Q8IA44 (GLT12_DROME) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Putative polypeptide N-acetylgalactosaminyltransferase 12
Short name=pp-GaNTase 12
EC=2.4.1.41

Alternative name(s):
Protein-UDP acetylgalactosaminyltransferase 12
UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 12

Gene names

Name:	pgant12
ORF Names:	CG7304

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	563 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.
Caution	Although strongly related to polypeptide N-acetylgalactosaminyltransferase proteins, it lacks the conserved Asp-Xaa-His motif in positions 209-211 and the conserved His residue in position 211. This suggests that it may have lost its activity.
Sequence caution	The sequence AAF49589.2 differs from that shown. Reason: Erroneous gene model prediction.

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 sequence or structural similarity. Source: UniProtKB 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 sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 563	563	Putative polypeptide N-acetylgalactosaminyltransferase 12		PRO_0000059166
Regions
	Topological domain	1 – 6	6	Cytoplasmic Potential
	Transmembrane	7 – 29	23	Helical; Signal-anchor for type II membrane protein; Potential
	Topological domain	30 – 563	534	Lumenal Potential
	Domain	433 – 549	117	Ricin B-type lectin
	Region	109 – 225	117	Catalytic subdomain A
	Region	280 – 342	63	Catalytic subdomain B
Amino acid modifications
	Glycosylation	50	1	N-linked (GlcNAc...) Potential
	Glycosylation	389	1	N-linked (GlcNAc...) Potential
	Glycosylation	428	1	N-linked (GlcNAc...) Potential
	Glycosylation	464	1	N-linked (GlcNAc...) Potential
	Glycosylation	469	1	N-linked (GlcNAc...) Potential
	Glycosylation	552	1	N-linked (GlcNAc...) Potential
	Disulfide bond	446 ↔ 461		By similarity
	Disulfide bond	485 ↔ 499		By similarity
	Disulfide bond	523 ↔ 537		By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8IA44 [UniParc]. Last modified March 1, 2003. Version 1. Checksum: F56D71430BD88B36	FASTA	563	65,108
	10 20 30 40 50 60 MEVFASVLNC CFKYIVLPVW IFIVLLLLHR DLSSWDGLMG PLSHPGLGEN GSASYLSVPS 70 80 90 100 110 120 WEIDEYTQGW RYYLYNSWLA ERIPLRRSLP DLRDHRCQKL EYDEDSDEMK PASIIMIFRN 130 140 150 160 170 180 EQLVVLLRTL HSLVERTPKY LYIELILVND HSDTDFWNDK LSLIFFDNYV HRYIHPKARI 190 200 210 220 230 240 LHLPEQVGLI KARNLAASEA KAENLVFVDA QVEFTNGWLS PLLDTIAEQS YTLATPILDN 250 260 270 280 290 300 LDEQTLAYQR SIERRGMYDW SLTRREVPLS RARRSHLPWP YEVAAVRTSV FAIPAVWFQD 310 320 330 340 350 360 ISNFDNNLRG FGAAELELSF KVWCTGGRIV QVPCSRVGHL QPKDEDYLKR YGDLHKMGEQ 370 380 390 400 410 420 KSRNLKRIIE VWTGDLKSAI YKYQPHLLNI SEGDLNEPRK LYKQNECQSF KEFINDITPG 430 440 450 460 470 480 LNHVAALNRT DYASGHVKTL EFPKKCLTIN AKSQNLFLER CSTNNTLQNW TLTYVKDLRV 490 500 510 520 530 540 AGNICAEVRP NLRLGYSFCH SLGGRQSWHY DSVSNQLMSN TKCLEFTDEL NIFLAICDAA 550 560 NGKQRWILDN INLSVMQSAN ILV

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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: GENOME REANNOTATION. Strain: Berkeley.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF324750 mRNA. Translation: AAN75749.1. AE014296 Genomic DNA. Translation: AAF49589.2. Sequence problems. AE014296 Genomic DNA. Translation: AAS64999.1.
RefSeq	NP_996098.1. NM_206376.1.
UniGene	Dm.14885.
3D structure databases
ProteinModelPortal	Q8IA44.
SMR	Q8IA44. Positions 46-560.
ModBase	Search...
Protein-protein interaction databases
STRING	7227.FBpp0075329.
Protein family/group databases
CAZy	CBM13. Carbohydrate-Binding Module Family 13. GT27. Glycosyltransferase Family 27.
Proteomic databases
PRIDE	Q8IA44.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblMetazoa	FBtr0075577; FBpp0075330; FBgn0036527.
GeneID	39713.
KEGG	dme:Dmel_CG7304.
UCSC	CG7304-RA. d. melanogaster.
Organism-specific databases
FlyBase	FBgn0036527. CG7304.
Phylogenomic databases
eggNOG	NOG252016.
GeneTree	ENSGT00670000097647.
InParanoid	Q8IA44.
KO	K00710.
OMA	QVPCSRV.
OrthoDB	EOG4CFXQD.
PhylomeDB	Q8IA44.
Enzyme and pathway databases
UniPathway	UPA00378.
Gene expression databases
Bgee	Q8IA44.
GermOnline	CG7304. 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
GenomeRNAi	39713.
NextBio	815001.

Entry information

Entry name

GLT12_DROME

Accession

Primary (citable) accession number: Q8IA44
Secondary accession number(s): Q9VUT4

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 16, 2004
Last sequence update:	March 1, 2003
Last modified:	May 1, 2013
This is version 76 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Drosophila annotation project