RUMI_DROPS
ID RUMI_DROPS Reviewed; 409 AA.
AC Q29AU6;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=O-glucosyltransferase rumi;
DE EC=2.4.1.- {ECO:0000250|UniProtKB:Q8T045};
DE Flags: Precursor;
GN Name=rumi {ECO:0000250|UniProtKB:Q8T045}; ORFNames=GA16050;
OS Drosophila pseudoobscura pseudoobscura (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=46245;
RN [1] {ECO:0000312|EMBL:EAL27253.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MV2-25 / Tucson 14011-0121.94;
RX PubMed=15632085; DOI=10.1101/gr.3059305;
RA Richards S., Liu Y., Bettencourt B.R., Hradecky P., Letovsky S.,
RA Nielsen R., Thornton K., Hubisz M.J., Chen R., Meisel R.P., Couronne O.,
RA Hua S., Smith M.A., Zhang P., Liu J., Bussemaker H.J., van Batenburg M.F.,
RA Howells S.L., Scherer S.E., Sodergren E., Matthews B.B., Crosby M.A.,
RA Schroeder A.J., Ortiz-Barrientos D., Rives C.M., Metzker M.L., Muzny D.M.,
RA Scott G., Steffen D., Wheeler D.A., Worley K.C., Havlak P., Durbin K.J.,
RA Egan A., Gill R., Hume J., Morgan M.B., Miner G., Hamilton C., Huang Y.,
RA Waldron L., Verduzco D., Clerc-Blankenburg K.P., Dubchak I., Noor M.A.F.,
RA Anderson W., White K.P., Clark A.G., Schaeffer S.W., Gelbart W.M.,
RA Weinstock G.M., Gibbs R.A.;
RT "Comparative genome sequencing of Drosophila pseudoobscura: chromosomal,
RT gene, and cis-element evolution.";
RL Genome Res. 15:1-18(2005).
CC -!- FUNCTION: Protein O-glucosyltransferase. Catalyzes the reaction that
CC attaches glucose through an O-glycosidic linkage to a conserved serine
CC residue found in the consensus sequence C-X-S-X-[PA]-C in epidermal
CC growth factor-like repeats. Regulates Notch signaling by glucosylating
CC Notch in the ER, glucosylation is required for the correct folding and
CC cleavage of Notch. {ECO:0000250|UniProtKB:Q8T045}.
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000250|UniProtKB:Q8T045}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen
CC {ECO:0000250|UniProtKB:Q8T045, ECO:0000255|PROSITE-ProRule:PRU10138}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 90 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EAL27253.1; Type=Erroneous gene model prediction; Evidence={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; CM000070; EAL27253.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_001358116.1; XM_001358079.3.
DR AlphaFoldDB; Q29AU6; -.
DR SMR; Q29AU6; -.
DR STRING; 7237.FBpp0283469; -.
DR EnsemblMetazoa; FBtr0285031; FBpp0283469; FBgn0076066.
DR GeneID; 4800928; -.
DR KEGG; dpo:Dpse_GA16050; -.
DR eggNOG; KOG2458; Eukaryota.
DR HOGENOM; CLU_041919_1_0_1; -.
DR InParanoid; Q29AU6; -.
DR OMA; DHCQYKY; -.
DR PhylomeDB; Q29AU6; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000001819; Chromosome 2.
DR Bgee; FBgn0076066; Expressed in female reproductive system and 2 other tissues.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; ISS:UniProtKB.
DR GO; GO:0140561; F:EGF-domain serine glucosyltransferase activity; IEA:EnsemblMetazoa.
DR GO; GO:0140562; F:EGF-domain serine xylosyltransferase activity; IEA:EnsemblMetazoa.
DR GO; GO:0046527; F:glucosyltransferase activity; ISS:UniProtKB.
DR GO; GO:0035251; F:UDP-glucosyltransferase activity; ISS:UniProtKB.
