EGH_DROME
ID EGH_DROME Reviewed; 457 AA.
AC O01346; O01347; Q9V3B0;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Beta-1,4-mannosyltransferase egh;
DE EC=2.4.1.-;
DE AltName: Full=Protein egghead;
DE AltName: Full=Protein zeste-white 4;
GN Name=egh; Synonyms=l(1)3Ae, zw4; ORFNames=CG9659;
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 / MRNA].
RX PubMed=9012507; DOI=10.1242/dev.122.12.3863;
RA Goode S., Melnick M., Chou T.-B., Perrimon N.;
RT "The neurogenic genes egghead and brainiac define a novel signaling pathway
RT essential for epithelial morphogenesis during Drosophila oogenesis.";
RL Development 122:3863-3879(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Oregon-R;
RA Simmerl E., Hollmann M., Lammermann U., Ruebsam R., Schaefer U.,
RA Buening J., Schaefer M.A.;
RT "Characterization of a viable egh allele.";
RL Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
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 GENOMIC DNA].
RC STRAIN=Oregon-R;
RX PubMed=10731137; DOI=10.1126/science.287.5461.2220;
RA Benos P.V., Gatt M.K., Ashburner M., Murphy L., Harris D., Barrell B.G.,
RA Ferraz C., Vidal S., Brun C., Demailles J., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Borkova D., Minana B., Kafatos F.C.,
RA Louis C., Siden-Kiamos I., Bolshakov S., Papagiannakis G., Spanos L.,
RA Cox S., Madueno E., de Pablos B., Modolell J., Peter A., Schoettler P.,
RA Werner M., Mourkioti F., Beinert N., Dowe G., Schaefer U., Jaeckle H.,
RA Bucheton A., Callister D.M., Campbell L.A., Darlamitsou A., Henderson N.S.,
RA McMillan P.J., Salles C., Tait E.A., Valenti P., Saunders R.D.C.,
RA Glover D.M.;
RT "From sequence to chromosome: the tip of the X chromosome of D.
RT melanogaster.";
RL Science 287:2220-2222(2000).
RN [6]
RP FUNCTION.
RX PubMed=12454022; DOI=10.1074/jbc.c200619200;
RA Wandall H.H., Pedersen J.W., Park C., Levery S.B., Pizette S., Cohen S.M.,
RA Schwientek T., Clausen H.;
RT "Drosophila egghead encodes a beta 1,4-mannosyltransferase predicted to
RT form the immediate precursor glycosphingolipid substrate for brainiac.";
RL J. Biol. Chem. 278:1411-1414(2003).
CC -!- FUNCTION: Glycosyltransferase with a proposed role in glycosphingolipid
CC biosynthesis. Neurogenic protein implicated in epithelial development.
CC Critical component of a differential oocyte-follicle cell adhesive
CC system. {ECO:0000269|PubMed:12454022}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. {ECO:0000305}.
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DR EMBL; U15602; AAB49734.1; -; mRNA.
DR EMBL; U21218; AAB49735.1; -; Genomic_DNA.
DR EMBL; AF233288; AAF43419.1; -; Genomic_DNA.
DR EMBL; AE014298; AAF45792.1; -; Genomic_DNA.
DR EMBL; AL138972; CAB72293.1; -; Genomic_DNA.
DR RefSeq; NP_001284829.1; NM_001297900.1.
DR RefSeq; NP_525052.1; NM_080313.3.
DR RefSeq; NP_726818.1; NM_166946.2.
DR AlphaFoldDB; O01346; -.
DR BioGRID; 57772; 7.
DR DIP; DIP-24087N; -.
DR IntAct; O01346; 1.
DR STRING; 7227.FBpp0070423; -.
DR CAZy; GT2; Glycosyltransferase Family 2.
DR PaxDb; O01346; -.
DR DNASU; 31239; -.
DR EnsemblMetazoa; FBtr0070439; FBpp0070423; FBgn0001404.
DR EnsemblMetazoa; FBtr0070440; FBpp0070424; FBgn0001404.
DR EnsemblMetazoa; FBtr0340091; FBpp0309090; FBgn0001404.
DR GeneID; 31239; -.
DR KEGG; dme:Dmel_CG9659; -.
DR CTD; 31239; -.
DR FlyBase; FBgn0001404; egh.
DR VEuPathDB; VectorBase:FBgn0001404; -.
DR eggNOG; ENOG502QTGI; Eukaryota.
