WBL_DROME
ID WBL_DROME Reviewed; 257 AA.
AC O44342; Q4V3T7;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Protein windbeutel;
DE AltName: Full=Erp29 homolog;
DE Flags: Precursor;
GN Name=wbl; Synonyms=wind; ORFNames=CG7225;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP AND MUTAGENESIS OF LEU-239.
RX PubMed=9420336; DOI=10.1101/gad.12.1.120;
RA Konsolaki M., Schuepbach T.;
RT "windbeutel, a gene required for dorsoventral patterning in Drosophila,
RT encodes a protein that has homologies to vertebrate proteins of the
RT endoplasmic reticulum.";
RL Genes Dev. 12:120-131(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley;
RA Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M.,
RA Park S., Wan K.H., Yu C., Celniker S.E.;
RL Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION.
RX PubMed=9568717; DOI=10.1016/s0092-8674(00)81576-7;
RA Nilson L.A., Schuepbach T.;
RT "Localized requirements for windbeutel and pipe reveal a dorsoventral
RT prepattern within the follicular epithelium of the Drosophila ovary.";
RL Cell 93:253-262(1998).
RN [6]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=11076773; DOI=10.1242/dev.127.24.5541;
RA Sen J., Goltz J.S., Konsolaki M., Schuepbach T., Stein D.;
RT "Windbeutel is required for function and correct subcellular localization
RT of the Drosophila patterning protein Pipe.";
RL Development 127:5541-5550(2000).
RN [7]
RP INTERACTION WITH PIP, AND MUTAGENESIS OF THR-25; VAL-28; ASP-29; ARG-41;
RP ASP-50; ILE-51; ALA-52; TYR-53; LYS-58; HIS-59; GLU-60; THR-63; LYS-84;
RP TYR-86; GLU-88; PRO-106; GLU-212; ARG-215; ARG-218 AND LEU-219.
RX PubMed=15252019; DOI=10.1074/jbc.m406839200;
RA Barnewitz K., Guo C., Sevvana M., Ma Q., Sheldrick G.M., Soeling H.-D.,
RA Ferrari D.M.;
RT "Mapping of a substrate binding site in the protein disulfide isomerase-
RT related chaperone wind based on protein function and crystal structure.";
RL J. Biol. Chem. 279:39829-39837(2004).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 10-257, SUBUNIT, AND MUTAGENESIS
RP OF 24-LYS--LEU-27; ASP-31 AND TYR-55.
RX PubMed=12941941; DOI=10.1074/jbc.m307966200;
RA Ma Q., Guo C., Barnewitz K., Sheldrick G.M., Soeling H.-D., Uson I.,
RA Ferrari D.M.;
RT "Crystal structure and functional analysis of Drosophila Wind, a protein-
RT disulfide isomerase-related protein.";
RL J. Biol. Chem. 278:44600-44607(2003).
CC -!- FUNCTION: Probable chaperone protein involved in dorsoventral axis
CC patterning in early embryos. Probably acts by folding and targeting
CC pipe (pip) into the Golgi. {ECO:0000269|PubMed:11076773,
CC ECO:0000269|PubMed:9568717}.
CC -!- SUBUNIT: Homodimer. Interacts directly with pip.
CC {ECO:0000269|PubMed:12941941, ECO:0000269|PubMed:15252019}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000255|PROSITE-
CC ProRule:PRU10138}.
CC -!- TISSUE SPECIFICITY: Briefly expressed in the follicle cells of the
CC ovary, at around the time when the dorsoventral axis of the egg chamber
CC is first established. {ECO:0000269|PubMed:9420336}.
CC -!- DEVELOPMENTAL STAGE: Expressed in ovaries, early embryo (0-4 hours) and
CC adult males. Almost undetectable in female carcasses. In ovaries, it is
CC not detected in the germarium or early stage egg-chambers and is first
CC detectable in the follicle cells of stage 8 egg-chambers. The peak of
CC expression occurs in the follicle cells of stages 9 and early 10, and
CC it disappears completely before stage 11. Not expressed in the germline
CC cells (nurse cells and oocyte), with the possible exception of late
CC stage 10 nurse cells. {ECO:0000269|PubMed:9420336}.
