C1GLT_DROME
ID C1GLT_DROME Reviewed; 388 AA.
AC Q7K237; A4V0G7;
DT 01-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Glycoprotein-N-acetylgalactosamine 3-beta-galactosyltransferase 1;
DE EC=2.4.1.122 {ECO:0000250|UniProtKB:Q9NS00};
DE AltName: Full=Core 1 O-glycan T-synthase;
DE AltName: Full=Core 1 UDP-galactose:N-acetylgalactosamine-alpha-R beta 1,3-galactosyltransferase 1;
DE AltName: Full=Core 1 beta1,3-galactosyltransferase 1;
DE Short=C1GalT1;
DE Short=Core 1 beta3-Gal-T1;
GN Name=C1GalTA; ORFNames=CG9520;
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 [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 [2]
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 [3]
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 [4]
RP FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=18985719; DOI=10.1002/dvdy.21775;
RA Lin Y.R., Reddy B.V., Irvine K.D.;
RT "Requirement for a core 1 galactosyltransferase in the Drosophila nervous
RT system.";
RL Dev. Dyn. 237:3703-3714(2008).
CC -!- FUNCTION: Glycosyltransferase that generates the core 1 O-glycan Gal-
CC beta1-3GalNAc-alpha1-Ser/Thr (T antigen), which is a precursor for many
CC extended O-glycans in glycoproteins. {ECO:0000269|PubMed:18985719}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an N-acetyl-alpha-D-galactosaminyl derivative + UDP-alpha-D-
CC galactose = a beta-D-galactosyl-(1->3)-N-acetyl-alpha-D-
CC galactosaminyl derivative + H(+) + UDP; Xref=Rhea:RHEA:15621,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:28257, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:66914, ChEBI:CHEBI:133470; EC=2.4.1.122;
CC Evidence={ECO:0000250|UniProtKB:Q9NS00};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC -!- SUBUNIT: Homodimer; disulfide-linked. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type II
CC membrane protein {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: In stage 12 embryos, expression is seen in the
CC amnioserosa and by stage 16, also in the central nervous system,
CC predominantly the ventral nerve cord and brain. Also in embryos,
CC preferential expression is seen in the ejaculatory duct and the nurse
CC cells (but not the oocyte). In larvae, expression is seen throughout
CC the nervous system and imaginal disks. Adult females show expression in
CC the nurse cells and adult males in the ejaculatory duct.
CC {ECO:0000269|PubMed:18985719}.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically in the
CC embryo and throughout development. {ECO:0000269|PubMed:18985719}.
CC -!- DISRUPTION PHENOTYPE: Morphogenetic defects in which the ventral nerve
CC cord is greatly elongated and the brain hemispheres are misshapen.
CC {ECO:0000269|PubMed:18985719}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 31 family. Beta3-Gal-T
CC subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE014134; AAF52724.1; -; Genomic_DNA.
DR EMBL; AE014134; AAF52725.1; -; Genomic_DNA.
DR EMBL; AY061283; AAL28831.1; -; mRNA.
DR RefSeq; NP_609258.1; NM_135414.3.
DR RefSeq; NP_723427.1; NM_164839.2.
DR RefSeq; NP_723428.1; NM_164840.2.
DR PDB; 7Q4I; X-ray; 2.40 A; A/B=73-388.
DR PDBsum; 7Q4I; -.
DR AlphaFoldDB; Q7K237; -.
DR SMR; Q7K237; -.
DR BioGRID; 60328; 20.
DR STRING; 7227.FBpp0079388; -.
DR CAZy; GT31; Glycosyltransferase Family 31.
DR GlyGen; Q7K237; 1 site.
DR PaxDb; Q7K237; -.
DR PRIDE; Q7K237; -.
DR DNASU; 34215; -.
DR EnsemblMetazoa; FBtr0079788; FBpp0079388; FBgn0032078.
DR EnsemblMetazoa; FBtr0079789; FBpp0079389; FBgn0032078.
