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Protein

Maternal effect protein staufen

Gene

stau

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Required both for the localization of maternal determinants to the posterior pole of the egg, oskar (osk) RNA, and for correct localization to the anterior pole, anchoring bicoid (bcd) RNA. Osk protein is required to keep osk RNA and stau protein at the posterior pole. Stau-bcd complexes form particles that show a microtubule-dependent localization.3 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei606RNA1
Binding sitei608RNA1
Binding sitei628RNA1
Binding sitei629RNA1
Binding sitei632RNA1

GO - Molecular functioni

  • double-stranded RNA binding Source: FlyBase
  • microtubule binding Source: FlyBase
  • mRNA 3'-UTR binding Source: FlyBase
  • mRNA binding Source: FlyBase

GO - Biological processi

  • anterior/posterior axis specification, embryo Source: FlyBase
  • asymmetric neuroblast division Source: FlyBase
  • asymmetric protein localization involved in cell fate determination Source: FlyBase
  • bicoid mRNA localization Source: FlyBase
  • intracellular mRNA localization Source: FlyBase
  • long-term memory Source: FlyBase
  • microtubule-based process Source: FlyBase
  • neuroblast fate determination Source: FlyBase
  • oogenesis Source: FlyBase
  • pole plasm assembly Source: FlyBase
  • pole plasm mRNA localization Source: FlyBase
  • pole plasm oskar mRNA localization Source: FlyBase
  • pole plasm protein localization Source: FlyBase
  • pole plasm RNA localization Source: FlyBase
  • positive regulation of cytoplasmic mRNA processing body assembly Source: FlyBase
  • positive regulation of oskar mRNA translation Source: FlyBase
  • positive regulation of synaptic growth at neuromuscular junction Source: FlyBase
  • protein localization Source: FlyBase
  • protein localization to synapse Source: FlyBase
  • regulation of oskar mRNA translation Source: FlyBase
  • regulation of pole plasm oskar mRNA localization Source: FlyBase
  • RNA localization Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Ligandi

RNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Maternal effect protein staufen
Gene namesi
Name:stau
ORF Names:CG5753
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 2R

Organism-specific databases

FlyBaseiFBgn0003520. stau.

Subcellular locationi

GO - Cellular componenti

  • apical cortex Source: FlyBase
  • apical part of cell Source: FlyBase
  • apical plasma membrane Source: FlyBase
  • basal cortex Source: FlyBase
  • basal plasma membrane Source: FlyBase
  • cell cortex Source: FlyBase
  • cytoplasm Source: FlyBase
  • cytoplasmic mRNA processing body Source: FlyBase
  • germ plasm Source: BHF-UCL
  • microtubule associated complex Source: FlyBase
  • subsynaptic reticulum Source: FlyBase
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi581 – 582SQ → AA: Affects RNA binding without altering the conformation of the domain. 1 Publication2
Mutagenesisi584 – 585HE → AA: Affects RNA binding without altering the conformation of the domain. 1 Publication2
Mutagenesisi586I → A: Crucial for the structure of DRBM 3. 1 Publication1
Mutagenesisi596F → A: Crucial for the structure of DRBM 3. 1 Publication1
Mutagenesisi599 – 602LREE → AAAA: Strongly reduces RNA binding. 1 Publication4
Mutagenesisi606H → A: Abolishes RNA binding without altering the conformation of the domain. 1 Publication1
Mutagenesisi608K → A: Abolishes RNA binding without altering the conformation of the domain. 1 Publication1
Mutagenesisi628 – 629KK → AA: Abolishes RNA binding without altering the conformation of the domain. 1 Publication2
Mutagenesisi632K → A: Abolishes RNA binding without altering the conformation of the domain. 1 Publication1
Mutagenesisi633 – 634KR → AA: No effect on RNA binding. 1 Publication2
Mutagenesisi635 – 636AA → SS: Crucial for the structure of DRBM 3. 1 Publication2

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000722501 – 1026Maternal effect protein staufenAdd BLAST1026

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei563Phosphoserine1 Publication1
Modified residuei570Phosphoserine1 Publication1
Modified residuei650Phosphothreonine1 Publication1
Modified residuei655Phosphothreonine1 Publication1
Modified residuei676Phosphoserine1 Publication1

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP25159.
PRIDEiP25159.

PTM databases

iPTMnetiP25159.

Expressioni

Tissue specificityi

Polar granules at the posterior pole of the oocyte, and by the time the egg is laid, at the anterior pole.2 Publications

Developmental stagei

Expressed both maternally and zygotically.2 Publications

Gene expression databases

BgeeiFBgn0003520.
ExpressionAtlasiP25159. baseline.
GenevisibleiP25159. DM.

Interactioni

GO - Molecular functioni

  • microtubule binding Source: FlyBase

Protein-protein interaction databases

BioGridi62749. 5 interactors.
IntActiP25159. 6 interactors.
MINTiMINT-112231.
STRINGi7227.FBpp0085962.

