Reviewed, UniProtKB/Swiss-Prot Q6WV20 (GALT1_DROME)

Names and origin

Protein names

Recommended name:
    Polypeptide N-acetylgalactosaminyltransferase 1
      Short name=pp-GaNTase 1
    EC=2.4.1.41
Alternative name(s):
    Protein-UDP acetylgalactosaminyltransferase 1
    UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 1

Gene names

Name:	GalNAc-T1
Synonyms:	pgant1
ORF Names:	CG8182

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	601 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript 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 the monoglycosylated Muc5AC-3 as substrate.
Catalytic activity	UDP-N-acetyl-D-galactosamine + polypeptide = UDP + N-acetyl-D-galactosaminyl-polypeptide. Ref.1
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.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
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.1 Inferred from direct assay. Source: UniProtKB
Cellular component	Golgi stack Ref.1 Non-traceable author statement. Source: UniProtKB 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 Ref.1 Inferred from direct assay. 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 – 601	601	Polypeptide N-acetylgalactosaminyltransferase 1		PRO_0000059155
Regions
	Topological domain	1 – 7	7	Cytoplasmic Potential
	Transmembrane	8 – 28	21	Signal-anchor for type II membrane protein Potential
	Topological domain	29 – 601	573	Lumenal Potential
	Domain	472 – 600	129	Ricin B-type lectin
	Region	148 – 260	113	Catalytic subdomain A
	Region	327 – 389	63	Catalytic subdomain B
Amino acid modifications
	Glycosylation	127	1	N-linked (GlcNAc...) Potential
	Disulfide bond	138 ↔ 381		By similarity
	Disulfide bond	372 ↔ 450		By similarity
	Disulfide bond	485 ↔ 504		By similarity
	Disulfide bond	528 ↔ 546		By similarity
	Disulfide bond	571 ↔ 588		By similarity
Experimental info
	Sequence conflict	146	1	D → E in AAQ56699. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q6WV20-1 [UniParc]. Last modified August 16, 2004. Version 2. Checksum: 81BAF81E04C35BC2	FASTA	601	68,961
	10 20 30 40 50 60 MLPRFRSFYG KLIIFILVAL CFILYSKVQQ NGSPEEPPVA PLVRAAALRG HGRERFEAYS 70 80 90 100 110 120 DSENEIARPA TQSPYEQIIQ LDLQKQKVGL GEQGVAVHLS GAAKERGDEI YKKIALNEEL 130 140 150 160 170 180 SEQLTYNRSV GDHRNPLCAK QRFDSDSLPT ASVVIIFFNE PYSVLLRTVH STLSTCNEKA 190 200 210 220 230 240 LKEIILVDDG SDNVELGAKL DYYVRTRIPS GKVTILRLKN RLGLIRARLA GARIATGDVL 250 260 270 280 290 300 IFLDAHCEGN IGWCEPLLQR IKESRTSVLV PIIDVIDAND FQYSTNGYKS FQVGGFQWNG 310 320 330 340 350 360 HFDWINLPER EKQRQRRECK QEREICPAYS PTMAGGLFAI DRRYFWEVGS YDEQMDGWGG 370 380 390 400 410 420 ENLEMSFRIW QCGGTIETIP CSRVGHIFRD FHPYKFPNDR DTHGINTARM ALVWMDEYIN 430 440 450 460 470 480 IFFLNRPDLK FHADIGDVTH RVMLRKKLRC KSFEWYLKNI YPEKFVPTKD VQGWGKVHAV 490 500 510 520 530 540 NSNICLDDLL QNNEKPYNAG LYPCGKVLQK SQLFSFTNTN VLRNELSCAT VQHSESPPYR 550 560 570 580 590 600 VVMVPCMEND EFNEQWRYEH QHIIHSNTGM CLDHQGLKSL DDAQVAPCDP HSESQRWTIE H

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]	"Cloning of Drosophila protein-UDP acetylgalactosaminyltransferase." Farkas R., Medvedova L., Mechler B.M. Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[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]	"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.
[5]	"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	AY268063 mRNA. Translation: AAQ56699.1. AF218236 mRNA. Translation: AAG13184.1. AE013599 Genomic DNA. Translation: AAM70974.1. AY113411 mRNA. Translation: AAM29416.1.
RefSeq	NP_611043.1. NP_725472.1.
UniGene	Dm.3404
3D structure databases
SMR	Q6WV20. Positions 87-601.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q6WV20. 2 interactions.
STRING	Q6WV20.
Protein family/group databases
CAZy	CBM13. Carbohydrate-Binding Module Family 13. GT27. Glycosyltransferase Family 27.
Genome annotation databases
Ensembl	FBtr0087331; FBpp0086464; FBgn0034025; Drosophila melanogaster. [Genome view] FBtr0087332; FBpp0086465; FBgn0034025; Drosophila melanogaster. [Genome view]
GeneID	36717.
KEGG	dme:Dmel_CG8182.
Organism-specific databases
CTD	36717.
FlyBase	FBgn0034025. GalNAc-T1.
Phylogenomic databases
eggNOG	inNOG04661.
InParanoid	Q6WV20.
OMA	HPYKFPN.
OrthoDB	EOG9X3H6X.
PhylomeDB	Q6WV20.
Enzyme and pathway databases
BRENDA	2.4.1.41. 48.
Gene expression databases
ArrayExpress	Q6WV20.
GermOnline	CG8182. Drosophila melanogaster.
Family and domain databases
InterPro	IPR001173. Glyco_trans_2. IPR008997. Ricin_B-rel_lectin. 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	800028.

Entry information

Entry name

GALT1_DROME

Accession

Primary (citable) accession number: Q6WV20
Secondary accession number(s): Q0E964, Q9V7C8

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 16, 2004
Last sequence update:	August 16, 2004
Last modified:	January 19, 2010
This is version 55 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Drosophila annotation project