DR GeneTree; ENSGT00520000061918; -.
DR HOGENOM; CLU_044554_0_0_1; -.
DR InParanoid; O01346; -.
DR OMA; DSDWIVH; -.
DR OrthoDB; 801915at2759; -.
DR PhylomeDB; O01346; -.
DR BioGRID-ORCS; 31239; 1 hit in 1 CRISPR screen.
DR GenomeRNAi; 31239; -.
DR PRO; PR:O01346; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0001404; Expressed in second segment of antenna (Drosophila) and 30 other tissues.
DR ExpressionAtlas; O01346; baseline and differential.
DR Genevisible; O01346; DM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; NAS:UniProtKB.
DR GO; GO:0019187; F:beta-1,4-mannosyltransferase activity; IDA:UniProtKB.
DR GO; GO:0007411; P:axon guidance; IMP:FlyBase.
DR GO; GO:0007298; P:border follicle cell migration; IMP:FlyBase.
DR GO; GO:0045165; P:cell fate commitment; IMP:UniProtKB.
DR GO; GO:0033227; P:dsRNA transport; IMP:FlyBase.
DR GO; GO:0007281; P:germ cell development; IMP:FlyBase.
DR GO; GO:0007293; P:germarium-derived egg chamber formation; IMP:FlyBase.
DR GO; GO:0006688; P:glycosphingolipid biosynthetic process; IDA:UniProtKB.
DR GO; GO:0001744; P:insect visual primordium formation; IMP:FlyBase.
DR GO; GO:0042248; P:maintenance of polarity of follicular epithelium; IMP:FlyBase.
DR GO; GO:0008049; P:male courtship behavior; IMP:FlyBase.
DR GO; GO:0016333; P:morphogenesis of follicular epithelium; IMP:FlyBase.
DR GO; GO:0045434; P:negative regulation of female receptivity, post-mating; IMP:FlyBase.
DR GO; GO:0030720; P:oocyte localization involved in germarium-derived egg chamber formation; IMP:FlyBase.
DR GO; GO:0016325; P:oocyte microtubule cytoskeleton organization; IMP:FlyBase.
DR GO; GO:0030707; P:ovarian follicle cell development; IMP:FlyBase.
DR GO; GO:0007299; P:ovarian follicle cell-cell adhesion; IMP:UniProtKB.
DR GO; GO:0048935; P:peripheral nervous system neuron development; IMP:FlyBase.
DR GO; GO:0046662; P:regulation of oviposition; IMP:FlyBase.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR027389; B_mannosylTrfase_Bre-3/Egh.
DR InterPro; IPR001173; Glyco_trans_2-like.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR PANTHER; PTHR16779; PTHR16779; 1.
DR Pfam; PF13632; Glyco_trans_2_3; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
PE 2: Evidence at transcript level;
KW Developmental protein; Glycosyltransferase; Membrane; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..457
FT /note="Beta-1,4-mannosyltransferase egh"
FT /id="PRO_0000059274"
FT TRANSMEM 8..28
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 35..55
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 57..77
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 346..366
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 378..398
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 415..435
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CONFLICT 262
FT /note="S -> R (in Ref. 1; AAB49735)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 457 AA; 51984 MW; F5781C27FAF4A4B5 CRC64;
MNSTTKHLLH CTLLITVIVT FEVFSGGIKI DENSFTLVDP WTEYGQLATV LLYLLRFLTL
LTLPQVLFNF CGLVFYNAFP EKVVLKGSPL LAPFICIRVV TRGDFPDLVK TNVLRNMNTC
LDTGLENFLI EVVTDKAVNL SQHRRIREIV VPKEYKTRTG ALFKSRALQY CLEDNVNVLN
DSDWIVHLDE ETLLTENSVR GIINFVLDGK HPFGQGLITY ANENVVNWLT TLADSFRVSD
DMGKLRLQFK LFHKPLFSWK GSYVVTQVSA ERSVSFDNGI DGSVAEDCFF AMRAFSQGYT
FNFIEGEMYE KSPFTLLDFL QQRKRWLQGI LLVVHSKMIP FKHKLLLGIS VYSWVTMPLS
TSNIIFAALY PIPCPNLVDF VCAFIAAINI YMYVFGVIKS FSLYRFGLFR FLACVLGAVC
TIPVNVVIEN VAVIWGLVGK KHKFYVVQKD VRVLETV
