Q8T045 (RUMI_DROME) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
O-glucosyltransferase rumi
EC=2.4.1.-

Gene names

Name:	rumi
ORF Names:	CG31152

Organism

Drosophila melanogaster (Fruit fly) [Reference proteome]

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Protostomia › Ecdysozoa › Panarthropoda › Arthropoda › Mandibulata › Pancrustacea › Hexapoda › Insecta › Dicondylia › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Eremoneura › Cyclorrhapha › Schizophora › Acalyptratae › Ephydroidea › Drosophilidae › Drosophilinae › Drosophilini › Drosophilina › Drosophiliti › Drosophila › Sophophora › melanogaster group › melanogaster subgroup

Protein attributes

Sequence length	411 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Protein O-glucosyltransferase. Catalyzes the reaction that attaches glucose through an O-glycosidic linkage to a conserved serine residue in epidermal growth factor-like repeats. Regulates Notch signaling by glucosylating Notch in the ER, glucosylation is required for the correct folding and cleavage of Notch. Ref.4
Pathway	Protein modification; protein glycosylation.
Subcellular location	Endoplasmic reticulum lumen Ref.4.
Developmental stage	Expressed both maternally and zygotically. Ref.4
Disruption phenotype	Flies exhibit a temperature-dependent loss of Notch signaling, resulting in bristle loss. Ref.4
Sequence similarities	Belongs to the glycosyltransferase 90 family.

Ontologies

Keywords
Biological process	Notch signaling pathway
Cellular component	Endoplasmic reticulum
Domain	Signal
Molecular function	Glycosyltransferase Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	Golgi organization Inferred from mutant phenotype PubMed 21383842. Source: FlyBase Notch signaling pathway Inferred from genetic interaction Ref.4. Source: FlyBase negative regulation of Notch signaling pathway Inferred from mutant phenotype Ref.4. Source: UniProtKB positive regulation of Notch signaling pathway Inferred from genetic interaction PubMed 21771811. Source: FlyBase protein glycosylation in endoplasmic reticulum Inferred from direct assay Ref.4. Source: UniProtKB regulation of stem cell division Inferred from mutant phenotype PubMed 21965616. Source: FlyBase
Cellular_component	endoplasmic reticulum lumen Inferred from direct assay Ref.4. Source: UniProtKB
Molecular_function	glucosyltransferase activity Inferred from direct assay Ref.4. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 20	20	Potential
	Chain	21 – 411	391	O-glucosyltransferase rumi		PRO_0000342687
Regions
	Motif	408 – 411	4	Prevents secretion from ER Ref.4
Experimental info
	Mutagenesis	189	1	G → E in rumi-79; complete loss of enzyme activity. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	Q8T045 [UniParc]. Last modified June 1, 2002. Version 1. Checksum: 785EA3A15977B69D	FASTA	411	47,735
	10 20 30 40 50 60 MLINHLIVVL LISLVGTGGA EDDGLCSADQ KSCAQSEPDQ INEDEFSFKI RRQIEKANAD 70 80 90 100 110 120 YKPCSSDPQD SDCSCHANVL KRDLAPYKST GVTRQMIESS ARYGTKYKIY GHRLYRDANC 130 140 150 160 170 180 MFPARCEGIE HFLLPLVATL PDMDLIINTR DYPQLNAAWG NAAGGPVFSF SKTKEYRDIM 190 200 210 220 230 240 YPAWTFWAGG PATKLHPRGI GRWDQMREKL EKRAAAIPWS QKRSLGFFRG SRTSDERDSL 250 260 270 280 290 300 ILLSRRNPEL VEAQYTKNQG WKSPKDTLDA PAADEVSFED HCKYKYLFNF RGVAASFRLK 310 320 330 340 350 360 HLFLCKSLVF HVGDEWQEFF YDQLKPWVHY VPLKSYPSQQ EYEHILSFFK KNDALAQEIA 370 380 390 400 410 QRGYDFIWEH LRMKDIKCYW RKLLKRYVKL LQYEVKPEDQ LIYIGPKKDE L

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The genome sequence of Drosophila melanogaster." Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D. , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C. Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Berkeley.
[2]	"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review." Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E. Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed] [Europe PMC] [Abstract] Cited for: GENOME REANNOTATION. Strain: Berkeley.
[3]	"A Drosophila full-length cDNA resource." Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E. Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Berkeley. Tissue: Embryo.
[4]	"Rumi is a CAP10 domain glycosyltransferase that modifies Notch and is required for Notch signaling." Acar M., Jafar-Nejad H., Takeuchi H., Rajan A., Ibrani D., Rana N.A., Pan H., Haltiwanger R.S., Bellen H.J. Cell 132:247-258(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, MUTAGENESIS OF GLY-189, DISRUPTION PHENOTYPE.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE014297 Genomic DNA. Translation: AAN13920.1. AY069564 mRNA. Translation: AAL39709.1.
RefSeq	NP_651095.1. NM_142838.3.
UniGene	Dm.1286.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
MINT	MINT-1699273.
STRING	7227.FBpp0083713.
Protein family/group databases
CAZy	GT90. Glycosyltransferase Family 90.
Proteomic databases
PaxDb	Q8T045.
PRIDE	Q8T045.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblMetazoa	FBtr0084320; FBpp0083713; FBgn0086253.
GeneID	326122.
KEGG	dme:Dmel_CG31152.
UCSC	CG31152-RA. d. melanogaster.
Organism-specific databases
CTD	326122.
FlyBase	FBgn0086253. rumi.
Phylogenomic databases
eggNOG	NOG248922.
GeneTree	ENSGT00530000063132.
InParanoid	Q8T045.
KO	K13667.
OMA	FSKTKEY.
OrthoDB	EOG4RN8QS.
PhylomeDB	Q8T045.
Enzyme and pathway databases
UniPathway	UPA00378.
Gene expression databases
Bgee	Q8T045.
Family and domain databases
InterPro	IPR006598. LipoPS_modifying. [Graphical view]
Pfam	PF05686. Glyco_transf_90. 1 hit. [Graphical view]
SMART	SM00672. CAP10. 1 hit. [Graphical view]
PROSITE	PS00014. ER_TARGET. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	326122.
NextBio	847167.

Entry information

Entry name

RUMI_DROME

Accession

Primary (citable) accession number: Q8T045

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 2008
Last sequence update:	June 1, 2002
Last modified:	April 3, 2013
This is version 73 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Drosophila annotation project