SER-2046; SER-2578;
RP THR-2595; THR-2622; SER-2811; SER-2860; SER-2866; SER-3022; SER-3301 AND
RP SER-3382, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [12]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-145; ARG-881; ARG-1792; ARG-1796;
RP ARG-1806; ARG-1818; ARG-2051; ARG-2081; ARG-2255; ARG-2265; ARG-2270;
RP ARG-3502 AND ARG-3823, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Brain;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [13]
RP FUNCTION, INTERACTION WITH ATG5, AND DISRUPTION PHENOTYPE.
RX PubMed=28231469; DOI=10.1016/j.neuron.2017.01.026;
RA Okerlund N.D., Schneider K., Leal-Ortiz S., Montenegro-Venegas C.,
RA Kim S.A., Garner L.C., Waites C.L., Gundelfinger E.D., Reimer R.J.,
RA Garner C.C.;
RT "Bassoon Controls Presynaptic Autophagy through Atg5.";
RL Neuron 93:897-913(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:12628168, PubMed:12628169, PubMed:19812333). After
CC synthesis, participates in the formation of Golgi-derived membranous
CC organelles termed Piccolo-Bassoon transport vesicles (PTVs) that are
CC transported along axons to sites of nascent synaptic contacts (By
CC similarity). At the presynaptic active zone, regulates the spatial
CC organization of synaptic vesicle cluster, the protein complexes that
CC execute membrane fusion and compensatory endocytosis (By similarity).
CC Functions also in processes other than assembly such as the regulation
CC of specific presynaptic protein ubiquitination by interacting with
CC SIAH1 or the regulation of presynaptic autophagy by associating with
CC ATG5 (By similarity) (PubMed:28231469). Mediates also synapse to
CC nucleus communication leading to reconfiguration of gene expression by
CC associating with the transcriptional corepressor CTBP1 and by
CC subsequently reducing the size of its pool available for nuclear import
CC (By similarity). {ECO:0000250|UniProtKB:O88778,
CC ECO:0000250|UniProtKB:Q9UPA5, ECO:0000269|PubMed:12628168,
CC ECO:0000269|PubMed:12628169, ECO:0000269|PubMed:19812333,
CC ECO:0000269|PubMed:28231469}.
CC -!- SUBUNIT: Interacts with PCLO, ERC2/CAST1, RIMS1 and UNC13A
CC (PubMed:19812333). Interacts with TPRG1L (PubMed:17869247). Interacts
CC with DYNLL1 and DYNLL2; these interactions potentially link PTVs to
CC dynein and myosin V motor complexes (By similarity). Interacts with
CC ATG5; this interaction is important for the regulation of presynaptic
CC autophagy (PubMed:28231469). Interacts (via C-terminus) with TRIO (via
CC N-terminus) (By similarity). Interacts with CTBP1 (By similarity).
CC Interacts with SIAH1; this interaction negatively regulates SIAH1 E3
CC ligase activity (By similarity). {ECO:0000250|UniProtKB:O88778,
CC ECO:0000250|UniProtKB:Q9UPA5, ECO:0000269|PubMed:17869247,
CC ECO:0000269|PubMed:19812333, ECO:0000269|PubMed:28231469}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O88778}.
CC Presynaptic active zone {ECO:0000269|PubMed:12628168,
CC ECO:0000269|PubMed:12628169}. Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:O88778}. Cytoplasmic vesicle, secretory vesicle,
CC synaptic vesicle membrane {ECO:0000269|PubMed:12628169}; Peripheral
CC membrane protein {ECO:0000250|UniProtKB:O88778}. Note=In retina, is
CC localized in the outer plexiform layer at ribbon synapses formed by
CC rods and cones but was absent from basal synaptic contacts formed by
CC cones. In the retinal inner plexiform layer localized to conventional
CC inhibitory GABAergic synapses, made by amacrine cells, but absent from
CC the bipolar cell ribbon synapses (By similarity).
CC {ECO:0000250|UniProtKB:O88778}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O88737-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O88737-2; Sequence=VSP_011375;
CC -!- TISSUE SPECIFICITY: Expressed in brain and retina.
CC {ECO:0000269|PubMed:12628168, ECO:0000269|PubMed:12628169,
CC ECO:0000269|PubMed:19812333}.
