ID   STAU1_MOUSE             Reviewed;         487 AA.
AC   Q9Z108;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   24-JAN-2024, entry version 156.
DE   RecName: Full=Double-stranded RNA-binding protein Staufen homolog 1;
GN   Name=Stau1; Synonyms=Stau;
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].
RC   TISSUE=Fetus;
RX   PubMed=10022909; DOI=10.1128/mcb.19.3.2220;
RA   Wickham L., Duchaine T., Luo M., Nabi I.R., DesGroseillers L.;
RT   "Mammalian Staufen is a double-stranded-RNA- and tubulin-binding protein
RT   which localizes to the rough endoplasmic reticulum.";
RL   Mol. Cell. Biol. 19:2220-2230(1999).
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Kidney, and Spleen;
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   [3]
RP   METHYLATION [LARGE SCALE ANALYSIS] AT ARG-20 AND ARG-27, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, and Embryo;
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).
CC   -!- FUNCTION: Binds double-stranded RNA (regardless of the sequence) and
CC       tubulin. May play a role in specific positioning of mRNAs at given
CC       sites in the cell by cross-linking cytoskeletal and RNA components, and
CC       in stimulating their translation at the site.
CC   -!- SUBUNIT: Binds tubulin. Identified in a mRNP complex, at least composed
CC       of DHX9, DDX3X, ELAVL1, HNRNPU, IGF2BP1, ILF3, PABPC1, PCBP2, PTBP2,
CC       STAU1, STAU2, SYNCRIP and YBX1. Binds with low affinity single-stranded
CC       RNA or DNA homopolymers. Interacts with CASC3 in an RNA-dependent
CC       manner (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Rough endoplasmic
CC       reticulum. Note=Localizes exclusively with the rough reticulum
CC       endoplasmic (RER).
CC   -!- DOMAIN: One of the DRDB could be involved in RER binding.
CC   -!- DOMAIN: The C-terminal contains the tubulin binding domain (TBD).
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AF061942; AAD17529.1; -; mRNA.
DR   CCDS; CCDS17093.1; -.
DR   RefSeq; NP_035620.1; NM_011490.4.
DR   AlphaFoldDB; Q9Z108; -.
DR   SMR; Q9Z108; -.
DR   BioGRID; 203528; 84.
DR   IntAct; Q9Z108; 5.
DR   MINT; Q9Z108; -.
DR   STRING; 10090.ENSMUSP00000104861; -.
DR   GlyGen; Q9Z108; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q9Z108; -.
DR   PhosphoSitePlus; Q9Z108; -.
DR   EPD; Q9Z108; -.
DR   MaxQB; Q9Z108; -.
DR   PaxDb; 10090-ENSMUSP00000104861; -.
DR   PeptideAtlas; Q9Z108; -.
DR   ProteomicsDB; 254581; -.
DR   Pumba; Q9Z108; -.
DR   Antibodypedia; 13554; 486 antibodies from 37 providers.
DR   DNASU; 20853; -.
DR   Ensembl; ENSMUST00000109236.9; ENSMUSP00000104859.3; ENSMUSG00000039536.17.
DR   GeneID; 20853; -.
DR   KEGG; mmu:20853; -.
DR   UCSC; uc008nyv.3; mouse.
DR   AGR; MGI:1338864; -.
DR   CTD; 6780; -.
DR   MGI; MGI:1338864; Stau1.
DR   VEuPathDB; HostDB:ENSMUSG00000039536; -.
DR   eggNOG; KOG3732; Eukaryota.
DR   GeneTree; ENSGT00940000157304; -.
DR   InParanoid; Q9Z108; -.
DR   OrthoDB; 2882160at2759; -.
DR   BioGRID-ORCS; 20853; 6 hits in 80 CRISPR screens.
DR   ChiTaRS; Stau1; mouse.
DR   PRO; PR:Q9Z108; -.
DR   Proteomes; UP000000589; Chromosome 2.
DR   RNAct; Q9Z108; Protein.
DR   Bgee; ENSMUSG00000039536; Expressed in embryonic post-anal tail and 262 other cell types or tissues.
DR   ExpressionAtlas; Q9Z108; baseline and differential.
DR   GO; GO:0044297; C:cell body; ISO:MGI.
DR   GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR   GO; GO:0036464; C:cytoplasmic ribonucleoprotein granule; ISO:MGI.
DR   GO; GO:0010494; C:cytoplasmic stress granule; IDA:BHF-UCL.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0030425; C:dendrite; ISO:MGI.
DR   GO; GO:0032839; C:dendrite cytoplasm; IEA:GOC.
DR   GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR   GO; GO:0098978; C:glutamatergic synapse; ISO:MGI.
DR   GO; GO:1990124; C:messenger ribonucleoprotein complex; IBA:GO_Central.