DR GO; GO:0045165; P:cell fate commitment; IEA:EnsemblMetazoa.
DR GO; GO:0060537; P:muscle tissue development; IEA:EnsemblMetazoa.
DR GO; GO:0045746; P:negative regulation of Notch signaling pathway; ISS:UniProtKB.
DR GO; GO:0007219; P:Notch signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0045747; P:positive regulation of Notch signaling pathway; IEA:EnsemblMetazoa.
DR GO; GO:0018242; P:protein O-linked glycosylation via serine; ISS:UniProtKB.
DR GO; GO:0042052; P:rhabdomere development; IEA:EnsemblMetazoa.
DR InterPro; IPR006598; CAP10.
DR Pfam; PF05686; Glyco_transf_90; 1.
DR SMART; SM00672; CAP10; 1.
DR PROSITE; PS00014; ER_TARGET; 1.
PE 3: Inferred from homology;
KW Disulfide bond; Endoplasmic reticulum; Glycosyltransferase;
KW Notch signaling pathway; Reference proteome; Signal; Transferase.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..409
FT /note="O-glucosyltransferase rumi"
FT /evidence="ECO:0000255"
FT /id="PRO_0000342688"
FT REGION 190..195
FT /note="Interaction with the consensus sequence C-X-S-X-
FT [PA]-C in peptide substrates"
FT /evidence="ECO:0000250|UniProtKB:Q8T045"
FT MOTIF 406..409
FT /note="Prevents secretion from ER"
FT /evidence="ECO:0000255"
FT ACT_SITE 149
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q8T045"
FT BINDING 227..231
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250|UniProtKB:Q8T045"
FT BINDING 235
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250|UniProtKB:Q8T045"
FT BINDING 274..276
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250|UniProtKB:Q8T045"
FT BINDING 292..296
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250|UniProtKB:Q8T045"
FT SITE 120
FT /note="Interaction with the consensus sequence C-X-S-X-
FT [PA]-C in peptide substrates"
FT /evidence="ECO:0000250|UniProtKB:Q8T045"
FT SITE 230
FT /note="Interaction with the consensus sequence C-X-S-X-
FT [PA]-C in peptide substrates"
FT /evidence="ECO:0000250|UniProtKB:Q8T045"
FT SITE 257
FT /note="Interaction with the consensus sequence C-X-S-X-
FT [PA]-C in peptide substrates"
FT /evidence="ECO:0000250|UniProtKB:Q8T045"
FT DISULFID 62..73
FT /evidence="ECO:0000250|UniProtKB:Q8T045"
FT DISULFID 71..376
FT /evidence="ECO:0000250|UniProtKB:Q8T045"
FT DISULFID 118..124
FT /evidence="ECO:0000250|UniProtKB:Q8T045"
FT DISULFID 280..303
FT /evidence="ECO:0000250|UniProtKB:Q8T045"
SQ SEQUENCE 409 AA; 47314 MW; EC695CBD0699DCE3 CRC64;
MLINVVLIIL LVGLNGKASG QNQGLCSPDE NASCADSSDT QDEFSFNILR KIKKALASYQ
PCSSDANDAN CSCHAAVIKS DLAPYKATGV SRQMIESSAR YGTRYKIYEK RLYREENCMF
PARCQGIEHF LLPLVATLPD MDLVINTRDY PQINMAWGNG AQGPILSFSK TKDHRDIMYP
AWTFWAGGPA TKLHPRGIGR WDLMREKLEK RAAAIPWSQK RELGFFRGSR TSDERDSLIL
LSRRNPELVE AQYTKNQGWK SPKDTLDAPP AGEVSFEDHC KYKYLFNFRG VAASFRLKHL
FLCQSLVFHV GDEWQEFFYD QLKPWVHYVP LKNYPSQQEY EELLTFFRKN DALAQEIAQR
GRDFIWQHLR MKDIKCYWRR LLKSYVKLLT YEVQPEDQLI HIQPAKDEL
