Q8IA42 (GALT4_DROME) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
N-acetylgalactosaminyltransferase 4
EC=2.4.1.-

Alternative name(s):
Protein-UDP acetylgalactosaminyltransferase 4
UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 4
Short name=pp-GaNTase 4

Gene names

Name:	pgant4
ORF Names:	CG31956

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	659 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	Expressed in developing oocytes and egg chambers. Ref.1
Developmental stage	Expressed during embryonic, larval, pupal and adult stages. Weakly expressed during early embryonic stages but displays a dramatic increase at 12-24 hours of embryonic development. Continues to be in adult but displays much lower levels in the female adult as compared with the male. 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 – 659	659	N-acetylgalactosaminyltransferase 4		PRO_0000059158
Regions
	Topological domain	1 – 25	25	Cytoplasmic Potential
	Transmembrane	26 – 48	23	Helical; Signal-anchor for type II membrane protein; Potential
	Topological domain	49 – 659	611	Lumenal Potential
	Domain	511 – 644	134	Ricin B-type lectin
	Region	192 – 303	112	Catalytic subdomain A
	Region	360 – 422	63	Catalytic subdomain B
Amino acid modifications
	Glycosylation	172	1	N-linked (GlcNAc...) Potential
	Glycosylation	194	1	N-linked (GlcNAc...) Potential
	Glycosylation	544	1	N-linked (GlcNAc...) Potential
	Glycosylation	580	1	N-linked (GlcNAc...) Potential
	Glycosylation	647	1	N-linked (GlcNAc...) Potential
	Disulfide bond	524 ↔ 541		By similarity
	Disulfide bond	571 ↔ 588		By similarity
	Disulfide bond	615 ↔ 632		By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8IA42 [UniParc]. Last modified August 16, 2004. Version 2. Checksum: 0182D42AEBAA1DD2	FASTA	659	75,806
	10 20 30 40 50 60 MPAVSILDFR RQDVHMAIKK RYVKRLLRKV VLLLVVIVTV SLVTTLVVER RMKNAAELTE 70 80 90 100 110 120 QLDPNGDPIT PVFRAANIHP TRKAPRPPFQ DRNSVVDIPR SDKLQGFRLP EPKGERKDWH 130 140 150 160 170 180 DYAAMEADRK RSGFGEHGVA VKIENPDEKQ LEKEHYEMNG FNGLISDRIS VNRSVPDLRL 190 200 210 220 230 240 EACKTRKYLA KLPNISVIFI FFNEHFNTLL RSIYSVINRT PPELLKQIVL VDDGSEWDVL 250 260 270 280 290 300 KQPLDDYVQQ HFPHLVTIVR NPERQGLIGA RIAGAKVAVG QVMVFFDSHI EVNYNWLPPL 310 320 330 340 350 360 IEPIAINPKI STCPMVDTIS HEDFSYFSGN KDGARGGFDW KMLYKQLPVL PEDALDKSMP 370 380 390 400 410 420 YRSPVMMGGL FAINTDFFWD LGGYDDQLDI WGGEQYELSF KIWMCGGMLL DVPCSRVAHI 430 440 450 460 470 480 FRGPMKPRGN PRGHNFVAKN HKRVAEVWMD EYKQYVYKRD PKTYDNLDAG DLTRQRGVRE 490 500 510 520 530 540 RLKCKSFHWF MTEVAPDFLV KFPPVEPPSY AAGIIQNVAN PVYCLDNMGK STEEAVGMFS 550 560 570 580 590 600 CADNRTHPQP NQFWELSIFR DLRMKGFDSV CLDVHEGPPN ATVWMWSCHS QGGNQFWYYD 610 620 630 640 650 RQTQRLVHGE NNKRCLEGFV ENGIAKVVAN SCENGNDRQR WEFGFVNHTM LDTFYDGLK

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]	"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 OF 16-659.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AY268065 mRNA. Translation: AAQ56701.1. AE014134 Genomic DNA. Translation: AAN10370.1. AF324752 mRNA. Translation: AAN75751.1.
RefSeq	NP_001137779.1. NM_001144307.1. NP_722910.1. NM_164539.1.
UniGene	Dm.14883.
3D structure databases
ProteinModelPortal	Q8IA42.
SMR	Q8IA42. Positions 116-645.
ModBase	Search...
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	FBtr0077523; FBpp0077212; FBgn0051956.
GeneID	261610.
KEGG	dme:Dmel_CG31956.
NMPDR	fig|7227.3.peg.595.
Organism-specific databases
CTD	261610.
FlyBase	FBgn0051956. pgant4.
Phylogenomic databases
eggNOG	inNOG06877.
GeneTree	EMGT00050000004060.
InParanoid	Q8IA42.
OMA	RPPFQDR.
OrthoDB	EOG4BRV1P.
PhylomeDB	Q8IA42.
Enzyme and pathway databases
BRENDA	2.4.1.41. 1994.
Gene expression databases
Bgee	Q8IA42.
GermOnline	CG31956. 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	843710.

Entry information

Entry name

GALT4_DROME

Accession

Primary (citable) accession number: Q8IA42
Secondary accession number(s): Q8IQ11

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 16, 2004
Last sequence update:	August 16, 2004
Last modified:	January 25, 2012
This is version 70 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Drosophila annotation project