Reviewed, UniProtKB/Swiss-Prot Q8MYY6 (GLT13_DROME)

Names and origin

Protein names

Recommended name:
    Putative polypeptide N-acetylgalactosaminyltransferase 13
      Short name=pp-GaNTase 13
    EC=2.4.1.41
Alternative name(s):
    Protein-UDP acetylgalactosaminyltransferase 13
    UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 13

Gene names

Name:	pgant13
ORF Names:	CG10000

Organism

Drosophila melanogaster (Fruit fly) [Complete proteome]

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

General annotation (Comments)

Function	May catalyze the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor By similarity.
Catalytic activity	UDP-N-acetyl-D-galactosamine + polypeptide = UDP + N-acetyl-D-galactosaminyl-polypeptide.
Cofactor	Manganese By similarity. Calcium By similarity.
Pathway	Protein modification; protein glycosylation.
Subcellular location	Golgi apparatus membrane; Single-pass type II membrane protein By similarity.
Domain	There are two conserved domains in the glycosyltransferase region: the N-terminal domain (domain A, also called GT1 motif), which is probably involved in manganese coordination and substrate binding and the C-terminal domain (domain B, also called Gal/GalNAc-T motif), which is probably involved in catalytic reaction and UDP-Gal binding By similarity. The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity By similarity.
Sequence similarities	Belongs to the glycosyltransferase 2 family. GalNAc-T subfamily. Contains 1 ricin B-type lectin domain.

Ontologies

Keywords
Cellular component	Golgi apparatus Membrane
Domain	Signal-anchor Transmembrane
Ligand	Calcium Lectin Manganese
Molecular function	Glycosyltransferase Transferase
PTM	Disulfide bond Glycoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	oligosaccharide biosynthetic process Inferred from sequence or structural similarity. Source: UniProtKB
Cellular component	Golgi apparatus Inferred from electronic annotation. Source: UniProtKB-KW integral to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	calcium ion binding Inferred from electronic annotation. Source: UniProtKB-KW manganese ion binding Inferred from electronic annotation. Source: UniProtKB-KW polypeptide N-acetylgalactosaminyltransferase activity Inferred from sequence or structural similarity. Source: UniProtKB sugar binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 558	558	Putative polypeptide N-acetylgalactosaminyltransferase 13		PRO_0000059167
Regions
	Topological domain	1 – 12	12	Cytoplasmic Potential
	Transmembrane	13 – 32	20	Signal-anchor for type II membrane protein Potential
	Topological domain	33 – 558	526	Lumenal Potential
	Domain	422 – 556	135	Ricin B-type lectin
	Region	109 – 225	117	Catalytic subdomain A
	Region	281 – 343	63	Catalytic subdomain B
Amino acid modifications
	Glycosylation	48	1	N-linked (GlcNAc...) Potential
	Glycosylation	111	1	N-linked (GlcNAc...) Potential
	Glycosylation	501	1	N-linked (GlcNAc...) Potential
	Disulfide bond	445 ↔ 460		By similarity
	Disulfide bond	484 ↔ 498		By similarity
	Disulfide bond	525 ↔ 539		By similarity
Experimental info
	Sequence conflict	171	1	G → E in AAM29489. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Q8MYY6-1 [UniParc]. Last modified August 16, 2004. Version 2. Checksum: B9CB8EDB60F8D245	FASTA	558	64,626
	10 20 30 40 50 60 MHAGGKYCGP RHCSFYIIAF LICQLFFLVI FIRNDDASSA NELLSFMNES EESDHLDWRV 70 80 90 100 110 120 FISHTPETSE DFYQYNIHLS NALGLIRKLP VTRHHSCTTR NSILPAPLEA NVSVVISFHN 130 140 150 160 170 180 EARSMLLRTI VSLLSRSPED YLHELILVDD GSQRDVTLLD DLKRWMGGVF GSRYRLGLTF 190 200 210 220 230 240 LRNQERMGLI WSRNRGASLA SGRYVLFLDS HCEVNEGWLE PLLERLALNT NLAVSPLLDP 250 260 270 280 290 300 IDPTTLSYRK GNELLKGGFD WSLHFHWLKR QLTNQESLEM PYQSPAFAGG VLMMSREWFL 310 320 330 340 350 360 KLGSFNPYLK IWGGESIELA IKLWLCGGQI EIVPCSRIGH IFRRRHAFDF PPQSDRQLSP 370 380 390 400 410 420 AQETYLHNSK IIAESWLDEY KNMFYALRPA ARRIPLDHTY DELQRMRKER RCHPFEWYLR 430 440 450 460 470 480 HVSPELRMHF DELSATGTLR NEDRCVHARQ KDSQPILASC YLSDITQWSM LRQSGQLSTH 490 500 510 520 530 540 RELCLAVGFG MRIALEPCGR NETVRRSQRW VRLGTHLLHA ESHLCLDNPL KDRLEMSTCR 550 SHAVSQSFQF ALEMEGQT

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: 10731132] [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: 12537572] [Abstract] Cited for: GENOME REANNOTATION.
[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: 12537569] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Berkeley. Tissue: Head.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE014297 Genomic DNA. Translation: AAF56810.2. AY113484 mRNA. Translation: AAM29489.1.
RefSeq	NP_651630.3.
UniGene	Dm.13252
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q8MYY6.
Protein family/group databases
CAZy	CBM13. Carbohydrate-Binding Module Family 13. GT27. Glycosyltransferase Family 27.
Genome annotation databases
Ensembl	FBtr0085315; FBpp0084684; FBgn0039596; Drosophila melanogaster. [Genome view]
GeneID	43394.
KEGG	dme:Dmel_CG10000.
NMPDR	fig|7227.3.peg.15116.
UCSC	CG10000-RA. d. melanogaster.
Organism-specific databases
FlyBase	FBgn0039596. CG10000.
Phylogenomic databases
HOGENOM	Q8MYY6.
Enzyme and pathway databases
BRENDA	2.4.1.41. 48.
Gene expression databases
GermOnline	CG10000. Drosophila melanogaster.
Family and domain databases
InterPro	IPR001173. Glyco_trans_2. IPR000772. Ricin_B_lectin. [Graphical view]
Pfam	PF00535. Glycos_transf_2. 1 hit. PF00652. Ricin_B_lectin. 1 hit. [Graphical view]
PROSITE	PS50231. RICIN_B_LECTIN. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	833701.

Entry information

Entry name

GLT13_DROME

Accession

Primary (citable) accession number: Q8MYY6
Secondary accession number(s): Q9VAT9

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 16, 2004
Last sequence update:	August 16, 2004
Last modified:	October 13, 2009
This is version 51 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Drosophila annotation project