Reviewed, UniProtKB/Swiss-Prot Q6WV19 (GALT2_DROME)

Names and origin

Protein names

Recommended name:
    Polypeptide N-acetylgalactosaminyltransferase 2
      Short name=pp-GaNTase 2
    EC=2.4.1.41
Alternative name(s):
    Protein-UDP acetylgalactosaminyltransferase 2
    UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 2

Gene names

Name:	pgant2
ORF Names:	CG3254

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	633 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.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 during embryonic, larval, pupal and adult stages. Weakly expressed in the male and female body and correspondingly low levels during early embryonic stages. Significantly expressed from embryonic stage 8-12 hours and reaches maximal levels in the pupae and male head. 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
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	oligosaccharide biosynthetic process Ref.4 Inferred from direct assay. Source: UniProtKB
Cellular component	Golgi stack Ref.4 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.4 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 – 633	633	Polypeptide N-acetylgalactosaminyltransferase 2		PRO_0000059156
Regions
	Topological domain	1 – 4	4	Cytoplasmic Potential
	Transmembrane	5 – 25	21	Signal-anchor for type II membrane protein Potential
	Topological domain	26 – 633	608	Lumenal Potential
	Domain	508 – 630	123	Ricin B-type lectin
	Region	201 – 306	106	Catalytic subdomain A
	Region	366 – 428	63	Catalytic subdomain B
	Compositional bias	67 – 141	75	Gly-rich
Amino acid modifications
	Disulfide bond	521 ↔ 538		By similarity
	Disulfide bond	561 ↔ 578		By similarity
	Disulfide bond	602 ↔ 618		By similarity
Experimental info
	Sequence conflict	134	1	P → L in AAQ56700. Ref.4
	Sequence conflict	617	1	H → R in AAQ22499. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Q6WV19-1 [UniParc]. Last modified August 16, 2004. Version 2. Checksum: 8DA64F627BCB08DB	FASTA	633	70,736
	10 20 30 40 50 60 MRRNIKLIVF VSIIWMFVMV YYFQSSTEKV ENRALRLREV ATAMQQYQDD SSSAAAASTA 70 80 90 100 110 120 RQWAPAGGGA GPGAAAGAAG SGADDPGGNV ILIGSVKDFE RNAVHGLKLN GIVALEETSQ 130 140 150 160 170 180 GLSGGTGGPG GRLPVAPSGR GTEVEYFNEA GYIRAGALRN GEDPYIRNRF NQEASDALPS 190 200 210 220 230 240 NRDIPDTRNP MCRTKKYRED LPETSVIITF HNEARSTLLR TIVSVLNRSP EHLIREIVLV 250 260 270 280 290 300 DDYSDHPEDG LELAKIDKVR VIRNDKREGL VRSRVKGADA AVSSVLTFLD SHVECNEMWL 310 320 330 340 350 360 EPLLERVRED PTRVVCPVID VISMDNFQYI GASADLRGGF DWNLIFKWEY LSPSERAMRH 370 380 390 400 410 420 NDPTTAIRTP MIAGGLFVID KAYFNKLGKY DMKMDVWGGE NLEISFRVWQ CGGSLEIIPC 430 440 450 460 470 480 SRVGHVFRKR HPYTFPGGSG NVFARNTRRA AEVWMDDYKQ HYYNAVPLAK NIPFGNIDDR 490 500 510 520 530 540 LALKEKLHCK PFKWYLENVY PDLQAPDPQE VGQFRQDSTE CLDTMGHLID GTVGIFPCHN 550 560 570 580 590 600 TGGNQEWAFT KRGEIKHDDL CLTLVTFARG SQVVLKACDD SENQRWIMRE GGLVRHYKIN 610 620 630 VCLDSRDQSQ QGVSAQHCNS ALGTQRWSFG KYA

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]	Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Champe M., Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A., Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., Miranda A. , Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., Patel S., Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E. Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Berkeley. Tissue: Embryo.
[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: NUCLEOTIDE SEQUENCE [MRNA] OF 19-633, ENZYME ACTIVITY, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE. Strain: Canton-S. Tissue: Embryo.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE014134 Genomic DNA. Translation: AAF51113.3. BT010030 mRNA. Translation: AAQ22499.1. AY268064 mRNA. Translation: AAQ56700.1.
RefSeq	NP_608773.2.
UniGene	Dm.11992
3D structure databases
SMR	Q6WV19. Positions 170-629.
ModBase	Search...
Protein-protein interaction databases
STRING	Q6WV19.
Protein family/group databases
CAZy	CBM13. Carbohydrate-Binding Module Family 13. GT27. Glycosyltransferase Family 27.
Genome annotation databases
Ensembl	FBtr0077592; FBpp0099799; FBgn0031530; Drosophila melanogaster. [Genome view]
GeneID	33556.
KEGG	dme:Dmel_CG3254.
Organism-specific databases
CTD	33556.
FlyBase	FBgn0031530. pgant2.
Phylogenomic databases
eggNOG	inNOG05585.
InParanoid	Q6WV19.
OMA	EDKYKAN.
OrthoDB	EOG90GCZC.
PhylomeDB	Q6WV19.
Enzyme and pathway databases
BRENDA	2.4.1.41. 48.
Gene expression databases
ArrayExpress	Q6WV19.
Bgee	Q6WV19.
GermOnline	CG3254. 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	784182.

Entry information

Entry name

GALT2_DROME

Accession

Primary (citable) accession number: Q6WV19
Secondary accession number(s): Q7KU27, Q7YU21, Q9VQQ2

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 16, 2004
Last sequence update:	August 16, 2004
Last modified:	January 19, 2010
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