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 24-JAN-2024, entry version 162. 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. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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.FBpp0309412; -. DR PaxDb; 7227-FBpp0085698; -. 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 AGR; FB:FBgn0004003; -. 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; KYVLVKF; -. DR OrthoDB; 5403558at2759; -. 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 cell types or tissues. DR ExpressionAtlas; O44342; baseline and differential. 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; Endoplasmic reticulum resident protein 29, C-terminal domain; 1. DR Gene3D; 3.40.30.10; Glutaredoxin; 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; ENDOPLASMIC RETICULUM PROTEIN ERP29; 1. DR PANTHER; PTHR12211:SF0; ENDOPLASMIC RETICULUM RESIDENT PROTEIN 29; 1. DR Pfam; PF07749; ERp29; 1. DR Pfam; PF07912; ERp29_N; 1. DR PIRSF; PIRSF027352; ER_p29; 1. DR SUPFAM; SSF47933; ERP29 C domain-like; 1. DR SUPFAM; SSF52833; Thioredoxin-like; 1. DR PROSITE; PS00014; ER_TARGET; 1. DR Genevisible; O44342; DM. 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 //