Q6WV16 (GALT6_DROME) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
N-acetylgalactosaminyltransferase 6
EC=2.4.1.-

Alternative name(s):
Protein-UDP acetylgalactosaminyltransferase 6
UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 6
Short name=pp-GaNTase 6

Gene names

Name:	pgant6
ORF Names:	CG2103

Organism

Drosophila melanogaster (Fruit fly)

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	666 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Glycopeptide transferase involved in O-linked oligosaccharide biosynthesis, which catalyzes the transfer of an N-acetyl-D-galactosamine residue to an already glycosylated peptide. In contrast to other proteins of the family, it does not act as a peptide transferase that transfers GalNAc onto serine or threonine residue on the protein receptor, but instead requires the prior addition of a GalNAc on a peptide before adding additional GalNAc moieties. Some peptide transferase activity is however not excluded, considering that its appropriate peptide substrate may remain unidentified. Prefers the diglycosylated Muc5AC-3/13 as substrate.
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.
Tissue specificity	In embryos, it is specifically expressed in the salivary glands from stage 12, becoming stronger at stage 13. Not expressed in other tissues. Further expressed during oogenesis, in the somatically derived follicle cells that surround the developing oocyte, which are involved in the maturation of the oocyte and construction of the egg shell, as well as playing a role in subsequent embryonic pattern formation. Ref.1
Developmental stage	Expressed throughout embryonic, larval, pupal and adult stages, with increasing levels during larval development. Ref.1
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 Transmembrane helix
Ligand	Calcium Lectin Manganese
Molecular function	Glycosyltransferase Transferase
PTM	Disulfide bond Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	oligosaccharide biosynthetic process Inferred from direct assay Ref.1. Source: UniProtKB
Cellular component	Golgi membrane Inferred from electronic annotation. Source: UniProtKB-SubCell Golgi stack Non-traceable author statement Ref.1. Source: UniProtKB integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	polypeptide N-acetylgalactosaminyltransferase activity Inferred from direct assay Ref.1. 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 – 666	666	N-acetylgalactosaminyltransferase 6		PRO_0000059160
Regions
	Topological domain	1 – 11	11	Cytoplasmic Potential
	Transmembrane	12 – 31	20	Helical; Signal-anchor for type II membrane protein; Potential
	Topological domain	32 – 666	635	Lumenal Potential
	Domain	518 – 648	131	Ricin B-type lectin
	Region	201 – 311	111	Catalytic subdomain A
	Region	367 – 429	63	Catalytic subdomain B
Amino acid modifications
	Glycosylation	181	1	N-linked (GlcNAc...) Potential
	Glycosylation	285	1	N-linked (GlcNAc...) Potential
	Glycosylation	651	1	N-linked (GlcNAc...) Potential
	Glycosylation	657	1	N-linked (GlcNAc...) Potential
	Disulfide bond	531 ↔ 548		By similarity
	Disulfide bond	577 ↔ 594		By similarity
	Disulfide bond	621 ↔ 636		By similarity
Experimental info
	Sequence conflict	95 – 96	2	EV → DA in AAQ56703. Ref.1
	Sequence conflict	107	1	Q → R in AAQ56703. Ref.1
	Sequence conflict	107	1	Q → R in AAL29177. Ref.4
	Sequence conflict	499	1	E → K in AAL29177. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	Q6WV16 [UniParc]. Last modified August 16, 2004. Version 2. Checksum: CAECA6CE4860600C	FASTA	666	76,972
