DISC1_MOUSE
ID DISC1_MOUSE Reviewed; 852 AA.
AC Q811T9; Q7TQ21; Q8CF87; Q8CF88; Q8CHP1; Q8CHP2;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2006, sequence version 2.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Disrupted in schizophrenia 1 homolog {ECO:0000305};
GN Name=Disc1 {ECO:0000312|MGI:MGI:2447658};
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 [MRNA] (ISOFORMS 1 AND 3), AND TISSUE SPECIFICITY.
RC STRAIN=BALB/cJ;
RX PubMed=12504857; DOI=10.1006/geno.2002.7012;
RA Ma L., Liu Y., Ky B., Shughrue P.J., Austin C.P., Morris J.A.;
RT "Cloning and characterization of Disc1, the mouse ortholog of DISC1
RT (Disrupted-in-Schizophrenia 1).";
RL Genomics 80:662-672(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), AND NUCLEOTIDE SEQUENCE [MRNA] OF
RP 1-594 (ISOFORM 1).
RC STRAIN=C57BL/6J;
RX PubMed=12573262; DOI=10.1016/s0888-7543(02)00026-5;
RA Taylor M.S., Devon R.S., Millar J.K., Porteous D.J.;
RT "Evolutionary constraints on the Disrupted in Schizophrenia locus.";
RL Genomics 81:67-77(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J;
RX PubMed=12506198; DOI=10.1073/pnas.0136913100;
RA Ozeki Y., Tomoda T., Kleiderlein J., Kamiya A., Bord L., Fujii K.,
RA Okawa M., Yamada N., Hatten M.E., Snyder S.H., Ross C.A., Sawa A.;
RT "Disrupted-in-Schizophrenia-1 (DISC-1): mutant truncation prevents binding
RT to NudE-like (NUDEL) and inhibits neurite outgrowth.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:289-294(2003).
RN [4]
RP ERRATUM OF PUBMED:12506198.
RA Ozeki Y., Tomoda T., Kleiderlein J., Kamiya A., Bord L., Fujii K.,
RA Okawa M., Yamada N., Hatten M.E., Snyder S.H., Ross C.A., Sawa A.;
RL Proc. Natl. Acad. Sci. U.S.A. 101:13969-13969(2004).
RN [5]
RP INTERACTION WITH NDEL1, AND SUBCELLULAR LOCATION.
RX PubMed=14962739; DOI=10.1016/j.mcn.2003.09.009;
RA Brandon N.J., Handford E.J., Schurov I., Rain J.-C., Pelling M.,
RA Duran-Jimeniz B., Camargo L.M., Oliver K.R., Beher D., Shearman M.S.,
RA Whiting P.J.;
RT "Disrupted in Schizophrenia 1 and Nudel form a neurodevelopmentally
RT regulated protein complex: implications for schizophrenia and other major
RT neurological disorders.";
RL Mol. Cell. Neurosci. 25:42-55(2004).
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=15797709; DOI=10.1016/j.mcn.2004.11.003;
RA Brandon N.J., Schurov I., Camargo L.M., Handford E.J., Duran-Jimeniz B.,
RA Hunt P., Millar J.K., Porteous D.J., Shearman M.S., Whiting P.J.;
RT "Subcellular targeting of DISC1 is dependent on a domain independent from
RT the Nudel binding site.";
RL Mol. Cell. Neurosci. 28:613-624(2005).
RN [7]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=17825401; DOI=10.1016/j.cell.2007.07.010;
RA Duan X., Chang J.H., Ge S., Faulkner R.L., Kim J.Y., Kitabatake Y.,
RA Liu X.B., Yang C.H., Jordan J.D., Ma D.K., Liu C.Y., Ganesan S.,
RA Cheng H.J., Ming G.L., Lu B., Song H.;
RT "Disrupted-In-Schizophrenia 1 regulates integration of newly generated
RT neurons in the adult brain.";
RL Cell 130:1146-1158(2007).
RN [8]
RP FUNCTION, INTERACTION WITH GSK3B, AND DEVELOPMENTAL STAGE.
