DOME_DROME
ID DOME_DROME Reviewed; 1282 AA.
AC Q9VWE0;
DT 02-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=Cytokine receptor;
DE AltName: Full=Protein domeless;
DE Flags: Precursor;
GN Name=dome; ORFNames=CG14226;
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 [MRNA], FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=11696329; DOI=10.1016/s0960-9822(01)00524-3;
RA Brown S., Hu N., Castelli-Gair Hombria J.;
RT "Identification of the first invertebrate interleukin JAK/STAT receptor,
RT the Drosophila gene domeless.";
RL Curr. Biol. 11:1700-1705(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=12403714; DOI=10.1242/dev.00116;
RA Ghiglione C., Devergne O., Georgenthum E., Carballes F., Medioni C.,
RA Cerezo D., Noselli S.;
RT "The Drosophila cytokine receptor Domeless controls border cell migration
RT and epithelial polarization during oogenesis.";
RL Development 129:5437-5447(2002).
RN [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-976, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
RN [7]
RP INTERACTION WITH WDP, AND LYSOSOMAL DEGRADATION.
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: Critical for epithelial morphogenesis during oogenesis;
CC border cell migration. Required in the germarium for the polarization
CC of follicle cells during encapsulation of germline cells. Required for
CC embryonic segmentation and trachea specification. Essential receptor
CC molecule for upd and JAK/STAT signaling during oogenesis.
CC {ECO:0000269|PubMed:11696329, ECO:0000269|PubMed:12403714}.
CC -!- SUBUNIT: Interacts with wdp; the interaction promotes internalization
CC of dome and its subsequent lysosomal degradation; thereby reducing
CC JAK/STAT signaling. {ECO:0000269|PubMed:25923769}.
CC -!- INTERACTION:
CC Q9VWE0; Q9VWE1: et; NbExp=4; IntAct=EBI-119639, EBI-92671;
CC -!- SUBCELLULAR LOCATION: Apicolateral cell membrane
CC {ECO:0000269|PubMed:12403714}; Single-pass type I membrane protein
CC {ECO:0000269|PubMed:12403714}. Note=Apicolateral membranes in follical
CC cells.
CC -!- TISSUE SPECIFICITY: In stage 11 embryos, tracheal pits show highest
CC expression, at stage 14 high expression is detected in the posterior
CC spiracles, gut and head. {ECO:0000269|PubMed:11696329}.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically in
CC embryos. {ECO:0000269|PubMed:11696329}.
CC -!- PTM: Undergoes lysosomal degradation. {ECO:0000269|PubMed:25923769}.
CC -!- SIMILARITY: Belongs to the type I cytokine receptor family.
CC {ECO:0000305}.
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DR EMBL; AJ420377; CAD12503.1; -; mRNA.
DR EMBL; AY147847; AAN64333.1; -; mRNA.
DR EMBL; AE014298; AAF49002.1; -; Genomic_DNA.
DR EMBL; AY075427; AAL68243.1; -; mRNA.
DR RefSeq; NP_523412.1; NM_078688.3.
DR AlphaFoldDB; Q9VWE0; -.
DR BioGRID; 59272; 37.
DR DIP; DIP-19869N; -.
DR IntAct; Q9VWE0; 2.
DR STRING; 7227.FBpp0074525; -.
DR GlyGen; Q9VWE0; 23 sites.
DR iPTMnet; Q9VWE0; -.
DR PaxDb; Q9VWE0; -.
DR PRIDE; Q9VWE0; -.
DR DNASU; 32976; -.
DR EnsemblMetazoa; FBtr0074756; FBpp0074525; FBgn0043903.
DR GeneID; 32976; -.
DR KEGG; dme:Dmel_CG14226; -.
DR CTD; 32976; -.
DR FlyBase; FBgn0043903; dome.
DR VEuPathDB; VectorBase:FBgn0043903; -.
DR eggNOG; ENOG502QTMM; Eukaryota.
DR HOGENOM; CLU_260365_0_0_1; -.
DR InParanoid; Q9VWE0; -.
DR OMA; NLTYCQR; -.
DR OrthoDB; 63696at2759; -.
DR PhylomeDB; Q9VWE0; -.
DR Reactome; R-DME-209209; Formation of the activated receptor complex.
DR Reactome; R-DME-209228; Formation of the activated STAT92E dimer and transport to the nucleus.
DR Reactome; R-DME-210688; Dephosphorylation by PTP61F phosphatases.
DR Reactome; R-DME-6798695; Neutrophil degranulation.
DR SignaLink; Q9VWE0; -.
DR BioGRID-ORCS; 32976; 0 hits in 3 CRISPR screens.
DR ChiTaRS; dome; fly.
DR GenomeRNAi; 32976; -.
DR PRO; PR:Q9VWE0; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0043903; Expressed in oviduct (Drosophila) and 34 other tissues.
DR ExpressionAtlas; Q9VWE0; baseline and differential.
DR Genevisible; Q9VWE0; DM.
DR GO; GO:0016324; C:apical plasma membrane; IDA:FlyBase.
DR GO; GO:0016327; C:apicolateral plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0004896; F:cytokine receptor activity; IDA:FlyBase.
DR GO; GO:0046982; F:protein heterodimerization activity; IPI:FlyBase.
DR GO; GO:1990782; F:protein tyrosine kinase binding; IPI:FlyBase.
DR GO; GO:0097678; F:SOCS family protein binding; IPI:FlyBase.
DR GO; GO:0097677; F:STAT family protein binding; IPI:FlyBase.
DR GO; GO:0007350; P:blastoderm segmentation; IMP:FlyBase.
DR GO; GO:0007298; P:border follicle cell migration; IMP:FlyBase.
