STAU1_MOUSE
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 03-AUG-2022, entry version 148.
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).
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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; 82.
DR IntAct; Q9Z108; 5.
DR MINT; Q9Z108; -.
DR STRING; 10090.ENSMUSP00000104861; -.
DR iPTMnet; Q9Z108; -.
DR PhosphoSitePlus; Q9Z108; -.
DR EPD; Q9Z108; -.
DR MaxQB; Q9Z108; -.
DR PaxDb; Q9Z108; -.
DR PeptideAtlas; Q9Z108; -.
DR PRIDE; Q9Z108; -.
DR ProteomicsDB; 254581; -.
DR Antibodypedia; 13554; 416 antibodies from 37 providers.
DR DNASU; 20853; -.
DR Ensembl; ENSMUST00000109236; ENSMUSP00000104859; ENSMUSG00000039536.
DR GeneID; 20853; -.
DR KEGG; mmu:20853; -.
DR UCSC; uc008nyv.3; mouse.
DR CTD; 6780; -.
DR MGI; MGI:1338864; Stau1.
DR VEuPathDB; HostDB:ENSMUSG00000039536; -.
DR eggNOG; KOG3732; Eukaryota.
DR GeneTree; ENSGT00940000157304; -.
DR InParanoid; Q9Z108; -.
DR BioGRID-ORCS; 20853; 5 hits in 75 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 259 other tissues.
DR ExpressionAtlas; Q9Z108; baseline and differential.
DR Genevisible; Q9Z108; MM.
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; ISO: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 InterPro; IPR014720; dsRBD_dom.
DR InterPro; IPR044475; STAU1_DSRM_3.
DR InterPro; IPR032478; Staufen_C.
DR Pfam; PF00035; dsrm; 2.
DR Pfam; PF16482; Staufen_C; 1.
DR SMART; SM00358; DSRM; 2.
DR PROSITE; PS50137; DS_RBD; 2.
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