	10 20 30 40 50 60 MRRPNLKWIV KASLLLLISL TLFVLITSWI SSTPYTNKPV HHGVEPVPEK AGLSGDVKVK 70 80 90 100 110 120 VPAIKQPEPQ KPQEPDFEED PELQKIDEPE PVEEEVDNPH PADDEPQQQP QEELQMAAPA 130 140 150 160 170 180 DASVKKDWHD YTFMEKDAKR VGLGEGGKAS TLDDESQRDL EKRMSLENGF NALLSDSISV 190 200 210 220 230 240 NRSVPDIRHP LCRKKEYVAK LPTVSVIIIF YNEYLSVLMR SVHSLINRSP PELMKEIILV 250 260 270 280 290 300 DDHSDREYLG KELETYIAEH FKWVRVVRLP RRTGLIGARA AGARNATAEV LIFLDSHVEA 310 320 330 340 350 360 NYNWLPPLLE PIALNKRTAV CPFIDVIDHT NFHYRAQDEG ARGAFDWEFF YKRLPLLPED 370 380 390 400 410 420 LKHPADPFKS PIMAGGLFAI SREFFWELGG YDEGLDIWGG EQYELSFKIW MCGGEMYDAP 430 440 450 460 470 480 CSRIGHIYRG PRNHQPSPRK GDYLHKNYKR VAEVWMDEYK NYLYSHGDGL YESVDPGDLT 490 500 510 520 530 540 EQKAIRTKLN CKSFKWFMEE VAFDLMKTYP PVDPPSYAMG ALQNVGNQNL CLDTLGRKKH 550 560 570 580 590 600 NKMGMYACAD NIKTPQRTQF WELSWKRDLR LRRKKECLDV QIWDANAPVW LWDCHSQGGN 610 620 630 640 650 660 QYWYYDYRHK QLKHGTEGRR CLELLPFSQE VVANKCDTDN RFQQWNFGSF NKTALDNYSQ DLVLSL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Functional characterization and expression analysis of members of the UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase family from Drosophila melanogaster." Ten Hagen K.G., Tran D.T., Gerken T.A., Stein D.S., Zhang Z. J. Biol. Chem. 278:35039-35048(2003) [PubMed: 12829714] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], ENZYME ACTIVITY, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE. Strain: Canton-S. Tissue: Embryo.
[2]	"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.
[3]	"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. Strain: Berkeley.
[4]	"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: Embryo.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AY268067 mRNA. Translation: AAQ56703.1. AE014296 Genomic DNA. Translation: AAF47689.1. AE014296 Genomic DNA. Translation: AAF47690.1. AY061629 mRNA. Translation: AAL29177.1.
RefSeq	NP_647749.2. NM_139492.2. NP_728779.1. NM_167966.1.
UniGene	Dm.3519.
3D structure databases
ProteinModelPortal	Q6WV16.
SMR	Q6WV16. Positions 123-661.
ModBase	Search...
Protein-protein interaction databases
MINT	MINT-877547.
Protein family/group databases
CAZy	CBM13. Carbohydrate-Binding Module Family 13. GT27. Glycosyltransferase Family 27.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblMetazoa	FBtr0072972; FBpp0072842; FBgn0035375. FBtr0072973; FBpp0072843; FBgn0035375.
GeneID	38346.
KEGG	dme:Dmel_CG2103.
Organism-specific databases
CTD	38346.
FlyBase	FBgn0035375. pgant6.
Phylogenomic databases
eggNOG	inNOG06877.
GeneTree	EMGT00050000004060.
InParanoid	Q6WV16.
OMA	IFLDSHV.
OrthoDB	EOG4GF1W4.
PhylomeDB	Q6WV16.
Enzyme and pathway databases
BRENDA	2.4.1.41. 1994.
Gene expression databases
ArrayExpress	Q6WV16.
Bgee	Q6WV16.
GermOnline	CG2103. Drosophila melanogaster.
Family and domain databases
InterPro	IPR001173. Glyco_trans_2. IPR008997. Ricin_B-rel_lectin. IPR000772. Ricin_B_lectin. [Graphical view]
KO	K00710.
Pfam	PF00535. Glycos_transf_2. 1 hit. PF00652. Ricin_B_lectin. 1 hit. [Graphical view]
SMART	SM00458. RICIN. 1 hit. [Graphical view]
SUPFAM	SSF50370. RicinB_like. 1 hit.
PROSITE	PS50231. RICIN_B_LECTIN. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	808136.

Entry information

Entry name

GALT6_DROME

Accession

Primary (citable) accession number: Q6WV16
Secondary accession number(s): Q0E8I9, Q95R40, Q9VZX5

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 16, 2004
Last sequence update:	August 16, 2004
Last modified:	January 25, 2012
This is version 66 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Drosophila annotation project