STAU2_RAT
ID STAU2_RAT Reviewed; 571 AA.
AC Q68SB1; Q68SB2; Q68SB3; Q68SB4; Q8R4C9; Q8R4D0;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Double-stranded RNA-binding protein Staufen homolog 2;
DE Short=r-staufen protein;
GN Name=Stau2;
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] (ISOFORMS 1 AND 4), FUNCTION, INTERACTION WITH
RP MICROTUBULES, DOMAIN FOR DENDRITIC TRANSPORT, AND TISSUE SPECIFICITY.
RC STRAIN=Sprague-Dawley;
RX PubMed=11709157; DOI=10.1016/s0896-6273(01)00493-7;
RA Tang S.J., Meulemans D., Vazquez L., Colaco N., Schuman E.;
RT "A role for a rat homolog of staufen in the transport of RNA to neuronal
RT dendrites.";
RL Neuron 32:463-475(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3), SUBCELLULAR LOCATION,
RP DOMAINS NES (ISOFORMS 2 AND 3) AND NUCLEAR LOCALIZATION SIGNAL, AND
RP MUTAGENESIS OF PHE-239.
RX PubMed=15364930; DOI=10.1074/jbc.m407883200;
RA Miki T., Yoneda Y.;
RT "Alternative splicing of Staufen2 creates the nuclear export signal for
RT CRM1 (Exportin 1).";
RL J. Biol. Chem. 279:47473-47479(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3 AND 4).
RC STRAIN=Sprague-Dawley;
RX PubMed=15970630; DOI=10.1385/nmm:6:2-3:127;
RA Monshausen M., Gehring N.H., Kosik K.S.;
RT "The mammalian RNA-binding protein Staufen2 links nuclear and cytoplasmic
RT RNA processing pathways in neurons.";
RL NeuroMolecular Med. 6:127-144(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC TISSUE=Heart;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP INTERACTION WITH RIBOSOMES, AND TISSUE SPECIFICITY.
RX PubMed=12140260; DOI=10.1242/jcs.115.16.3285;
RA Duchaine T.F., Hemraj I., Furic L., Deitinghoff A., Kiebler M.A.,
RA DesGroseillers L.;
RT "Staufen2 isoforms localize to the somatodendritic domain of neurons and
RT interact with different organelles.";
RL J. Cell Sci. 115:3285-3295(2002).
RN [6]
RP IDENTIFICATION WITHIN RIBONUCLEOPROTEIN PARTICLES.
RX PubMed=12592035; DOI=10.1073/pnas.0334355100;
RA Mallardo M., Deitinghoff A., Mueller J., Goetze B., Macchi P., Peters C.,
RA Kiebler M.A.;
RT "Isolation and characterization of Staufen-containing ribonucleoprotein
RT particles from rat brain.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:2100-2105(2003).
RN [7]
RP SUBCELLULAR LOCATION.
RX PubMed=15525674; DOI=10.1091/mbc.e04-06-0516;
RA Thomas M.G., Martinez Tosar L.J., Loschi M., Pasquini J.M., Correale J.,
RA Kindler S., Boccaccio G.L.;
RT "Staufen recruitment into stress granules does not affect early mRNA
RT transport in oligodendrocytes.";
RL Mol. Biol. Cell 16:405-420(2005).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9; SER-13; THR-18 AND SER-21
RP (ISOFORMS 2 AND 3), AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RX PubMed=16641100; DOI=10.1073/pnas.0600895103;
RA Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.;
RT "Quantitative phosphoproteomics of vasopressin-sensitive renal cells:
RT regulation of aquaporin-2 phosphorylation at two sites.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006).
CC -!- FUNCTION: RNA-binding protein required for the microtubule-dependent
CC transport of neuronal RNA from the cell body to the dendrite. As
CC protein synthesis occurs within the dendrite, the localization of
CC specific mRNAs to dendrites may be a prerequisite for neurite outgrowth
CC and plasticity at sites distant from the cell body.
CC {ECO:0000269|PubMed:11709157}.