RX PubMed=19303846; DOI=10.1016/j.cell.2008.12.044;
RA Mao Y., Ge X., Frank C.L., Madison J.M., Koehler A.N., Doud M.K., Tassa C.,
RA Berry E.M., Soda T., Singh K.K., Biechele T., Petryshen T.L., Moon R.T.,
RA Haggarty S.J., Tsai L.H.;
RT "Disrupted in schizophrenia 1 regulates neuronal progenitor proliferation
RT via modulation of GSK3beta/beta-catenin signaling.";
RL Cell 136:1017-1031(2009).
RN [9]
RP FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=19502360; DOI=10.1093/hmg/ddp266;
RA Meyer K.D., Morris J.A.;
RT "Disc1 regulates granule cell migration in the developing hippocampus.";
RL Hum. Mol. Genet. 18:3286-3297(2009).
RN [10]
RP FUNCTION, AND INTERACTION WITH CCDC88A.
RX PubMed=19778506; DOI=10.1016/j.neuron.2009.08.008;
RA Kim J.Y., Duan X., Liu C.Y., Jang M.H., Guo J.U., Pow-anpongkul N.,
RA Kang E., Song H., Ming G.L.;
RT "DISC1 regulates new neuron development in the adult brain via modulation
RT of AKT-mTOR signaling through KIAA1212.";
RL Neuron 63:761-773(2009).
RN [11]
RP INTERACTION WITH CCDC141.
RX PubMed=20956536; DOI=10.1074/jbc.m110.179481;
RA Fukuda T., Sugita S., Inatome R., Yanagi S.;
RT "CAMDI, a novel disrupted in schizophrenia 1 (DISC1)-binding protein, is
RT required for radial migration.";
RL J. Biol. Chem. 285:40554-40561(2010).
RN [12]
RP SUBCELLULAR LOCATION.
RX PubMed=22072671; DOI=10.1523/jneurosci.5877-10.2011;
RA Carlisle H.J., Luong T.N., Medina-Marino A., Schenker L., Khorosheva E.,
RA Indersmitten T., Gunapala K.M., Steele A.D., O'Dell T.J., Patterson P.H.,
RA Kennedy M.B.;
RT "Deletion of densin-180 results in abnormal behaviors associated with
RT mental illness and reduces mGluR5 and DISC1 in the postsynaptic density
RT fraction.";
RL J. Neurosci. 31:16194-16207(2011).
RN [13] {ECO:0007744|PDB:6IRR}
RP STRUCTURE BY NMR OF 314-349 IN COMPLEX WITH ATF4, FUNCTION, INTERACTION
RP WITH ATF4, AND MUTAGENESIS OF LEU-822.
RX PubMed=31444471; DOI=10.1038/s41380-019-0485-2;
RA Wang X., Ye F., Wen Z., Guo Z., Yu C., Huang W.K., Rojas Ringeling F.,
RA Su Y., Zheng W., Zhou G., Christian K.M., Song H., Zhang M., Ming G.L.;
RT "Structural interaction between DISC1 and ATF4 underlying transcriptional
RT and synaptic dysregulation in an iPSC model of mental disorders.";
RL Mol. Psychiatry 26:1346-1360(2021).
CC -!- FUNCTION: Involved in the regulation of multiple aspects of embryonic
CC and adult neurogenesis (PubMed:17825401, PubMed:19502360,
CC PubMed:31444471). Required for neural progenitor proliferation in the
CC ventrical/subventrical zone during embryonic brain development and in
CC the adult dentate gyrus of the hippocampus (PubMed:17825401,
CC PubMed:19502360). Participates in the Wnt-mediated neural progenitor
CC proliferation as a positive regulator by modulating GSK3B activity and
CC CTNNB1 abundance (PubMed:19303846). Plays a role as a modulator of the
CC AKT-mTOR signaling pathway controlling the tempo of the process of
CC newborn neurons integration during adult neurogenesis, including neuron
CC positioning, dendritic development and synapse formation
CC (PubMed:19778506). Inhibits the activation of AKT-mTOR signaling upon
CC interaction with CCDC88A (PubMed:19778506). Regulates the migration of
CC early-born granule cell precursors toward the dentate gyrus during the
CC hippocampal development (PubMed:19502360). Inhibits ATF4 transcription
CC factor activity in neurons by disrupting ATF4 dimerization and DNA-
CC binding (PubMed:31444471). Plays a role, together with PCNT, in the
CC microtubule network formation (By similarity).
