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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
 
 
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