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Protein

Protein windbeutel

Gene

wbl

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

Functioni

Probable chaperone protein involved in dorsoventral axis patterning in early embryos. Probably acts by folding and targeting pipe (pip) into the Golgi.2 Publications

GO - Molecular functioni

  1. protein homodimerization activity Source: UniProtKB

GO - Biological processi

  1. dorsal/ventral axis specification Source: UniProtKB
  2. embryo development ending in birth or egg hatching Source: FlyBase
  3. maternal specification of dorsal/ventral axis, oocyte, soma encoded Source: FlyBase
  4. protein processing Source: FlyBase
  5. protein secretion Source: InterPro
  6. protein targeting to Golgi Source: FlyBase
  7. regulation of multicellular organism growth Source: FlyBase
  8. Toll signaling pathway Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Chaperone, Developmental protein

Names & Taxonomyi

Protein namesi
Recommended name:
Protein windbeutel
Alternative name(s):
Erp29 homolog
Gene namesi
Name:wbl
Synonyms:wind
ORF Names:CG7225
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803 Componenti: Chromosome 2R

Organism-specific databases

FlyBaseiFBgn0004003. wbl.

Subcellular locationi

Endoplasmic reticulum lumen PROSITE-ProRule annotation

GO - Cellular componenti

  1. endomembrane system Source: FlyBase
  2. endoplasmic reticulum Source: UniProtKB
  3. endoplasmic reticulum lumen Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi24 – 274CTGC → STGS: Affects subcellular targeting of pip. 1 Publication
Mutagenesisi25 – 251T → K: Does not affect subcellular targeting of pip. 1 Publication
Mutagenesisi28 – 281V → D or N: Abolishes homodimerization and subcellular targeting of pip. 1 Publication
Mutagenesisi29 – 291D → N: Does not affect subcellular targeting of pip. 1 Publication
Mutagenesisi31 – 311D → N: Impairs homodimerization. Abolishes homodimerization and subcellular targeting of pip; when associated with S-41. 1 Publication
Mutagenesisi41 – 411R → S: Does not affect homodimerization. Abolishes homodimerization and subcellular targeting of pip; when associated with N-31. 1 Publication
Mutagenesisi50 – 501D → A or S: Affects subcellular targeting of pip but not homodimerization. 1 Publication
Mutagenesisi50 – 501D → A: Affects subcellular targeting of pip but not homodimerization. 1 Publication
Mutagenesisi51 – 511I → R or S: Does not affect subcellular targeting of pip. 1 Publication
Mutagenesisi52 – 521A → S: Does not affect subcellular targeting of pip. 1 Publication
Mutagenesisi53 – 531Y → S: Affects subcellular targeting of pip. 1 Publication
Mutagenesisi55 – 551Y → K: Affects subcellular targeting of pip but not homodimerization. 1 Publication
Mutagenesisi58 – 581K → S: Does not affect subcellular targeting of pip. 1 Publication
Mutagenesisi59 – 591H → Y: Does not affect subcellular targeting of pip. 1 Publication
Mutagenesisi60 – 601E → Q: Affects subcellular targeting of pip. 1 Publication
Mutagenesisi63 – 631T → K: Does not affect subcellular targeting of pip. 1 Publication
Mutagenesisi84 – 841K → D or Y: Affects subcellular targeting of pip. 1 Publication
Mutagenesisi84 – 841K → S or N: Does not affect subcellular targeting of pip. 1 Publication
Mutagenesisi86 – 861Y → Q or L: Affects subcellular targeting of pip. 1 Publication
Mutagenesisi86 – 861Y → S or F: Does not affect subcellular targeting of pip. 1 Publication
Mutagenesisi88 – 881E → K or Q: Does not affect subcellular targeting of pip. 1 Publication
Mutagenesisi106 – 1061P → D: Affects subcellular targeting of pip. 1 Publication
Mutagenesisi212 – 2121E → Q: Affects subcellular targeting of pip; when associated with S-219. 1 Publication
Mutagenesisi215 – 2151R → A: Affects subcellular targeting of pip. 1 Publication
Mutagenesisi218 – 2181R → D: Affects subcellular targeting of pip. 1 Publication
Mutagenesisi219 – 2191L → S: Affects subcellular targeting of pip; when associated with Q-212. 1 Publication
Mutagenesisi239 – 2391L → P in T6; induces dorsalized embryos. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2121Sequence AnalysisAdd
BLAST
Chaini22 – 257236Protein windbeutelPRO_0000022690Add
BLAST

Proteomic databases

PaxDbiO44342.
PRIDEiO44342.