CC -!- PTM: Myristoylated. The N-terminal myristoylation is not sufficient for
CC presynaptic localization (By similarity). {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Mice show a reduced excitability attributed to
CC inactivation of a fraction of brain glutamatergic synapses. At these
CC synapses, vesicles are clustered and docked in normal numbers, but were
CC unable to fuse. In retina, mutants lacking functional BSN showed normal
CC retinal anatomy, but synapses lacked anchoring of the photoreceptor
CC ribbon to the presynaptic active zone resulting in impaired
CC photoreceptor synaptic transmission (PubMed:12628168). Knockdown of
CC both Bassoon/BSN and Piccolo/PCLO leads to the formation of presynaptic
CC autophagosomes. {ECO:0000269|PubMed:12628168,
CC ECO:0000269|PubMed:28231469}.
CC -!- MISCELLANEOUS: [Isoform 2]: Incompl. {ECO:0000305}.
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DR EMBL; Y17034; CAA76598.1; -; Genomic_DNA.
DR EMBL; Y17035; CAA76598.1; JOINED; Genomic_DNA.
DR EMBL; Y17036; CAA76598.1; JOINED; Genomic_DNA.
DR EMBL; Y17037; CAA76598.1; JOINED; Genomic_DNA.
DR EMBL; Y17038; CAA76598.1; JOINED; Genomic_DNA.
DR EMBL; AC137678; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC168217; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK129141; BAC97951.1; -; mRNA.
DR CCDS; CCDS23517.1; -. [O88737-1]
DR PIR; T42730; T42730.
DR RefSeq; NP_031593.2; NM_007567.2. [O88737-1]
DR RefSeq; XP_006511697.1; XM_006511634.3. [O88737-1]
DR SMR; O88737; -.
DR BioGRID; 198393; 12.
DR IntAct; O88737; 8.
DR MINT; O88737; -.
DR STRING; 10090.ENSMUSP00000035208; -.
DR GlyGen; O88737; 8 sites.
DR iPTMnet; O88737; -.
DR PhosphoSitePlus; O88737; -.
DR SwissPalm; O88737; -.
DR MaxQB; O88737; -.
DR PaxDb; O88737; -.
DR PeptideAtlas; O88737; -.
DR PRIDE; O88737; -.
DR ProteomicsDB; 273847; -. [O88737-1]
DR ProteomicsDB; 273848; -. [O88737-2]
DR ABCD; O88737; 1 sequenced antibody.
DR Antibodypedia; 13612; 142 antibodies from 23 providers.
DR DNASU; 12217; -.
DR Ensembl; ENSMUST00000035208; ENSMUSP00000035208; ENSMUSG00000032589. [O88737-1]
DR GeneID; 12217; -.
DR KEGG; mmu:12217; -.
DR UCSC; uc009rov.1; mouse. [O88737-1]
DR CTD; 8927; -.
DR MGI; MGI:1277955; Bsn.
DR VEuPathDB; HostDB:ENSMUSG00000032589; -.
DR eggNOG; ENOG502QSYS; Eukaryota.
DR GeneTree; ENSGT00620000087961; -.
DR HOGENOM; CLU_000104_1_0_1; -.
DR InParanoid; O88737; -.
DR OMA; AHYYSDS; -.
DR PhylomeDB; O88737; -.
DR TreeFam; TF326082; -.
DR BioGRID-ORCS; 12217; 3 hits in 71 CRISPR screens.
DR ChiTaRS; Bsn; mouse.
DR PRO; PR:O88737; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; O88737; protein.
DR Bgee; ENSMUSG00000032589; Expressed in subiculum and 108 other tissues.
DR ExpressionAtlas; O88737; baseline and differential.
DR Genevisible; O88737; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030424; C:axon; IDA:MGI.
DR GO; GO:1904115; C:axon cytoplasm; ISO:MGI.
DR GO; GO:0009986; C:cell surface; IDA:CACAO.
DR GO; GO:0048788; C:cytoskeleton of presynaptic active zone; ISO:MGI.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0030425; C:dendrite; IDA:BHF-UCL.
DR GO; GO:0060076; C:excitatory synapse; ISS:ParkinsonsUK-UCL.
DR GO; GO:0019898; C:extrinsic component of membrane; ISO:MGI.
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; ISO:MGI.
