Unreviewed, UniProtKB/TrEMBL Q60GL7 (Q60GL7_DROME)

Names and origin

Protein names

Submitted name:
    UDP-GlcNAc:a-3-D-mannoside-beta-1, 2-N-acetylglucosaminyltransferase I EMBL AAF57454.1
    EC=2.4.1.- EMBL AAF57454.1
    EC=2.4.1.101 EMBL AAF57454.1
Submitted name:
    Alpha1,3-mannose beta1,2-N-acetylglucosaminyltransferase 1 EMBL BAD54756.1
    LD23909p EMBL ACD81852.1

Gene names

Name:	Mgat1 FlyBase FBgn0034521
Synonyms:	CG13431-RA EMBL ACD81852.1, MGAT1 EMBL BAD54756.1
ORF Names:	CG13431 FlyBase FBgn0034521, Dmel_CG13431 EMBL AAF57454.1

Organism

Drosophila melanogaster (Fruit fly) [Complete proteome] EMBL BAD54756.1

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora

Protein attributes

Sequence length	458 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at transcript level.

Ontologies

Keywords
Molecular function	Glycosyltransferase EMBL BAD54756.1 Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	adult locomotory behavior Inferred from mutant phenotype. Source: FlyBase determination of adult lifespan Inferred from mutant phenotype. Source: FlyBase mushroom body development Inferred from mutant phenotype. Source: FlyBase protein amino acid N-linked glycosylation via asparagine Inferred from direct assay. Source: FlyBase
Cellular component	Golgi membrane Inferred from electronic annotation. Source: InterPro
Molecular function	alpha-1,3-mannosylglycoprotein 2-beta-N-acetylglucosaminyltransferase activity Inferred from direct assay. Source: FlyBase
Complete GO annotation...

Sequences

	Sequence		Length	Mass (Da)
	Q60GL7-1 [UniParc]. Last modified October 3, 2006. Version 1. Checksum: 6E5CB2B7B3C41CD1	FASTA	458	53,193
	10 20 30 40 50 60 MRTRKVLLVI GFLVTWTYAT YYLLLRQTGI HTSRHQSLQA YKLNSQARDA NMQSHHLAKN 70 80 90 100 110 120 VFEFVKLKYL EKQPPSVAST PQISIIAAEI SAELPEQHVA KSATARIPTK TYLANGEPVF 130 140 150 160 170 180 PVVVFACNRV SVKKCIDNLV QYRPSVEQFP IIVSQDCGDE PTKEAILSYG KQVTLIEQPD 190 200 210 220 230 240 LSDITVLPKE KKFKGYYKIA RHYGWALNTT FAVGFEFVII VEDDLNVAPD FFEYFLGTHK 250 260 270 280 290 300 LLKQDPSLWC VSAWNDNGKA AVVDAAQPEL LYRTDFFPGL GWMLTKDLWA ELSVKWPKSF 310 320 330 340 350 360 WDDWIRHPAQ RKDRVCIRPE ISRTRTFGKI GVSNGLFFDK YLKHIKLSED FVQFTKINMS 370 380 390 400 410 420 YLLKDNYDNT FLRRVYTYPI VTYDELRRNL IRIEGPVRIQ YTTREQYKRT TKMLGLMDDF 430 440 450 KSGVPRTAYH GIVSFYYNKR RVHLAPNANW KGYELSWS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The twisted abdomen phenotype of Drosophila POMT1 and POMT2 mutants coincides with their heterophilic protein O-mannosyltransferase activity." Ichimiya T., Manya H., Ohmae Y., Yoshida H., Takahashi K., Ueda R., Endo T., Nishihara S. J. Biol. Chem. 279:42638-42647(2004) [PubMed: 15271988] [Abstract] Cited for: NUCLEOTIDE SEQUENCE.
[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: 12537572] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Berkeley.
[3]	"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: 10731132] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Berkeley.
[4]	Carlson J., Booth B., Frise E., Park S., Wan K., Yu C., Celniker S. Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE. Strain: Berkeley EMBL ACD81852.1.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE013599 Genomic DNA. Translation: AAF57454.1. BT032838 mRNA. Translation: ACD81852.1. AB176552 mRNA. Translation: BAD54756.1.
RefSeq	NP_525117.2.
UniGene	Dm.1662
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q60GL7.
Protein family/group databases
CAZy	GT13. Glycosyltransferase Family 13.
Proteomic databases
PRIDE	Q60GL7.
Genome annotation databases
Ensembl	FBtr0086259; FBpp0085571; FBgn0034521; Drosophila melanogaster. [Genome view]
GeneID	37323.
KEGG	dme:Dmel_CG13431.
NMPDR	fig|7227.3.peg.6489.
UCSC	CG13431-RA. d. melanogaster.
Organism-specific databases
CTD	37323.
FlyBase	FBgn0034521. Mgat1.
Phylogenomic databases
InParanoid	Q60GL7.
OMA	LWEELEP.
OrthoDB	EOG9SXNKZ.
PhylomeDB	Q60GL7.
Gene expression databases
ArrayExpress	Q60GL7.
Family and domain databases
InterPro	IPR004139. Glyco_trans_13. [Graphical view]
PANTHER	PTHR10468. Glyco_trans_13. 1 hit.
Pfam	PF03071. GNT-I. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	Dmel_CG13431. 803117.

Entry information

Entry name

Q60GL7_DROME

Accession

Primary (citable) accession number: Q60GL7

Entry history

Integrated into UniProtKB/TrEMBL:	October 3, 2006
Last sequence update:	October 3, 2006
Last modified:	December 15, 2009
This is version 37 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)