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Protein

Beta-1,3-galactosyltransferase brn

Gene

brn

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

Neurogenic protein essential for the development and maintenance of epithelial structure. Required in the germline for establishing the follicular epithelium and for determining the dorsal-ventral polarity. Collaborates with Notch on the apical surface of follicle cells to mediate germline-follicle cell adhesion. Brn has a role in chorion formation.1 Publication

Catalytic activityi

UDP-alpha-D-galactose + an N-acetyl-beta-D-galactosaminyl-(1->4)-(alpha-N-acetylneuraminyl-(2->3))-beta-D-galactosyl-(1->4)-beta-D-glucosyl-(1<->1)-ceramide = UDP + a beta-D-galactosyl-(1->3)-N-acetyl-beta-D-galactosaminyl-(1->4)-(alpha-N-acetylneuraminyl-(2->3))-beta-D-galactosyl-(1->4)-beta-D-glucosyl-(1<->1)-ceramide.

GO - Molecular functioni

GO - Biological processi

  • border follicle cell migration Source: FlyBase
  • germarium-derived egg chamber formation Source: FlyBase
  • glycosphingolipid biosynthetic process Source: FlyBase
  • maintenance of polarity of follicular epithelium Source: FlyBase
  • morphogenesis of follicular epithelium Source: FlyBase
  • Notch signaling pathway Source: UniProtKB-KW
  • oogenesis Source: FlyBase
  • optic lobe placode formation Source: FlyBase
  • ovarian follicle cell-cell adhesion Source: FlyBase
  • ovarian follicle cell development Source: FlyBase
  • protein glycosylation Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, Glycosyltransferase, Transferase

Keywords - Biological processi

Notch signaling pathway

Enzyme and pathway databases

BRENDAi2.4.1.62. 1994.
SignaLinkiQ24157.

Protein family/group databases

CAZyiGT31. Glycosyltransferase Family 31.

Names & Taxonomyi

Protein namesi
Recommended name:
Beta-1,3-galactosyltransferase brn (EC:2.4.1.62)
Alternative name(s):
Brainiac protein
Neurogenic secreted-signaling protein brn
Gene namesi
Name:brn
ORF Names:CG4934
OrganismiDrosophila melanogaster (Fruit fly)Imported
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome X

Organism-specific databases

FlyBaseiFBgn0000221. brn.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 77CytoplasmicSequence analysis
Transmembranei8 – 2821Helical; Signal-anchor for type II membrane proteinSequence analysisAdd
BLAST
Topological domaini29 – 325297LumenalSequence analysisAdd
BLAST

GO - Cellular componenti

  • extracellular region Source: FlyBase
  • Golgi membrane Source: UniProtKB-SubCell
  • Golgi stack Source: UniProtKB
  • integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 325325Beta-1,3-galactosyltransferase brnPRO_0000219174Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi149 – 1491N-linked (GlcNAc...)Sequence analysis
Glycosylationi166 – 1661N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Glycoprotein

Proteomic databases

PaxDbiQ24157.
PRIDEiQ24157.

Expressioni

Gene expression databases

BgeeiQ24157.
GenevisibleiQ24157. DM.

Interactioni

Protein-protein interaction databases

BioGridi57876. 2 interactions.
IntActiQ24157. 2 interactions.
MINTiMINT-283889.
STRINGi7227.FBpp0070606.

Structurei

3D structure databases

ProteinModelPortaliQ24157.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyltransferase 31 family.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG2287. Eukaryota.
ENOG410ZZ1B. LUCA.
GeneTreeiENSGT00840000129975.
InParanoidiQ24157.
KOiK02175.
OMAiFERHFHY.
OrthoDBiEOG708W0K.
PhylomeDBiQ24157.

Family and domain databases

InterProiIPR002659. Glyco_trans_31.
IPR029044. Nucleotide-diphossugar_trans.
[Graphical view]
PANTHERiPTHR11214. PTHR11214. 1 hit.
PfamiPF01762. Galactosyl_T. 1 hit.
[Graphical view]
SUPFAMiSSF53448. SSF53448. 1 hit.

Sequencei

Sequence statusi: Complete.

