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Protein

Polypeptide N-acetylgalactosaminyltransferase 2

Gene

Galnt2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

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).By similarity

Catalytic activityi

UDP-N-acetyl-alpha-D-galactosamine + polypeptide = UDP + N-acetyl-alpha-D-galactosaminyl-polypeptide.

Cofactori

Mn2+By similarity

Pathway:iprotein glycosylation

This protein is involved in the pathway protein glycosylation, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein glycosylation and in Protein modification.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei142 – 1421SubstrateBy similarity
Binding sitei175 – 1751SubstrateBy similarity
Binding sitei200 – 2001SubstrateBy similarity
Metal bindingi223 – 2231ManganeseBy similarity
Binding sitei224 – 2241SubstrateBy similarity
Metal bindingi225 – 2251ManganeseBy similarity
Binding sitei330 – 3301SubstrateBy similarity
Metal bindingi358 – 3581ManganeseBy similarity
Binding sitei361 – 3611SubstrateBy similarity
Binding sitei364 – 3641SubstrateBy similarity
Binding sitei366 – 3661SubstrateBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Ligandi

Lectin, Manganese, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_278772. O-linked glycosylation of mucins.
UniPathwayiUPA00378.

Protein family/group databases

CAZyiCBM13. Carbohydrate-Binding Module Family 13.
GT27. Glycosyltransferase Family 27.

Names & Taxonomyi

Protein namesi
Recommended 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
Cleaved into the following chain:
Gene namesi
Name:Galnt2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 8

Organism-specific databases

MGIiMGI:894694. Galnt2.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 66CytoplasmicSequence Analysis
Transmembranei7 – 2418Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST
Topological domaini25 – 570546LumenalSequence AnalysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus, Membrane, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 570570Polypeptide N-acetylgalactosaminyltransferase 2PRO_0000223392Add
BLAST
Chaini51 – 570520Polypeptide N-acetylgalactosaminyltransferase 2 soluble formPRO_0000012267Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi125 ↔ 353PROSITE-ProRule annotation
Disulfide bondi344 ↔ 422PROSITE-ProRule annotation
Disulfide bondi455 ↔ 472PROSITE-ProRule annotation
Disulfide bondi495 ↔ 512PROSITE-ProRule annotation
Glycosylationi515 – 5151N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi538 ↔ 554PROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiQ6PB93.
PaxDbiQ6PB93.
PRIDEiQ6PB93.

PTM databases

PhosphoSiteiQ6PB93.

Expressioni

Tissue specificityi

Widely expressed at high level.1 Publication

Gene expression databases

BgeeiQ6PB93.
ExpressionAtlasiQ6PB93. baseline and differential.
GenevisibleiQ6PB93. MM.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000034458.

Structurei

3D structure databases

ProteinModelPortaliQ6PB93.
SMRiQ6PB93. Positions 74-567.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini442 – 565124Ricin B-type lectinPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni134 – 239106Catalytic subdomain AAdd
BLAST
Regioni299 – 36163Catalytic subdomain BAdd
BLAST

Domaini

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 similaritiesi

Contains 1 ricin B-type lectin domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG5533.
GeneTreeiENSGT00760000118828.
HOVERGENiHBG051699.
InParanoidiQ6PB93.
KOiK00710.
OMAiGKVRWPD.
OrthoDBiEOG7J9VP2.
PhylomeDBiQ6PB93.
TreeFamiTF313267.

Family and domain databases

Gene3Di3.90.550.10. 1 hit.
InterProiIPR001173. Glyco_trans_2-like.
IPR029044. Nucleotide-diphossugar_trans.
IPR000772. Ricin_B_lectin.
[Graphical view]
PfamiPF00535. Glycos_transf_2. 1 hit.
PF00652. Ricin_B_lectin. 1 hit.
[Graphical view]
SMARTiSM00458. RICIN. 1 hit.
[Graphical view]
SUPFAMiSSF50370. SSF50370. 1 hit.
SSF53448. SSF53448. 1 hit.
PROSITEiPS50231. RICIN_B_LECTIN. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q6PB93-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MRRRSRMLLC FALLWVLGIA YYMYSGGGSA LAAGGGGAGR KGDWNDIDSI
60 70 80 90 100
KKKDLHHSRG DEKAQGVETL PPGKVRWPDF NQEAYVGGTM VRSGQDPYAR
110 120 130 140 150
NKFNQVESDK LHMDRGIPDT RHDQCQRKQW RVDLPATSVV ITFHNEARSA
160 170 180 190 200
LLRTVVSVLK RSPPHLIKEI ILVDDYSNDP EDGALLGKIE KVRVLRNDRR
210 220 230 240 250
EGLMRSRVRG ADAAQAKVLT FLDSHCECNE RWLEPLLERV AEDRTRVVSP
260 270 280 290 300
IIDVINMDNF QYVGASADLK GGFDWNLVFK WDYMTPEQRR SRQGNPVAPI
310 320 330 340 350
KTPMIAGGLF VMDKLYFEEL GKYDMMMDVW GGENLEISFR VWQCGGSLEI
360 370 380 390 400
IPCSRVGHVF RKQHPYTFPG GSGTVFARNT RRAAEVWMDE YKHFYYAAVP
410 420 430 440 450
SARNVPYGNI QSRLELRKKL GCKPFKWYLD NVYPELRVPD HQDIAFGALQ
460 470 480 490 500
QGTNCLDTLG HFADGVVGIY ECHNAGGNQE WALTKEKSVK HMDLCLTVVD
510 520 530 540 550
RSPGSLIRLQ GCRENDSRQK WEQIEGNSKL RHVGSNLCLD SRTAKSGGLS
560 570
VEVCGPALSQ QWKFSLNLQQ
Length:570
Mass (Da):64,514
Last modified:July 5, 2004 - v1
Checksum:i90D5DC02C85A8EEA
GO
Isoform 2 (identifier: Q6PB93-2) [UniParc]FASTAAdd to basket

