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Q6PB93

- GALT2_MOUSE

UniProt

Q6PB93 - GALT2_MOUSE

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Protein

Polypeptide N-acetylgalactosaminyltransferase 2

Gene

Galnt2

Organism
Mus musculus (Mouse)
Status
Reviewed - 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

Manganese.By similarity

Pathwayi

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

  1. carbohydrate binding Source: UniProtKB-KW
  2. manganese ion binding Source: UniProtKB
  3. polypeptide N-acetylgalactosaminyltransferase activity Source: UniProtKB

GO - Biological processi

  1. protein O-linked glycosylation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Ligandi

Lectin, Manganese, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_198517. 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: Chromosome 8

Organism-specific databases

MGIiMGI:894694. Galnt2.

Subcellular locationi

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.

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-KW
  2. Golgi lumen Source: MGI
  3. integral component of membrane Source: UniProtKB-KW
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. differential.
GenevestigatoriQ6PB93.

Structurei

3D structure databases

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

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 66CytoplasmicSequence Analysis
Topological domaini25 – 570546LumenalSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei7 – 2418Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST

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.
OMAiDDYSDNP.
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. Align

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. 1 PublicationCurated
Sequence conflicti226 – 2261C → Y in BAC32790. (PubMed:16141072)Curated
Sequence conflicti516 – 5183DSR → NSK in AAK37548. 1 PublicationCurated
Sequence conflicti564 – 5641F → V in AAK37548. 1 PublicationCurated

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:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS22769.1. [Q6PB93-1 ]
RefSeqi NP_644678.2. NM_139272.2. [Q6PB93-1 ]
UniGenei Mm.33808.

3D structure databases

ProteinModelPortali Q6PB93.
SMRi Q6PB93. Positions 74-567.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

CAZyi CBM13. Carbohydrate-Binding Module Family 13.
GT27. Glycosyltransferase Family 27.

PTM databases

PhosphoSitei Q6PB93.

Proteomic databases

MaxQBi Q6PB93.
PaxDbi Q6PB93.
PRIDEi Q6PB93.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000034458 ; ENSMUSP00000034458 ; ENSMUSG00000089704 . [Q6PB93-1 ]
ENSMUST00000127664 ; ENSMUSP00000118564 ; ENSMUSG00000092329 . [Q6PB93-2 ]
GeneIDi 108148.
KEGGi mmu:108148.
UCSCi uc009nwz.2. mouse. [Q6PB93-1 ]

Organism-specific databases

CTDi 2590.
MGIi MGI:894694. Galnt2.

Phylogenomic databases

eggNOGi COG5533.
GeneTreei ENSGT00760000118828.
HOVERGENi HBG051699.
InParanoidi Q6PB93.
KOi K00710.
OMAi DDYSDNP.
OrthoDBi EOG7J9VP2.
PhylomeDBi Q6PB93.
TreeFami TF313267.

Enzyme and pathway databases

UniPathwayi UPA00378 .
Reactomei REACT_198517. O-linked glycosylation of mucins.

Miscellaneous databases

NextBioi 360162.
PROi Q6PB93.
SOURCEi Search...

Gene expression databases

Bgeei Q6PB93.
ExpressionAtlasi Q6PB93. differential.
Genevestigatori Q6PB93.

Family and domain databases

Gene3Di 3.90.550.10. 1 hit.
InterProi IPR001173. Glyco_trans_2-like.
IPR029044. Nucleotide-diphossugar_trans.
IPR000772. Ricin_B_lectin.
[Graphical view ]
Pfami PF00535. Glycos_transf_2. 1 hit.
PF00652. Ricin_B_lectin. 1 hit.
[Graphical view ]
SMARTi SM00458. RICIN. 1 hit.
[Graphical view ]
SUPFAMi SSF50370. SSF50370. 1 hit.
SSF53448. SSF53448. 1 hit.
PROSITEi PS50231. RICIN_B_LECTIN. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: October 29, 2014
This is version 107 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