CC -!- SUBUNIT: Identified in a mRNP complex, at least composed of DHX9,
CC DDX3X, ELAVL1, HNRNPU, IGF2BP1, ILF3, PABPC1, PCBP2, PTBP2, STAU1,
CC STAU2, SYNCRIP and YBX1. Interacts with the exportin XPO5. This
CC requires RNA and RAN bound to GTP (By similarity). Interacts with
CC microtubules. Isoform 2 and isoform 3 may also interact with ribosomes,
CC and this association is independent of translation. Interacts with
CC TRIM71 (via NHL repeats) in an RNA-dependent manner (By similarity).
CC {ECO:0000250|UniProtKB:Q9NUL3, ECO:0000269|PubMed:11709157,
CC ECO:0000269|PubMed:12140260}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus. Nucleus. Cytoplasm.
CC Endoplasmic reticulum. Note=Shuttles between the nucleolus, nucleus and
CC the cytoplasm. Nuclear export of isoform 1 is independent of XPO1/CRM1
CC and may require the exportin XPO5. Nuclear export of isoform 2 and
CC isoform 3 can occur by both XPO1/CRM1-dependent and XPO1/CRM1-
CC independent pathways. Found in large cytoplasmic ribonucleoprotein
CC (RNP) granules which are present in the actin rich regions of
CC myelinating processes and associated with microtubules, polysomes and
CC the endoplasmic reticulum. Also recruited to stress granules (SGs) upon
CC inhibition of translation or oxidative stress. These structures are
CC thought to harbor housekeeping mRNAs when translation is aborted.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1; Synonyms=LL, A;
CC IsoId=Q68SB1-1; Sequence=Displayed;
CC Name=2; Synonyms=SL;
CC IsoId=Q68SB1-2; Sequence=VSP_015385, VSP_015386;
CC Name=3; Synonyms=SS;
CC IsoId=Q68SB1-3; Sequence=VSP_015385, VSP_015386, VSP_015387,
CC VSP_015388;
CC Name=4; Synonyms=LS, B;
CC IsoId=Q68SB1-4; Sequence=VSP_015387, VSP_015388;
CC -!- TISSUE SPECIFICITY: Expressed in both somata and dendrites of
CC hippocampal neurons. {ECO:0000269|PubMed:11709157,
CC ECO:0000269|PubMed:12140260}.
CC -!- DOMAIN: The DRBM 3 domain appears to be the major RNA-binding
CC determinant (By similarity). This domain also mediates interaction with
CC XPO5 and is required for XPO1/CRM1-independent nuclear export.
CC {ECO:0000250, ECO:0000269|PubMed:11709157}.
CC -!- MISCELLANEOUS: [Isoform 2]: XPO1/CRM1-dependent nuclear export is
CC mediated by residues 4-14 and is abrogated by mutagenesis of Ile-4 or
CC Leu-12. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 3]: XPO1/CRM1-dependent nuclear export is
CC mediated by residues 4-14 and is abrogated by mutagenesis of Ile-4 or
CC Leu-12. {ECO:0000305}.
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DR EMBL; AF483620; AAL89718.1; -; mRNA.
DR EMBL; AF483621; AAL89719.1; -; mRNA.
DR EMBL; AY684789; AAU21478.1; -; mRNA.
DR EMBL; AY684790; AAU21479.1; -; mRNA.
DR EMBL; AY549445; AAT36670.1; -; mRNA.
DR EMBL; AY549446; AAT36671.1; -; mRNA.
DR EMBL; AY549447; AAT36672.1; -; mRNA.
DR EMBL; AY549448; AAT36673.1; -; mRNA.
DR EMBL; BC085705; AAH85705.1; -; mRNA.
DR RefSeq; NP_001007150.1; NM_001007149.1. [Q68SB1-1]
DR RefSeq; NP_001007151.1; NM_001007150.1. [Q68SB1-3]
DR RefSeq; NP_604461.2; NM_134466.2. [Q68SB1-4]
DR AlphaFoldDB; Q68SB1; -.
DR SMR; Q68SB1; -.
DR BioGRID; 251277; 5.
DR PhosphoSitePlus; Q68SB1; -.
DR PaxDb; Q68SB1; -.
DR PRIDE; Q68SB1; -.
DR Ensembl; ENSRNOT00000066590; ENSRNOP00000060092; ENSRNOG00000042458. [Q68SB1-4]
DR Ensembl; ENSRNOT00000090346; ENSRNOP00000074008; ENSRNOG00000042458. [Q68SB1-3]
DR Ensembl; ENSRNOT00000100311; ENSRNOP00000087673; ENSRNOG00000042458. [Q68SB1-2]
DR Ensembl; ENSRNOT00000120142; ENSRNOP00000092247; ENSRNOG00000042458. [Q68SB1-1]
DR GeneID; 171500; -.
DR KEGG; rno:171500; -.
DR UCSC; RGD:621479; rat. [Q68SB1-1]
DR CTD; 27067; -.
DR RGD; 621479; Stau2.
DR eggNOG; KOG3732; Eukaryota.
DR GeneTree; ENSGT00940000154977; -.
DR InParanoid; Q68SB1; -.
DR OrthoDB; 823092at2759; -.
DR PhylomeDB; Q68SB1; -.
DR PRO; PR:Q68SB1; -.
DR Proteomes; UP000002494; Chromosome 5.
DR GO; GO:0030424; C:axon; IDA:RGD.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0010494; C:cytoplasmic stress granule; IDA:RGD.
DR GO; GO:0030425; C:dendrite; IDA:RGD.
DR GO; GO:0032839; C:dendrite cytoplasm; IEA:GOC.
DR GO; GO:0043198; C:dendritic shaft; IDA:RGD.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:1990124; C:messenger ribonucleoprotein complex; IDA:RGD.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0031965; C:nuclear membrane; IDA:RGD.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0003725; F:double-stranded RNA binding; ISO:RGD.
DR GO; GO:0030544; F:Hsp70 protein binding; IDA:RGD.
DR GO; GO:0019894; F:kinesin binding; IDA:RGD.
DR GO; GO:0051019; F:mitogen-activated protein kinase binding; IDA:RGD.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0043022; F:ribosome binding; IDA:RGD.
DR GO; GO:0098964; P:anterograde dendritic transport of messenger ribonucleoprotein complex; IMP:SynGO.
DR GO; GO:0034599; P:cellular response to oxidative stress; IEP:RGD.
DR GO; GO:0048592; P:eye morphogenesis; IMP:RGD.
DR GO; GO:0007281; P:germ cell development; IBA:GO_Central.
DR GO; GO:0008298; P:intracellular mRNA localization; IBA:GO_Central.
DR GO; GO:0061003; P:positive regulation of dendritic spine morphogenesis; IMP:RGD.
DR GO; GO:1900454; P:positive regulation of long-term synaptic depression; IMP:RGD.
DR GO; GO:0051965; P:positive regulation of synapse assembly; IMP:RGD.
DR GO; GO:0035418; P:protein localization to synapse; IBA:GO_Central.
DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; IMP:RGD.
DR GO; GO:0051489; P:regulation of filopodium assembly; IMP:RGD.
DR GO; GO:0010468; P:regulation of gene expression; IMP:RGD.
DR CDD; cd19880; DSRM_STAU2_rpt1; 1.
DR CDD; cd19882; DSRM_STAU2_rpt2; 1.
DR CDD; cd19884; DSRM_STAU2_rpt3; 1.
DR CDD; cd19886; DSRM_STAU2_rpt4; 1.
DR InterPro; IPR014720; dsRBD_dom.
DR InterPro; IPR044476; STAU2_DSRM_1.
DR InterPro; IPR044464; STAU2_DSRM_2.
DR InterPro; IPR044473; STAU2_DSRM_3.
DR InterPro; IPR044474; STAU2_DSRM_4.
DR InterPro; IPR032478; Staufen_C.
DR Pfam; PF00035; dsrm; 4.
DR Pfam; PF16482; Staufen_C; 1.
DR SMART; SM00358; DSRM; 4.
DR PROSITE; PS50137; DS_RBD; 4.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Endoplasmic reticulum; Microtubule;
KW Nucleus; Phosphoprotein; Reference proteome; Repeat; RNA-binding;
KW Transport.