Expressioni

Tissue specificityi

Briefly expressed in the follicle cells of the ovary, at around the time when the dorsoventral axis of the egg chamber is first established.1 Publication

Developmental stagei

Expressed in ovaries, early embryo (0-4 hours) and adult males. Almost undetectable in female carcasses. In ovaries, it is not detected in the germarium or early stage egg-chambers and is first detectable in the follicle cells of stage 8 egg-chambers. The peak of expression occurs in the follicle cells of stages 9 and early 10, and it disappears completely before stage 11. Not expressed in the germline cells (nurse cells and oocyte), with the possible exception of late stage 10 nurse cells.1 Publication

Gene expression databases

BgeeiO44342.

Interactioni

Subunit structurei

Homodimer. Interacts directly with pip.2 Publications

Protein-protein interaction databases

BioGridi62871. 1 interaction.
IntActiO44342. 1 interaction.
STRINGi7227.FBpp0085698.

Structurei

Secondary structure

1
257
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi28 – 303Combined sources
Turni32 – 343Combined sources
Helixi35 – 395Combined sources
Beta strandi42 – 5312Combined sources
Helixi57 – 7216Combined sources
Beta strandi74 – 8310Combined sources
Beta strandi86 – 883Combined sources
Helixi92 – 976Combined sources
Helixi102 – 1043Combined sources
Beta strandi107 – 12014Combined sources
Helixi129 – 13911Combined sources
Helixi151 – 1577Combined sources
Helixi160 – 1623Combined sources
Helixi165 – 18117Combined sources
Helixi185 – 20420Combined sources
Helixi207 – 22014Combined sources
Helixi226 – 24116Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1OVNX-ray1.90A/B22-257[»]
2C0EX-ray2.35A/B23-257[»]
2C0FX-ray2.28A/B22-257[»]
2C0GX-ray1.75A/B22-257[»]
2C1YX-ray2.25A/B22-257[»]
ProteinModelPortaliO44342.
SMRiO44342. Positions 24-252.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO44342.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni24 – 274CXXC motif

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi254 – 2574Prevents secretion from ERCurated

Domaini

The CXXC motif was initially thought to constitute the active site of a potential protein disulfide isomerase activity. However, such motif is not essential, suggesting that it has no disulfide isomerase activity. Its precise role remains unclear.

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG82861.
GeneTreeiENSGT00390000018566.
InParanoidiO44342.
KOiK09586.
OMAiGEKYKLD.
OrthoDBiEOG7XH6RH.
PhylomeDBiO44342.

Family and domain databases

Gene3Di1.20.1150.12. 1 hit.
3.40.30.10. 1 hit.
InterProiIPR016855. ER_p29.
IPR011679. ER_p29_C.
IPR012883. ERp29_N.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamiPF07749. ERp29. 1 hit.
PF07912. ERp29_N. 1 hit.
[Graphical view]
PIRSFiPIRSF027352. ER_p29. 1 hit.
SUPFAMiSSF47933. SSF47933. 1 hit.
SSF52833. SSF52833. 1 hit.
PROSITEiPS00014. ER_TARGET. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O44342-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MMHILVTLLL VAIHSIPTTW AVTCTGCVDL DELSFEKTVE RFPYSVVKFD
60 70 80 90 100
IAYPYGEKHE AFTAFSKSAH KATKDLLIAT VGVKDYGELE NKALGDRYKV
110 120 130 140 150
DDKNFPSIFL FKGNADEYVQ LPSHVDVTLD NLKAFVSANT PLYIGRDGCI
160 170 180 190 200
KEFNEVLKNY ANIPDAEQLK LIEKLQAKQE QLTDPEQQQN ARAYLIYMRK
210 220 230 240 250
IHEVGYDFLE EETKRLLRLK AGKVTEAKKE ELLRKLNILE VFRVHKVTKT

APEKEEL
Length:257
Mass (Da):29,444
Last modified:June 1, 1998 - v1
Checksum:iA2BD08EC9535B1C8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF025408 Genomic DNA. Translation: AAC02944.1.
AE013599 Genomic DNA. Translation: AAF57590.1.
BT023269 mRNA. Translation: AAY55685.1.
RefSeqiNP_001286609.1. NM_001299680.1.
NP_725867.1. NM_166339.2.
UniGeneiDm.23938.

