Reviewed, UniProtKB/Swiss-Prot Q8MVS5 (GLT35_DROME)

Names and origin

Protein names

Recommended name:
    Polypeptide N-acetylgalactosaminyltransferase 35A
    EC=2.4.1.41
Alternative name(s):
    Protein-UDP acetylgalactosaminyltransferase 35A
    UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 35A
      Short name=pp-GaNTase 35A
    Protein l(2)35Aa
    dGalNAc-T1

Gene names

Name:	Pgant35A
ORF Names:	CG7480

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

General annotation (Comments)

Function	Essential glycotransferase, which 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.
Catalytic activity	UDP-N-acetyl-D-galactosamine + polypeptide = UDP + N-acetyl-D-galactosaminyl-polypeptide.
Cofactor	Manganese By similarity. Calcium By similarity.
Pathway	Protein modification; protein glycosylation.
Subcellular location	Golgi apparatus membrane; Single-pass type II membrane proteinBy similarity.
Tissue specificity	Expressed at high level in ovaries. Expressed at low level in testis. Expressed at higher level in adult females than males. During oogenesis, it is detected in germ cells and follicle epithelia of all developmental stages. Initially expressed during early stages of oogenesis in region I and reaches high levels in regions IIa and IIb of the germarium. Highly expressed in stage 2 egg chambers. Remains highly expressed during later stages of oogenesis.
Developmental stage	Expressed both maternally and zygotically. Expressed throughout embryonic, larval, pupal and adult stages, with increasing levels during larval development.
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.
Biophysicochemical properties	Kinetic parameters: KM=8.5 µM for UDP-GalNAc KM=0.35 mM for EA2 acceptor peptide

Ontologies

Keywords
Cellular component	Golgi apparatus Membrane
Domain	Signal-anchor Transmembrane
Ligand	Calcium Lectin Manganese
Molecular function	Glycosyltransferase Transferase
PTM	Glycoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	oligosaccharide biosynthetic process Ref.1 Ref.2 Inferred from direct assay. Source: UniProtKB open tracheal system development Inferred from mutant phenotype. Source: FlyBase
Cellular component	Golgi membrane Inferred from electronic annotation. Source: UniProtKB-SubCell Golgi stack Ref.1 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.1 Ref.2 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 – 632	632	Polypeptide N-acetylgalactosaminyltransferase 35A		PRO_0000059168
Regions
	Topological domain	1 – 6	6	Cytoplasmic Potential
	Transmembrane	7 – 29	23	Signal-anchor for type II membrane protein Potential
	Topological domain	30 – 632	603	Lumenal Potential
	Domain	526 – 632	107	Ricin B-type lectin
	Region	147 – 259	113	Catalytic subdomain A
	Region	317 – 379	63	Catalytic subdomain B
Amino acid modifications
	Glycosylation	49	1	N-linked (GlcNAc...)
	Glycosylation	69	1	N-linked (GlcNAc...) Potential
	Glycosylation	264	1	N-linked (GlcNAc...) Potential
	Disulfide bond	539 ↔ 553		By similarity
	Disulfide bond	580 ↔ 597		By similarity
Experimental info
	Mutagenesis	227	1	R → W in SF32; induces lethality
	Sequence conflict	72	1	I → T in AAM62405. Ref.1
	Sequence conflict	628	1	S → T in AAL49213. Ref.6

Sequences

	Sequence		Length	Mass (Da)
	Q8MVS5-1 [UniParc]. Last modified August 16, 2004. Version 2. Checksum: E726B9F32481E4E9	FASTA	632	71,828
	10 20 30 40 50 60 MMQIKRLLCK SCGLGTLLVA VVWLLALLFY SHSLRSSIRS AGWRIDEGNA TPRAELSYQA 70 80 90 100 110 120 RVTVGCTPNA SITTGESPAA PKPPSDPEQL ELLGVVRNKQ DKYIRDIGYK HHAFNALVSN 130 140 150 160 170 180 NIGLFRAIPD TRHKVCDRQE TTEAENLPQA SIVMCFYNEH KMTLMRSIKT VLERTPSYLL 190 200 210 220 230 240 REIILVDDHS DLPELEFHLH GDLRARLKYD NLRYIKNEQR EGLIRSRVIG AREAVGDVLV 250 260 270 280 290 300 FLDSHIEVNQ QWLEPLLRLI KSENATLAVP VIDLINADTF EYTPSPLVRG GFNWGLHFRW 310 320 330 340 350 360 ENLPEGTLKV PEDFRGPFRS PTMAGGLFAV NRKYFQHLGE YDMAMDIWGG ENIEISFRAW 370 380 390 400 410 420 QCGGAIKIVP CSRVGHIFRK RRPYTSPDGA NTMLKNSLRL AHVWMDQYKD YYLKHEKVPK 430 440 450 460 470 480 TYDYGDISDR LKLRERLQCR DFAWYLKNVY PELHVPGEES KKSAAAPIFQ PWHSRKRNYV 490 500 510 520 530 540 DTFQLRLTGT ELCAAVVAPK VKGFWKKGSS LQLQTCRRTP NQLWYETEKA EIVLDKLLCL 550 560 570 580 590 600 EASGDAQVTV NKCHEMLGDQ QWRHTRNANS PVYNMAKGTC LRAAAPTTGA LISLDLCSKS 610 620 630 NGAGGSWDIV QLKKPTEAEG RAKEARNSDK AL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase is essential for viability in Drosophila melanogaster." Ten Hagen K.G., Tran D.T. J. Biol. Chem. 277:22616-22622(2002) [PubMed: 11925446] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], ENZYME ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, DEVELOPMENTAL STAGE, MUTANT SF32. Strain: Canton-S. Tissue: Embryo.
[2]	"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, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, MUTANT SF32.
[3]	"An exploration of the sequence of a 2.9-Mb region of the genome of Drosophila melanogaster: the Adh region." Ashburner M., Misra S., Roote J., Lewis S.E., Blazej R.G., Davis T., Doyle C., Galle R.F., George R.A., Harris N.L., Hartzell G., Harvey D.A., Hong L., Houston K.A., Hoskins R.A., Johnson G., Martin C., Moshrefi A.R. , Palazzolo M., Reese M.G., Spradling A.C., Tsang G., Wan K.H., Whitelaw K., Celniker S.E., Rubin G.M. Genetics 153:179-219(1999) [PubMed: 10471707] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Berkeley.
[4]	"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.
[5]	"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.
[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]. Strain: Berkeley. Tissue: Embryo.
[7]	"Identification of N-glycosylated proteins from the central nervous system of Drosophila melanogaster." Koles K., Lim J.-M., Aoki K., Porterfield M., Tiemeyer M., Wells L., Panin V. Glycobiology 17:1388-1403(2007) [PubMed: 17893096] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-49, MASS SPECTROMETRY. Tissue: Head.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF478697 mRNA. Translation: AAM62405.1. AF478698 Genomic DNA. Translation: AAM62406.1. AF478699 Genomic DNA. Translation: AAM62407.1. AF478700 Genomic DNA. Translation: AAM62408.1. AF158747 mRNA. Translation: AAK66862.1. Different initiation. AE014134 Genomic DNA. Translation: AAF53391.1. AY071591 mRNA. Translation: AAL49213.1.
RefSeq	NP_652069.2.
UniGene	Dm.1528
3D structure databases
ModBase	Search...
Genome annotation databases
Ensembl	CG7480. Drosophila melanogaster. [Contig view]
GeneID	48775.
KEGG	dme:Dmel_CG7480.
NMPDR	fig|7227.3.peg.2407.
Organism-specific databases
FlyBase	FBgn0001970. Pgant35A.
Gene expression databases
ArrayExpress	Q8MVS5.
GermOnline	CG7480. 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	839543.

Entry information

Entry name

GLT35_DROME

Accession

Primary (citable) accession number: Q8MVS5
Secondary accession number(s): Q8MVS2 , Q8MVS3, Q8MVS4, Q8SYF1, Q965E4, Q9V3C9

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 16, 2004
Last sequence update:	August 16, 2004
Last modified:	November 25, 2008
This is version 45 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Drosophila annotation project