Q8MV48 (GALT7_DROME) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
N-acetylgalactosaminyltransferase 7
EC=2.4.1.-

Alternative name(s):
Protein-UDP acetylgalactosaminyltransferase 7
UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 7
Short name=pp-GaNTase 7
dGalNAc-T2

Gene names

Name:	GalNAc-T2
Synonyms:	pgant7
ORF Names:	CG6394

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	591 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 monoglycosylated Muc5AC-3 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	Expressed in developing oocytes and egg chambers. Ref.2
Developmental stage	Expressed throughout embryonic, larval, pupal and adult stages, with increasing levels during larval development. Ref.2
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.
Sequence caution	The sequence AAL13889.1 differs from that shown. Reason: Erroneous initiation. The sequence AAL28887.1 differs from that shown. Reason: Erroneous initiation.

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.1Ref.2. Source: UniProtKB
Cellular component	Golgi membrane Inferred from electronic annotation. Source: UniProtKB-SubCell Golgi stack Non-traceable author statement Ref.2. Source: UniProtKB integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	polypeptide N-acetylgalactosaminyltransferase activity Inferred from direct assay Ref.1Ref.2. 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 – 591	591	N-acetylgalactosaminyltransferase 7		PRO_0000059161
Regions
	Topological domain	1 – 11	11	Cytoplasmic Potential
	Transmembrane	12 – 29	18	Helical; Signal-anchor for type II membrane protein; Potential
	Topological domain	30 – 591	562	Lumenal Potential
	Domain	466 – 585	120	Ricin B-type lectin
	Region	141 – 251	111	Catalytic subdomain A
	Region	313 – 375	63	Catalytic subdomain B
Amino acid modifications
	Glycosylation	30	1	N-linked (GlcNAc...) Potential
	Glycosylation	576	1	N-linked (GlcNAc...) Potential
	Disulfide bond	479 ↔ 496		By similarity
	Disulfide bond	519 ↔ 532		By similarity
	Disulfide bond	558 ↔ 573		By similarity
Experimental info
	Sequence conflict	84	1	P → S in AAM62412. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q8MV48 [UniParc]. Last modified August 16, 2004. Version 2. Checksum: 6CC2F7DC38E4CF17	FASTA	591	68,333
	10 20 30 40 50 60 MRVSTIRSGR ICRLALCLLV LLPLLYLLAN WSDHHKRVQE AYHTRFGGPK FAHQRLEGRP 70 80 90 100 110 120 REVPKLVDGL GNFEPKDVKP RSGPGENGEA HSLSPDKKHM SDASEMEYGM NIACSDEISM 130 140 150 160 170 180 HRSVRDTRLE ECRHWDYPFD LPRTSVIIVF HNEGFSVLMR TVHSVIDRSP THMLHEIILV 190 200 210 220 230 240 DDFSDKENLR SQLDEYVLQF KGLVKVIRNK EREGLIRTRS RGAMEATGEV IVFLDAHCEV 250 260 270 280 290 300 NTNWLPPLLA PIYRDRTVMT VPIIDGIDHK NFEYRPVYGT DNHFRGIFEW GMLYKENEVP 310 320 330 340 350 360 RREQRRRAHN SEPYRSPTHA GGLFAINREY FLELGAYDPG LLVWGGENFE LSFKIWQCGG 370 380 390 400 410 420 SIEWVPCSRV GHVYRGFMPY NFGKLASKKK GPLITINYKR VIETWFDDTH KEYFYTREPL 430 440 450 460 470 480 ARYLDMGDIS EQLALKKRLN CKSFQWFMDH IAYDVYDKFP GLPANLHWGE LRSVASDGCL 490 500 510 520 530 540 DSMGHQPPAI MGLTYCHGGG NNQLVRLNAA GQLGVGERCV EADRQGIKLA VCRLGTVDGP 550 560 570 580 590 WQYNEHTKHL MHRVHKKCMA LHPATQQLSL GHCDVNDSYQ QWWFKEIRPR W

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Functional conservation of subfamilies of putative UDP-N-acetylgalactosamine:polypeptide N-acetylgalactosaminyltransferases in Drosophila, Caenorhabditis elegans, and mammals. One subfamily composed of l(2)35Aa is essential in Drosophila." Schwientek T., Bennett E.P., Flores C., Thacker J., Hollmann M., Reis C.A., Behrens J., Mandel U., Keck B., Schaefer M.A., Haselmann K., Zubarev R., Roepstorff P., Burchell J.M., Taylor-Papadimitriou J., Hollingsworth M.A., Clausen H. J. Biol. Chem. 277:22623-22638(2002) [PubMed: 11925450] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], ENZYME ACTIVITY.
[2]	"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.
[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. Strain: Berkeley.
[5]	Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M., Park S., Wan K.H., Yu C., Rubin G.M., Celniker S.E. Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Berkeley. Tissue: Embryo.
[6]	"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] OF 101-591. Strain: Berkeley. Tissue: Embryo.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF493067 mRNA. Translation: AAM62412.1. AY268068 mRNA. Translation: AAQ56704.1. AE014298 Genomic DNA. Translation: AAF48851.1. AE014298 Genomic DNA. Translation: AAN09470.1. BT016123 mRNA. Translation: AAV37008.1. AY058660 mRNA. Translation: AAL13889.1. Different initiation. AY061339 mRNA. Translation: AAL28887.1. Different initiation.
RefSeq	NP_573301.2. NM_133073.2. NP_728178.1. NM_167623.1.
UniGene	Dm.7692.
3D structure databases
ProteinModelPortal	Q8MV48.
SMR	Q8MV48. Positions 463-586.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q8MV48. 3 interactions.
MINT	MINT-325977.
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	FBtr0074624; FBpp0074395; FBgn0030930. FBtr0074625; FBpp0074396; FBgn0030930.
GeneID	32836.
KEGG	dme:Dmel_CG6394.
Organism-specific databases
CTD	32836.
FlyBase	FBgn0030930. GalNAc-T2.
Phylogenomic databases
eggNOG	inNOG08521.
GeneTree	EMGT00050000004060.
InParanoid	Q8MV48.
OMA	ECKHWDY.
OrthoDB	EOG4THT88.
PhylomeDB	Q8MV48.
Gene expression databases
ArrayExpress	Q8MV48.
Bgee	Q8MV48.
GermOnline	CG6394. 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	780630.

Entry information

Entry name

GALT7_DROME

Accession

Primary (citable) accession number: Q8MV48
Secondary accession number(s): A4V4R2 , Q5U0W9, Q95RJ3, Q95TN2, Q9VWT6

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 16, 2004
Last sequence update:	August 16, 2004
Last modified:	January 25, 2012
This is version 74 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Drosophila annotation project