Q6WV17 (GALT5_DROME) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Polypeptide N-acetylgalactosaminyltransferase 5
Short name=pp-GaNTase 5
EC=2.4.1.41

Alternative name(s):
Protein-UDP acetylgalactosaminyltransferase 5
UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 5

Gene names

Name:	pgant5
ORF Names:	CG31651

Organism

Drosophila melanogaster (Fruit fly) [Reference proteome]

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Protostomia › Ecdysozoa › Panarthropoda › Arthropoda › Mandibulata › Pancrustacea › Hexapoda › Insecta › Dicondylia › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Eremoneura › Cyclorrhapha › Schizophora › Acalyptratae › Ephydroidea › Drosophilidae › Drosophilinae › Drosophilini › Drosophilina › Drosophiliti › Drosophila › Sophophora › melanogaster group › melanogaster subgroup

Protein attributes

Sequence length	630 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 EA2 as substrate.
Catalytic activity	UDP-N-acetyl-alpha-D-galactosamine + polypeptide = UDP + N-acetyl-alpha-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	In embryos, it is specifically expressed in the salivary glands, and not in other tissues. Exhibits conspicuous expression in the hindgut of stage 16 embryo. Further expressed during oogenesis, in the somatically derived follicle cells that surround the developing oocyte, which are involved in the maturation of the oocyte and construction of the egg shell, as well as playing a role in subsequent embryonic pattern formation. Ref.4
Developmental stage	Expressed throughout embryonic, larval, pupal and adult stages, with increasing levels during larval development. 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.
Sequence caution	The sequence AAL25377.1 differs from that shown. Reason: Erroneous termination at position 29. Translated as Trp.

Ontologies

Keywords
Cellular component	Golgi apparatus Membrane
Coding sequence diversity	Alternative splicing
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.4. Source: UniProtKB protein glycosylation Inferred from electronic annotation. Source: UniProtKB-UniPathway
Cellular_component	Golgi membrane Inferred from electronic annotation. Source: UniProtKB-SubCell Golgi stack Non-traceable author statement Ref.4. Source: UniProtKB integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	polypeptide N-acetylgalactosaminyltransferase activity Inferred from direct assay Ref.4. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform A (identifier: Q6WV17-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform B (identifier: Q6WV17-2)

The sequence of this isoform differs from the canonical sequence as follows:
     398-457: IWQCGGILEI...WRDFYYSMST → VWMCGGVLEI...WKEFYYSFYP

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 630	630	Polypeptide N-acetylgalactosaminyltransferase 5		PRO_0000059159
Regions
	Topological domain	1 – 20	20	Cytoplasmic Potential
	Transmembrane	21 – 38	18	Helical; Signal-anchor for type II membrane protein; Potential
	Topological domain	39 – 630	592	Lumenal Potential
	Domain	500 – 622	123	Ricin B-type lectin
	Region	186 – 296	111	Catalytic subdomain A
	Region	356 – 418	63	Catalytic subdomain B
Amino acid modifications
	Glycosylation	166	1	N-linked (GlcNAc...) Potential
	Disulfide bond	513 ↔ 530		By similarity
	Disulfide bond	553 ↔ 568		By similarity
	Disulfide bond	594 ↔ 611		By similarity
Natural variations
	Alternative sequence	398 – 457	60	IWQCG…YSMST → VWMCGGVLEIAPCSRVGHVF RKSTPYTFPGGTTEIVNHNN ARLVEVWLDDWKEFYYSFYP in isoform B.		VSP_034631
Experimental info
	Sequence conflict	591	1	T → S in AAQ56702. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	Isoform A [UniParc]. Last modified August 16, 2004. Version 2. Checksum: A822748C9EC96175	FASTA	630	72,097
	10 20 30 40 50 60 MTFSTFTRKM RGRMRSNTCR IVLLTSLVWV IFDFVLIARY SDCIGKDGWR CKRSGEYDVE 70 80 90 100 110 120 LPNAERLVDD NQLVDDNEIN TEKSLDGESG GALIMGQGFA SGGISMTYPS VVLKKWFLAP 130 140 150 160 170 180 SVQEAKGKPG EMGKPVKIPA DMKDLMKEKF KENQFNLLAS DMISLNRSLT DVRHEGCRRK 190 200 210 220 230 240 HYASKLPTTS IVIVFHNEAW TTLLRTVWSV INRSPRALLK EIILVDDASE RDFLGKQLEE 250 260 270 280 290 300 YVAKLPVKTF VLRTEKRSGL IRARLLGAEH VSGEVITFLD AHCECTEGWL EPLLARIVQN 310 320 330 340 350 360 RRTVVCPIID VISDETFEYI TASDSTWGGF NWKLNFRWYR VPSREMARRN NDRTAPLRTP 370 380 390 400 410 420 TMAGGLFSID KDYFYEIGSY DEGMDIWGGE NLEMSFRIWQ CGGILEIIPC SHVGHVFRDK 430 440 450 460 470 480 SPYTFPGGVA KIVLHNAARV AEVWLDEWRD FYYSMSTGAR KASAGDVSDR KALRDRLKCK 490 500 510 520 530 540 SFRWYLENVY PESLMPLDYY YLGEIRNAET ETCLDTMGRK YNEKVGISYC HGLGGNQVFA 550 560 570 580 590 600 YTKRQQIMSD DLCLDASSSN GPVNMVRCHN MGGNQEWVYD AEEKWIRHTN TGQCLQRATR 610 620 630 DDANTPLLRP CSYGKGQQWL MESKFKWQAH
	Isoform B [UniParc]. Checksum: 51E9F2F0F41525AE	FASTA	630	72,214
	10 20 30 40 50 60 MTFSTFTRKM RGRMRSNTCR IVLLTSLVWV IFDFVLIARY SDCIGKDGWR CKRSGEYDVE 70 80 90 100 110 120 LPNAERLVDD NQLVDDNEIN TEKSLDGESG GALIMGQGFA SGGISMTYPS VVLKKWFLAP 130 140 150 160 170 180 SVQEAKGKPG EMGKPVKIPA DMKDLMKEKF KENQFNLLAS DMISLNRSLT DVRHEGCRRK 190 200 210 220 230 240 HYASKLPTTS IVIVFHNEAW TTLLRTVWSV INRSPRALLK EIILVDDASE RDFLGKQLEE 250 260 270 280 290 300 YVAKLPVKTF VLRTEKRSGL IRARLLGAEH VSGEVITFLD AHCECTEGWL EPLLARIVQN 310 320 330 340 350 360 RRTVVCPIID VISDETFEYI TASDSTWGGF NWKLNFRWYR VPSREMARRN NDRTAPLRTP 370 380 390 400 410 420 TMAGGLFSID KDYFYEIGSY DEGMDIWGGE NLEMSFRVWM CGGVLEIAPC SRVGHVFRKS 430 440 450 460 470 480 TPYTFPGGTT EIVNHNNARL VEVWLDDWKE FYYSFYPGAR KASAGDVSDR KALRDRLKCK 490 500 510 520 530 540 SFRWYLENVY PESLMPLDYY YLGEIRNAET ETCLDTMGRK YNEKVGISYC HGLGGNQVFA 550 560 570 580 590 600 YTKRQQIMSD DLCLDASSSN GPVNMVRCHN MGGNQEWVYD AEEKWIRHTN TGQCLQRATR 610 620 630 DDANTPLLRP CSYGKGQQWL MESKFKWQAH

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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: GENOME REANNOTATION, ALTERNATIVE SPLICING. Strain: Berkeley.
[3]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A). Strain: Berkeley. Tissue: Head.
[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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 14-630 (ISOFORM A), 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: AAF52218.2. AE014134 Genomic DNA. Translation: ABI31292.1. AY060338 mRNA. Translation: AAL25377.1. Sequence problems. AY268066 mRNA. Translation: AAQ56702.1.
RefSeq	NP_001036338.1. NM_001042873.2. NP_608906.2. NM_135062.4.
UniGene	Dm.4033.
3D structure databases
ProteinModelPortal	Q6WV17.
SMR	Q6WV17. Positions 166-623.
ModBase	Search...
Protein family/group databases
CAZy	CBM13. Carbohydrate-Binding Module Family 13. GT27. Glycosyltransferase Family 27.
Proteomic databases
PaxDb	Q6WV17.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblMetazoa	FBtr0079026; FBpp0078663; FBgn0031681.
GeneID	326151.
KEGG	dme:Dmel_CG31651.
Organism-specific databases
CTD	326151.
FlyBase	FBgn0031681. pgant5.
Phylogenomic databases
eggNOG	NOG239675.
GeneTree	ENSGT00700000104138.
InParanoid	Q6WV17.
KO	K00710.
OMA	DETFEYM.
OrthoDB	EOG431ZD4.
PhylomeDB	Q6WV17.
Enzyme and pathway databases
BRENDA	2.4.1.41. 1994.
UniPathway	UPA00378.
Gene expression databases
Bgee	Q6WV17.
GermOnline	CG31651. 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]
SUPFAM	SSF50370. RicinB_like. 1 hit.
PROSITE	PS50231. RICIN_B_LECTIN. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	pgant5. drosophila.
GenomeRNAi	326151.
NextBio	847327.

Entry information

Entry name

GALT5_DROME

Accession

Primary (citable) accession number: Q6WV17
Secondary accession number(s): Q0E8T2, Q95T43, Q9VMU3

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 16, 2004
Last sequence update:	August 16, 2004
Last modified:	May 1, 2013
This is version 82 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Drosophila annotation project