STAU1_AILME
ID STAU1_AILME Reviewed; 580 AA.
AC D2GVP7;
DT 08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT 09-FEB-2010, sequence version 1.
DT 25-MAY-2022, entry version 38.
DE RecName: Full=Double-stranded RNA-binding protein Staufen homolog 1;
GN Name=STAU1; ORFNames=PANDA_000813;
OS Ailuropoda melanoleuca (Giant panda).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ailuropoda.
OX NCBI_TaxID=9646;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20010809; DOI=10.1038/nature08696;
RA Li R., Fan W., Tian G., Zhu H., He L., Cai J., Huang Q., Cai Q., Li B.,
RA Bai Y., Zhang Z., Zhang Y., Wang W., Li J., Wei F., Li H., Jian M., Li J.,
RA Zhang Z., Nielsen R., Li D., Gu W., Yang Z., Xuan Z., Ryder O.A.,
RA Leung F.C., Zhou Y., Cao J., Sun X., Fu Y., Fang X., Guo X., Wang B.,
RA Hou R., Shen F., Mu B., Ni P., Lin R., Qian W., Wang G., Yu C., Nie W.,
RA Wang J., Wu Z., Liang H., Min J., Wu Q., Cheng S., Ruan J., Wang M.,
RA Shi Z., Wen M., Liu B., Ren X., Zheng H., Dong D., Cook K., Shan G.,
RA Zhang H., Kosiol C., Xie X., Lu Z., Zheng H., Li Y., Steiner C.C.,
RA Lam T.T., Lin S., Zhang Q., Li G., Tian J., Gong T., Liu H., Zhang D.,
RA Fang L., Ye C., Zhang J., Hu W., Xu A., Ren Y., Zhang G., Bruford M.W.,
RA Li Q., Ma L., Guo Y., An N., Hu Y., Zheng Y., Shi Y., Li Z., Liu Q.,
RA Chen Y., Zhao J., Qu N., Zhao S., Tian F., Wang X., Wang H., Xu L., Liu X.,
RA Vinar T., Wang Y., Lam T.W., Yiu S.M., Liu S., Zhang H., Li D., Huang Y.,
RA Wang X., Yang G., Jiang Z., Wang J., Qin N., Li L., Li J., Bolund L.,
RA Kristiansen K., Wong G.K., Olson M., Zhang X., Li S., Yang H., Wang J.,
RA Wang J.;
RT "The sequence and de novo assembly of the giant panda genome.";
RL Nature 463:311-317(2010).
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 (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Binds tubulin. Binds with low affinity single-stranded RNA or
CC DNA homopolymers. Interacts with CASC3 in an RNA-dependent manner.
CC Identified in a mRNP complex, at least composed of DHX9, DDX3X, ELAVL1,
CC HNRNPU, IGF2BP1, ILF3, PABPC1, PCBP2, PTBP2, STAU1, STAU2, SYNCRIP and
CC YBX1. Interacts with the influenza virus nonstructural protein NS1.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Rough endoplasmic
CC reticulum {ECO:0000250}. Note=Localizes exclusively with the rough
CC reticulum endoplasmic (RER). {ECO:0000250}.
CC -!- DOMAIN: One of the DRDB could be involved in RER binding.
CC {ECO:0000250}.
CC -!- DOMAIN: The C-terminal contains the tubulin binding domain (TBD).
CC {ECO:0000250}.
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DR EMBL; GL192351; EFB26691.1; -; Genomic_DNA.
DR AlphaFoldDB; D2GVP7; -.
DR SMR; D2GVP7; -.
DR PRIDE; D2GVP7; -.
DR eggNOG; KOG3732; Eukaryota.
DR InParanoid; D2GVP7; -.
DR Proteomes; UP000008912; Unassembled WGS sequence.
DR GO; GO:0005791; C:rough endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
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; 3.
DR Pfam; PF16482; Staufen_C; 1.
DR SMART; SM00358; DSRM; 3.
DR PROSITE; PS50137; DS_RBD; 3.
PE 3: Inferred from homology;
KW Acetylation; Cytoplasm; Endoplasmic reticulum; Methylation; Phosphoprotein;
KW Reference proteome; Repeat; RNA-binding.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:O95793"
FT CHAIN 2..580
FT /note="Double-stranded RNA-binding protein Staufen homolog
FT 1"
FT /id="PRO_0000405778"
FT DOMAIN 72..162
FT /note="DRBM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00266"
FT DOMAIN 191..258
FT /note="DRBM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00266"
FT DOMAIN 293..361
FT /note="DRBM 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00266"
FT REGION 34..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 158..189
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 367..404
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 165..189
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 375..389
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:O95793"
FT MOD_RES 108
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:O95793"
FT MOD_RES 115
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:O95793"
FT MOD_RES 115
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:O95793"
FT MOD_RES 183
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95793"
FT MOD_RES 285
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95793"
FT MOD_RES 397
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95793"
SQ SEQUENCE 580 AA; 63510 MW; A01C217B764D5677 CRC64;
MSQVQVQVQN PSAALSGSQI LSKNQSLLSQ PLMSIPSTTS SLPSENAGRP IQNSALPSAS
LTPTSAAAES ITPTVELNAL CMKLGKKPMY KPVDPYSRMQ STYNYNMRGG AYPPRYFYPF
PVPPLLYQVE LSVGGQQFNG KGKTRQAAKH DAAAKALRTL QSEPLPERPE GRRPGEQVNG
RESEEENLNK SEISQVFEIA LKRNLPVNFE VARESGPPHM KSFVTRVSVG EFVGEGEGKS
KKISKKNAAI AVLEELKKLP PLPTFERVKP RIKKKTKSIV RLQGSTDCSQ GMNPISRLAQ
IQQAKKEKEP EYLLLTERGL PRRREFVMQV KVGNHTAEGT GTNKKVAKRN AAENMLEILG
FKVPQAQPTK PALKSEEKTP IKKPGDGRKV TFFEPGSGDE NGTSNKEDEF RLPYLSHQQL
PAGILPMVPE VAQAVGVSQG HHTKDFTRVA PNPAKATVTA MIARELLYGG TSPTAETILK
NNISSGHVPH GPLTRPSEQL DYLSRVQGFQ VEYKDFPKNN KNEFVSLINC SSQPPLISHG
IGKDVESCHD MAALNILKLL SELDQPSTEM PRTGNGPMSV
