O44342 (WBL_DROME) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Protein windbeutel

Alternative name(s):
Erp29 homolog

Gene names

Name:	wbl
Synonyms:	wind
ORF Names:	CG7225

Organism

Drosophila melanogaster (Fruit fly) [Reference proteome]

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Protostomia › Ecdysozoa › Panarthropoda › Arthropoda › Mandibulata › Pancrustacea › Hexapoda › Insecta › Dicondylia › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Eremoneura › Cyclorrhapha › Schizophora › Acalyptratae › Ephydroidea › Drosophilidae › Drosophilinae › Drosophilini › Drosophilina › Drosophiliti › Drosophila › Sophophora › melanogaster group › melanogaster subgroup

Protein attributes

Sequence length	257 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.

Ontologies

Keywords
Cellular component	Endoplasmic reticulum
Domain	Signal
Molecular function	Chaperone Developmental protein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	Toll signaling pathway Traceable author statement PubMed 1425342. Source: FlyBase embryo development ending in birth or egg hatching Traceable author statement PubMed 12766950. Source: FlyBase maternal specification of dorsal/ventral axis, oocyte, soma encoded Traceable author statement PubMed 1425342. Source: FlyBase protein processing Inferred from genetic interaction PubMed 1425342. Source: FlyBase protein secretion Inferred from electronic annotation. Source: InterPro protein targeting to Golgi Inferred from genetic interaction Ref.6. Source: FlyBase regulation of multicellular organism growth Inferred from mutant phenotype PubMed 16049108. Source: FlyBase
Cellular_component	endoplasmic reticulum Inferred from direct assay Ref.6. Source: UniProtKB endoplasmic reticulum lumen Inferred from electronic annotation. Source: UniProtKB-SubCell
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 21

21

Potential

Chain

22 – 257

236

Protein windbeutel

PRO_0000022690

Regions

Region

24 – 27

4

CXXC motif

Motif

254 – 257

4

Prevents secretion from ER Probable

Experimental info

Mutagenesis

24 – 27

4

CTGC → STGS: Affects subcellular targeting of pip. Ref.8

Mutagenesis

25

1

T → K: Does not affect subcellular targeting of pip. Ref.7

Mutagenesis

28

1

V → D or N: Abolishes homodimerization and subcellular targeting of pip. Ref.7

Mutagenesis

29

1

D → N: Does not affect subcellular targeting of pip. Ref.7

Mutagenesis

31

1

D → N: Impairs homodimerization. Abolishes homodimerization and subcellular targeting of pip; when associated with S-41. Ref.8

Mutagenesis

41

1

R → S: Does not affect homodimerization. Abolishes homodimerization and subcellular targeting of pip; when associated with N-31. Ref.7

Mutagenesis

50

1

D → A or S: Affects subcellular targeting of pip but not homodimerization. Ref.7

Mutagenesis

50

1

D → A: Affects subcellular targeting of pip but not homodimerization. Ref.7

Mutagenesis

51

1

I → R or S: Does not affect subcellular targeting of pip. Ref.7

Mutagenesis

52

1

A → S: Does not affect subcellular targeting of pip. Ref.7

Mutagenesis

53

1

Y → S: Affects subcellular targeting of pip. Ref.7

Mutagenesis

55

1

Y → K: Affects subcellular targeting of pip but not homodimerization. Ref.8

Mutagenesis

58

1

K → S: Does not affect subcellular targeting of pip. Ref.7

Mutagenesis

59

1

H → Y: Does not affect subcellular targeting of pip. Ref.7

Mutagenesis

60

1

E → Q: Affects subcellular targeting of pip. Ref.7

Mutagenesis

63

1

T → K: Does not affect subcellular targeting of pip. Ref.7

Mutagenesis

84

1

K → D or Y: Affects subcellular targeting of pip. Ref.7

Mutagenesis

84

1

K → S or N: Does not affect subcellular targeting of pip. Ref.7

Mutagenesis

86

1

Y → Q or L: Affects subcellular targeting of pip. Ref.7

Mutagenesis

86

1

Y → S or F: Does not affect subcellular targeting of pip. Ref.7

Mutagenesis

88

1

E → K or Q: Does not affect subcellular targeting of pip. Ref.7

Mutagenesis

106

1

P → D: Affects subcellular targeting of pip. Ref.7

Mutagenesis

212

1

E → Q: Affects subcellular targeting of pip; when associated with S-219. Ref.7

Mutagenesis

215

1

R → A: Affects subcellular targeting of pip. Ref.7

Mutagenesis

218

1

R → D: Affects subcellular targeting of pip. Ref.7

Mutagenesis

219

1

L → S: Affects subcellular targeting of pip; when associated with Q-212. Ref.7

Mutagenesis

239

1

L → P in T6; induces dorsalized embryos. Ref.1

Secondary structure

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257

Helix Strand Turn

Details...

Beta strand

28 – 30

3

Turn

32 – 34

3

Helix

35 – 39

5

Beta strand

42 – 53

12

Helix

57 – 72

16

Beta strand

74 – 83

10

Beta strand

86 – 88

3

Helix

92 – 97

6

Helix

102 – 104

3

Beta strand

107 – 120

14

Helix

129 – 139

11

Helix

151 – 157

7

Helix

160 – 162

3

Helix

165 – 181

17

Helix

185 – 204

20

Helix

207 – 220

14

Helix

226 – 241

16

Sequences

	Sequence		Length	Mass (Da)
	O44342 [UniParc]. Last modified June 1, 1998. Version 1. Checksum: A2BD08EC9535B1C8	FASTA	257	29,444
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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.

RefSeq

NP_725867.1. NM_166339.1.

UniGene

Dm.23938.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

O44342.

SMR

O44342. Positions 24-252.

ModBase

Search...

Protein-protein interaction databases

STRING

7227.FBpp0085698.

Proteomic databases

PaxDb

O44342.

PRIDE

O44342.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblMetazoa

FBtr0086510; FBpp0085698; FBgn0004003.

GeneID

37206.

KEGG

dme:Dmel_CG7225.

UCSC

CG7225-RA. d. melanogaster.

Organism-specific databases

CTD

37206.

FlyBase

FBgn0004003. wbl.

Phylogenomic databases

eggNOG

NOG82861.

GeneTree

ENSGT00390000018566.

InParanoid

O44342.

KO

K09586.

OMA

TITFYKV.

OrthoDB

EOG4VQ85Q.

PhylomeDB

O44342.

Gene expression databases

Bgee

O44342.

GermOnline

CG7225. Drosophila melanogaster.

Family and domain databases

Gene3D

1.20.1150.12. 1 hit.
3.40.30.10. 1 hit.

InterPro

IPR016855. ER_p29.
IPR011679. ER_p29_C.
IPR012883. ERp29_N.
IPR012336. Thioredoxin-like_fold.
[Graphical view]

Pfam

PF07749. ERp29. 1 hit.
PF07912. ERp29_N. 1 hit.
[Graphical view]

PIRSF

PIRSF027352. ER_p29. 1 hit.

SUPFAM

SSF47933. ERP29_C. 1 hit.
SSF52833. Thiordxn-like_fd. 1 hit.

PROSITE

PS00014. ER_TARGET. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

O44342.

GenomeRNAi

37206.

NextBio

802516.

Entry information

Entry name

WBL_DROME

Accession

Primary (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 3, 2013
This is version 98 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Drosophila annotation project