RUMI_AEDAE
ID RUMI_AEDAE Reviewed; 402 AA.
AC Q16QY8;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=O-glucosyltransferase rumi homolog;
DE EC=2.4.1.- {ECO:0000250|UniProtKB:Q8T045};
DE Flags: Precursor;
GN ORFNames=AAEL011121;
OS Aedes aegypti (Yellowfever mosquito) (Culex aegypti).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Culicinae; Aedini; Aedes; Stegomyia.
OX NCBI_TaxID=7159;
RN [1] {ECO:0000312|EMBL:EAT36834.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LVPib12;
RX PubMed=17510324; DOI=10.1126/science.1138878;
RA Nene V., Wortman J.R., Lawson D., Haas B.J., Kodira C.D., Tu Z.J.,
RA Loftus B.J., Xi Z., Megy K., Grabherr M., Ren Q., Zdobnov E.M., Lobo N.F.,
RA Campbell K.S., Brown S.E., Bonaldo M.F., Zhu J., Sinkins S.P.,
RA Hogenkamp D.G., Amedeo P., Arensburger P., Atkinson P.W., Bidwell S.L.,
RA Biedler J., Birney E., Bruggner R.V., Costas J., Coy M.R., Crabtree J.,
RA Crawford M., DeBruyn B., DeCaprio D., Eiglmeier K., Eisenstadt E.,
RA El-Dorry H., Gelbart W.M., Gomes S.L., Hammond M., Hannick L.I.,
RA Hogan J.R., Holmes M.H., Jaffe D., Johnston S.J., Kennedy R.C., Koo H.,
RA Kravitz S., Kriventseva E.V., Kulp D., Labutti K., Lee E., Li S.,
RA Lovin D.D., Mao C., Mauceli E., Menck C.F., Miller J.R., Montgomery P.,
RA Mori A., Nascimento A.L., Naveira H.F., Nusbaum C., O'Leary S.B., Orvis J.,
RA Pertea M., Quesneville H., Reidenbach K.R., Rogers Y.-H.C., Roth C.W.,
RA Schneider J.R., Schatz M., Shumway M., Stanke M., Stinson E.O.,
RA Tubio J.M.C., Vanzee J.P., Verjovski-Almeida S., Werner D., White O.R.,
RA Wyder S., Zeng Q., Zhao Q., Zhao Y., Hill C.A., Raikhel A.S., Soares M.B.,
RA Knudson D.L., Lee N.H., Galagan J., Salzberg S.L., Paulsen I.T.,
RA Dimopoulos G., Collins F.H., Bruce B., Fraser-Liggett C.M., Severson D.W.;
RT "Genome sequence of Aedes aegypti, a major arbovirus vector.";
RL Science 316:1718-1723(2007).
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}. Secreted {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 90 family.
CC {ECO:0000305}.
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DR EMBL; CH477727; EAT36834.1; -; Genomic_DNA.
DR RefSeq; XP_001655120.1; XM_001655070.1.
DR AlphaFoldDB; Q16QY8; -.
DR SMR; Q16QY8; -.
DR STRING; 7159.AAEL011121-PA; -.
DR CAZy; GT90; Glycosyltransferase Family 90.
DR GeneID; 5574413; -.
DR KEGG; aag:5574413; -.
DR VEuPathDB; VectorBase:AAEL011121; -.
DR eggNOG; KOG2458; Eukaryota.
DR HOGENOM; CLU_041919_1_0_1; -.
DR InParanoid; Q16QY8; -.
DR OMA; DHCQYKY; -.
DR OrthoDB; 1106728at2759; -.
DR PhylomeDB; Q16QY8; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000008820; Chromosome 3.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0035251; F:UDP-glucosyltransferase activity; ISS:UniProtKB.
DR GO; GO:0018242; P:protein O-linked glycosylation via serine; ISS:UniProtKB.
DR InterPro; IPR006598; CAP10.
DR Pfam; PF05686; Glyco_transf_90; 1.
DR SMART; SM00672; CAP10; 1.
PE 3: Inferred from homology;
KW Disulfide bond; Endoplasmic reticulum; Glycoprotein; Glycosyltransferase;
KW Reference proteome; Secreted; Signal; Transferase.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..402
FT /note="O-glucosyltransferase rumi homolog"
FT /id="PRO_0000342689"
FT REGION 189..194
FT /note="Interaction with the consensus sequence C-X-S-X-
FT [PA]-C in peptide substrates"
FT /evidence="ECO:0000250|UniProtKB:Q8T045"
FT ACT_SITE 149
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q8T045"
FT BINDING 226..230
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250|UniProtKB:Q8T045"
FT BINDING 234
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250|UniProtKB:Q8T045"
FT BINDING 273..275
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250|UniProtKB:Q8T045"
FT BINDING 291..295
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 229
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 256
FT /note="Interaction with the consensus sequence C-X-S-X-
FT [PA]-C in peptide substrates"
FT /evidence="ECO:0000250|UniProtKB:Q8T045"
FT CARBOHYD 71
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 67..74
FT /evidence="ECO:0000250|UniProtKB:Q8T045"
FT DISULFID 72..375
FT /evidence="ECO:0000250|UniProtKB:Q8T045"
FT DISULFID 118..124
FT /evidence="ECO:0000250|UniProtKB:Q8T045"
FT DISULFID 279..302
FT /evidence="ECO:0000250|UniProtKB:Q8T045"
SQ SEQUENCE 402 AA; 47356 MW; FE2BD601F1C7D7D0 CRC64;
MPYLEIVLAL LVLSFQLGHS DDDSGMCMAK EPCSEAPQQE TKVDLYKATD NKYVALIQEA
LASYEPCQQA NCSCHADVLK TDLRPFKGGI SEQMVERARS YGTKYQIVDH RLYRQKDCMF
PARCSGVEHF IKPNLPHLPD MELIINCRDW PQINRHWKQE KLPVLSFSKT DDYLDIMYPT
WGFWEGGPAI SLYPTGLGRW DQHRVSIKKA ADSWKWEKKK AKAFFRGSRT SDERDPLVLL
SRRKPELVDA QYTKNQAWKS PKDTLNAKPA QEVRLEDHCQ YKYLFNFRGV AASFRFKHLF
LCRSLVFHVG SEWQEFFYPS LKPWVHYVPV RVGATQEELE ELIEFFAEHD DLAREIADRG
FEHVWKHLRM KDVECYWRKL LRRYGKLVKY EVKRDHSLVE VY