Structurei

Secondary structure

11026
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi579 – 589Combined sources11
Beta strandi595 – 601Combined sources7
Beta strandi604 – 606Combined sources3
Beta strandi610 – 616Combined sources7
Beta strandi619 – 623Combined sources5
Beta strandi630 – 632Combined sources3
Helixi633 – 643Combined sources11
Helixi953 – 962Combined sources10
Beta strandi967 – 972Combined sources6
Beta strandi977 – 986Combined sources10
Beta strandi992 – 1000Combined sources9
Helixi1001 – 1018Combined sources18

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1EKZNMR-A571-646[»]
1STUNMR-A579-646[»]
5CFFX-ray2.50E/F/G/H953-1019[»]
ProteinModelPortaliP25159.
SMRiP25159.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP25159.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini311 – 378DRBM 1PROSITE-ProRule annotationAdd BLAST68
Domaini490 – 557DRBM 2PROSITE-ProRule annotationAdd BLAST68
Domaini578 – 645DRBM 3PROSITE-ProRule annotationAdd BLAST68
Domaini711 – 781DRBM 4PROSITE-ProRule annotationAdd BLAST71
Domaini951 – 1018DRBM 5PROSITE-ProRule annotationAdd BLAST68

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi3 – 82Gln/His/Pro-richAdd BLAST80
Compositional biasi134 – 177Pro-richAdd BLAST44
Compositional biasi421 – 521Pro-richAdd BLAST101
Compositional biasi873 – 947Ser-richAdd BLAST75

Domaini

Contains a proline-rich domain. The insertion of this domain in the DRBM 2 domain is required for stau-oskar mRNA localization.
DRBM 3 domain binds optimally to stem-loops containing 12 bp (in vitro).

Sequence similaritiesi

Contains 5 DRBM (double-stranded RNA-binding) domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG3732. Eukaryota.
ENOG410XSCK. LUCA.
GeneTreeiENSGT00830000128290.
InParanoidiP25159.
KOiK17597.
OMAiERGPAHC.
OrthoDBiEOG091G07A0.
PhylomeDBiP25159.

Family and domain databases

Gene3Di3.30.160.20. 5 hits.
InterProiIPR014720. dsRBD_dom.
IPR032478. Staufen_C.
[Graphical view]
PfamiPF00035. dsrm. 4 hits.
PF16482. Staufen_C. 1 hit.
[Graphical view]
SMARTiSM00358. DSRM. 4 hits.
[Graphical view]
PROSITEiPS50137. DS_RBD. 5 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform A (identifier: P25159-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MQHNVHAARP APHIRAAHHH SHSHAHMHLH PGMEQHLGPS LQQQQQPPPP
60 70 80 90 100
PQQPPHRDLH ARLNHHHLHA QQQQQQQTSS NQAGAVAAAG AAYHHGNINS
110 120 130 140 150
NSGSNISSNS NQMQKIRQQH QHLSSSNGLL GNQPPGPPPQ AFNPLAGNPA
160 170 180 190 200
ALAYNQLPPH PPHHMAAHLG SYAAPPPHYY MSQAKPAKYN HYGSNANSNS
210 220 230 240 250
GSNNSNSNYA PKAILQNTYR NQKVVVPPVV QEVTPVPEPP VTTNNATTNS
260 270 280 290 300
TSNSTVIASE PVTQEDTSQK PETRQEPASA DDHVSTGNID ATGALSNEDT
310 320 330 340 350
SSSGRGGKDK TPMCLVNELA RYNKITHQYR LTEERGPAHC KTFTVTLMLG
360 370 380 390 400
DEEYSADGFK IKKAQHLAAS KAIEETMYKH PPPKIRRSEE GGPMRTHITP
410 420 430 440 450
TVELNALAMK LGQRTFYLLD PTQIPPTDSI VPPEFAGGHL LTAPGPGMPQ
460 470 480 490 500
PPPPPAYALR QRLGNGFVPI PSQPMHPHFF HGPGQRPFPP KFPSRFALPP
510 520 530 540 550
PLGAHVHHGP NGPFPSVPTP PSKITLFVGK QKFVGIGRTL QQAKHDAAAR
560 570 580 590 600
ALQVLKTQAI SASEEALEDS MDEGDKKSPI SQVHEIGIKR NMTVHFKVLR
610 620 630 640 650
EEGPAHMKNF ITACIVGSIV TEGEGNGKKV SKKRAAEKML VELQKLPPLT
660 670 680 690 700
PTKQTPLKRI KVKTPGKSGA AAREGSVVSG TDGPTQTGKP ERRKRLNPPK
710 720 730 740 750
DKLIDMDDAD NPITKLIQLQ QTRKEKEPIF ELIAKNGNET ARRREFVMEV
760 770 780 790 800
SASGSTARGT GNSKKLAKRN AAQALFELLE AVQVTPTNET QSSEECSTSA
810 820 830 840 850
TMSAVTAPAV EATAEGKVPM VATPVGPMPG ILILRQNKKP AKKRDQIVIV
860 870 880 890 900
KSNVESKEEE ANKEVAVAAE ENSNNSANSG DSSNSSSGDS QATEAASESA
910 920 930 940 950
LNTSTGSNTS GVSSNSSNVG ANTDGNNHAE SKNNTESSSN STSNTQSAGV
960 970 980 990 1000
HMKEQLLYLS KLLDFEVNFS DYPKGNHNEF LTIVTLSTHP PQICHGVGKS
1010 1020
SEESQNDAAS NALKILSKLG LNNAMK
Length:1,026
Mass (Da):110,283
Last modified:July 19, 2005 - v2
Checksum:i3D390391F988B0A2
GO
Isoform B (identifier: P25159-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-112: Missing.

