Q8MRC9 (GALT9_DROME) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Putative polypeptide N-acetylgalactosaminyltransferase 9
Short name=pp-GaNTase 9
EC=2.4.1.41

Alternative name(s):
Protein-UDP acetylgalactosaminyltransferase 9
UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 9

Gene names

Name:	pgant9
ORF Names:	CG30463

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	650 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	May catalyze 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 By similarity.
Catalytic activity	UDP-N-acetyl-alpha-D-galactosamine + polypeptide = UDP + N-acetyl-alpha-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 protein By similarity.
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 ABL75647.1 differs from that shown. Reason: Intron retention. The sequence ABL75689.1 differs from that shown. Reason: Intron retention.

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	protein glycosylation Inferred from electronic annotation. Source: UniProtKB-UniPathway
Cellular_component	Golgi membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	polypeptide N-acetylgalactosaminyltransferase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]

Isoform A (identifier: Q8MRC9-1)

Also known as: D;

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.

Note: No experimental confirmation available.

Isoform B (identifier: Q8MRC9-2)

Also known as: C;

The sequence of this isoform differs from the canonical sequence as follows:
     526-556: RNLGYGGRTCLDAPAGKKHQKKAVGTYPCHR → ANVPNGMCLDAKEKSEEETPVSIYECHG

Note: No experimental confirmation available.

Isoform E (identifier: Q8MRC9-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-383: Missing.
     526-556: RNLGYGGRTCLDAPAGKKHQKKAVGTYPCHR → ANVPNGMCLDAKEKSEEETPVSIYECHG

Note: No experimental confirmation available.

Isoform F (identifier: Q8MRC9-4)

The sequence of this isoform differs from the canonical sequence as follows:
     2-22: AFIWRRRSTTIVKLVAFALAI → NFYLSSWHCQVTQSGLVAGLE
     23-273: Missing.
     526-556: RNLGYGGRTCLDAPAGKKHQKKAVGTYPCHR → ANVPNGMCLDAKEKSEEETPVSIYECHG