CC {ECO:0000250|UniProtKB:Q9NRI5, ECO:0000269|PubMed:17825401,
CC ECO:0000269|PubMed:19303846, ECO:0000269|PubMed:19502360,
CC ECO:0000269|PubMed:19778506, ECO:0000269|PubMed:31444471}.
CC -!- SUBUNIT: Interacts with NDEL1 (PubMed:14962739). Interacts with CCDC88A
CC (via C-terminus); the interaction is direct (PubMed:19778506).
CC Interacts with GSK3B (PubMed:19303846). Interacts with tubulin alpha,
CC ACTN2, ANKHD1, ATF4, ATF5, CEP63, EIF3S3, MAP1A, NDEL1, PAFAH1B1,
CC RANBP9, SPTBN4, SYNE1 and TRAF3IP1 (By similarity). Interaction with
CC microtubules may be mediated in part by TRAF3IP1. Interacts (via C-
CC terminal) with PCNT (By similarity). Interacts with CHCHD6 (By
CC similarity). Interacts with CCDC141 (PubMed:20956536). Interacts with
CC FBXW7, the substrate-recognition component of a SCF (SKP1-CUL1-F-box
CC protein) E3 ubiquitin-protein ligase complex; the interaction targets
CC DISC1 for proteasomal degradation (By similarity). Interacts with
CC ZNF365 (By similarity). Interacts with ATF4; inhibiting ATF4
CC transcription factor activity by disrupting ATF4 dimerization and DNA-
CC binding (PubMed:31444471). Interacts with PDE4B (By similarity).
CC {ECO:0000250|UniProtKB:Q9NRI5, ECO:0000269|PubMed:14962739,
CC ECO:0000269|PubMed:19303846, ECO:0000269|PubMed:19778506,
CC ECO:0000269|PubMed:20956536, ECO:0000269|PubMed:31444471}.
CC -!- INTERACTION:
CC Q811T9; Q811T9: Disc1; NbExp=2; IntAct=EBI-2298259, EBI-2298259;
CC Q811T9; Q91VR7: Map1lc3a; NbExp=2; IntAct=EBI-2298259, EBI-2933755;
CC Q811T9; P49841: GSK3B; Xeno; NbExp=4; IntAct=EBI-2298259, EBI-373586;
CC Q811T9-1; O75962-4: TRIO; Xeno; NbExp=2; IntAct=EBI-15881527, EBI-15915736;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14962739}.
CC Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q9NRI5}. Mitochondrion
CC {ECO:0000250|UniProtKB:Q9NRI5}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome {ECO:0000250|UniProtKB:Q9NRI5}.
CC Postsynaptic density {ECO:0000269|PubMed:22072671}. Note=Colocalizes
CC with NDEL1 in the perinuclear region and the centrosome
CC (PubMed:14962739). Localizes to punctate cytoplasmic foci which overlap
CC in part with mitochondria. Colocalizes with PCNT at the centrosome (By
CC similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q9NRI5,
CC ECO:0000269|PubMed:14962739}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q811T9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q811T9-2; Sequence=VSP_019318;
CC Name=3;
CC IsoId=Q811T9-3; Sequence=VSP_019321;
CC Name=4; Synonyms=ES;
CC IsoId=Q811T9-4; Sequence=VSP_019319, VSP_019320;
CC -!- TISSUE SPECIFICITY: Expressed in granule cell precursors within the
CC dentate migratory stream during the first week of postnatal life and in
CC differentiated granule cells of the hippocampus (at protein level).
CC Detected in heart, brain, kidney, and testis (PubMed:12504857).
CC Expressed in dentate gyrus, hippocampus and in the olfactory bulb.
CC {ECO:0000269|PubMed:12504857, ECO:0000269|PubMed:17825401,
CC ECO:0000269|PubMed:19502360}.