Note: No experimental confirmation available.
Show »
Length:914
Mass (Da):98,029
Checksum:iAB307F84F318C6E5
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti84G → A in AAA73062 (PubMed:1712672).Curated1
Sequence conflicti684 – 685PT → TM in AAA73062 (PubMed:1712672).Curated2
Sequence conflicti797S → C in AAA73062 (PubMed:1712672).Curated1
Sequence conflicti841Missing in AAQ23615 (Ref. 4) Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0147811 – 112Missing in isoform B. 1 PublicationAdd BLAST112

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M69111 mRNA. Translation: AAA73062.1.
AE013599 Genomic DNA. Translation: AAF57752.1.
AE013599 Genomic DNA. Translation: AAF57753.1.
BT003228 mRNA. Translation: AAO24983.1.
BT010297 mRNA. Translation: AAQ23615.1.
PIRiA40315.
RefSeqiNP_001163185.1. NM_001169714.2.
NP_476751.1. NM_057403.4. [P25159-1]
NP_725748.1. NM_166263.2. [P25159-2]
UniGeneiDm.4722.

Genome annotation databases

EnsemblMetazoaiFBtr0086783; FBpp0085962; FBgn0003520. [P25159-1]
GeneIDi37065.
KEGGidme:Dmel_CG5753.
UCSCiCG5753-RA. d. melanogaster. [P25159-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M69111 mRNA. Translation: AAA73062.1.
AE013599 Genomic DNA. Translation: AAF57752.1.
AE013599 Genomic DNA. Translation: AAF57753.1.
BT003228 mRNA. Translation: AAO24983.1.
BT010297 mRNA. Translation: AAQ23615.1.
PIRiA40315.
RefSeqiNP_001163185.1. NM_001169714.2.
NP_476751.1. NM_057403.4. [P25159-1]
NP_725748.1. NM_166263.2. [P25159-2]
UniGeneiDm.4722.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1EKZNMR-A571-646[»]
1STUNMR-A579-646[»]
5CFFX-ray2.50E/F/G/H953-1019[»]
ProteinModelPortaliP25159.
SMRiP25159.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi62749. 5 interactors.
IntActiP25159. 6 interactors.
MINTiMINT-112231.
STRINGi7227.FBpp0085962.

PTM databases

iPTMnetiP25159.

Proteomic databases

PaxDbiP25159.
PRIDEiP25159.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0086783; FBpp0085962; FBgn0003520. [P25159-1]
GeneIDi37065.
KEGGidme:Dmel_CG5753.
UCSCiCG5753-RA. d. melanogaster. [P25159-1]

Organism-specific databases

CTDi37065.
FlyBaseiFBgn0003520. stau.

Phylogenomic databases

eggNOGiKOG3732. Eukaryota.
ENOG410XSCK. LUCA.
GeneTreeiENSGT00830000128290.
InParanoidiP25159.
KOiK17597.
OMAiERGPAHC.
OrthoDBiEOG091G07A0.
PhylomeDBiP25159.

Miscellaneous databases

EvolutionaryTraceiP25159.
GenomeRNAii37065.
PROiP25159.

Gene expression databases

BgeeiFBgn0003520.
ExpressionAtlasiP25159. baseline.
GenevisibleiP25159. DM.

Family and domain databases

Gene3Di3.30.160.20. 5 hits.
InterProiIPR014720. dsRBD_dom.
IPR032478. Staufen_C.
[Graphical view]
PfamiPF00035. dsrm. 4 hits.
PF16482. Staufen_C. 1 hit.
[Graphical view]
SMARTiSM00358. DSRM. 4 hits.
[Graphical view]
PROSITEiPS50137. DS_RBD. 5 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiSTAU_DROME
AccessioniPrimary (citable) accession number: P25159
Secondary accession number(s): Q6NQY8
, Q86PB7, Q9V8B8, Q9V8B9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: July 19, 2005
Last modified: November 30, 2016
This is version 151 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.