Q24157-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQSKHRKLLL RCLLVLPLIL LVDYCGLLTH LHELNFERHF HYPLNDDTGS
60 70 80 90 100
GSASSGLDKF AYLRVPSFTA EVPVDQPARL TMLIKSAVGN SRRREAIRRT
110 120 130 140 150
WGYEGRFSDV HLRRVFLLGT AEDSEKDVAW ESREHGDILQ AEFTDAYFNN
160 170 180 190 200
TLKTMLGMRW ASDQFNRSEF YLFVDDDYYV SAKNVLKFLG RGRQSHQPEL
210 220 230 240 250
LFAGHVFQTS PLRHKFSKWY VSLEEYPFDR WPPYVTAGAF ILSQKALRQL
260 270 280 290 300
YAASVHLPLF RFDDVYLGIV ALKAGISLQH CDDFRFHRPA YKGPDSYSSV
310 320
IASHEFGDPE EMTRVWNECR SANYA
Length:325
Mass (Da):37,620
Last modified:May 10, 2004 - v2
Checksum:i0DF89B720F43657B
GO

Sequence cautioni

The sequence AAL48007.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti142 – 1421E → D in AAA85211 (PubMed:9012507).Curated
Sequence conflicti163 – 1631D → E in AAA85211 (PubMed:9012507).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U41449 mRNA. Translation: AAA85211.1.
AE014298 Genomic DNA. Translation: AAF45918.1.
AL033125 Genomic DNA. Translation: CAA21833.1.
BT021250 mRNA. Translation: AAX33398.1.
AY070536 mRNA. Translation: AAL48007.1. Different initiation.
RefSeqiNP_476901.1. NM_057553.5.
UniGeneiDm.1589.

Genome annotation databases

EnsemblMetazoaiFBtr0070638; FBpp0070606; FBgn0000221.
GeneIDi31358.
KEGGidme:Dmel_CG4934.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U41449 mRNA. Translation: AAA85211.1.
AE014298 Genomic DNA. Translation: AAF45918.1.
AL033125 Genomic DNA. Translation: CAA21833.1.
BT021250 mRNA. Translation: AAX33398.1.
AY070536 mRNA. Translation: AAL48007.1. Different initiation.
RefSeqiNP_476901.1. NM_057553.5.
UniGeneiDm.1589.

3D structure databases

ProteinModelPortaliQ24157.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi57876. 2 interactions.
IntActiQ24157. 2 interactions.
MINTiMINT-283889.
STRINGi7227.FBpp0070606.

Protein family/group databases

CAZyiGT31. Glycosyltransferase Family 31.

Proteomic databases

PaxDbiQ24157.
PRIDEiQ24157.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0070638; FBpp0070606; FBgn0000221.
GeneIDi31358.
KEGGidme:Dmel_CG4934.

Organism-specific databases

CTDi31358.
FlyBaseiFBgn0000221. brn.

Phylogenomic databases

eggNOGiKOG2287. Eukaryota.
ENOG410ZZ1B. LUCA.
GeneTreeiENSGT00840000129975.
InParanoidiQ24157.
KOiK02175.
OMAiFERHFHY.
OrthoDBiEOG708W0K.
PhylomeDBiQ24157.

Enzyme and pathway databases

BRENDAi2.4.1.62. 1994.
SignaLinkiQ24157.

Miscellaneous databases

GenomeRNAii31358.
NextBioi773230.
PROiQ24157.

Gene expression databases

BgeeiQ24157.
GenevisibleiQ24157. DM.

Family and domain databases

InterProiIPR002659. Glyco_trans_31.
IPR029044. Nucleotide-diphossugar_trans.
[Graphical view]
PANTHERiPTHR11214. PTHR11214. 1 hit.
PfamiPF01762. Galactosyl_T. 1 hit.
[Graphical view]
SUPFAMiSSF53448. SSF53448. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The neurogenic genes egghead and brainiac define a novel signaling pathway essential for epithelial morphogenesis during Drosophila oogenesis."
    Goode S., Melnick M., Chou T.-B., Perrimon N.
    Development 122:3863-3879(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
  2. "The genome sequence of Drosophila melanogaster."
    Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
    , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
    Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley1 Publication.
  3. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Oregon-R1 Publication.
  5. Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M., Park S., Wan K.H., Yu C., Rubin G.M., Celniker S.E.
    Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
    Tissue: Embryo.
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-325.
    Strain: Berkeley1 Publication.
    Tissue: Embryo1 Publication.

Entry informationi

Entry nameiBRN_DROME
AccessioniPrimary (citable) accession number: Q24157
Secondary accession number(s): Q5BIH4, Q8SZS9, Q9W4N0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 10, 2004
Last sequence update: May 10, 2004
Last modified: May 11, 2016
This is version 126 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.