DR GO; GO:0098686; C:hippocampal mossy fiber to CA3 synapse; ISO:MGI.
DR GO; GO:0060077; C:inhibitory synapse; ISO:MGI.
DR GO; GO:0044306; C:neuron projection terminus; IDA:MGI.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:1990257; C:piccolo-bassoon transport vesicle; ISO:MGI.
DR GO; GO:0014069; C:postsynaptic density; IDA:MGI.
DR GO; GO:0098793; C:presynapse; IDA:MGI.
DR GO; GO:0048786; C:presynaptic active zone; IDA:MGI.
DR GO; GO:0098831; C:presynaptic active zone cytoplasmic component; IDA:SynGO.
DR GO; GO:0097470; C:ribbon synapse; ISO:MGI.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IDA:SynGO.
DR GO; GO:0045202; C:synapse; IDA:MGI.
DR GO; GO:0097060; C:synaptic membrane; ISO:MGI.
DR GO; GO:0008021; C:synaptic vesicle; ISS:UniProtKB.
DR GO; GO:0030672; C:synaptic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005802; C:trans-Golgi network; ISO:MGI.
DR GO; GO:0045503; F:dynein light chain binding; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0098882; F:structural constituent of presynaptic active zone; IDA:SynGO.
DR GO; GO:0001222; F:transcription corepressor binding; ISO:MGI.
DR GO; GO:0008088; P:axo-dendritic transport; ISO:MGI.
DR GO; GO:0099526; P:presynapse to nucleus signaling pathway; IMP:SynGO.
DR GO; GO:1904071; P:presynaptic active zone assembly; ISO:MGI.
DR GO; GO:0035418; P:protein localization to synapse; IGI:ParkinsonsUK-UCL.
DR GO; GO:0098693; P:regulation of synaptic vesicle cycle; IDA:SynGO.
DR GO; GO:1904666; P:regulation of ubiquitin protein ligase activity; ISO:MGI.
DR GO; GO:0008090; P:retrograde axonal transport; ISO:MGI.
DR GO; GO:0050808; P:synapse organization; ISO:MGI.
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 Alternative splicing; Cell projection; Coiled coil; Cytoplasm;
KW Cytoplasmic vesicle; Cytoskeleton; Glycoprotein; Lipoprotein; Membrane;
KW Metal-binding; Methylation; Myristate; Phosphoprotein; Reference proteome;
KW Repeat; Synapse; Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:O88778"
FT CHAIN 2..3942
FT /note="Protein bassoon"
FT /id="PRO_0000065003"
FT REPEAT 570..576
FT /note="1"
FT REPEAT 577..583
FT /note="2"
FT REPEAT 584..590
FT /note="3"
FT REPEAT 591..597
FT /note="4"
FT REPEAT 598..604
FT /note="5"
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 464..487
FT /note="C4-type"
FT /evidence="ECO:0000255"
FT ZN_FING 492..514
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..71
FT /note="5 X 2 AA tandem repeats of P-G"
FT REGION 228..341
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 362..457
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 525..937
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 570..604
FT /note="5 X 7 AA tandem repeats of K-A-S-P-Q-[AT]-[AT]"
FT REGION 950..1258
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1309..1553
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1573..1625
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1831..1865
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1926..1977
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2327..2378
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2476..2504
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2524..2663
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2854..2874
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3051..3409
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3431..3560
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3581..3917
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 2366..2422
FT /evidence="ECO:0000255"
FT COILED 2453..2483
FT /evidence="ECO:0000255"
FT COMPBIAS 55..75
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 83..99
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 110..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 325..339
