WDP_DROME
ID WDP_DROME Reviewed; 677 AA.
AC Q9W266; E1NZE9; Q8IGN2; Q95U72;
DT 11-NOV-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Protein windpipe {ECO:0000303|PubMed:11804792};
DE Flags: Precursor;
GN Name=wdp {ECO:0000312|FlyBase:FBgn0034718};
GN ORFNames=CG3413 {ECO:0000312|FlyBase:FBgn0034718};
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 {ECO:0000312|EMBL:AAK77868.1};
RN [1] {ECO:0000312|EMBL:AAK77868.1}
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=11804792; DOI=10.1016/s0925-4773(01)00609-8;
RA Huff J.L., Kingsley K.L., Miller J.M., Hoshizaki D.K.;
RT "Drosophila windpipe codes for a leucine-rich repeat protein expressed in
RT the developing trachea.";
RL Mech. Dev. 111:173-176(2002).
RN [2] {ECO:0000312|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
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] {ECO:0000312|Proteomes:UP000000803}
RP GENOME REANNOTATION.
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
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] {ECO:0000312|EMBL:AAL13499.1, ECO:0000312|EMBL:AAN71448.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAL13499.1, ECO:0000312|EMBL:AAN71448.1};
RC TISSUE=Embryo {ECO:0000312|EMBL:AAN71448.1}, and
RC Head {ECO:0000312|EMBL:AAL13499.1};
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [5] {ECO:0000312|EMBL:ADO16264.1, ECO:0000312|EMBL:AGW52158.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000312|EMBL:ADO16264.1, ECO:0000312|EMBL:AGW52158.1};
RA Carlson J., Booth B., Frise E., Park S., Wan K., Yu C., Celniker S.;
RL Submitted (SEP-2013) to the EMBL/GenBank/DDBJ databases.
RN [6] {ECO:0000305}
RP FUNCTION, INTERACTION WITH DOME, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP AND DISRUPTION PHENOTYPE.
RX PubMed=25923769; DOI=10.1371/journal.pgen.1005180;
RA Ren W., Zhang Y., Li M., Wu L., Wang G., Baeg G.H., You J., Li Z., Lin X.;
RT "Windpipe controls Drosophila intestinal homeostasis by regulating JAK/STAT
RT pathway via promoting receptor endocytosis and lysosomal degradation.";
RL PLoS Genet. 11:E1005180-E1005180(2015).
CC -!- FUNCTION: Plays a role in negative regulation of the JAK/STAT pathway
CC by binding to the receptor dome and promoting its internalization for
CC subsequent lysosomal degradation, thereby reducing JAK/STAT signaling.
CC {ECO:0000269|PubMed:25923769}.
CC -!- SUBUNIT: Interacts with dome; the interaction promotes internalization
CC of dome and its subsequent lysosomal degradation.
CC {ECO:0000269|PubMed:25923769}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:25923769};
CC Single-pass type I membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: In adult intestine, expressed in both small
CC progenitor cells and large nuclei enterocytes (at protein level)
CC (PubMed:25923769). During embryogenesis, restricted to the developing
CC trachea (PubMed:11804792). {ECO:0000269|PubMed:11804792,
CC ECO:0000269|PubMed:25923769}.
CC -!- DEVELOPMENTAL STAGE: Detected in embryo, third instar larva and adult.
CC {ECO:0000269|PubMed:11804792}.
CC -!- DISRUPTION PHENOTYPE: Homozygotes are semi-lethal with a few escapers
CC displaying no visual phenotype but showing disruption of midgut
CC homeostasis under normal conditions and enhanced tissue damage-induced
CC midgut regeneration. {ECO:0000269|PubMed:25923769}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL13499.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF395331; AAK77868.1; -; mRNA.
DR EMBL; AE013599; AAF46829.1; -; Genomic_DNA.
DR EMBL; AE013599; AAF46830.1; -; Genomic_DNA.
DR EMBL; AE013599; AAM68219.1; -; Genomic_DNA.
DR EMBL; AE013599; AAM68220.1; -; Genomic_DNA.
DR EMBL; AE013599; AHN56507.1; -; Genomic_DNA.
DR EMBL; AY058270; AAL13499.1; ALT_INIT; mRNA.
DR EMBL; BT001693; AAN71448.1; -; mRNA.
DR EMBL; BT125698; ADO16264.1; -; mRNA.
DR EMBL; BT150349; AGW52158.1; -; mRNA.
DR RefSeq; NP_001286712.1; NM_001299783.1.
DR RefSeq; NP_611661.1; NM_137817.3.
DR RefSeq; NP_726187.1; NM_166524.2.
DR RefSeq; NP_726188.1; NM_166525.2.
DR RefSeq; NP_726189.1; NM_166526.2.
DR AlphaFoldDB; Q9W266; -.
DR SMR; Q9W266; -.
DR IntAct; Q9W266; 1.
DR STRING; 7227.FBpp0071760; -.
DR GlyGen; Q9W266; 4 sites.
DR SwissPalm; Q9W266; -.
DR PaxDb; Q9W266; -.
DR PRIDE; Q9W266; -.
DR EnsemblMetazoa; FBtr0071849; FBpp0071760; FBgn0034718.
