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Protein

Protein windbeutel

Gene

wbl

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: -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

Miscellaneous

'Windbeutel' means 'profiteroles' in German.

GO - Molecular functioni

  • protein homodimerization activity Source: UniProtKB

GO - Biological processi

  • dorsal/ventral axis specification Source: UniProtKB
  • embryo development ending in birth or egg hatching Source: FlyBase
  • maternal specification of dorsal/ventral axis, oocyte, soma encoded Source: FlyBase
  • protein folding Source: GO_Central
  • protein folding in endoplasmic reticulum Source: FlyBase
  • protein processing Source: FlyBase
  • protein secretion Source: InterPro
  • regulation of multicellular organism growth Source: FlyBase

Keywordsi

Molecular functionChaperone, 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 lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraHolometabolaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 2R

Organism-specific databases

FlyBaseiFBgn0004003 wbl

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Endoplasmic reticulum

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi24 – 27CTGC → STGS: Affects subcellular targeting of pip. 1 Publication4
Mutagenesisi25T → K: Does not affect subcellular targeting of pip. 1 Publication1
Mutagenesisi28V → D or N: Abolishes homodimerization and subcellular targeting of pip. 1 Publication1
Mutagenesisi29D → N: Does not affect subcellular targeting of pip. 1 Publication1
Mutagenesisi31D → N: Impairs homodimerization. Abolishes homodimerization and subcellular targeting of pip; when associated with S-41. 1 Publication1
Mutagenesisi41R → S: Does not affect homodimerization. Abolishes homodimerization and subcellular targeting of pip; when associated with N-31. 1 Publication1
Mutagenesisi50D → A or S: Affects subcellular targeting of pip but not homodimerization. 1 Publication1
Mutagenesisi50D → A: Affects subcellular targeting of pip but not homodimerization. 1 Publication1
Mutagenesisi51I → R or S: Does not affect subcellular targeting of pip. 1 Publication1
Mutagenesisi52A → S: Does not affect subcellular targeting of pip. 1 Publication1
Mutagenesisi53Y → S: Affects subcellular targeting of pip. 1 Publication1
Mutagenesisi55Y → K: Affects subcellular targeting of pip but not homodimerization. 1 Publication1
Mutagenesisi58K → S: Does not affect subcellular targeting of pip. 1 Publication1
Mutagenesisi59H → Y: Does not affect subcellular targeting of pip. 1 Publication1
Mutagenesisi60E → Q: Affects subcellular targeting of pip. 1 Publication1
Mutagenesisi63T → K: Does not affect subcellular targeting of pip. 1 Publication1
Mutagenesisi84K → D or Y: Affects subcellular targeting of pip. 1 Publication1
Mutagenesisi84K → S or N: Does not affect subcellular targeting of pip. 1 Publication1
Mutagenesisi86Y → Q or L: Affects subcellular targeting of pip. 1 Publication1
Mutagenesisi86Y → S or F: Does not affect subcellular targeting of pip. 1 Publication1
Mutagenesisi88E → K or Q: Does not affect subcellular targeting of pip. 1 Publication1
Mutagenesisi106P → D: Affects subcellular targeting of pip. 1 Publication1
Mutagenesisi212E → Q: Affects subcellular targeting of pip; when associated with S-219. 1 Publication1
Mutagenesisi215R → A: Affects subcellular targeting of pip. 1 Publication1
Mutagenesisi218R → D: Affects subcellular targeting of pip. 1 Publication1
Mutagenesisi219L → S: Affects subcellular targeting of pip; when associated with Q-212. 1 Publication1
Mutagenesisi239L → P in T6; induces dorsalized embryos. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 21Sequence analysisAdd BLAST21
ChainiPRO_000002269022 – 257Protein windbeutelAdd BLAST236

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

BgeeiFBgn0004003
ExpressionAtlasiO44342 baseline and differential
GenevisibleiO44342 DM

Interactioni

Subunit structurei

Homodimer. Interacts directly with pip.2 Publications

GO - Molecular functioni

  • protein homodimerization activity Source: UniProtKB

Protein-protein interaction databases

BioGridi62871, 1 interactor
IntActiO44342, 1 interactor
STRINGi7227.FBpp0085698

Structurei

Secondary structure

1257
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi28 – 30Combined sources3
Turni32 – 34Combined sources3
Helixi35 – 39Combined sources5
Beta strandi42 – 53Combined sources12
Helixi57 – 72Combined sources16
Beta strandi74 – 83Combined sources10
Beta strandi86 – 88Combined sources3
Helixi92 – 97Combined sources6
Helixi102 – 104Combined sources3
Beta strandi107 – 120Combined sources14
Helixi129 – 139Combined sources11
Helixi151 – 157Combined sources7
Helixi160 – 162Combined sources3
Helixi165 – 181Combined sources17
Helixi185 – 204Combined sources20
Helixi207 – 220Combined sources14
Helixi226 – 241Combined sources16

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO44342

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni24 – 27CXXC motif4

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi254 – 257Prevents secretion from ERCurated4

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

eggNOGiENOG410IX2F Eukaryota
ENOG4111I8S LUCA
GeneTreeiENSGT00390000018566
InParanoidiO44342
KOiK09586
OMAiDGCIKEF
OrthoDBiEOG091G0NH4
PhylomeDBiO44342

Family and domain databases

CDDicd00238 ERp29c, 1 hit
cd03007 PDI_a_ERp29_N, 1 hit
Gene3Di1.20.1150.12, 1 hit
InterProiView protein in InterPro
IPR016855 ERp29
IPR011679 ERp29_C
IPR036356 ERp29_C_sf
IPR012883 ERp29_N
IPR036249 Thioredoxin-like_sf
PfamiView protein in Pfam
PF07749 ERp29, 1 hit
PF07912 ERp29_N, 1 hit
PIRSFiPIRSF027352 ER_p29, 1 hit
SUPFAMiSSF47933 SSF47933, 1 hit
SSF52833 SSF52833, 1 hit
PROSITEiView protein in PROSITE
PS00014 ER_TARGET, 1 hit

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

Similar proteinsi

Entry informationi

Entry nameiWBL_DROME
AccessioniPrimary (citable) accession number: O44342
Secondary accession number(s): Q4V3T7
Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: June 1, 1998
Last modified: May 23, 2018
This is version 137 of the entry and version 1 of the sequence. See 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

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