CC -!- DEVELOPMENTAL STAGE: Expressed in neuronal progenitors residing in the
CC ventricular and subventriculare zones and in postmitotic neurons in the
CC cortical plate of the cerebral cortex at 15 dpc. Expressed in granule
CC cell precursors within the dentate migratory stream of the hippocampus
CC at 19 dpc (at protein level). {ECO:0000269|PubMed:19303846,
CC ECO:0000269|PubMed:19502360}.
CC -!- PTM: Ubiquitinated. Ubiquitination with 'Lys-48'-linked polyubiquitin
CC chains leads to its proteasomal degradation.
CC {ECO:0000250|UniProtKB:Q9NRI5}.
CC -!- DISRUPTION PHENOTYPE: Loss of function of DISC1 in the dentate gyrus of
CC adult mice results in reduced neural progenitor cell proliferation and
CC the appearance of schizophrenic and depressive-like behaviors.
CC {ECO:0000269|PubMed:19502360}.
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DR EMBL; AF513723; AAN77091.1; -; mRNA.
DR EMBL; AF513724; AAN77092.1; -; mRNA.
DR EMBL; AJ506179; CAD44629.1; -; mRNA.
DR EMBL; AJ506180; CAD44630.1; -; mRNA.
DR EMBL; AY177673; AAO19641.1; -; mRNA.
DR EMBL; AY320287; AAP83943.1; -; mRNA.
DR CCDS; CCDS40517.1; -. [Q811T9-3]
DR CCDS; CCDS52707.1; -. [Q811T9-1]
DR RefSeq; NP_777278.2; NM_174853.2. [Q811T9-3]
DR RefSeq; NP_777279.2; NM_174854.2. [Q811T9-1]
DR RefSeq; XP_011246690.1; XM_011248388.2. [Q811T9-1]
DR PDB; 5YI4; NMR; -; A=765-852.
DR PDB; 6IRR; NMR; -; A=765-852.
DR PDBsum; 5YI4; -.
DR PDBsum; 6IRR; -.
DR AlphaFoldDB; Q811T9; -.
DR SMR; Q811T9; -.
DR BioGRID; 232675; 16.
DR CORUM; Q811T9; -.
DR DIP; DIP-54914N; -.
DR IntAct; Q811T9; 11.
DR MINT; Q811T9; -.
DR STRING; 10090.ENSMUSP00000112410; -.
DR iPTMnet; Q811T9; -.
DR PhosphoSitePlus; Q811T9; -.
DR MaxQB; Q811T9; -.
DR PaxDb; Q811T9; -.
DR PRIDE; Q811T9; -.
DR ProteomicsDB; 279693; -. [Q811T9-1]
DR ProteomicsDB; 279694; -. [Q811T9-2]
DR ProteomicsDB; 279695; -. [Q811T9-3]
DR ProteomicsDB; 279696; -. [Q811T9-4]
DR Antibodypedia; 34687; 653 antibodies from 39 providers.
DR DNASU; 244667; -.
DR Ensembl; ENSMUST00000075730; ENSMUSP00000075145; ENSMUSG00000043051. [Q811T9-3]
DR Ensembl; ENSMUST00000098311; ENSMUSP00000095914; ENSMUSG00000043051. [Q811T9-1]
DR Ensembl; ENSMUST00000117658; ENSMUSP00000112757; ENSMUSG00000043051. [Q811T9-3]
DR Ensembl; ENSMUST00000118942; ENSMUSP00000112410; ENSMUSG00000043051. [Q811T9-1]
DR Ensembl; ENSMUST00000121953; ENSMUSP00000112929; ENSMUSG00000043051. [Q811T9-2]
DR Ensembl; ENSMUST00000122389; ENSMUSP00000112593; ENSMUSG00000043051. [Q811T9-4]
DR GeneID; 244667; -.
DR KEGG; mmu:244667; -.
DR UCSC; uc009nyb.1; mouse. [Q811T9-4]
DR UCSC; uc009nyc.1; mouse. [Q811T9-1]
DR UCSC; uc009nyd.1; mouse. [Q811T9-3]
DR UCSC; uc012gnb.1; mouse. [Q811T9-2]
DR CTD; 27185; -.