DR EnsemblMetazoa; FBtr0071850; FBpp0071761; FBgn0034718.
DR EnsemblMetazoa; FBtr0071851; FBpp0071762; FBgn0034718.
DR EnsemblMetazoa; FBtr0071852; FBpp0071763; FBgn0034718.
DR EnsemblMetazoa; FBtr0342984; FBpp0309748; FBgn0034718.
DR GeneID; 37548; -.
DR KEGG; dme:Dmel_CG3413; -.
DR UCSC; CG3413-RA; d. melanogaster.
DR UCSC; CG3413-RB; d. melanogaster.
DR CTD; 37548; -.
DR FlyBase; FBgn0034718; wdp.
DR VEuPathDB; VectorBase:FBgn0034718; -.
DR eggNOG; KOG0619; Eukaryota.
DR HOGENOM; CLU_024471_0_0_1; -.
DR InParanoid; Q9W266; -.
DR OMA; PLELTHM; -.
DR OrthoDB; 284329at2759; -.
DR PhylomeDB; Q9W266; -.
DR Reactome; R-DME-193634; Axonal growth inhibition (RHOA activation).
DR Reactome; R-DME-388844; Receptor-type tyrosine-protein phosphatases.
DR SignaLink; Q9W266; -.
DR BioGRID-ORCS; 37548; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 37548; -.
DR PRO; PR:Q9W266; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0034718; Expressed in adult midgut (Drosophila) and 34 other tissues.
DR Genevisible; Q9W266; DM.
DR GO; GO:0016021; C:integral component of membrane; ISM:FlyBase.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0046426; P:negative regulation of receptor signaling pathway via JAK-STAT; IMP:UniProtKB.
DR GO; GO:2000647; P:negative regulation of stem cell proliferation; IMP:UniProtKB.
DR GO; GO:0045807; P:positive regulation of endocytosis; IMP:UniProtKB.
DR GO; GO:0008039; P:synaptic target recognition; IMP:FlyBase.
DR GO; GO:0001894; P:tissue homeostasis; IMP:UniProtKB.
DR GO; GO:0060438; P:trachea development; IEP:FlyBase.
DR Gene3D; 3.80.10.10; -; 1.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR032675; LRR_dom_sf.
DR PROSITE; PS51450; LRR; 4.
PE 1: Evidence at protein level;
KW Cell membrane; Glycoprotein; Leucine-rich repeat; Membrane;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..677
FT /note="Protein windpipe"
FT /evidence="ECO:0000255"
FT /id="PRO_0000434607"
FT TOPO_DOM 21..451
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 452..472
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 473..677
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REPEAT 91..116
FT /note="LRR 1"
FT /evidence="ECO:0000255"
FT REPEAT 118..133
FT /note="LRR 2"
FT /evidence="ECO:0000255"
FT REPEAT 134..156
FT /note="LRR 3"
FT /evidence="ECO:0000255"
FT REPEAT 158..183
FT /note="LRR 4"
FT /evidence="ECO:0000255"
FT DOMAIN 184..216
FT /note="LRRCT"
FT /evidence="ECO:0000255"
FT REGION 264..285
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 298..317
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 325..385
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 502..523
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 539..677
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 349..374
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 586..612
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 645..659
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 53
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 80
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 145
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 170
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CONFLICT 490
FT /note="R -> Q (in Ref. 4; AAN71448)"
FT /evidence="ECO:0000305"
FT CONFLICT 518
FT /note="S -> T (in Ref. 4; AAN71448)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 677 AA; 74711 MW; 5D65987391A11B0F CRC64;
MERVHLTAWL ALFLIVVANA TPTPARTPTG CPADCTCSLS QHTHKPLYHL KCNSTRGLRL
TEKTFQSTVP VHSIDLSHLN LTRLSHLLDK LPELTSADLS HNQLKDLGHL GKGLKRLNLK
HNQLTSDKLR KLPQHLQVLN LQHNNITHLP LELTHMHQLH QLELSHNAIN CSCQTLEVRN
WLVERIVYME HPVVCSYPLE FRGRSWLQLK QDEICKKEKY QWFDTEENEL MMGDQPAAVS
AEREDEEELG KDFLPIVGNP AATAKKVRSP QIPLPSDQVE GSGDLSETNM ELKLPEETVA
EPEAAESQLV DAAASPSVLE EHIVKDEDED DEGSGSGGGL LIIPDPSKVK ITSEDDIDSD
GKPEESDVRP LENPENSENP DTVFSNKIGI YEGDQEEKKP VEEDNIVPVV MTNLDTGLES
DVVTDGPLDS SKESEDILTA KIGKPKDDSS AIYYLLAVIG LIVVGLVLFV AIKRCKYDSN
AAARDAEAQR QTELLDMDKK QLGKPLHKNG HGNGQEHSPL IGEKTKLDEA QIVKKPYENG
EAKDGAGQQP LLNGNGSANG GTKEAPETGE PAAHEYYPIT PRYPTPQSPR ASKYAQQQQL
AEQNNNEPDG AYLPSSPKSG RYSPVYSPET GRVKIKLTET PKPKTPMLVT RSKSNAGDII
TTPVRPIEPT HQVINGH
