Reviewed, UniProtKB/Swiss-Prot Q8CF93 (GLT13_MOUSE)

Names and origin

Protein names

Recommended name:
    Polypeptide N-acetylgalactosaminyltransferase 13
    EC=2.4.1.41
Alternative name(s):
    Polypeptide GalNAc transferase 13
      Short name=pp-GaNTase 13
      Short name=GalNAc-T13
    Protein-UDP acetylgalactosaminyltransferase 13
    UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 13

Gene names

Name:

Galnt13

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	556 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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. Has a much stronger activity than GALNT1 to transfer GalNAc to mucin peptides, such as Muc5Ac and Muc7. Able to glycosylate SDC3. Probably responsible for the synthesis of Tn antigen in neuronal cells. Ref.1 Ref.3
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 protein By similarity.
Tissue specificity	Specifically expressed in neuronal cells. Not expressed in glial cells such as astrocytes. Expressed at low level. Ref.1 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.
Disruption phenotype	No visible phenotype. It however abolishes Tn antigen in neuronal cells. Ref.3
Sequence similarities	Belongs to the glycosyltransferase 2 family. GalNAc-T subfamily. Contains 1 ricin B-type lectin domain.
Caution	Was initially wrongly assigned as Galnt8.

Ontologies

Keywords
Cellular component	Golgi apparatus Membrane
Coding sequence diversity	Alternative splicing
Domain	Signal-anchor Transmembrane
Ligand	Calcium Lectin Manganese
Molecular function	Glycosyltransferase Transferase
PTM	Disulfide bond Glycoprotein
Gene Ontology (GO)
Biological process	protein amino acid O-linked glycosylation Ref.1 Inferred from direct assay. Source: MGI
Cellular component	Golgi apparatus Inferred from electronic annotation. Source: UniProtKB-KW integral to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
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 Inferred from direct assay. Source: MGI sugar binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Alternative products

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

Isoform 1 (identifier: Q8CF93-1)

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 2 (identifier: Q8CF93-2)

The sequence of this isoform differs from the canonical sequence as follows:
     466-466: V → VHDLCLSAPSLGVGAEECCSNHPLYGLVYTPTINEQV

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 556	556	Polypeptide N-acetylgalactosaminyltransferase 13		PRO_0000059131
Regions
	Topological domain	1 – 4	4	Cytoplasmic Potential
	Transmembrane	5 – 27	23	Signal-anchor for type II membrane protein Potential
	Topological domain	28 – 556	529	Lumenal Potential
	Domain	428 – 550	123	Ricin B-type lectin
	Region	114 – 224	111	Catalytic subdomain A
	Region	284 – 346	63	Catalytic subdomain B
Amino acid modifications
	Glycosylation	94	1	N-linked (GlcNAc...) Potential
	Glycosylation	116	1	N-linked (GlcNAc...) Potential
	Glycosylation	551	1	N-linked (GlcNAc...) Potential
	Disulfide bond	441 ↔ 458		By similarity
	Disulfide bond	481 ↔ 496		By similarity
	Disulfide bond	522 ↔ 539		By similarity
Natural variations
	Alternative sequence	466	1	V → VHDLCLSAPSLGVGAEECCS NHPLYGLVYTPTINEQV in isoform 2.		VSP_011220
Experimental info
	Sequence conflict	457	1	N → K in BAC32353. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified March 1, 2003. Version 1. Checksum: 593934CFD0AED148	FASTA	556	63,983
	10 20 30 40 50 60 MRRFVYCKVV LATSLMWVLV DVFLLLYFSE CNKCDDKKER SLLPALRAVI SRNQEGPGEM 70 80 90 100 110 120 GKAVLIPKDD QEKMKELFKI NQFNLMASDL IALNRSLPDV RLEGCKTKVY PDELPNTSVV 130 140 150 160 170 180 IVFHNEAWST LLRTVYSVIN RSPHYLLSEV ILVDDASERD FLKLTLENYV KTLEVPVKII 190 200 210 220 230 240 RMEERSGLIR ARLRGAAASK GQVITFLDAH CECTLGWLEP LLARIKEDRK TVVCPIIDVI 250 260 270 280 290 300 SDDTFEYMAG SDMTYGGFNW KLNFRWYPVP QREMDRRKGD RTLPVRTPTM AGGLFSIDRN 310 320 330 340 350 360 YFEEIGTYDA GMDIWGGENL EMSFRIWQCG GSLEIVTCSH VGHVFRKATP YTFPGGTGHV 370 380 390 400 410 420 INKNNRRLAE VWMDEFKDFF YIISPGVVKV DYGDVSVRKT LRENLKCKPF SWYLENIYPD 430 440 450 460 470 480 SQIPRRYYSL GEIRNVETNQ CLDNMGRKEN EKVGIFNCHG MGGNQVFSYT ADKEIRTDDL 490 500 510 520 530 540 CLDVSRLSGP VIMLKCHHMR GNQLWEYDAE RLTLRHANSN QCLDEPSEED KMVPTMQDCS 550 GSRSQQWLLR NMTLGT
	Isoform 2. Checksum: 54A13935542D268C	FASTA	592	67,796
	10 20 30 40 50 60 MRRFVYCKVV LATSLMWVLV DVFLLLYFSE CNKCDDKKER SLLPALRAVI SRNQEGPGEM 70 80 90 100 110 120 GKAVLIPKDD QEKMKELFKI NQFNLMASDL IALNRSLPDV RLEGCKTKVY PDELPNTSVV 130 140 150 160 170 180 IVFHNEAWST LLRTVYSVIN RSPHYLLSEV ILVDDASERD FLKLTLENYV KTLEVPVKII 190 200 210 220 230 240 RMEERSGLIR ARLRGAAASK GQVITFLDAH CECTLGWLEP LLARIKEDRK TVVCPIIDVI 250 260 270 280 290 300 SDDTFEYMAG SDMTYGGFNW KLNFRWYPVP QREMDRRKGD RTLPVRTPTM AGGLFSIDRN 310 320 330 340 350 360 YFEEIGTYDA GMDIWGGENL EMSFRIWQCG GSLEIVTCSH VGHVFRKATP YTFPGGTGHV 370 380 390 400 410 420 INKNNRRLAE VWMDEFKDFF YIISPGVVKV DYGDVSVRKT LRENLKCKPF SWYLENIYPD 430 440 450 460 470 480 SQIPRRYYSL GEIRNVETNQ CLDNMGRKEN EKVGIFNCHG MGGNQVHDLC LSAPSLGVGA 490 500 510 520 530 540 EECCSNHPLY GLVYTPTINE QVFSYTADKE IRTDDLCLDV SRLSGPVIML KCHHMRGNQL 550 560 570 580 590 WEYDAERLTL RHANSNQCLD EPSEEDKMVP TMQDCSGSRS QQWLLRNMTL GT