DR MGI; MGI:2447658; Disc1.
DR VEuPathDB; HostDB:ENSMUSG00000043051; -.
DR eggNOG; ENOG502S3S3; Eukaryota.
DR GeneTree; ENSGT00390000006176; -.
DR HOGENOM; CLU_016380_1_0_1; -.
DR InParanoid; Q811T9; -.
DR OrthoDB; 254709at2759; -.
DR PhylomeDB; Q811T9; -.
DR TreeFam; TF332357; -.
DR BioGRID-ORCS; 244667; 3 hits in 72 CRISPR screens.
DR ChiTaRS; Disc1; mouse.
DR PRO; PR:Q811T9; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q811T9; protein.
DR Bgee; ENSMUSG00000043051; Expressed in CA2 field of hippocampus and 60 other tissues.
DR ExpressionAtlas; Q811T9; baseline and differential.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030424; C:axon; ISO:MGI.
DR GO; GO:0044297; C:cell body; ISO:MGI.
DR GO; GO:0090724; C:central region of growth cone; ISO:MGI.
DR GO; GO:0005813; C:centrosome; IDA:MGI.
DR GO; GO:0036064; C:ciliary basal body; IDA:MGI.
DR GO; GO:0097546; C:ciliary base; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0030286; C:dynein complex; ISO:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0045111; C:intermediate filament cytoskeleton; ISO:MGI.
DR GO; GO:0005871; C:kinesin complex; ISO:MGI.
DR GO; GO:0005874; C:microtubule; ISO:MGI.
DR GO; GO:0005739; C:mitochondrion; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0014069; C:postsynaptic density; IDA:MGI.
DR GO; GO:0008021; C:synaptic vesicle; IDA:MGI.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0019894; F:kinesin binding; ISO:MGI.
DR GO; GO:0060090; F:molecular adaptor activity; IDA:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0060070; P:canonical Wnt signaling pathway; IMP:DFLAT.
DR GO; GO:0021846; P:cell proliferation in forebrain; IMP:DFLAT.
DR GO; GO:0021799; P:cerebral cortex radially oriented cell migration; IMP:DFLAT.
DR GO; GO:0060271; P:cilium assembly; ISO:MGI.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; ISO:MGI.
DR GO; GO:0051560; P:mitochondrial calcium ion homeostasis; IMP:MGI.
DR GO; GO:0032091; P:negative regulation of protein binding; IDA:ARUK-UCL.
DR GO; GO:0007399; P:nervous system development; ISO:MGI.
DR GO; GO:0070050; P:neuron cellular homeostasis; IMP:MGI.
DR GO; GO:0001764; P:neuron migration; IMP:UniProtKB.
DR GO; GO:1905515; P:non-motile cilium assembly; IMP:MGI.
DR GO; GO:0045773; P:positive regulation of axon extension; ISO:MGI.
DR GO; GO:0001954; P:positive regulation of cell-matrix adhesion; ISO:MGI.
DR GO; GO:0002052; P:positive regulation of neuroblast proliferation; IMP:UniProtKB.
DR GO; GO:0010976; P:positive regulation of neuron projection development; ISO:MGI.
DR GO; GO:2000060; P:positive regulation of ubiquitin-dependent protein catabolic process; IMP:MGI.
DR GO; GO:0030177; P:positive regulation of Wnt signaling pathway; IMP:UniProtKB.
DR GO; GO:0008104; P:protein localization; IDA:MGI.
DR GO; GO:0071539; P:protein localization to centrosome; ISO:MGI.
DR GO; GO:0021852; P:pyramidal neuron migration to cerebral cortex; ISO:MGI.
DR GO; GO:0060998; P:regulation of dendritic spine development; ISO:MGI.
DR GO; GO:0010975; P:regulation of neuron projection development; IMP:UniProtKB.
DR GO; GO:0090128; P:regulation of synapse maturation; IMP:UniProtKB.
DR GO; GO:0051966; P:regulation of synaptic transmission, glutamatergic; ISO:MGI.
DR GO; GO:0051602; P:response to electrical stimulus; IEA:Ensembl.