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 650	650	Putative polypeptide N-acetylgalactosaminyltransferase 9		PRO_0000059163
Regions
	Topological domain	1 – 11	11	Cytoplasmic Potential
	Transmembrane	12 – 31	20	Helical; Signal-anchor for type II membrane protein; Potential
	Topological domain	32 – 650	619	Lumenal Potential
	Domain	521 – 643	123	Ricin B-type lectin
	Region	208 – 317	110	Catalytic subdomain A
	Region	378 – 440	63	Catalytic subdomain B
	Compositional bias	43 – 90	48	Gly-rich
Amino acid modifications
	Glycosylation	321	1	N-linked (GlcNAc...) Potential
	Glycosylation	373	1	N-linked (GlcNAc...) Potential
	Disulfide bond	535 ↔ 554		By similarity
	Disulfide bond	577 ↔ 590		By similarity
	Disulfide bond	616 ↔ 631		By similarity
Natural variations
	Alternative sequence	1 – 383	383	Missing in isoform E.		VSP_034632
	Alternative sequence	2 – 22	21	AFIWR…FALAI → NFYLSSWHCQVTQSGLVAGL E in isoform F.		VSP_034633
	Alternative sequence	23 – 273	251	Missing in isoform F.		VSP_034634
	Alternative sequence	526 – 556	31	RNLGY…YPCHR → ANVPNGMCLDAKEKSEEETP VSIYECHG in isoform B, isoform E and isoform F.		VSP_034635
Experimental info
	Sequence conflict	145	1	N → D in AAM51988. Ref.3
	Sequence conflict	454	1	L → P in AAM51988. Ref.3
	Sequence conflict	472	1	Y → C in AAM51988. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Isoform A (D) [UniParc]. Last modified August 16, 2004. Version 2. Checksum: AC847736AD1C07CA	FASTA	650	73,193
	10 20 30 40 50 60 MAFIWRRRST TIVKLVAFAL AIWFCIAFLV YTDDTRRRAA QEGAGASGAG SAPGVGGGAG 70 80 90 100 110 120 GLGDPIALAL RNEPAGEDFG INGNVIGGGG QKQAHDEADI PPTVGKHKAD LQAERMRKKA 130 140 150 160 170 180 AEQPKKKPQE DSKKVIDPPA NFEENPGELG KPVRLPKEMS DEMKKAVDDG WTKNAFNQYV 190 200 210 220 230 240 SDLISVHRTL PDPRDAWCKD EARYLTNLPK TDVIICFHNE AWTVLLRTVH SVLDRSPEHL 250 260 270 280 290 300 IGKIILVDDY SDMPHLKRQL EDYFAAYPKV QIIRGQKREG LIRARILGAN HAKSPVLTYL 310 320 330 340 350 360 DSHCECTEGW LEPLLDRIAR NSTTVVCPVI DVISDETLEY HYRDSGGVNV GGFDWNLQFS 370 380 390 400 410 420 WHPVPERERK RHNSTAEPVY SPTMAGGLFS IDREFFDRLG TYDSGFDIWG GENLELSFKT 430 440 450 460 470 480 WMCGGTLEIV PCSHVGHIFR KRSPYKWRSG VNVLKKNSVR LAEVWMDEYS QYYYHRIGND 490 500 510 520 530 540 KGDWGDVSDR RKLRNDLKCK SFKWYLDNIY PELFIPGDSV AHGEIRNLGY GGRTCLDAPA 550 560 570 580 590 600 GKKHQKKAVG TYPCHRQGGN QYWMLSKAGE IRRDDSCLDY AGKDVTLFGC HGGKGNQFWT 610 620 630 640 650 YRENTKQLHH GTSGKCLAIS ESKDKLLMEE CSASLSRQQW TLENYDSSKL
	Isoform B (C) [UniParc]. Checksum: A25855E919100BFE	FASTA	647	72,860
	10 20 30 40 50 60 MAFIWRRRST TIVKLVAFAL AIWFCIAFLV YTDDTRRRAA QEGAGASGAG SAPGVGGGAG 70 80 90 100 110 120 GLGDPIALAL RNEPAGEDFG INGNVIGGGG QKQAHDEADI PPTVGKHKAD LQAERMRKKA 130 140 150 160 170 180 AEQPKKKPQE DSKKVIDPPA NFEENPGELG KPVRLPKEMS DEMKKAVDDG WTKNAFNQYV 190 200 210 220 230 240 SDLISVHRTL PDPRDAWCKD EARYLTNLPK TDVIICFHNE AWTVLLRTVH SVLDRSPEHL 250 260 270 280 290 300 IGKIILVDDY SDMPHLKRQL EDYFAAYPKV QIIRGQKREG LIRARILGAN HAKSPVLTYL 310 320 330 340 350 360 DSHCECTEGW LEPLLDRIAR NSTTVVCPVI DVISDETLEY HYRDSGGVNV GGFDWNLQFS 370 380 390 400 410 420 WHPVPERERK RHNSTAEPVY SPTMAGGLFS IDREFFDRLG TYDSGFDIWG GENLELSFKT 430 440 450 460 470 480 WMCGGTLEIV PCSHVGHIFR KRSPYKWRSG VNVLKKNSVR LAEVWMDEYS QYYYHRIGND 490 500 510 520 530 540 KGDWGDVSDR RKLRNDLKCK SFKWYLDNIY PELFIPGDSV AHGEIANVPN GMCLDAKEKS 550 560 570 580 590 600 EEETPVSIYE CHGQGGNQYW MLSKAGEIRR DDSCLDYAGK DVTLFGCHGG KGNQFWTYRE 610 620 630 640 NTKQLHHGTS GKCLAISESK DKLLMEECSA SLSRQQWTLE NYDSSKL
	Isoform E [UniParc]. Checksum: 06D95D4D4B3D00E8	FASTA	264	30,256
	10 20 30 40 50 60 MAGGLFSIDR EFFDRLGTYD SGFDIWGGEN LELSFKTWMC GGTLEIVPCS HVGHIFRKRS 70 80 90 100 110 120 PYKWRSGVNV LKKNSVRLAE VWMDEYSQYY YHRIGNDKGD WGDVSDRRKL RNDLKCKSFK 130 140 150 160 170 180 WYLDNIYPEL FIPGDSVAHG EIANVPNGMC LDAKEKSEEE TPVSIYECHG QGGNQYWMLS 190 200 210 220 230 240 KAGEIRRDDS CLDYAGKDVT LFGCHGGKGN QFWTYRENTK QLHHGTSGKC LAISESKDKL 250 260 LMEECSASLS RQQWTLENYD SSKL
	Isoform F [UniParc]. Checksum: 8AB540EC2C239DF6	FASTA	396	45,208
	10 20 30 40 50 60 MNFYLSSWHC QVTQSGLVAG LERGQKREGL IRARILGANH AKSPVLTYLD SHCECTEGWL 70 80 90 100 110 120 EPLLDRIARN STTVVCPVID VISDETLEYH YRDSGGVNVG GFDWNLQFSW HPVPERERKR 130 140 150 160 170 180 HNSTAEPVYS PTMAGGLFSI DREFFDRLGT YDSGFDIWGG ENLELSFKTW MCGGTLEIVP 190 200 210 220 230 240 CSHVGHIFRK RSPYKWRSGV NVLKKNSVRL AEVWMDEYSQ YYYHRIGNDK GDWGDVSDRR 250 260 270 280 290 300 KLRNDLKCKS FKWYLDNIYP ELFIPGDSVA HGEIANVPNG MCLDAKEKSE EETPVSIYEC 310 320 330 340 350 360 HGQGGNQYWM LSKAGEIRRD DSCLDYAGKD VTLFGCHGGK GNQFWTYREN TKQLHHGTSG 370 380 390 KCLAISESKD KLLMEECSAS LSRQQWTLEN YDSSKL

