Reviewed, UniProtKB/Swiss-Prot Q9Y117 (GALT3_DROME)

Names and origin

Protein names

Recommended name:
    Polypeptide N-acetylgalactosaminyltransferase 3
      Short name=pp-GaNTase 3
    EC=2.4.1.41
Alternative name(s):
    Protein-UDP acetylgalactosaminyltransferase 3
    UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 3

Gene names

Name:	pgant3
ORF Names:	CG4445

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

General annotation (Comments)

Function	Catalyzes 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. It can both act as a peptide transferase that transfers GalNAc onto unmodified peptide substrates, and as a glycopeptide transferase that requires the prior addition of a GalNAc on a peptide before adding additional GalNAc moieties. Prefers EA2 as substrate. Has weak activity toward Muc5AC-3, -13 and -3/13 substrates.
Catalytic activity	UDP-N-acetyl-D-galactosamine + polypeptide = UDP + N-acetyl-D-galactosaminyl-polypeptide. Ref.4
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	Expressed in developing oocytes and egg chambers. Ref.4
Developmental stage	Expressed throughout embryonic, larval, pupal and adult stages, with increasing levels during larval development. Ref.4
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 Ref.4 Inferred from direct assay. Source: UniProtKB
Cellular component	Golgi membrane Inferred from electronic annotation. Source: UniProtKB-SubCell Golgi stack Ref.4 Non-traceable author statement. Source: UniProtKB integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
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 Ref.4 Inferred from direct assay. Source: UniProtKB protein binding Inferred from physical interaction. Source: IntAct sugar binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
	Q8SWU4	1	EBI-154332,EBI-180052

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 667	667	Polypeptide N-acetylgalactosaminyltransferase 3		PRO_0000059157
Regions
	Topological domain	1 – 12	12	Cytoplasmic Potential
	Transmembrane	13 – 35	23	Signal-anchor for type II membrane protein Potential
	Topological domain	36 – 667	632	Lumenal Potential
	Domain	513 – 661	149	Ricin B-type lectin
	Region	149 – 259	111	Catalytic subdomain A
	Region	321 – 383	63	Catalytic subdomain B
Amino acid modifications
	Glycosylation	75	1	N-linked (GlcNAc...) Potential
	Glycosylation	129	1	N-linked (GlcNAc...) Potential
	Glycosylation	279	1	N-linked (GlcNAc...) Potential
	Glycosylation	313	1	N-linked (GlcNAc...) Potential
	Glycosylation	433	1	N-linked (GlcNAc...) Potential
	Glycosylation	590	1	N-linked (GlcNAc...) Potential
	Disulfide bond	526 ↔ 547		By similarity
	Disulfide bond	572 ↔ 601		By similarity
	Disulfide bond	626 ↔ 649		By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9Y117-1 [UniParc]. Last modified November 1, 1999. Version 1. Checksum: B8C6924AA8E19805	FASTA	667	76,807
	10 20 30 40 50 60 MGLRFQQLKK LWLLYLFLLF FAFFMFAISI NLYVASIQGG DAEMRHPKPP PKRRSLWPHK 70 80 90 100 110 120 NIVAHYIGKG DIFGNMTADD YNINLFQPIN GEGADGRPVV VPPRDRFRMQ RFFRLNSFNL 130 140 150 160 170 180 LASDRIPLNR TLKDYRTPEC RDKKYASGLP STSVIIVFHN EAWSVLLRTI TSVINRSPRH 190 200 210 220 230 240 LLKEIILVDD ASDRSYLKRQ LESYVKVLAV PTRIFRMKKR SGLVPARLLG AENARGDVLT 250 260 270 280 290 300 FLDAHCECSR GWLEPLLSRI KESRKVVICP VIDIISDDNF SYTKTFENHW GAFNWQLSFR 310 320 330 340 350 360 WFSSDRKRQT AGNSSKDSTD PIATPGMAGG LFAIDRKYFY EMGSYDSNMR VWGGENVEMS 370 380 390 400 410 420 FRIWQCGGRV EISPCSHVGH VFRSSTPYTF PGGMSEVLTD NLARAATVWM DDWQYFIMLY 430 440 450 460 470 480 TSGLTLGAKD KVNVTERVAL RERLQCKPFS WYLENIWPEH FFPAPDRFFG KIIWLDGETE 490 500 510 520 530 540 CAQAYSKHMK NLPGRALSRE WKRAFEEIDS KAEELMALID LERDKCLRPL KEDVPRSSLS 550 560 570 580 590 600 AVTVGDCTSH AQSMDMFVIT PKGQIMTNDN VCLTYRQQKL GVIKMLKNRN ATTSNVMLAQ 610 620 630 640 650 660 CASDSSQLWT YDMDTQQISH RDTKLCLTLK AATNSRLQKV EKVVLSMECD FKDITQKWGF IPLPWRM

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.
[4]	"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: ENZYME ACTIVITY, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AE013599 Genomic DNA. Translation: AAF59298.1. AF145655 mRNA. Translation: AAD38630.1.
RefSeq	NP_610256.1.
UniGene	Dm.3144
3D structure databases
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9Y117. 5 interactions.
Protein family/group databases
CAZy	CBM13. Carbohydrate-Binding Module Family 13. GT27. Glycosyltransferase Family 27.
Proteomic databases
PRIDE	Q9Y117.
Genome annotation databases
Ensembl	FBgn0027558. Drosophila melanogaster. [Contig view]
GeneID	35627.
KEGG	dme:Dmel_CG4445.
NMPDR	fig|7227.3.peg.3584.
Organism-specific databases
FlyBase	FBgn0027558. pgant3.
Phylogenomic databases
HOGENOM	Q9Y117.
OMA	Q9Y117. MFAISIN.
Enzyme and pathway databases
BRENDA	2.4.1.41. 48.
Gene expression databases
ArrayExpress	Q9Y117.
GermOnline	CG4445. 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]
SMART	SM00458. RICIN. 1 hit. [Graphical view]
PROSITE	PS50231. RICIN_B_LECTIN. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	794347.

Entry information

Entry name

GALT3_DROME

Accession

Primary (citable) accession number: Q9Y117

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 16, 2004
Last sequence update:	November 1, 1999
Last modified:	June 16, 2009
This is version 60 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Drosophila annotation project