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 362..383
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 559..624
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 684..722
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 800..833
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 851..866
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 897..911
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 961..989
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 990..1015
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1016..1034
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1061..1102
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1117..1131
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1166..1190
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1227..1241
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1317..1345
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1367..1439
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1474..1496
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1506..1523
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1531..1553
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1573..1607
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2327..2343
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2363..2378
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2556..2576
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2591..2621
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3073..3096
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3097..3112
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3150..3164
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3174..3188
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3210..3237
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3296..3321
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3450..3466
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3467..3487
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3584..3609
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3620..3648
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3662..3689
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3708..3724
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3734..3828
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3833..3851
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 142
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 145
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 241
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 245
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 881
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 980
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1050
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1051
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1100
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1102
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1108
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16452087,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 1114
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1236
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16452087,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 1482
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1491
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1493
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1792
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 1796
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 1806
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 1806
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 1818
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 1990
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 2046
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 2051
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 2081
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 2255
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 2265
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 2270
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 2578
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16452087,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 2595
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:16452087,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 2622
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:16452087,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 2811
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 2860
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 2866
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 3022
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 3301
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 3382
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16452087,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 3502
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 3823
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000250"
FT CARBOHYD 1354
FT /note="O-linked (GlcNAc) threonine"
FT /evidence="ECO:0000250"
FT CARBOHYD 1395
FT /note="O-linked (GlcNAc) threonine"
FT /evidence="ECO:0000269|PubMed:16452088"
FT CARBOHYD 1707
FT /note="O-linked (GlcNAc) serine"
FT /evidence="ECO:0000269|PubMed:16452088"
FT CARBOHYD 1934
FT /note="O-linked (GlcNAc) threonine"
FT /evidence="ECO:0000269|PubMed:16452088"
FT CARBOHYD 2318
FT /note="O-linked (GlcNAc) threonine"
FT /evidence="ECO:0000269|PubMed:16452088"
FT CARBOHYD 2524
FT /note="O-linked (GlcNAc) threonine"
FT /evidence="ECO:0000269|PubMed:16452088"
FT CARBOHYD 2700
FT /note="O-linked (GlcNAc) threonine"
FT /evidence="ECO:0000269|PubMed:16452088"
FT CARBOHYD 2945
FT /note="O-linked (GlcNAc) threonine"
FT /evidence="ECO:0000269|PubMed:16452088"
FT VAR_SEQ 2831..2889
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14621295"
FT /id="VSP_011375"
FT CONFLICT 381
FT /note="Q -> P (in Ref. 1; CAA76598)"
FT /evidence="ECO:0000305"
FT CONFLICT 418
FT /note="M -> T (in Ref. 1; CAA76598)"
FT /evidence="ECO:0000305"
FT CONFLICT 462
FT /note="S -> A (in Ref. 1; CAA76598)"
FT /evidence="ECO:0000305"
FT CONFLICT 473
FT /note="M -> V (in Ref. 1; CAA76598)"
FT /evidence="ECO:0000305"
FT CONFLICT 624..626
FT /note="VTS -> ATP (in Ref. 1; CAA76598)"
FT /evidence="ECO:0000305"
FT CONFLICT 783
FT /note="T -> M (in Ref. 1; CAA76598)"
FT /evidence="ECO:0000305"
FT CONFLICT 2292
FT /note="A -> T (in Ref. 1; CAA76598)"
FT /evidence="ECO:0000305"
FT CONFLICT 2349
FT /note="V -> A (in Ref. 1; CAA76598)"
FT /evidence="ECO:0000305"
FT CONFLICT 2892
FT /note="A -> V (in Ref. 1; CAA76598)"
FT /evidence="ECO:0000305"
FT CONFLICT 3902
FT /note="S -> G (in Ref. 1; CAA76598)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 3942 AA; 418843 MW; E8BEE60189570857 CRC64;
MGNEASLEGG AGEGPLPPGG SGLGPGPGAG KPPSALAGGG QLPVAGAARA AGPPTPGLGP
VPGPGPGPGP GSVPRRLDPK EPLGSQRTTS PTPKQASATA PGRESPRETR AQGPSGQEAE
SPRRTLQVDS RTQRSGRSPS VSPDRGSTPT SPYSVPQIAP LPSSTLCPIC KTSDLTSTPS
QPNFNTCTQC HNKVCNQCGF NPNPHLTQVK EWLCLNCQMQ RALGMDMTTA PRSKSQQQLH
SPALSPAHSP AKQPLGKPEQ ERSPRGPGAT QSGPRQAEAA RATSVPGPTQ ATAPPEVGRV
SPQPPLSTKP STAEPRPPAG EAQGKSATTV PSGLGAGEQT QEGLTGKLFG LGASLLTQAS
TLMSVQPEAD TQGQPSPSKG QPKIVFSDAS KEAGPRPPGS GPGPGPTPGA KTEPGARMGP
GSGPGALAKT GGTASPKHGR AEHQAASKAA AKPKTMPKER ASACPLCQAE LNMGSRGPAN
YNTCTACKLQ VCNLCGFNPT PHLVEKTEWL CLNCQTKRLL EGSLGEPAPL PLPTPQQPPA