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and characterization of a new human UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase, designated pp-GalNAc-T13, that is specifically expressed in neurons and synthesizes GalNAc alpha-serine/threonine antigen." Zhang Y., Iwasaki H., Wang H., Kudo T., Kalka T.B., Hennet T., Kubota T., Cheng L., Inaba N., Gotoh M., Togayachi A., Guo J.-M., Hisatomi H., Nakajima K., Nishihara S., Nakamura M., Marth J.D., Narimatsu H. J. Biol. Chem. 278:573-584(2003) [PubMed: 12407114] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY. Tissue: Brain.
[2]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). Strain: C57BL/6J. Tissue: Corpora quadrigemina and Hypothalamus.
[3]	"T-cell-specific deletion of a polypeptide N-acetylgalactosaminyl-transferase gene by site-directed recombination." Hennet T., Hagen F.K., Tabak L.A., Marth J.D. Proc. Natl. Acad. Sci. U.S.A. 92:12070-12074(1995) [PubMed: 8618846] [Abstract] Cited for: FUNCTION, DISRUPTION PHENOTYPE.
[4]	"Expression of UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase isoforms in murine tissues determined by real-time PCR: a new view of a large family." Young W.W. Jr., Holcomb D.R., Ten Hagen K.G., Tabak L.A. Glycobiology 13:549-557(2003) [PubMed: 12651884] [Abstract] Cited for: TISSUE SPECIFICITY.

Web resources

Functional Glycomics Gateway - GTase

Polypeptide N-acetylgalactosaminyltransferase 13

Cross-references

Sequence databases
EMBLGenBankDDBJ	AB082928 mRNA. Translation: BAC54546.1. AK038387 mRNA. Translation: BAC29981.1. AK045417 mRNA. Translation: BAC32353.1.
IPI	IPI00227277. IPI00461477.
RefSeq	NP_766618.2.
UniGene	Mm.330227 Mm.461530
3D structure databases
SMR	Q8CF93. Positions 94-552.
ModBase	Search...
Protein-protein interaction databases
STRING	Q8CF93.
Protein family/group databases
CAZy	CBM13. Carbohydrate-Binding Module Family 13. GT27. Glycosyltransferase Family 27.
Proteomic databases
PRIDE	Q8CF93.
Genome annotation databases
Ensembl	ENSMUST00000068595; ENSMUSP00000063464; ENSMUSG00000060988; Mus musculus. [Genome view] ENSMUST00000112634; ENSMUSP00000108253; ENSMUSG00000060988; Mus musculus. [Genome view] ENSMUST00000112635; ENSMUSP00000108254; ENSMUSG00000060988; Mus musculus. [Genome view] ENSMUST00000112636; ENSMUSP00000108255; ENSMUSG00000060988; Mus musculus. [Genome view]
GeneID	271786.
KEGG	mmu:271786.
UCSC	uc008jrq.1. mouse.
Organism-specific databases
CTD	271786.
MGI	MGI:2139447. Galnt13.
Phylogenomic databases
HOGENOM	Q8CF93.
HOVERGEN	Q8CF93.
OMA	YFEEIGS.
Enzyme and pathway databases
BRENDA	2.4.1.41. 244.
Gene expression databases
ArrayExpress	Q8CF93.
Bgee	Q8CF93.
Genevestigator	Q8CF93.
GermOnline	ENSMUSG00000060988. Mus musculus.
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	393497.
SOURCE	Search...

Entry information

Entry name

GLT13_MOUSE

Accession

Primary (citable) accession number: Q8CF93
Secondary accession number(s): Q8BLE4, Q8BYT3

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 16, 2004
Last sequence update:	March 1, 2003
Last modified:	November 3, 2009
This is version 63 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)