Genome annotation databases

EnsemblMetazoaiFBtr0086510; FBpp0085698; FBgn0004003.
FBtr0340470; FBpp0309412; FBgn0004003.
GeneIDi37206.
KEGGidme:Dmel_CG7225.
UCSCiCG7225-RA. d. melanogaster.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF025408 Genomic DNA. Translation: AAC02944.1.
AE013599 Genomic DNA. Translation: AAF57590.1.
BT023269 mRNA. Translation: AAY55685.1.
RefSeqiNP_001286609.1. NM_001299680.1.
NP_725867.1. NM_166339.2.
UniGeneiDm.23938.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1OVNX-ray1.90A/B22-257[»]
2C0EX-ray2.35A/B23-257[»]
2C0FX-ray2.28A/B22-257[»]
2C0GX-ray1.75A/B22-257[»]
2C1YX-ray2.25A/B22-257[»]
ProteinModelPortaliO44342.
SMRiO44342. Positions 24-252.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi62871. 1 interaction.
IntActiO44342. 1 interaction.
STRINGi7227.FBpp0085698.

Proteomic databases

PaxDbiO44342.
PRIDEiO44342.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0086510; FBpp0085698; FBgn0004003.
FBtr0340470; FBpp0309412; FBgn0004003.
GeneIDi37206.
KEGGidme:Dmel_CG7225.
UCSCiCG7225-RA. d. melanogaster.

Organism-specific databases

CTDi37206.
FlyBaseiFBgn0004003. wbl.

Phylogenomic databases

eggNOGiNOG82861.
GeneTreeiENSGT00390000018566.
InParanoidiO44342.
KOiK09586.
OMAiGEKYKLD.
OrthoDBiEOG7XH6RH.
PhylomeDBiO44342.

Miscellaneous databases

EvolutionaryTraceiO44342.
GenomeRNAii37206.
NextBioi802516.
PROiO44342.

Gene expression databases

BgeeiO44342.

Family and domain databases

Gene3Di1.20.1150.12. 1 hit.
3.40.30.10. 1 hit.
InterProiIPR016855. ER_p29.
IPR011679. ER_p29_C.
IPR012883. ERp29_N.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamiPF07749. ERp29. 1 hit.
PF07912. ERp29_N. 1 hit.
[Graphical view]
PIRSFiPIRSF027352. ER_p29. 1 hit.
SUPFAMiSSF47933. SSF47933. 1 hit.
SSF52833. SSF52833. 1 hit.
PROSITEiPS00014. ER_TARGET. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "windbeutel, a gene required for dorsoventral patterning in Drosophila, encodes a protein that has homologies to vertebrate proteins of the endoplasmic reticulum."
    Konsolaki M., Schuepbach T.
    Genes Dev. 12:120-131(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, MUTAGENESIS OF LEU-239.
  2. "The genome sequence of Drosophila melanogaster."
    Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
    , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
    Science 287:2185-2195(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  3. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  4. Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M., Park S., Wan K.H., Yu C., Celniker S.E.
    Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
  5. "Localized requirements for windbeutel and pipe reveal a dorsoventral prepattern within the follicular epithelium of the Drosophila ovary."
    Nilson L.A., Schuepbach T.
    Cell 93:253-262(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  6. "Windbeutel is required for function and correct subcellular localization of the Drosophila patterning protein Pipe."
    Sen J., Goltz J.S., Konsolaki M., Schuepbach T., Stein D.
    Development 127:5541-5550(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  7. "Mapping of a substrate binding site in the protein disulfide isomerase-related chaperone wind based on protein function and crystal structure."
    Barnewitz K., Guo C., Sevvana M., Ma Q., Sheldrick G.M., Soeling H.-D., Ferrari D.M.
    J. Biol. Chem. 279:39829-39837(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PIP, MUTAGENESIS OF THR-25; VAL-28; ASP-29; ARG-41; ASP-50; ILE-51; ALA-52; TYR-53; LYS-58; HIS-59; GLU-60; THR-63; LYS-84; TYR-86; GLU-88; PRO-106; GLU-212; ARG-215; ARG-218 AND LEU-219.
  8. "Crystal structure and functional analysis of Drosophila Wind, a protein-disulfide isomerase-related protein."
    Ma Q., Guo C., Barnewitz K., Sheldrick G.M., Soeling H.-D., Uson I., Ferrari D.M.
    J. Biol. Chem. 278:44600-44607(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 10-257, SUBUNIT, MUTAGENESIS OF 24-LYS--LEU-27; ASP-31 AND TYR-55.

Entry informationi

Entry nameiWBL_DROME
AccessioniPrimary (citable) accession number: O44342
Secondary accession number(s): Q4V3T7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: June 1, 1998
Last modified: March 4, 2015
This is version 110 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Miscellaneous

'Windbeutel' means 'profiteroles' in German.

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

External Data

Dasty 3

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 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.