CC -!- DOMAIN: The CXXC motif was initially thought to constitute the active
CC site of a potential protein disulfide isomerase activity. However, such
CC motif is not essential, suggesting that it has no disulfide isomerase
CC activity. Its precise role remains unclear.
CC -!- MISCELLANEOUS: 'Windbeutel' means 'profiteroles' in German.
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DR EMBL; AF025408; AAC02944.1; -; Genomic_DNA.
DR EMBL; AE013599; AAF57590.1; -; Genomic_DNA.
DR EMBL; BT023269; AAY55685.1; -; mRNA.
DR RefSeq; NP_001286609.1; NM_001299680.1.
DR RefSeq; NP_725867.1; NM_166339.2.
DR PDB; 1OVN; X-ray; 1.90 A; A/B=22-257.
DR PDB; 2C0E; X-ray; 2.35 A; A/B=23-257.
DR PDB; 2C0F; X-ray; 2.28 A; A/B=22-257.
DR PDB; 2C0G; X-ray; 1.75 A; A/B=22-257.
DR PDB; 2C1Y; X-ray; 2.25 A; A/B=22-257.
DR PDBsum; 1OVN; -.
DR PDBsum; 2C0E; -.
DR PDBsum; 2C0F; -.
DR PDBsum; 2C0G; -.
DR PDBsum; 2C1Y; -.
DR AlphaFoldDB; O44342; -.
DR SMR; O44342; -.
DR BioGRID; 62871; 2.
DR IntAct; O44342; 8.
DR STRING; 7227.FBpp0085698; -.
DR PaxDb; O44342; -.
DR PRIDE; O44342; -.
DR DNASU; 37206; -.
DR EnsemblMetazoa; FBtr0086510; FBpp0085698; FBgn0004003.
DR EnsemblMetazoa; FBtr0340470; FBpp0309412; FBgn0004003.
DR GeneID; 37206; -.
DR KEGG; dme:Dmel_CG7225; -.
DR UCSC; CG7225-RA; d. melanogaster.
DR CTD; 37206; -.
DR FlyBase; FBgn0004003; wbl.
DR VEuPathDB; VectorBase:FBgn0004003; -.
DR eggNOG; ENOG502QSHC; Eukaryota.
DR GeneTree; ENSGT00390000018566; -.
DR HOGENOM; CLU_061309_0_0_1; -.
DR InParanoid; O44342; -.
DR OMA; DGCIKEF; -.
DR OrthoDB; 1535651at2759; -.
DR PhylomeDB; O44342; -.
DR BioGRID-ORCS; 37206; 0 hits in 1 CRISPR screen.
DR EvolutionaryTrace; O44342; -.
DR GenomeRNAi; 37206; -.
DR PRO; PR:O44342; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0004003; Expressed in male reproductive gland and 31 other tissues.
DR ExpressionAtlas; O44342; baseline and differential.
DR Genevisible; O44342; DM.
DR GO; GO:0012505; C:endomembrane system; HDA:FlyBase.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
DR GO; GO:0009950; P:dorsal/ventral axis specification; IMP:UniProtKB.
DR GO; GO:0009792; P:embryo development ending in birth or egg hatching; TAS:FlyBase.
DR GO; GO:0007313; P:maternal specification of dorsal/ventral axis, oocyte, soma encoded; TAS:FlyBase.
DR GO; GO:0034975; P:protein folding in endoplasmic reticulum; IGI:FlyBase.
DR GO; GO:0009306; P:protein secretion; IEA:InterPro.
DR GO; GO:0040014; P:regulation of multicellular organism growth; IMP:FlyBase.
DR CDD; cd00238; ERp29c; 1.
DR CDD; cd03007; PDI_a_ERp29_N; 1.
