Reviewed, UniProtKB/Swiss-Prot Q6PB93 (GALT2_MOUSE)

Names and origin

Protein names

Recommended name:
    Polypeptide N-acetylgalactosaminyltransferase 2
    EC=2.4.1.41
Alternative name(s):
    Polypeptide GalNAc transferase 2
      Short name=pp-GaNTase 2
      Short name=GalNAc-T2
    Protein-UDP acetylgalactosaminyltransferase 2
    UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 2
Cleaved into the following chain:
    1- Recommended name:
            Polypeptide N-acetylgalactosaminyltransferase 2 soluble form

Gene names

Name:

Galnt2

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	570 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
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 broad spectrum of substrates for peptides such as EA2, Muc5AC, Muc1a, Muc1b. Probably involved in O-linked glycosylation of the immunoglobulin A1 (IgA1) hinge region By similarity.
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 › Golgi stack membrane; Single-pass type II membrane protein. Secreted. Note: Resides preferentially in the trans and medial parts of the Golgi stack. A secreted form also exists.
Tissue specificity	Widely expressed at high level. 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.

Ontologies

Keywords
Cellular component	Golgi apparatus Membrane Secreted
Coding sequence diversity	Alternative splicing
Domain	Signal-anchor Transmembrane
Ligand	Calcium Lectin Manganese
Molecular function	Glycosyltransferase Transferase
PTM	Disulfide bond Glycoprotein
Gene Ontology (GO)
Cellular component	Golgi lumen Traceable author statement. Source: MGI extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell 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 Inferred from electronic annotation. Source: EC 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: Q6PB93-1)

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: Q6PB93-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-41: MRRRSRMLLCFALLWVLGIAYYMYSGGGSALAAGGGGAGRK → MALHNPQ

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 570	570	Polypeptide N-acetylgalactosaminyltransferase 2		PRO_0000223392
	Chain	51 – 570	520	Polypeptide N-acetylgalactosaminyltransferase 2 soluble form		PRO_0000012267
Regions
	Topological domain	1 – 6	6	Cytoplasmic Potential
	Transmembrane	7 – 24	18	Signal-anchor for type II membrane protein Potential
	Topological domain	25 – 570	546	Lumenal Potential
	Domain	442 – 565	124	Ricin B-type lectin
	Region	134 – 239	106	Catalytic subdomain A
	Region	299 – 361	63	Catalytic subdomain B
Amino acid modifications
	Glycosylation	515	1	N-linked (GlcNAc...) Potential
	Disulfide bond	455 ↔ 472		By similarity
	Disulfide bond	495 ↔ 512		By similarity
	Disulfide bond	538 ↔ 554		By similarity
Natural variations
	Alternative sequence	1 – 41	41	MRRRS…GAGRK → MALHNPQ in isoform 2.		VSP_011201
Experimental info
	Sequence conflict	2	1	R → L in AAK37548. Ref.1
	Sequence conflict	226	1	C → Y in BAC32790. Ref.2
	Sequence conflict	516 – 518	3	DSR → NSK in AAK37548. Ref.1
	Sequence conflict	564	1	F → V in AAK37548. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified July 5, 2004. Version 1. Checksum: 90D5DC02C85A8EEA	FASTA	570	64,514
	10 20 30 40 50 60 MRRRSRMLLC FALLWVLGIA YYMYSGGGSA LAAGGGGAGR KGDWNDIDSI KKKDLHHSRG 70 80 90 100 110 120 DEKAQGVETL PPGKVRWPDF NQEAYVGGTM VRSGQDPYAR NKFNQVESDK LHMDRGIPDT 130 140 150 160 170 180 RHDQCQRKQW RVDLPATSVV ITFHNEARSA LLRTVVSVLK RSPPHLIKEI ILVDDYSNDP 190 200 210 220 230 240 EDGALLGKIE KVRVLRNDRR EGLMRSRVRG ADAAQAKVLT FLDSHCECNE RWLEPLLERV 250 260 270 280 290 300 AEDRTRVVSP IIDVINMDNF QYVGASADLK GGFDWNLVFK WDYMTPEQRR SRQGNPVAPI 310 320 330 340 350 360 KTPMIAGGLF VMDKLYFEEL GKYDMMMDVW GGENLEISFR VWQCGGSLEI IPCSRVGHVF 370 380 390 400 410 420 RKQHPYTFPG GSGTVFARNT RRAAEVWMDE YKHFYYAAVP SARNVPYGNI QSRLELRKKL 430 440 450 460 470 480 GCKPFKWYLD NVYPELRVPD HQDIAFGALQ QGTNCLDTLG HFADGVVGIY ECHNAGGNQE 490 500 510 520 530 540 WALTKEKSVK HMDLCLTVVD RSPGSLIRLQ GCRENDSRQK WEQIEGNSKL RHVGSNLCLD 550 560 570 SRTAKSGGLS VEVCGPALSQ QWKFSLNLQQ
	Isoform 2. Checksum: 58DC49843190D2E4	FASTA	536	60,985
	10 20 30 40 50 60 MALHNPQGDW NDIDSIKKKD LHHSRGDEKA QGVETLPPGK VRWPDFNQEA YVGGTMVRSG 70 80 90 100 110 120 QDPYARNKFN QVESDKLHMD RGIPDTRHDQ CQRKQWRVDL PATSVVITFH NEARSALLRT 130 140 150 160 170 180 VVSVLKRSPP HLIKEIILVD DYSNDPEDGA LLGKIEKVRV LRNDRREGLM RSRVRGADAA 190 200 210 220 230 240 QAKVLTFLDS HCECNERWLE PLLERVAEDR TRVVSPIIDV INMDNFQYVG ASADLKGGFD 250 260 270 280 290 300 WNLVFKWDYM TPEQRRSRQG NPVAPIKTPM IAGGLFVMDK LYFEELGKYD MMMDVWGGEN 310 320 330 340 350 360 LEISFRVWQC GGSLEIIPCS RVGHVFRKQH PYTFPGGSGT VFARNTRRAA EVWMDEYKHF 370 380 390 400 410 420 YYAAVPSARN VPYGNIQSRL ELRKKLGCKP FKWYLDNVYP ELRVPDHQDI AFGALQQGTN 430 440 450 460 470 480 CLDTLGHFAD GVVGIYECHN AGGNQEWALT KEKSVKHMDL CLTVVDRSPG SLIRLQGCRE 490 500 510 520 530 NDSRQKWEQI EGNSKLRHVG SNLCLDSRTA KSGGLSVEVC GPALSQQWKF SLNLQQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	Miyahara N., Kanoh A., Irimura T. Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Colon adenocarcinoma.
[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] (ISOFORM 1). Strain: C57BL/6J. Tissue: Adipose tissue.
[3]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). Strain: C57BL/6 and Czech II. Tissue: Brain and Mammary tumor.
[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.
+	Additional computationally mapped references.