FT CHAIN 1..571
FT /note="Double-stranded RNA-binding protein Staufen homolog
FT 2"
FT /id="PRO_0000072248"
FT DOMAIN 8..75
FT /note="DRBM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00266"
FT DOMAIN 95..181
FT /note="DRBM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00266"
FT DOMAIN 207..274
FT /note="DRBM 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00266"
FT DOMAIN 307..375
FT /note="DRBM 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00266"
FT REGION 71..94
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 178..203
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 381..571
FT /note="Required for dendritic transport"
FT REGION 382..413
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 546..571
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 273..317
FT /note="Nuclear localization signal 1"
FT MOTIF 373..412
FT /note="Nuclear localization signal 2"
FT COMPBIAS 552..571
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 188
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NUL3"
FT MOD_RES 395
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NUL3"
FT MOD_RES 416
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NUL3"
FT MOD_RES 426
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NUL3"
FT MOD_RES 440
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NUL3"
FT MOD_RES 456
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NUL3"
FT MOD_RES 493
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NUL3"
FT VAR_SEQ 1..32
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:15364930,
FT ECO:0000303|PubMed:15970630"
FT /id="VSP_015385"
FT VAR_SEQ 33..38
FT /note="GPAHSK -> MLQINQ (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:15364930,
FT ECO:0000303|PubMed:15970630"
FT /id="VSP_015386"
FT VAR_SEQ 512
FT /note="A -> V (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:11709157,
FT ECO:0000303|PubMed:15364930, ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:15970630"
FT /id="VSP_015387"
FT VAR_SEQ 513..571
FT /note="Missing (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:11709157,
FT ECO:0000303|PubMed:15364930, ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:15970630"
FT /id="VSP_015388"
FT MUTAGEN 239
FT /note="F->A: Abrogates CRM1-independent nuclear export."
FT /evidence="ECO:0000269|PubMed:15364930"
FT CONFLICT 339
FT /note="E -> K (in Ref. 1; AAL89718/AAL89719)"
FT /evidence="ECO:0000305"
FT CONFLICT 538
FT /note="S -> F (in Ref. 1; AAL89718)"
FT /evidence="ECO:0000305"
FT MOD_RES Q68SB1-2:9
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16641100"
FT MOD_RES Q68SB1-2:13
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16641100"
FT MOD_RES Q68SB1-2:18
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:16641100"
FT MOD_RES Q68SB1-2:21
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16641100"
FT MOD_RES Q68SB1-3:9
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16641100"
FT MOD_RES Q68SB1-3:13
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16641100"
FT MOD_RES Q68SB1-3:18
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:16641100"
FT MOD_RES Q68SB1-3:21
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16641100"
SQ SEQUENCE 571 AA; 62681 MW; 778DDC940C66075D CRC64;
MANPKEKTPM CLVNELARFH SIQPQYKLLN ESGPAHSKMF SVQLSLGEQT WESEGSSIKK
AQQAVANKAL TESTLPKPVQ KPPKSNVNNN PGSITPTVEL NGLAMKRGEP AIYRPLDPKP
FPNYRANYNF RGMYNQRYHC PMPKIFYVQL TVGNNEFFGE GKTRQAARHN AAMKALQALQ
NEPIPEKSPQ NGESGKEMDD DKDANKSEIS LVFEIALKRN MPVSFEVIKE SGPPHMKSFV
TRVSVGEFSA EGEGNSKKLS KKRAATTVLQ ELKKLPPLPV IEKPKLFFKK RPKTIIKAGP
EYGQGMNPIS RLAQIQQARK EKEPDYVLLS ERGMPRRREF VMQVKVGNEV ATGTGPNKKI
AKKNAAEAML LQLGYKASTS LQDQLDKTGE NKGWSGPKPG FPEPANNTPK GILHLSPDVY
QEMEASRHRV TSGTTLGYLS PKDMNQPSSS FFSVESPSPT SSAPAARELL MNGTSPAAEA
IGLKGSSPTP PCSSVQPSKQ LEYLARIQGF QAALSALKQF SEQGLESIDG VVNVENGSLE
KQAKHLREKA DNNQANPGSI TQDCKKSKSV I
