BRN_DROME
ID BRN_DROME Reviewed; 325 AA.
AC Q24157; Q5BIH4; Q8SZS9; Q9W4N0;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2004, sequence version 2.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Beta-1,3-galactosyltransferase brn;
DE EC=2.4.1.62;
DE AltName: Full=Brainiac protein;
DE AltName: Full=Neurogenic secreted-signaling protein brn;
GN Name=brn; ORFNames=CG4934;
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:AAL48007.1};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
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] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000269|PubMed:10731132};
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] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Oregon-R {ECO:0000269|PubMed:10731137};
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Embryo;
RA Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M.,
RA Park S., Wan K.H., Yu C., Rubin G.M., Celniker S.E.;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [6] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-325.
RC STRAIN=Berkeley {ECO:0000269|PubMed:12537569};
RC TISSUE=Embryo {ECO:0000269|PubMed:12537569};
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).
CC -!- FUNCTION: Neurogenic protein essential for the development and
CC maintenance of epithelial structure. Required in the germline for
CC establishing the follicular epithelium and for determining the dorsal-
CC ventral polarity. Collaborates with Notch on the apical surface of
CC follicle cells to mediate germline-follicle cell adhesion. Brn has a
CC role in chorion formation. {ECO:0000269|PubMed:9012507}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ganglioside GM2 (d18:1(4E)) + UDP-alpha-D-galactose =
CC ganglioside GM1 (d18:1(4E)) + H(+) + UDP; Xref=Rhea:RHEA:16773,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:66914,
CC ChEBI:CHEBI:71502, ChEBI:CHEBI:77709; EC=2.4.1.62;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000305}; Single-
CC pass type II membrane protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 31 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL48007.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; U41449; AAA85211.1; -; mRNA.
DR EMBL; AE014298; AAF45918.1; -; Genomic_DNA.
DR EMBL; AL033125; CAA21833.1; -; Genomic_DNA.
DR EMBL; BT021250; AAX33398.1; -; mRNA.
DR EMBL; AY070536; AAL48007.1; ALT_INIT; mRNA.
DR RefSeq; NP_476901.1; NM_057553.5.
DR AlphaFoldDB; Q24157; -.
DR SMR; Q24157; -.
DR BioGRID; 57876; 2.
DR IntAct; Q24157; 2.
DR STRING; 7227.FBpp0070606; -.
DR CAZy; GT31; Glycosyltransferase Family 31.
DR GlyGen; Q24157; 2 sites.
DR PaxDb; Q24157; -.
DR PRIDE; Q24157; -.
DR DNASU; 31358; -.
DR EnsemblMetazoa; FBtr0070638; FBpp0070606; FBgn0000221.
DR GeneID; 31358; -.
DR KEGG; dme:Dmel_CG4934; -.
DR CTD; 31358; -.
DR FlyBase; FBgn0000221; brn.
DR VEuPathDB; VectorBase:FBgn0000221; -.
DR eggNOG; KOG2287; Eukaryota.
DR GeneTree; ENSGT00940000173583; -.
DR HOGENOM; CLU_036849_2_2_1; -.
DR InParanoid; Q24157; -.
DR OMA; ILLVDYC; -.
DR OrthoDB; 1037602at2759; -.
DR PhylomeDB; Q24157; -.
DR BRENDA; 2.4.1.62; 1994.
DR Reactome; R-DME-9037629; Lewis blood group biosynthesis.
DR SignaLink; Q24157; -.
DR BioGRID-ORCS; 31358; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 31358; -.
DR PRO; PR:Q24157; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0000221; Expressed in mouthpart and 19 other tissues.
DR Genevisible; Q24157; DM.
DR GO; GO:0000139; C:Golgi membrane; IBA:GO_Central.
DR GO; GO:0005795; C:Golgi stack; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0046981; F:beta-1,4-mannosylglycolipid beta-1,3-N-acetylglucosaminyltransferase activity; IDA:FlyBase.
DR GO; GO:0047915; F:ganglioside galactosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0016757; F:glycosyltransferase activity; IBA:GO_Central.
DR GO; GO:0008194; F:UDP-glycosyltransferase activity; IBA:GO_Central.
DR GO; GO:0007298; P:border follicle cell migration; IMP:FlyBase.
DR GO; GO:0007293; P:germarium-derived egg chamber formation; IMP:FlyBase.
DR GO; GO:0006688; P:glycosphingolipid biosynthetic process; IDA:FlyBase.
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:0016333; P:morphogenesis of follicular epithelium; IMP:FlyBase.
DR GO; GO:0007219; P:Notch signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0030707; P:ovarian follicle cell development; IMP:FlyBase.
DR GO; GO:0007299; P:ovarian follicle cell-cell adhesion; IMP:FlyBase.
DR GO; GO:0006486; P:protein glycosylation; IEA:InterPro.
DR InterPro; IPR002659; Glyco_trans_31.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR PANTHER; PTHR11214; PTHR11214; 1.
DR Pfam; PF01762; Galactosyl_T; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
PE 2: Evidence at transcript level;
KW Developmental protein; Glycoprotein; Glycosyltransferase; Golgi apparatus;
KW Membrane; Notch signaling pathway; Reference proteome; Signal-anchor;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..325
FT /note="Beta-1,3-galactosyltransferase brn"
FT /id="PRO_0000219174"
FT TOPO_DOM 1..7
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 8..28
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 29..325
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT CARBOHYD 149
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 166
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 142
FT /note="E -> D (in Ref. 1; AAA85211)"
FT /evidence="ECO:0000305"
FT CONFLICT 163
FT /note="D -> E (in Ref. 1; AAA85211)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 325 AA; 37620 MW; 0DF89B720F43657B CRC64;
MQSKHRKLLL RCLLVLPLIL LVDYCGLLTH LHELNFERHF HYPLNDDTGS GSASSGLDKF
AYLRVPSFTA EVPVDQPARL TMLIKSAVGN SRRREAIRRT WGYEGRFSDV HLRRVFLLGT
AEDSEKDVAW ESREHGDILQ AEFTDAYFNN TLKTMLGMRW ASDQFNRSEF YLFVDDDYYV
SAKNVLKFLG RGRQSHQPEL LFAGHVFQTS PLRHKFSKWY VSLEEYPFDR WPPYVTAGAF
ILSQKALRQL YAASVHLPLF RFDDVYLGIV ALKAGISLQH CDDFRFHRPA YKGPDSYSSV
IASHEFGDPE EMTRVWNECR SANYA