DR Gene3D; 1.20.1150.12; -; 1.
DR InterPro; IPR016855; ERp29.
DR InterPro; IPR011679; ERp29_C.
DR InterPro; IPR036356; ERp29_C_sf.
DR InterPro; IPR012883; ERp29_N.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR PANTHER; PTHR12211; PTHR12211; 1.
DR Pfam; PF07749; ERp29; 1.
DR Pfam; PF07912; ERp29_N; 1.
DR PIRSF; PIRSF027352; ER_p29; 1.
DR SUPFAM; SSF47933; SSF47933; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR PROSITE; PS00014; ER_TARGET; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chaperone; Developmental protein; Endoplasmic reticulum;
KW Reference proteome; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..257
FT /note="Protein windbeutel"
FT /id="PRO_0000022690"
FT REGION 24..27
FT /note="CXXC motif"
FT MOTIF 254..257
FT /note="Prevents secretion from ER"
FT /evidence="ECO:0000305"
FT MUTAGEN 24..27
FT /note="CTGC->STGS: Affects subcellular targeting of pip."
FT /evidence="ECO:0000269|PubMed:12941941"
FT MUTAGEN 25
FT /note="T->K: Does not affect subcellular targeting of pip."
FT /evidence="ECO:0000269|PubMed:15252019"
FT MUTAGEN 28
FT /note="V->D,N: Abolishes homodimerization and subcellular
FT targeting of pip."
FT /evidence="ECO:0000269|PubMed:15252019"
FT MUTAGEN 29
FT /note="D->N: Does not affect subcellular targeting of pip."
FT /evidence="ECO:0000269|PubMed:15252019"
FT MUTAGEN 31
FT /note="D->N: Impairs homodimerization. Abolishes
FT homodimerization and subcellular targeting of pip; when
FT associated with S-41."
FT /evidence="ECO:0000269|PubMed:12941941"
FT MUTAGEN 41
FT /note="R->S: Does not affect homodimerization. Abolishes
FT homodimerization and subcellular targeting of pip; when
FT associated with N-31."
FT /evidence="ECO:0000269|PubMed:15252019"
FT MUTAGEN 50
FT /note="D->A,S: Affects subcellular targeting of pip but not
FT homodimerization."
FT /evidence="ECO:0000269|PubMed:15252019"
FT MUTAGEN 50
FT /note="D->A: Affects subcellular targeting of pip but not
FT homodimerization."
FT /evidence="ECO:0000269|PubMed:15252019"
FT MUTAGEN 51
FT /note="I->R,S: Does not affect subcellular targeting of
FT pip."
FT /evidence="ECO:0000269|PubMed:15252019"
FT MUTAGEN 52
FT /note="A->S: Does not affect subcellular targeting of pip."
FT /evidence="ECO:0000269|PubMed:15252019"
FT MUTAGEN 53
FT /note="Y->S: Affects subcellular targeting of pip."
FT /evidence="ECO:0000269|PubMed:15252019"
FT MUTAGEN 55
FT /note="Y->K: Affects subcellular targeting of pip but not
FT homodimerization."
FT /evidence="ECO:0000269|PubMed:12941941"
FT MUTAGEN 58
FT /note="K->S: Does not affect subcellular targeting of pip."
FT /evidence="ECO:0000269|PubMed:15252019"
FT MUTAGEN 59
FT /note="H->Y: Does not affect subcellular targeting of pip."
FT /evidence="ECO:0000269|PubMed:15252019"
FT MUTAGEN 60
FT /note="E->Q: Affects subcellular targeting of pip."
FT /evidence="ECO:0000269|PubMed:15252019"
FT MUTAGEN 63
FT /note="T->K: Does not affect subcellular targeting of pip."
FT /evidence="ECO:0000269|PubMed:15252019"
FT MUTAGEN 84
FT /note="K->D,Y: Affects subcellular targeting of pip."
