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O44342

- WBL_DROME

UniProt

O44342 - WBL_DROME

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Protein
Protein windbeutel
Gene
wbl, wind, CG7225
Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - 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 binding Source: UniProtKB
  2. protein homodimerization activity Source: UniProtKB

GO - Biological processi

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

Organism-specific databases

FlyBaseiFBgn0004003. wbl.

Subcellular locationi

Endoplasmic reticulum lumen By similarity 1 Publication

GO - Cellular componenti

  1. endoplasmic reticulum Source: UniProtKB
  2. 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 – 2121 Reviewed prediction
Add
BLAST
Chaini22 – 257236Protein windbeutel
PRO_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.
STRINGi7227.FBpp0085698.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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.

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 ER Inferred

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.
OMAiPYGEKHE.
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

MMHILVTLLL VAIHSIPTTW AVTCTGCVDL DELSFEKTVE RFPYSVVKFD    50
IAYPYGEKHE AFTAFSKSAH KATKDLLIAT VGVKDYGELE NKALGDRYKV 100
DDKNFPSIFL FKGNADEYVQ LPSHVDVTLD NLKAFVSANT PLYIGRDGCI 150
KEFNEVLKNY ANIPDAEQLK LIEKLQAKQE QLTDPEQQQN ARAYLIYMRK 200
IHEVGYDFLE EETKRLLRLK AGKVTEAKKE ELLRKLNILE VFRVHKVTKT 250
APEKEEL 257
Length:257
Mass (Da):29,444
Last modified:June 1, 1998 - v1
Checksum:iA2BD08EC9535B1C8
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF025408 Genomic DNA. Translation: AAC02944.1.
AE013599 Genomic DNA. Translation: AAF57590.1.
BT023269 mRNA. Translation: AAY55685.1.
RefSeqiNP_725867.1. NM_166339.1.
UniGeneiDm.23938.

Genome annotation databases

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

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF025408 Genomic DNA. Translation: AAC02944.1 .
AE013599 Genomic DNA. Translation: AAF57590.1 .
BT023269 mRNA. Translation: AAY55685.1 .
RefSeqi NP_725867.1. NM_166339.1.
UniGenei Dm.23938.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1OVN X-ray 1.90 A/B 22-257 [» ]
2C0E X-ray 2.35 A/B 23-257 [» ]
2C0F X-ray 2.28 A/B 22-257 [» ]
2C0G X-ray 1.75 A/B 22-257 [» ]
2C1Y X-ray 2.25 A/B 22-257 [» ]
ProteinModelPortali O44342.
SMRi O44342. Positions 24-252.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 62871. 1 interaction.
STRINGi 7227.FBpp0085698.

Proteomic databases

PaxDbi O44342.
PRIDEi O44342.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblMetazoai FBtr0086510 ; FBpp0085698 ; FBgn0004003 .
GeneIDi 37206.
KEGGi dme:Dmel_CG7225.
UCSCi CG7225-RA. d. melanogaster.

Organism-specific databases

CTDi 37206.
FlyBasei FBgn0004003. wbl.

Phylogenomic databases

eggNOGi NOG82861.
GeneTreei ENSGT00390000018566.
InParanoidi O44342.
KOi K09586.
OMAi PYGEKHE.
OrthoDBi EOG7XH6RH.
PhylomeDBi O44342.

Miscellaneous databases

EvolutionaryTracei O44342.
GenomeRNAii 37206.
NextBioi 802516.
PROi O44342.

Gene expression databases

Bgeei O44342.

Family and domain databases

Gene3Di 1.20.1150.12. 1 hit.
3.40.30.10. 1 hit.
InterProi IPR016855. ER_p29.
IPR011679. ER_p29_C.
IPR012883. ERp29_N.
IPR012336. Thioredoxin-like_fold.
[Graphical view ]
Pfami PF07749. ERp29. 1 hit.
PF07912. ERp29_N. 1 hit.
[Graphical view ]
PIRSFi PIRSF027352. ER_p29. 1 hit.
SUPFAMi SSF47933. SSF47933. 1 hit.
SSF52833. SSF52833. 1 hit.
PROSITEi PS00014. ER_TARGET. 1 hit.
[Graphical view ]
ProtoNeti Search...

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(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.
    , 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. 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.

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: July 9, 2014
This is version 105 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

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