DR EnsemblMetazoa; FBtr0079790; FBpp0079390; FBgn0032078.
DR GeneID; 34215; -.
DR KEGG; dme:Dmel_CG9520; -.
DR CTD; 34215; -.
DR FlyBase; FBgn0032078; C1GalTA.
DR VEuPathDB; VectorBase:FBgn0032078; -.
DR eggNOG; KOG2246; Eukaryota.
DR GeneTree; ENSGT00940000164002; -.
DR HOGENOM; CLU_035857_0_0_1; -.
DR InParanoid; Q7K237; -.
DR OMA; PYGIINT; -.
DR OrthoDB; 1407357at2759; -.
DR PhylomeDB; Q7K237; -.
DR BRENDA; 2.4.1.122; 1994.
DR Reactome; R-DME-913709; O-linked glycosylation of mucins.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 34215; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 34215; -.
DR PRO; PR:Q7K237; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0032078; Expressed in embryonic/larval hemocyte (Drosophila) and 35 other tissues.
DR ExpressionAtlas; Q7K237; baseline and differential.
DR Genevisible; Q7K237; DM.
DR GO; GO:0016021; C:integral component of membrane; ISS:UniProtKB.
DR GO; GO:0048531; F:beta-1,3-galactosyltransferase activity; IDA:FlyBase.
DR GO; GO:0016263; F:glycoprotein-N-acetylgalactosamine 3-beta-galactosyltransferase activity; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0021551; P:central nervous system morphogenesis; IMP:FlyBase.
DR GO; GO:0009247; P:glycolipid biosynthetic process; IDA:FlyBase.
DR GO; GO:0055001; P:muscle cell development; IMP:FlyBase.
DR GO; GO:1902037; P:negative regulation of hematopoietic stem cell differentiation; IMP:FlyBase.
DR GO; GO:0007528; P:neuromuscular junction development; IMP:FlyBase.
DR GO; GO:0016267; P:O-glycan processing, core 1; IMP:FlyBase.
DR GO; GO:0006486; P:protein glycosylation; IDA:FlyBase.
DR GO; GO:0051489; P:regulation of filopodium assembly; IMP:FlyBase.
DR InterPro; IPR026842; C1GALT1.
DR InterPro; IPR003378; Fringe-like.
DR PANTHER; PTHR23033:SF13; PTHR23033:SF13; 1.
DR Pfam; PF02434; Fringe; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Disulfide bond; Glycoprotein; Glycosyltransferase; Magnesium;
KW Membrane; Metal-binding; Reference proteome; Signal-anchor; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..388
FT /note="Glycoprotein-N-acetylgalactosamine 3-beta-
FT galactosyltransferase 1"
FT /id="PRO_0000285072"
FT TOPO_DOM 1..21
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 22..42
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 43..388
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 368..388
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 368..382
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 88
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 388 AA; 44323 MW; BC71E4F97CE1178A CRC64;
MTANSLLGRS ILNEGRSNKR SFVSLIVGLI VGFCLAELFV YSTPERSEFM PYDGHRHGDV
NDAHHSHDMM EMSGPEQDVG GHEHVHENST IAERLYSEVR VLCWIMTNPS NHQKKARHVK
RTWGKRCNKL IFMSSAKDDE LDAVALPVGE GRNNLWGKTK EAYKYIYEHH INDADWFLKA
DDDTYTIVEN MRYMLYPYSP ETPVYFGCKF KPYVKQGYMS GGAGYVLSRE AVRRFVVEAL
PNPKLCKSDN SGAEDVEIGK CLQNVNVLAG DSRDSNGRGR FFPFVPEHHL IPSHTDKKFW
YWQYIFYKTD EGLDCCSDNA ISFHYVSPNQ MYVLDYLIYH LRPYGIINTP DALPNKLAVG
ELMPEIKEQA TESTSDGVSK RSAETKTQ