FT /evidence="ECO:0000269|PubMed:15252019"
FT MUTAGEN 84
FT /note="K->S,N: Does not affect subcellular targeting of
FT pip."
FT /evidence="ECO:0000269|PubMed:15252019"
FT MUTAGEN 86
FT /note="Y->Q,L: Affects subcellular targeting of pip."
FT /evidence="ECO:0000269|PubMed:15252019"
FT MUTAGEN 86
FT /note="Y->S,F: Does not affect subcellular targeting of
FT pip."
FT /evidence="ECO:0000269|PubMed:15252019"
FT MUTAGEN 88
FT /note="E->K,Q: Does not affect subcellular targeting of
FT pip."
FT /evidence="ECO:0000269|PubMed:15252019"
FT MUTAGEN 106
FT /note="P->D: Affects subcellular targeting of pip."
FT /evidence="ECO:0000269|PubMed:15252019"
FT MUTAGEN 212
FT /note="E->Q: Affects subcellular targeting of pip; when
FT associated with S-219."
FT /evidence="ECO:0000269|PubMed:15252019"
FT MUTAGEN 215
FT /note="R->A: Affects subcellular targeting of pip."
FT /evidence="ECO:0000269|PubMed:15252019"
FT MUTAGEN 218
FT /note="R->D: Affects subcellular targeting of pip."
FT /evidence="ECO:0000269|PubMed:15252019"
FT MUTAGEN 219
FT /note="L->S: Affects subcellular targeting of pip; when
FT associated with Q-212."
FT /evidence="ECO:0000269|PubMed:15252019"
FT MUTAGEN 239
FT /note="L->P: In T6; induces dorsalized embryos."
FT /evidence="ECO:0000269|PubMed:9420336"
FT STRAND 28..30
FT /evidence="ECO:0007829|PDB:1OVN"
FT TURN 32..34
FT /evidence="ECO:0007829|PDB:2C0G"
FT HELIX 35..39
FT /evidence="ECO:0007829|PDB:2C0G"
FT STRAND 42..53
FT /evidence="ECO:0007829|PDB:2C0G"
FT HELIX 57..72
FT /evidence="ECO:0007829|PDB:2C0G"
FT STRAND 74..83
FT /evidence="ECO:0007829|PDB:2C0G"
FT STRAND 86..88
FT /evidence="ECO:0007829|PDB:1OVN"
FT HELIX 92..97
FT /evidence="ECO:0007829|PDB:2C0G"
FT HELIX 102..104
FT /evidence="ECO:0007829|PDB:1OVN"
FT STRAND 107..120
FT /evidence="ECO:0007829|PDB:2C0G"
FT HELIX 129..139
FT /evidence="ECO:0007829|PDB:2C0G"
FT HELIX 151..157
FT /evidence="ECO:0007829|PDB:2C0G"
FT HELIX 160..162
FT /evidence="ECO:0007829|PDB:2C0G"
FT HELIX 165..181
FT /evidence="ECO:0007829|PDB:2C0G"
FT HELIX 185..204
FT /evidence="ECO:0007829|PDB:2C0G"
FT HELIX 207..220
FT /evidence="ECO:0007829|PDB:2C0G"
FT HELIX 226..241
FT /evidence="ECO:0007829|PDB:2C0G"
SQ SEQUENCE 257 AA; 29444 MW; A2BD08EC9535B1C8 CRC64;
MMHILVTLLL VAIHSIPTTW AVTCTGCVDL DELSFEKTVE RFPYSVVKFD IAYPYGEKHE
AFTAFSKSAH KATKDLLIAT VGVKDYGELE NKALGDRYKV DDKNFPSIFL FKGNADEYVQ
LPSHVDVTLD NLKAFVSANT PLYIGRDGCI KEFNEVLKNY ANIPDAEQLK LIEKLQAKQE
QLTDPEQQQN ARAYLIYMRK IHEVGYDFLE EETKRLLRLK AGKVTEAKKE ELLRKLNILE
VFRVHKVTKT APEKEEL