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

Note: No experimental confirmation available.
Show »
Length:536
Mass (Da):60,985
Checksum:i58DC49843190D2E4
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti2 – 21R → L in AAK37548 (Ref. 1) Curated
Sequence conflicti226 – 2261C → Y in BAC32790 (PubMed:16141072).Curated
Sequence conflicti516 – 5183DSR → NSK in AAK37548 (Ref. 1) Curated
Sequence conflicti564 – 5641F → V in AAK37548 (Ref. 1) Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 4141MRRRS…GAGRK → MALHNPQ in isoform 2. 1 PublicationVSP_011201Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS22769.1. [Q6PB93-1]
RefSeqiNP_644678.2. NM_139272.2. [Q6PB93-1]
UniGeneiMm.33808.

Genome annotation databases

EnsembliENSMUST00000034458; ENSMUSP00000034458; ENSMUSG00000089704. [Q6PB93-1]
ENSMUST00000127664; ENSMUSP00000118564; ENSMUSG00000092329. [Q6PB93-2]
GeneIDi108148.
KEGGimmu:108148.
UCSCiuc009nwz.2. mouse. [Q6PB93-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Web resourcesi

Functional Glycomics Gateway - GTase

Polypeptide N-acetylgalactosaminyltransferase 2

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS22769.1. [Q6PB93-1]
RefSeqiNP_644678.2. NM_139272.2. [Q6PB93-1]
UniGeneiMm.33808.

3D structure databases

ProteinModelPortaliQ6PB93.
SMRiQ6PB93. Positions 74-567.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000034458.

Protein family/group databases

CAZyiCBM13. Carbohydrate-Binding Module Family 13.
GT27. Glycosyltransferase Family 27.

PTM databases

PhosphoSiteiQ6PB93.

Proteomic databases

MaxQBiQ6PB93.
PaxDbiQ6PB93.
PRIDEiQ6PB93.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000034458; ENSMUSP00000034458; ENSMUSG00000089704. [Q6PB93-1]
ENSMUST00000127664; ENSMUSP00000118564; ENSMUSG00000092329. [Q6PB93-2]
GeneIDi108148.
KEGGimmu:108148.
UCSCiuc009nwz.2. mouse. [Q6PB93-1]

Organism-specific databases

CTDi2590.
MGIiMGI:894694. Galnt2.

Phylogenomic databases

eggNOGiCOG5533.
GeneTreeiENSGT00760000118828.
HOVERGENiHBG051699.
InParanoidiQ6PB93.
KOiK00710.
OMAiGKVRWPD.
OrthoDBiEOG7J9VP2.
PhylomeDBiQ6PB93.
TreeFamiTF313267.

Enzyme and pathway databases

UniPathwayiUPA00378.
ReactomeiREACT_278772. O-linked glycosylation of mucins.

Miscellaneous databases

NextBioi360162.
PROiQ6PB93.
SOURCEiSearch...

Gene expression databases

BgeeiQ6PB93.
ExpressionAtlasiQ6PB93. baseline and differential.
GenevisibleiQ6PB93. MM.

Family and domain databases

Gene3Di3.90.550.10. 1 hit.
InterProiIPR001173. Glyco_trans_2-like.
IPR029044. Nucleotide-diphossugar_trans.
IPR000772. Ricin_B_lectin.
[Graphical view]
PfamiPF00535. Glycos_transf_2. 1 hit.
PF00652. Ricin_B_lectin. 1 hit.
[Graphical view]
SMARTiSM00458. RICIN. 1 hit.
[Graphical view]
SUPFAMiSSF50370. SSF50370. 1 hit.
SSF53448. SSF53448. 1 hit.
PROSITEiPS50231. RICIN_B_LECTIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [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.

Entry informationi

Entry nameiGALT2_MOUSE
AccessioniPrimary (citable) accession number: Q6PB93
Secondary accession number(s): Q7TSI5
, Q8BL27, Q922K5, Q99ME1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: July 5, 2004
Last modified: June 24, 2015
This is version 114 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.