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O44342

- WBL_DROME

UniProt

O44342 - WBL_DROME

Protein

Protein windbeutel

Gene

wbl

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 106 (01 Oct 2014)
      Sequence version 1 (01 Jun 1998)
      Previous versions | rss
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    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. 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

    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 PROSITE-ProRule annotation

    GO - Cellular componenti

    1. endoplasmic reticulum Source: UniProtKB
    2. endoplasmic reticulum lumen Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Endoplasmic reticulum

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi24 – 274CTGC → STGS: Affects subcellular targeting of pip.
    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.
    STRINGi7227.FBpp0085698.

    Structurei

    Secondary structure

    1
    257
    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.
    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.
    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

    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: October 1, 2014
    This is version 106 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