DR GO; GO:0031929; P:TOR signaling; IMP:UniProtKB.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IMP:MGI.
DR InterPro; IPR026081; DISC1.
DR PANTHER; PTHR14332; PTHR14332; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Coiled coil; Cytoplasm; Cytoskeleton;
KW Developmental protein; Microtubule; Mitochondrion; Neurogenesis;
KW Reference proteome; Synapse; Ubl conjugation; Wnt signaling pathway.
FT CHAIN 1..852
FT /note="Disrupted in schizophrenia 1 homolog"
FT /id="PRO_0000240230"
FT REGION 1..294
FT /note="Interaction with MAP1A"
FT /evidence="ECO:0000250"
FT REGION 1..86
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 236..264
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 280..320
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 295..693
FT /note="Interaction with TRAF3IP1"
FT /evidence="ECO:0000250"
FT REGION 437..594
FT /note="Required for localization to punctate cytoplasmic
FT foci"
FT /evidence="ECO:0000250"
FT REGION 443..852
FT /note="Necessary and sufficient for interaction with PCNT
FT and localization at the centrosome"
FT /evidence="ECO:0000250"
FT REGION 595..852
FT /note="Interaction with ATF4 and ATF5"
FT /evidence="ECO:0000250"
FT REGION 706..746
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 728..852
FT /note="Interaction with NDEL1 and PAFAH1B1"
FT /evidence="ECO:0000250"
FT REGION 728..852
FT /note="Interaction with PAFAH1B1"
FT /evidence="ECO:0000250"
FT REGION 802..835
FT /note="Interaction with NDEL1"
FT /evidence="ECO:0000250"
FT REGION 833..852
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 367..397
FT /evidence="ECO:0000255"
FT COILED 449..496
FT /evidence="ECO:0000255"
FT COMPBIAS 64..82
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 280..312
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..18
FT /note="MQGGGPRGAPIHSPSHGA -> MEAENSSWLTLPCLLY (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:12506198"
FT /id="VSP_019318"
FT VAR_SEQ 374..387
FT /note="AETLRQRLEELEQE -> GESKAVRRQFHLSP (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:12573262"
FT /id="VSP_019319"
FT VAR_SEQ 388..852
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:12573262"
FT /id="VSP_019320"
FT VAR_SEQ 595..658
FT /note="GSCFSTAKELTEEIWALSSEREGLEMFLGRLLALSSRNSRRLGIVKEDHLRC
FT RQDLALQDAAHK -> E (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:12504857"
FT /id="VSP_019321"
FT MUTAGEN 822
FT /note="L->Q: Abolished interaction with ATF4."
FT /evidence="ECO:0000269|PubMed:31444471"
FT CONFLICT 8
FT /note="G -> D (in Ref. 1; AAN77091/AAN77092)"
FT /evidence="ECO:0000305"
FT CONFLICT 120
FT /note="S -> F (in Ref. 3; AAO19641/AAP83943)"
FT /evidence="ECO:0000305"
FT CONFLICT 129
FT /note="A -> G (in Ref. 1; AAN77091/AAN77092)"
FT /evidence="ECO:0000305"
FT CONFLICT 141
FT /note="R -> K (in Ref. 1; AAN77091/AAN77092)"
FT /evidence="ECO:0000305"
FT CONFLICT 153
FT /note="F -> C (in Ref. 1; AAN77091/AAN77092)"
FT /evidence="ECO:0000305"
FT CONFLICT 176
FT /note="K -> T (in Ref. 1; AAN77091/AAN77092)"
FT /evidence="ECO:0000305"
FT CONFLICT 190
FT /note="P -> S (in Ref. 1; AAN77091/AAN77092)"
FT /evidence="ECO:0000305"
FT CONFLICT 199
FT /note="A -> P (in Ref. 1; AAN77091/AAN77092)"
FT /evidence="ECO:0000305"
FT CONFLICT 289
FT /note="S -> P (in Ref. 1; AAN77091/AAN77092)"
FT /evidence="ECO:0000305"
FT CONFLICT 295
FT /note="Missing (in Ref. 1; AAN77091/AAN77092)"
FT /evidence="ECO:0000305"
FT CONFLICT 302
FT /note="G -> V (in Ref. 1; AAN77091/AAN77092)"
FT /evidence="ECO:0000305"
FT CONFLICT 365
FT /note="V -> A (in Ref. 1; AAN77091/AAN77092)"
FT /evidence="ECO:0000305"
FT CONFLICT 390
FT /note="R -> H (in Ref. 1; AAN77091/AAN77092)"
FT /evidence="ECO:0000305"
FT CONFLICT 441
FT /note="A -> T (in Ref. 2; CAD44629)"
FT /evidence="ECO:0000305"
FT CONFLICT 461
FT /note="R -> Q (in Ref. 1; AAN77091/AAN77092)"
FT /evidence="ECO:0000305"
FT CONFLICT 474
FT /note="S -> Y (in Ref. 2; CAD44629)"
FT /evidence="ECO:0000305"
FT CONFLICT 533
FT /note="Q -> H (in Ref. 1; AAN77091/AAN77092)"
FT /evidence="ECO:0000305"
FT CONFLICT 639
FT /note="V -> L (in Ref. 1; AAN77091)"
FT /evidence="ECO:0000305"
FT CONFLICT 643
FT /note="H -> Y (in Ref. 1; AAN77091)"
FT /evidence="ECO:0000305"
FT CONFLICT 788
FT /note="K -> R (in Ref. 1; AAN77091/AAN77092)"
FT /evidence="ECO:0000305"
FT STRAND 768..772
FT /evidence="ECO:0007829|PDB:5YI4"
FT HELIX 773..800
FT /evidence="ECO:0007829|PDB:5YI4"
FT TURN 801..803
FT /evidence="ECO:0007829|PDB:5YI4"
FT HELIX 806..829
FT /evidence="ECO:0007829|PDB:5YI4"
FT STRAND 848..852
FT /evidence="ECO:0007829|PDB:5YI4"
SQ SEQUENCE 852 AA; 92525 MW; B55A850B15028E6F CRC64;
MQGGGPRGAP IHSPSHGADS GHGLPPAVAP QRRRLTRRPG YMRSTAGSGI GFLSPAVGMP
HPSSAGLTGQ QSQHSQSKAG QCGLDPGSHC QASLVGKPFL KSSLVPAVAS EGHLHPAQRS
MRKRPVHFAV HSKNDSRQSE RLTGSFKPGD SGFWQELLSS DSFKSLAPSL DAPWNKGSRG
LKTVKPLASP ALNGPADIAS LPGFQDTFTS SFSFIQLSLG AAGERGEAEG CLPSREAEPL
HQRPQEMAAE ASSSDRPHGD PRHLWTFSLH AAPGLADLAQ VTRSSSRQSE CGTVSSSSSD
TGFSSQDASS AGGRGDQGGG WADAHGWHTL LREWEPMLQD YLLSNRRQLE VTSLILKLQK
CQEKVVEDGD YDTAETLRQR LEELEQEKGR LSWALPSQQP ALRSFLGYLA AQIQVALHGA
TQRAGSDDPE APLEGQLRTT AQDSLPASIT RRDWLIREKQ RLQKEIEALQ ARMSALEAKE
KRLSQELEEQ EVLLRWPGCD LMALVAQMSP GQLQEVSKAL GETLTSANQA PFQVEPPETL
RSLRERTKSL NLAVRELTAQ VCSGEKLCSS LRRRLSDLDT RLPALLEAKM LALSGSCFST
AKELTEEIWA LSSEREGLEM FLGRLLALSS RNSRRLGIVK EDHLRCRQDL ALQDAAHKTR
MKANTVKCME VLEGQLSSCR CPLLGRVWKA DLETCQLLMQ SLQLQEAGSS PHAEDEEQVH
STGEAAQTAA LAVPRTPHPE EEKSPLQVLQ EWDTHSALSP HCAAGPWKED SHIVSAEVGE
KCEAIGVKLL HLEDQLLGAM YSHDEALFQS LQGELQTVKE TLQAMILQLQ PTKEAGEASA
SYPTAGAQET EA
