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Protein

Polypeptide N-acetylgalactosaminyltransferase 6

Gene

Galnt6

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. May participate in synthesis of oncofetal fibronectin. Has activity toward Muc1a, Muc2, EA2 and fibronectin peptides (By similarity).By similarity

Catalytic activityi

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

Cofactori

Mn2+By similarity

Pathwayi: protein 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)DescriptionActionsGraphical viewLength
Binding sitei217SubstrateBy similarity1
Binding sitei246SubstrateBy similarity1
Metal bindingi269ManganeseBy similarity1
Metal bindingi271ManganeseBy similarity1
Binding sitei379SubstrateBy similarity1
Metal bindingi407ManganeseBy similarity1
Binding sitei410SubstrateBy similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Ligandi

Lectin, Manganese, Metal-binding

Enzyme and pathway databases

ReactomeiR-MMU-913709. 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 6 (EC:2.4.1.41)
Alternative name(s):
Polypeptide GalNAc transferase 6
Short name:
GalNAc-T6
Short name:
pp-GaNTase 6
Protein-UDP acetylgalactosaminyltransferase 6
UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 6
Gene namesi
Name:Galnt6
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 15

Organism-specific databases

MGIiMGI:1891640. Galnt6.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 8CytoplasmicSequence analysis8
Transmembranei9 – 28Helical; Signal-anchor for type II membrane proteinSequence analysisAdd BLAST20
Topological domaini29 – 622LumenalSequence analysisAdd BLAST594

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000591151 – 622Polypeptide N-acetylgalactosaminyltransferase 6Add BLAST622

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi86N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi165 ↔ 402PROSITE-ProRule annotation
Disulfide bondi393 ↔ 474PROSITE-ProRule annotation
Glycosylationi476N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi509 ↔ 527PROSITE-ProRule annotation
Disulfide bondi553 ↔ 566PROSITE-ProRule annotation
Disulfide bondi597 ↔ 610PROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

EPDiQ8C7U7.
MaxQBiQ8C7U7.
PaxDbiQ8C7U7.
PeptideAtlasiQ8C7U7.
PRIDEiQ8C7U7.

PTM databases

PhosphoSitePlusiQ8C7U7.

Expressioni

Gene expression databases

BgeeiENSMUSG00000037280.
GenevisibleiQ8C7U7. MM.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000056705.

Structurei

3D structure databases

ProteinModelPortaliQ8C7U7.
SMRiQ8C7U7.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini496 – 622Ricin B-type lectinPROSITE-ProRule annotationAdd BLAST127

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni176 – 285Catalytic subdomain AAdd BLAST110
Regioni348 – 410Catalytic subdomain BAdd BLAST63

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

eggNOGiKOG3736. Eukaryota.
ENOG410XPMK. LUCA.
GeneTreeiENSGT00760000118828.
HOGENOMiHOG000038227.
HOVERGENiHBG051699.
InParanoidiQ8C7U7.
KOiK00710.
OMAiNQCLDVG.
OrthoDBiEOG091G085O.
PhylomeDBiQ8C7U7.
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]

Sequencei

Sequence statusi: Complete.

Q8C7U7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRLLRRRHMS LRLAMLGSVF MLFLFIRQKD VSNQEQAMEK PWLKSLAGQK
60 70 80 90 100
DQVLDFMLGA VNNIRDVMPK LQIRAPEPPQ TLVSTNHSCL PGFYTPAELK
110 120 130 140 150
PFWDRPPQDP NSPGADGKAF QKKEWTNLET KEKEEGYKKH CFNAFASDRI
160 170 180 190 200
SLQRSLGPDT RPPECVDQKF RRCPPLPTTS VIIVFHNEAW STLLRTVYSV
210 220 230 240 250
LHTSPAILLK EIILVDDAST DEHLKERLEQ YVQQLQIVRV VRQRERKGLI
260 270 280 290 300
TARLLGASVA QAEVLTFLDA HCECFHGWLE PLLARIAEDK TAVVSPDIVT
310 320 330 340 350
IDLNTFQFSR PVQRGKAHSR GNFDWSLTFG WEMLPEHEKQ RRKDETYPIK
360 370 380 390 400
SPTFAGGLFS ISKAYFEHIG TYDNQMEIWG GENVEMSFRV WQCGGQLEII
410 420 430 440 450
PCSVVGHVFR TKSPHTFPKG TSVIARNQVR LAEVWMDDYK KIFYRRNLQA
460 470 480 490 500
AKMVQENNFG DISERLRLRE QLRCHNFSWY LHNVYPEMFV PDLNPTFYGA
510 520 530 540 550
IKNLGTNQCL DVGENNRGGK PLIMYVCHNL GGNQYFEYTS QRDLRHNIGK
560 570 580 590 600
QLCLHASGST LGLRSCQFVG KNSRVPKDEE WELTQDQLIR NSGSGTCLTS
610 620
QDKKPAMAPC NPRDPYQLWL FV
Length:622
Mass (Da):71,537
Last modified:March 1, 2003 - v1
Checksum:i6DBCA3A2CCFDBDAA
GO