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: Embryo.
[4]	Stapleton M., Carlson J.W., Frise E., Kapadia B., Park S., Wan K.H., Yu C., Celniker S.E. Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM F). Strain: Berkeley.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE013599 Genomic DNA. Translation: AAF57964.3. AE013599 Genomic DNA. Translation: AAF57966.2. AE013599 Genomic DNA. Translation: ABV53822.1. AE013599 Genomic DNA. Translation: ABV53823.1. AE013599 Genomic DNA. Translation: ABV53824.1. AY121661 mRNA. Translation: AAM51988.1. BT029588 mRNA. Translation: ABL75647.1. Sequence problems. BT029630 mRNA. Translation: ABL75689.1. Sequence problems.
RefSeq	NP_001097341.1. NM_001103871.1. NP_001097342.1. NM_001103872.1. NP_001097343.1. NM_001103873.1. NP_725602.1. NM_166188.1. NP_725603.2. NM_166189.2.
UniGene	Dm.24533.
3D structure databases
ProteinModelPortal	Q8MRC9.
SMR	Q8MRC9. Positions 147-650.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q8MRC9. 1 interaction.
MINT	MINT-964044.
Protein family/group databases
CAZy	CBM13. Carbohydrate-Binding Module Family 13. GT27. Glycosyltransferase Family 27.
Proteomic databases
PaxDb	Q8MRC9.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblMetazoa	FBtr0087112; FBpp0086258; FBgn0050463. FBtr0113380; FBpp0112292; FBgn0050463.
GeneID	246627.
KEGG	dme:Dmel_CG30463.
UCSC	CG30463-RA. d. melanogaster.
Organism-specific databases
FlyBase	FBgn0050463. CG30463.
Phylogenomic databases
eggNOG	NOG239675.
GeneTree	ENSGT00700000104138.
InParanoid	Q8MRC9.
KO	K00710.
OMA	RSTTIVK.
OrthoDB	EOG46WWQF.
PhylomeDB	Q8MRC9.
Enzyme and pathway databases
UniPathway	UPA00378.
Gene expression databases
Bgee	Q8MRC9.
GermOnline	CG30463. 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	CG30463. drosophila.
GenomeRNAi	246627.
NextBio	843268.

Entry information

Entry name

GALT9_DROME

Accession

Primary (citable) accession number: Q8MRC9
Secondary accession number(s): A1A6R7 , A1A6V9, A8DYG1, A8DYG2, A8DYG3, Q0E950, Q9V7T0

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 16, 2004
Last sequence update:	August 16, 2004
Last modified:	May 1, 2013
This is version 92 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Drosophila annotation project