RUMI_ANOGA
ID RUMI_ANOGA Reviewed; 399 AA.
AC A0NDG6;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=O-glucosyltransferase rumi homolog;
DE EC=2.4.1.- {ECO:0000250|UniProtKB:Q8T045};
DE Flags: Precursor;
GN ORFNames=AGAP004267;
OS Anopheles gambiae (African malaria mosquito).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=7165;
RN [1] {ECO:0000312|EMBL:EAU76986.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PEST;
RX PubMed=12364791; DOI=10.1126/science.1076181;
RA Holt R.A., Subramanian G.M., Halpern A., Sutton G.G., Charlab R.,
RA Nusskern D.R., Wincker P., Clark A.G., Ribeiro J.M.C., Wides R.,
RA Salzberg S.L., Loftus B.J., Yandell M.D., Majoros W.H., Rusch D.B., Lai Z.,
RA Kraft C.L., Abril J.F., Anthouard V., Arensburger P., Atkinson P.W.,
RA Baden H., de Berardinis V., Baldwin D., Benes V., Biedler J., Blass C.,
RA Bolanos R., Boscus D., Barnstead M., Cai S., Center A., Chaturverdi K.,
RA Christophides G.K., Chrystal M.A.M., Clamp M., Cravchik A., Curwen V.,
RA Dana A., Delcher A., Dew I., Evans C.A., Flanigan M.,
RA Grundschober-Freimoser A., Friedli L., Gu Z., Guan P., Guigo R.,
RA Hillenmeyer M.E., Hladun S.L., Hogan J.R., Hong Y.S., Hoover J.,
RA Jaillon O., Ke Z., Kodira C.D., Kokoza E., Koutsos A., Letunic I.,
RA Levitsky A.A., Liang Y., Lin J.-J., Lobo N.F., Lopez J.R., Malek J.A.,
RA McIntosh T.C., Meister S., Miller J.R., Mobarry C., Mongin E., Murphy S.D.,
RA O'Brochta D.A., Pfannkoch C., Qi R., Regier M.A., Remington K., Shao H.,
RA Sharakhova M.V., Sitter C.D., Shetty J., Smith T.J., Strong R., Sun J.,
RA Thomasova D., Ton L.Q., Topalis P., Tu Z.J., Unger M.F., Walenz B.,
RA Wang A.H., Wang J., Wang M., Wang X., Woodford K.J., Wortman J.R., Wu M.,
RA Yao A., Zdobnov E.M., Zhang H., Zhao Q., Zhao S., Zhu S.C., Zhimulev I.,
RA Coluzzi M., della Torre A., Roth C.W., Louis C., Kalush F., Mural R.J.,
RA Myers E.W., Adams M.D., Smith H.O., Broder S., Gardner M.J., Fraser C.M.,
RA Birney E., Bork P., Brey P.T., Venter J.C., Weissenbach J., Kafatos F.C.,
RA Collins F.H., Hoffman S.L.;
RT "The genome sequence of the malaria mosquito Anopheles gambiae.";
RL Science 298:129-149(2002).
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; AAAB01008880; EAU76986.1; -; Genomic_DNA.
DR RefSeq; XP_001230897.1; XM_001230896.3.
DR AlphaFoldDB; A0NDG6; -.
DR SMR; A0NDG6; -.
DR STRING; 7165.AGAP004267-PA; -.
DR PaxDb; A0NDG6; -.
DR PRIDE; A0NDG6; -.
DR GeneID; 4576887; -.
DR KEGG; aga:AgaP_AGAP004267; -.
DR CTD; 4576887; -.
DR VEuPathDB; VectorBase:AGAP004267; -.
DR eggNOG; KOG2458; Eukaryota.
DR HOGENOM; CLU_041919_1_0_1; -.
DR InParanoid; A0NDG6; -.
DR OMA; DHCQYKY; -.
DR OrthoDB; 1106728at2759; -.
DR PhylomeDB; A0NDG6; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000007062; Chromosome 2R.
DR GO; GO:0012505; C:endomembrane system; IBA:GO_Central.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0046527; F:glucosyltransferase activity; IBA:GO_Central.
DR GO; GO:0035251; F:UDP-glucosyltransferase activity; ISS:UniProtKB.
DR GO; GO:0035252; F:UDP-xylosyltransferase activity; IBA:GO_Central.
DR GO; GO:0045747; P:positive regulation of Notch signaling pathway; IBA:GO_Central.
DR GO; GO:0006493; P:protein O-linked glycosylation; IBA:GO_Central.
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..18
FT /evidence="ECO:0000255"
FT CHAIN 19..399
FT /note="O-glucosyltransferase rumi homolog"
FT /id="PRO_0000342690"
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 224..228
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250|UniProtKB:Q8T045"
FT BINDING 232
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250|UniProtKB:Q8T045"
FT BINDING 271..273
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250|UniProtKB:Q8T045"
FT BINDING 289..293
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 227
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 254
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 19
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 67
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 66..73
FT /evidence="ECO:0000250|UniProtKB:Q8T045"
FT DISULFID 71..373
FT /evidence="ECO:0000250|UniProtKB:Q8T045"
FT DISULFID 118..124
FT /evidence="ECO:0000250|UniProtKB:Q8T045"
FT DISULFID 277..300
FT /evidence="ECO:0000250|UniProtKB:Q8T045"
SQ SEQUENCE 399 AA; 46360 MW; 7AE9EC6E94A5FD91 CRC64;
MHFIIGIVIC LSLSVIQSNT SDEGMCMAKE QCTDPEESTT GRSLYSADYN KYFNAIETAL
AGYVACNSTN CNCHADVLKA DLKPFKAHGI TKEMINRAKQ YGTHYQVIGH KLYRQRECMF
PARCSGVEHF VRPLLPLLPD MDLIVNCRDW PQIHRHWSKE KIPVLSFSKT AEYLDIMYPA
WAFWEGGPAI ALYPTGLGRW DLHRQTITKA SADWEAKEPK AFFRGSRTSD ERDALVLLSR
AQPSLVDAQY TKNQAWKSPQ DTLNAEPARE VTLEEHCRYR FLFNFRGVAA SFRFKHLFLC
RSLVFHVGDE WQEFFYPSLK PWVHYVPVPV RSTPEELEAL ITFFQEHDQL ARAIAERGYE
HIWNHLRMAD VECYWKKLLK RYGKLIRYTV ERDSTLIEV