Sequence cautioni

The sequence CAB55352 differs from that shown. Reason: Frameshift at position 622.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti14A → T in CAB55352 (PubMed:10464263).Curated1
Sequence conflicti100K → R in CAB55352 (PubMed:10464263).Curated1
Sequence conflicti210K → N in BAC25984 (PubMed:16141072).Curated1
Sequence conflicti215V → M in BAC25984 (PubMed:16141072).Curated1
Sequence conflicti247K → G in BAC25984 (PubMed:16141072).Curated1
Sequence conflicti263 – 275EVLTF…HCECF → KGAHVSWTPTVSVS (PubMed:10464263).CuratedAdd BLAST13
Sequence conflicti292A → P in CAB55352 (PubMed:10464263).Curated1
Sequence conflicti336E → Q in CAB55352 (PubMed:10464263).Curated1
Sequence conflicti398E → G in BAC25984 (PubMed:16141072).Curated1
Sequence conflicti467R → Q in CAB55352 (PubMed:10464263).Curated1
Sequence conflicti562G → S in CAB55352 (PubMed:10464263).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ133523 mRNA. Translation: CAB55352.1. Frameshift.
AK028506 mRNA. Translation: BAC25984.1.
AK049222 mRNA. Translation: BAC33618.1.
AK155008 mRNA. Translation: BAE32989.1.
AK159721 mRNA. Translation: BAE35316.1.
BC119324 mRNA. Translation: AAI19325.1.
BC119326 mRNA. Translation: AAI19327.1.
CCDSiCCDS27843.1.
RefSeqiNP_001155239.1. NM_001161767.1.
NP_001155240.1. NM_001161768.1.
NP_766039.2. NM_172451.3.
UniGeneiMm.22969.

Genome annotation databases

EnsembliENSMUST00000052069; ENSMUSP00000056705; ENSMUSG00000037280.
ENSMUST00000159715; ENSMUSP00000123848; ENSMUSG00000037280.
ENSMUST00000161514; ENSMUSP00000124793; ENSMUSG00000037280.
GeneIDi207839.
KEGGimmu:207839.
UCSCiuc007xrz.2. mouse.

Cross-referencesi

Web resourcesi

Functional Glycomics Gateway - GTase

Polypeptide N-acetylgalactosaminyltransferase 6

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ133523 mRNA. Translation: CAB55352.1. Frameshift.
AK028506 mRNA. Translation: BAC25984.1.
AK049222 mRNA. Translation: BAC33618.1.
AK155008 mRNA. Translation: BAE32989.1.
AK159721 mRNA. Translation: BAE35316.1.
BC119324 mRNA. Translation: AAI19325.1.
BC119326 mRNA. Translation: AAI19327.1.
CCDSiCCDS27843.1.
RefSeqiNP_001155239.1. NM_001161767.1.
NP_001155240.1. NM_001161768.1.
NP_766039.2. NM_172451.3.
UniGeneiMm.22969.

3D structure databases

ProteinModelPortaliQ8C7U7.
SMRiQ8C7U7.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000056705.

Protein family/group databases

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

PTM databases

PhosphoSitePlusiQ8C7U7.

Proteomic databases

EPDiQ8C7U7.
MaxQBiQ8C7U7.
PaxDbiQ8C7U7.
PeptideAtlasiQ8C7U7.
PRIDEiQ8C7U7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000052069; ENSMUSP00000056705; ENSMUSG00000037280.
ENSMUST00000159715; ENSMUSP00000123848; ENSMUSG00000037280.
ENSMUST00000161514; ENSMUSP00000124793; ENSMUSG00000037280.
GeneIDi207839.
KEGGimmu:207839.
UCSCiuc007xrz.2. mouse.

Organism-specific databases

CTDi11226.
MGIiMGI:1891640. Galnt6.

Phylogenomic databases

eggNOGiKOG3736. Eukaryota.
ENOG410XPMK. LUCA.
GeneTreeiENSGT00760000118828.
HOGENOMiHOG000038227.
HOVERGENiHBG051699.
InParanoidiQ8C7U7.
KOiK00710.
OMAiNQCLDVG.
OrthoDBiEOG091G085O.
PhylomeDBiQ8C7U7.
TreeFamiTF313267.

Enzyme and pathway databases

UniPathwayiUPA00378.
ReactomeiR-MMU-913709. O-linked glycosylation of mucins.

Miscellaneous databases

PROiQ8C7U7.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000037280.
GenevisibleiQ8C7U7. 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...

Entry informationi

Entry nameiGALT6_MOUSE
AccessioniPrimary (citable) accession number: Q8C7U7
Secondary accession number(s): Q0VE84
, Q3TWF0, Q8CED2, Q9QZ16
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: March 1, 2003
Last modified: November 2, 2016
This is version 121 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

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 one 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.