Web resources

Functional Glycomics Gateway - GTase

Polypeptide N-acetylgalactosaminyltransferase 2

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF348968 mRNA. Translation: AAK37548.1. AK046567 mRNA. Translation: BAC32790.1. BC007172 mRNA. Translation: AAH07172.1. BC053063 mRNA. Translation: AAH53063.1. BC059818 mRNA. Translation: AAH59818.1.
IPI	IPI00420710. IPI00460865.
RefSeq	NP_644678.2.
UniGene	Mm.33808
3D structure databases
SMR	Q6PB93. Positions 40-566, 74-567.
ModBase	Search...
Protein-protein interaction databases
STRING	Q6PB93.
Protein family/group databases
CAZy	CBM13. Carbohydrate-Binding Module Family 13. GT27. Glycosyltransferase Family 27.
Proteomic databases
PRIDE	Q6PB93.
Genome annotation databases
Ensembl	ENSMUST00000034458; ENSMUSP00000034458; ENSMUSG00000031977; Mus musculus. [Genome view]
GeneID	108148.
KEGG	mmu:108148.
UCSC	uc009nwz.1. mouse.
Organism-specific databases
CTD	108148.
MGI	MGI:894694. Galnt2.
Phylogenomic databases
HOVERGEN	Q6PB93.
InParanoid	Q6PB93.
OMA	QRRSRQG.
OrthoDB	EOG9HB161.
PhylomeDB	Q6PB93.
Enzyme and pathway databases
BRENDA	2.4.1.41. 244.
Gene expression databases
ArrayExpress	Q6PB93.
Bgee	Q6PB93.
Genevestigator	Q6PB93.
GermOnline	ENSMUSG00000031977. Mus musculus.
Family and domain databases
InterPro	IPR001173. Glyco_trans_2. IPR008997. Ricin_B-rel_lectin. 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	360162.
SOURCE	Search...

Entry information

Entry name

GALT2_MOUSE

Accession

Primary (citable) accession number: Q6PB93
Secondary accession number(s): Q7TSI5 , Q8BL27, Q922K5, Q99ME1

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 16, 2004
Last sequence update:	July 5, 2004
Last modified:	January 19, 2010
This is version 65 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)