GVPHRAAGAA PLKQKGPQGL GQPSGSLPAK ASPQATKASP QATKASPQAT KASPQTTKAS
PQAKPLRATE PSKTSSSAQE KKTVTSAKAE PVPKPPPETT VPPGTPKAKS GVKRTDPATP
VVKPVPEAPK GGEAEEPVPK PYSQDLSRSP QSLSDTGYSS DGVSSSQSEI TGVVQQEVEQ
LDSAGVTGPR PPSPSELHKV GSSLRPSLEA QAVAPSAEWS KPPRSSSSAV EDQKRRPHSL
SITPEAFDSD EELGDILEED DSLAWGRQRE QQDTAESSDD FGSQLRHDYV EDSSEGGLSP
LPPQPPARAD MTDEEFMRRQ ILEMSAEEDN LEEDDTAVSG RGLAKHSAQK ASARPRPESS
QEPKRRLPHN ATTGYEELLS EAGPAEPTDS SGALQGGLRR FKTIELNSTG SYGHELDLGQ
GPDPNLDREP ELEMESLTGS PEDRSRGEHS STLPASTPSY TSGTSPTSLS SLEEDSDSSP
SRRQRLEEAK QQRKARHRSH GPLLPTIEDS SEEEELREEE ELLREQEKMR EVEQQRIRST
ARKTRRDKEE LRAQRRRERS KTPPSNLSPI EDASPTEELR QAAEMEELHR SSCSEYSPSP
SLDSEAETLD GGPTRLYKSG SEYNLPAFMS LYSPTETPSG SSTTPSSGRP LKSAEEAYED
MMRKAEMLQR QQGQVAGARG PHGGPSQPTG PRSQGSFEYQ DTQDHDYGGR ASQPVAESTP
AGLGAAVYEE ILQTSQSIAR MRQASSRDLG FTEDKKKEKQ FLNAESAYMD PMKQNGGPLT
PGTSPTQLAA PVSFSTSTSS DSSGGRVIPD VRVTQHFAKE PQDPLKLHSS PVSSTLTSKE
VGMTFSQGPG SPATTASPTR GYMTPTSPAG SERSPSTSST IHSYGQPPTT ANYGSQTEEL
PHAPSGPPGS GRAPREKPLS GGDSEVGAPQ PSRGYSYFTG SSPPLSPSTP SESPTFSPGK
LGPRATAEFS TQTPSLTLSS DIPRSPGPPS PMVAQGTQTP HRPSTPRLVW QQSSQEAPIM
VITLASDASS QTRMVHASAS TSPLCSPTDS QPTSHSYSQT TPPSASQMPS EPAGPPGFPR
APSAGTDGPL ALYGWGALPA ENISLCRISS VPGTSRVEPG PRPPGTAVVD LRTAVKPTPI
ILTDQGMDLT SLAVEARKYG LALDPVSGRQ STAVQPLVIN LNAQEQTHTF LATATTVSIT
MASSVLMAQQ KQPVVYGDPF QSRLDFGQGS GSPVCLAQVK QVEQAVQTAP YRGGPRGRPR
EAKFARYNLP NQVTPLARRD ILITQMGTAQ GVGLKPGPVP EPGAEPHRAT PAELRSHAPP
GTRKPHTVVV QMGEGTAGTV TTLLPEEPAG ALDLTGMRPE SQLACCDMVY KFPFGSSCTG
TFHPAPSAPD KSVTDTALPG QSSGPFYSPR DPEPPEPLTF RTQGVVGPGP HEEQRPYPQG
LPGRLYSSMS DTNLAEAGLN YHAQRLGQLF QGPGRDSAVD LSSLKHSYSL GFADGRYLGQ
GLQYGSFTDL RHPTDLLSHP LPLRRYSSVS NIYSDHRYGP RGDAVGFQEA SLAQYSATTA
REISRMCAAL NSMDQYGGRH GSGSGGPDLV QYQPQHGPGL SAPQGLAPLR SGLLGNPTYP
EGQPSPGNLA QYGPAASQAT AVRQLLPSTA TVRAADGMIY STINTPIAAT LPITTQPASV
LRPMVRGGMY RPYVSGGVTA VPLTSLTRVP MIAPRVPLGP AGLYRYPAPR FPIASSVPPA
EGPVYLGKPA AAKASGAGGP PRPELPAGVA REEPFSTTAP AVIKEAPVAP APGPAPAPPP
GQKPAGEAVA GSGSGVLSRP ASEKEEASQE DRQRKQQEQL LQLERERVEL EKLRQLRLQE
ELERERVELQ RHREEEQLLV QRELQELQTI KQHVLQQQQE ERQAQFALQR EQLAQQRLQL
EQIQQLQQQL QLQLEEQKQR QKAPFPATCE APSRGPPPAA TELAQNGQYW PPLTHAAFIA
VAGTEGPGQP REPVLHRGLP SSASDMSLQT EEQWEAGRSG IKKRHSMPRL RDACEPESGP
DPSTVRRIAD SSVQTDDEEG EGRYLVTRRR RTRRSADCSV QTDDEDNADW EQPVRRRRSR
LSRHSDSGSD SKHDATASSS TTAAATARAM SSVGIQTISD CSVQTEPEQL PRVSPAIHIT
AATDPKVEIV RYISAPEKTG RGESLACQTE PDGQAQGVAG PQLIGPTAIS PYLPGIQIVT
PGALGRFEKK KPDPLEIGYQ AHLPPESLSQ LVSRQPPKSP QVLYSPVSPL SPHRLLDTSF
ASSERLNKAH VSPQKQFIAD STLRQQTLPR PMKTLQRSLS DPKPLSPTAE ESAKERFSLY
QHQGGLGSQV SALPPNGLVR KVKRTLPSPP PEEAHLPLAG QVPSQLYAAS LLQRGLAGPT
TVPATKASLL RELDRDLRLV EHESTKLRKK QAELDEEEKE IDAKLKYLEL GITQRKESLA
KDRGGRDYPP LRGLGEHRDY LSDSELNQLR LQGCTTPAGQ YVDYPASAAV PATPSGPTAF
QQPRFPPAAP QYTAGSSGPT QNGFPAHQAP TYTGPSTYPA PTYPPGTGYP AEPGLPSQPA
FHPTGHYAAP TPMPTTQSAP FPVQADSRAA HQKPRQTSLA DLEQKVPTNY EVIGSPAVTM
SSAPPETGYS GPAVSGSYEQ GKAPEHPRGS DRSSVSQSPA PTYPSDSHYT SLEQNVPRNY
VMIDDISELT KDSTPTASES QRLEPLGPGG VSGRPGKDPG EPAVLEGPTL PCCYGRGEEE
SEEDSYDPRG KSGHHRSMES NGRPSTHYYG DSDYRHGARA DKYGPGPMGP KHPSKSLAPA
AISSKRSKHR KQGMEQKISK FSPIEEAKDV ESDLASYPPP TVSSSLTSRG RKFQDEITYG
LKKNVYEQQR YYGVSSRDAA EEDERMYGSS SRSRMASAYS GEKLSSHDYS SRGKGYERER
DTAERLQKAG SKPSSLSMAH GRARPPMRSQ ASEEESPVSP LGRPRPAGGA LPPGDTCPQF
CSSHSMPDVQ EHVKDGPRAH AYKREEGYML DDSHCVVSDS EAYHLGQEET DWFDKPRDAR
SDRFRHHGGH TVSSSQKRGP ARHSYHDYDE PPEEGLWPHD EGGPGRHTSA KEHRHHSDHG
RHSGRHAGEE PGRRAAKPHA RDMGRHEARP HPQASPAPAM QKKGQPGYPS SADYSQSSRA
PSAYHHASES KKGSRQAHTG PSALQPKADT QAQPQMQGRQ AAPGPQQSQP PSSRQTPSGT
ASRQPQTQQQ QQQQQQQQGL GQQAPQQAPS QARLQPQSQP TTRGTAPAAS QPAGKPQPGP
TTAPGPQPAG PPRAEQASSS KPPAAKAPQQ GRAPQAQTTP GPGPAGAKPG ARPGGTPGAP
ASQPGAEGES VFSKILPGGA AEQAGKLTEA VSAFGKKFSS FW