DR   GO; GO:0043005; C:neuron projection; IDA:MGI.
DR   GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR   GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR   GO; GO:1990904; C:ribonucleoprotein complex; IDA:MGI.
DR   GO; GO:0005791; C:rough endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR   GO; GO:0003725; F:double-stranded RNA binding; ISO:MGI.
DR   GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR   GO; GO:0008157; F:protein phosphatase 1 binding; ISO:MGI.
DR   GO; GO:0003723; F:RNA binding; IDA:MGI.
DR   GO; GO:0098964; P:anterograde dendritic transport of messenger ribonucleoprotein complex; IBA:GO_Central.
DR   GO; GO:0098963; P:dendritic transport of messenger ribonucleoprotein complex; IDA:SynGO.
DR   GO; GO:0007281; P:germ cell development; IBA:GO_Central.
DR   GO; GO:0008298; P:intracellular mRNA localization; IDA:MGI.
DR   GO; GO:0099010; P:modification of postsynaptic structure; ISO:MGI.
DR   GO; GO:0050804; P:modulation of chemical synaptic transmission; ISO:MGI.
DR   GO; GO:0046726; P:positive regulation by virus of viral protein levels in host cell; ISO:MGI.
DR   GO; GO:1900273; P:positive regulation of long-term synaptic potentiation; ISO:MGI.
DR   GO; GO:0045070; P:positive regulation of viral genome replication; ISO:MGI.
DR   GO; GO:0035418; P:protein localization to synapse; IBA:GO_Central.
DR   CDD; cd19883; DSRM_STAU1_rpt3; 1.
DR   CDD; cd19885; DSRM_STAU1_rpt4; 1.
DR   Gene3D; 3.30.160.20; -; 3.
DR   Gene3D; 6.10.250.1360; -; 1.
DR   InterPro; IPR014720; dsRBD_dom.
DR   InterPro; IPR044475; STAU1_DSRM_3.
DR   InterPro; IPR032478; Staufen_C.
DR   PANTHER; PTHR46054:SF2; DOUBLE-STRANDED RNA-BINDING PROTEIN STAUFEN HOMOLOG 1; 1.
DR   PANTHER; PTHR46054; MATERNAL EFFECT PROTEIN STAUFEN; 1.
DR   Pfam; PF00035; dsrm; 2.
DR   Pfam; PF16482; Staufen_C; 1.
DR   SMART; SM00358; DSRM; 2.
DR   SUPFAM; SSF54768; dsRNA-binding domain-like; 3.
DR   PROSITE; PS50137; DS_RBD; 2.
DR   Genevisible; Q9Z108; MM.
PE   1: Evidence at protein level;
KW   Cytoplasm; Endoplasmic reticulum; Methylation; Reference proteome; Repeat;
KW   RNA-binding.
FT   CHAIN           1..487
FT                   /note="Double-stranded RNA-binding protein Staufen homolog
FT                   1"
FT                   /id="PRO_0000072244"
FT   DOMAIN          96..163
FT                   /note="DRBM 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00266"
FT   DOMAIN          196..264
FT                   /note="DRBM 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00266"
FT   REGION          175..196
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          270..310
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        278..292
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         20
FT                   /note="Asymmetric dimethylarginine"
FT                   /evidence="ECO:0007744|PubMed:24129315"
FT   MOD_RES         27
FT                   /note="Asymmetric dimethylarginine; alternate"
FT                   /evidence="ECO:0007744|PubMed:24129315"
FT   MOD_RES         27
FT                   /note="Omega-N-methylarginine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:O95793"
SQ   SEQUENCE   487 AA;  53925 MW;  840260693DC49180 CRC64;
     MYKPVDPHSR MQSTYSYGMR GGAYPPRYFY PFPVPPLLYQ VELSVGGQQF NGKGKMRPPV
     KHDAPARALR TLQSEPLPER LEVNGREAEE ENLNKSEISQ VFEIALKRNL PVNFEVARES
     GPPHMKNFVT RVSVGEFVGE GEGKSKKISK KNAARAVLEQ LRRLPPLPAV ERVKPRIKKK
     SQPTCKTAPD YGQGMNPISR LAQIQQAKKE KEPEYMLLTE RGLPRRREFV MQVKVGHHTA
     EGVGTNKKVA KRNAAENMLE ILGFKVPQAQ PAKPALKSEE KTPVKKPGDG RKVTFFEPSP
     GDENGTSNKD EEFRMPYLSH QQLPAGILPM VPEVAQAVGV SQGHHTKDFT RAAPNPAKAT
     VTAMIARELL YGGTSPTAET ILKSNISSGH VPHGPRTRPS EQLYYLSRAQ GFQVEYKDFP
     KNNKNECVSL INCSSQPPLV SHGIGKDVES CHDMAALNIL KLLSELDQQS TEMPRTGNGP
     VSACGRC
//