DR GO; GO:0001745; P:compound eye morphogenesis; IMP:FlyBase.
DR GO; GO:0019221; P:cytokine-mediated signaling pathway; IGI:FlyBase.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; HMP:FlyBase.
DR GO; GO:0007442; P:hindgut morphogenesis; IMP:FlyBase.
DR GO; GO:0045475; P:locomotor rhythm; IMP:FlyBase.
DR GO; GO:0007616; P:long-term memory; IMP:FlyBase.
DR GO; GO:0007424; P:open tracheal system development; IMP:FlyBase.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:FlyBase.
DR GO; GO:0007259; P:receptor signaling pathway via JAK-STAT; IDA:FlyBase.
DR GO; GO:0042246; P:tissue regeneration; IMP:FlyBase.
DR GO; GO:0007472; P:wing disc morphogenesis; IMP:FlyBase.
DR CDD; cd00063; FN3; 3.
DR Gene3D; 2.60.40.10; -; 5.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR Pfam; PF00041; fn3; 2.
DR SMART; SM00060; FN3; 5.
DR SUPFAM; SSF49265; SSF49265; 4.
DR PROSITE; PS50853; FN3; 6.
PE 1: Evidence at protein level;
KW Cell membrane; Developmental protein; Disulfide bond; Glycoprotein;
KW Membrane; Phosphoprotein; Receptor; Reference proteome; Repeat; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..1282
FT /note="Cytokine receptor"
FT /id="PRO_0000010999"
FT TOPO_DOM 24..889
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 890..910
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 911..1282
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 124..220
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 227..327
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 329..431
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 436..535
FT /note="Fibronectin type-III 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 537..631
FT /note="Fibronectin type-III 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 635..735
FT /note="Fibronectin type-III 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 736..836
FT /note="Fibronectin type-III 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REGION 989..1092
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1238..1258
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1030..1063
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1064..1092
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 976
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT CARBOHYD 44
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 86
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 87
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 114
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 143
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 156
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 184
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 230
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 235
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 278
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 298
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 310
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 376
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 448
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 466
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 568
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 581
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 626
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 676
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 703
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 777
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 790
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 862
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 47..106
FT /evidence="ECO:0000250"
FT DISULFID 132..142
FT /evidence="ECO:0000250"
FT DISULFID 173..183
FT /evidence="ECO:0000250"
FT DISULFID 472..482
FT /evidence="ECO:0000250"
SQ SEQUENCE 1282 AA; 142361 MW; 22CE960963B17011 CRC64;
MVAQEQLVLL LMLLAGCRGG ANAILDPGWV IPSKVEQLIG GDFNLSCTLN EDYFNGKSAE
DCPVEKLYFT GGGRVYRDSK HIRILNNTTI LFSDTNAVEQ ENDYHCMCDE YVINKSKVYV
GTRPLLVRDF NCLDYDFQFM VCNFTQPPNT VITKYNISYN TNNDWRYSNT LDCNFDSAPV
VTCNLTDDNY KRFSETFYFR LSISNALGHE TQPITINHFE RLVPARPGQN LTLLNRTESS
VCLSWEMPRR SNYNRGLVWQ VRVTPQNFEP ITRPSWRNHT LTIKDTLCLT ELPFAGYNYT
LRVRVRANQN NTLWSEPMIY AFATAPAPPR RPPRVTYGSF YVYSSEKAMR FYWEPLEEHE
LNGPDFRYSI SEYRINGTAV DPGLIKVESN SAMIDHWSMS AVHHFLIRSS NSQGLSVNAT
PMTIGPISNR DFKVREPRNI RSVYHPTNKS YTLSWDPPSD QRELQNYTVF WCVPKPGLQS
ECEGSIRFAE VASGLHHFTT SPDQLLTLHM AVSANYQSHN TGLHWAICSS DKKDDLAKME
PSIDVATSTS LTVSWSERVC AVILAGYNLT YCQRSAGRPD NCTTVTIDRY TNKHVIQNLV
PYTDYSVKML MYSDSRVSKY SDELVNRTGE AAPSQPRELQ LIRVTSDSVE LAWKPPLLAN
GVVRAYEGTF RSLHDNVTDT FRVSASADEL VNNEKPITYR LGNLTAFTKY EISVRARTVY
PSEPSNVILF STAIGVPSPP QLYVINNPDQ SSRLDWEPPR TPAGRIDFYE ISLRDNNASC
LTSTILPGRN LSYVMATPRC TSHNPFQLAV RAINVEQHPQ LNGADAAEGA VLLMSTNGKG
CEARTDALGE EERLQFEAYA ANMTAYRLYR SDWGIYGFIC TPDTHSVKAM YQTIEVTVAI
LVLGVIFYLV YKKYRKMSDI GLVLPQGIME TMKKPIDMGG LGLGLGPDSS VSGGIVCTRV
DDSPPYTPQD LPHDFSSCGS ESSKLLLRTA SSSGGGGCVD RDGYDDNHET GPISAVGPPT
SYLAMRHGLL VQNDRERERE RDREQERERE QQQQQRESEM DREQSCTNGY IKPTQMKSWG
GNGPSDNDHT FSVPSTAMTA PMSQPLSQIP LSGYVPVPIP QSRFNPAPVQ PFGSPAVPSA
ATAAAASTFF PPAHLLNMDN YVQASDLHKL KPLVAAPLSQ TGGPAFAGSS PATSPPLQLP
PVHAASPAAA TPKMADIGYT TMEQLQLTGL IKPPLAATVG SPTHAAGGAP GGGNQHSRLQ
PQINGYVTPQ DLNAMAHNRH VL
