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Q6PB93 (GALT2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 104. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Polypeptide N-acetylgalactosaminyltransferase 2

EC=2.4.1.41
Alternative name(s):
Polypeptide GalNAc transferase 2
Short name=GalNAc-T2
Short name=pp-GaNTase 2
Protein-UDP acetylgalactosaminyltransferase 2
UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 2
Gene names
Name:Galnt2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length570 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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-alpha-D-galactosamine + polypeptide = UDP + N-acetyl-alpha-D-galactosaminyl-polypeptide.

Cofactor

Manganese By similarity.

Pathway

Protein modification; protein glycosylation.

Subcellular location

Golgi apparatusGolgi 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.

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 570570Polypeptide N-acetylgalactosaminyltransferase 2
PRO_0000223392
Chain51 – 570520Polypeptide N-acetylgalactosaminyltransferase 2 soluble form
PRO_0000012267

Regions

Topological domain1 – 66Cytoplasmic Potential
Transmembrane7 – 2418Helical; Signal-anchor for type II membrane protein; Potential
Topological domain25 – 570546Lumenal Potential
Domain442 – 565124Ricin B-type lectin
Region134 – 239106Catalytic subdomain A
Region299 – 36163Catalytic subdomain B

Sites

Metal binding2231Manganese By similarity
Metal binding2251Manganese By similarity
Metal binding3581Manganese By similarity
Binding site1421Substrate By similarity
Binding site1751Substrate By similarity
Binding site2001Substrate By similarity
Binding site2241Substrate By similarity
Binding site3301Substrate By similarity
Binding site3611Substrate By similarity
Binding site3641Substrate By similarity
Binding site3661Substrate By similarity

Amino acid modifications

Glycosylation5151N-linked (GlcNAc...) Potential
Disulfide bond125 ↔ 353 By similarity
Disulfide bond344 ↔ 422 By similarity
Disulfide bond455 ↔ 472 By similarity
Disulfide bond495 ↔ 512 By similarity
Disulfide bond538 ↔ 554 By similarity

Natural variations

Alternative sequence1 – 4141MRRRS…GAGRK → MALHNPQ in isoform 2.
VSP_011201

Experimental info

Sequence conflict21R → L in AAK37548. Ref.1
Sequence conflict2261C → Y in BAC32790. Ref.2
Sequence conflict516 – 5183DSR → NSK in AAK37548. Ref.1
Sequence conflict5641F → V in AAK37548. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 90D5DC02C85A8EEA

FASTA57064,514
        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 

« Hide

Isoform 2 [UniParc].

Checksum: 58DC49843190D2E4
Show »

FASTA53660,985

References

« Hide '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. expand/collapse author list , 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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.
CCDSCCDS22769.1. [Q6PB93-1]
RefSeqNP_644678.2. NM_139272.2. [Q6PB93-1]
UniGeneMm.33808.

3D structure databases

ProteinModelPortalQ6PB93.
SMRQ6PB93. Positions 74-567.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyCBM13. Carbohydrate-Binding Module Family 13.
GT27. Glycosyltransferase Family 27.

PTM databases

PhosphoSiteQ6PB93.

Proteomic databases

MaxQBQ6PB93.
PaxDbQ6PB93.
PRIDEQ6PB93.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000034458; ENSMUSP00000034458; ENSMUSG00000089704. [Q6PB93-1]
ENSMUST00000127664; ENSMUSP00000118564; ENSMUSG00000092329. [Q6PB93-2]
GeneID108148.
KEGGmmu:108148.
UCSCuc009nwz.2. mouse. [Q6PB93-1]

Organism-specific databases

CTD2590.
MGIMGI:894694. Galnt2.

Phylogenomic databases

eggNOGCOG5533.
GeneTreeENSGT00750000117385.
HOVERGENHBG051699.
InParanoidQ6PB93.
KOK00710.
OMADDYSDNP.
OrthoDBEOG7J9VP2.
PhylomeDBQ6PB93.
TreeFamTF313267.

Enzyme and pathway databases

UniPathwayUPA00378.

Gene expression databases

BgeeQ6PB93.
GenevestigatorQ6PB93.

Family and domain databases

Gene3D3.90.550.10. 1 hit.
InterProIPR001173. Glyco_trans_2-like.
IPR029044. Nucleotide-diphossugar_trans.
IPR000772. Ricin_B_lectin.
[Graphical view]
PfamPF00535. Glycos_transf_2. 1 hit.
PF00652. Ricin_B_lectin. 1 hit.
[Graphical view]
SMARTSM00458. RICIN. 1 hit.
[Graphical view]
SUPFAMSSF50370. SSF50370. 1 hit.
SSF53448. SSF53448. 1 hit.
PROSITEPS50231. RICIN_B_LECTIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio360162.
PROQ6PB93.
SOURCESearch...

Entry information

Entry nameGALT2_MOUSE
AccessionPrimary (citable) accession number: Q6PB93
Secondary accession number(s): Q7TSI5 expand/collapse secondary AC list , Q8BL27, Q922K5, Q99ME1
Entry history
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: July 5, 2004
Last modified: July 9, 2014
This is version 104 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot