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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

  • 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 processing Source: FlyBase
  • protein secretion Source: InterPro
  • protein targeting to Golgi Source: FlyBase
  • regulation of multicellular organism growth Source: FlyBase
  • sensory perception of pain Source: FlyBase
  • 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
Proteomesi
  • UP000000803 Componenti: Chromosome 2R

Organism-specific databases

FlyBaseiFBgn0004003. wbl.

Subcellular locationi

  • Endoplasmic reticulum lumen PROSITE-ProRule annotation

GO - Cellular componenti

  • endomembrane system Source: FlyBase
  • endoplasmic reticulum Source: UniProtKB
  • endoplasmic reticulum lumen Source: UniProtKB-SubCell
Complete GO annotation...

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.
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.
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
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...

Protein-protein interaction databases

BioGridi62871. 1 interactor.
IntActiO44342. 1 interactor.
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

eggNOGiENOG410IX2F. Eukaryota.
ENOG4111I8S. LUCA.
GeneTreeiENSGT00390000018566.
InParanoidiO44342.
KOiK09586.
OMAiDGCIKEF.
OrthoDBiEOG091G0NH4.
PhylomeDBiO44342.

Miscellaneous databases

EvolutionaryTraceiO44342.
GenomeRNAii37206.
PROiO44342.

Gene expression databases

BgeeiFBgn0004003.
ExpressionAtlasiO44342. baseline.
GenevisibleiO44342. DM.

Family and domain databases

CDDicd00238. ERp29c. 1 hit.
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...

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: November 30, 2016
This is version 123 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

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 one 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.