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O44342 (WBL_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 103. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Protein windbeutel
Alternative name(s):
Erp29 homolog
Gene names
Name:wbl
Synonyms:wind
ORF Names:CG7225
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length257 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Probable chaperone protein involved in dorsoventral axis patterning in early embryos. Probably acts by folding and targeting pipe (pip) into the Golgi. Ref.5 Ref.6

Subunit structure

Homodimer. Interacts directly with pip. Ref.7 Ref.8

Subcellular location

Endoplasmic reticulum lumen By similarity Ref.6.

Tissue specificity

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

Developmental stage

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. Ref.1

Domain

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.

Miscellaneous

'Windbeutel' means 'profiteroles' in German.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2121 Potential
Chain22 – 257236Protein windbeutel
PRO_0000022690

Regions

Region24 – 274CXXC motif
Motif254 – 2574Prevents secretion from ER Probable

Experimental info

Mutagenesis24 – 274CTGC → STGS: Affects subcellular targeting of pip. Ref.8
Mutagenesis251T → K: Does not affect subcellular targeting of pip. Ref.7
Mutagenesis281V → D or N: Abolishes homodimerization and subcellular targeting of pip. Ref.7
Mutagenesis291D → N: Does not affect subcellular targeting of pip. Ref.7
Mutagenesis311D → N: Impairs homodimerization. Abolishes homodimerization and subcellular targeting of pip; when associated with S-41. Ref.8
Mutagenesis411R → S: Does not affect homodimerization. Abolishes homodimerization and subcellular targeting of pip; when associated with N-31. Ref.7
Mutagenesis501D → A or S: Affects subcellular targeting of pip but not homodimerization. Ref.7
Mutagenesis501D → A: Affects subcellular targeting of pip but not homodimerization. Ref.7
Mutagenesis511I → R or S: Does not affect subcellular targeting of pip. Ref.7
Mutagenesis521A → S: Does not affect subcellular targeting of pip. Ref.7
Mutagenesis531Y → S: Affects subcellular targeting of pip. Ref.7
Mutagenesis551Y → K: Affects subcellular targeting of pip but not homodimerization. Ref.8
Mutagenesis581K → S: Does not affect subcellular targeting of pip. Ref.7
Mutagenesis591H → Y: Does not affect subcellular targeting of pip. Ref.7
Mutagenesis601E → Q: Affects subcellular targeting of pip. Ref.7
Mutagenesis631T → K: Does not affect subcellular targeting of pip. Ref.7
Mutagenesis841K → D or Y: Affects subcellular targeting of pip. Ref.7
Mutagenesis841K → S or N: Does not affect subcellular targeting of pip. Ref.7
Mutagenesis861Y → Q or L: Affects subcellular targeting of pip. Ref.7
Mutagenesis861Y → S or F: Does not affect subcellular targeting of pip. Ref.7
Mutagenesis881E → K or Q: Does not affect subcellular targeting of pip. Ref.7
Mutagenesis1061P → D: Affects subcellular targeting of pip. Ref.7
Mutagenesis2121E → Q: Affects subcellular targeting of pip; when associated with S-219. Ref.7
Mutagenesis2151R → A: Affects subcellular targeting of pip. Ref.7
Mutagenesis2181R → D: Affects subcellular targeting of pip. Ref.7
Mutagenesis2191L → S: Affects subcellular targeting of pip; when associated with Q-212. Ref.7
Mutagenesis2391L → P in T6; induces dorsalized embryos. Ref.1

Secondary structure

.................................. 257
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O44342 [UniParc].

Last modified June 1, 1998. Version 1.
Checksum: A2BD08EC9535B1C8

FASTA25729,444
        10         20         30         40         50         60 
MMHILVTLLL VAIHSIPTTW AVTCTGCVDL DELSFEKTVE RFPYSVVKFD IAYPYGEKHE 

        70         80         90        100        110        120 
AFTAFSKSAH KATKDLLIAT VGVKDYGELE NKALGDRYKV DDKNFPSIFL FKGNADEYVQ 

       130        140        150        160        170        180 
LPSHVDVTLD NLKAFVSANT PLYIGRDGCI KEFNEVLKNY ANIPDAEQLK LIEKLQAKQE 

       190        200        210        220        230        240 
QLTDPEQQQN ARAYLIYMRK IHEVGYDFLE EETKRLLRLK AGKVTEAKKE ELLRKLNILE 

       250 
VFRVHKVTKT APEKEEL 

« Hide

References

« Hide 'large scale' references
[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(1998) [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. expand/collapse author list , 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(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Berkeley.
[3]"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review."
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. expand/collapse author list , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed] [Europe PMC] [Abstract]
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 (MAY-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(1998) [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(2000) [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(2004) [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(2003) [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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF025408 Genomic DNA. Translation: AAC02944.1.
AE013599 Genomic DNA. Translation: AAF57590.1.
BT023269 mRNA. Translation: AAY55685.1.
RefSeqNP_725867.1. NM_166339.1.
UniGeneDm.23938.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortalO44342.
SMRO44342. Positions 24-252.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid62871. 1 interaction.
STRING7227.FBpp0085698.

Proteomic databases

PaxDbO44342.
PRIDEO44342.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0086510; FBpp0085698; FBgn0004003.
GeneID37206.
KEGGdme:Dmel_CG7225.
UCSCCG7225-RA. d. melanogaster.

Organism-specific databases

CTD37206.
FlyBaseFBgn0004003. wbl.

Phylogenomic databases

eggNOGNOG82861.
GeneTreeENSGT00390000018566.
InParanoidO44342.
KOK09586.
OMAPYGEKHE.
OrthoDBEOG7XH6RH.
PhylomeDBO44342.

Gene expression databases

BgeeO44342.

Family and domain databases

Gene3D1.20.1150.12. 1 hit.
3.40.30.10. 1 hit.
InterProIPR016855. ER_p29.
IPR011679. ER_p29_C.
IPR012883. ERp29_N.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamPF07749. ERp29. 1 hit.
PF07912. ERp29_N. 1 hit.
[Graphical view]
PIRSFPIRSF027352. ER_p29. 1 hit.
SUPFAMSSF47933. SSF47933. 1 hit.
SSF52833. SSF52833. 1 hit.
PROSITEPS00014. ER_TARGET. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceO44342.
GenomeRNAi37206.
NextBio802516.
PROO44342.

Entry information

Entry nameWBL_DROME
AccessionPrimary (citable) accession number: O44342
Secondary accession number(s): Q4V3T7
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: June 1, 1998
Last modified: April 16, 2014
This is version 103 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase