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Protein

Polypeptide N-acetylgalactosaminyltransferase 1

Gene

Galnt1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein 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 and Muc7.1 Publication

Catalytic activityi

UDP-N-acetyl-alpha-D-galactosamine + polypeptide = UDP + N-acetyl-alpha-D-galactosaminyl-polypeptide.1 Publication

Cofactori

Mn2+1 Publication

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 sitei156SubstrateBy similarity1
Binding sitei186SubstrateBy similarity1
Metal bindingi209Manganese1 Publication1
Metal bindingi211Manganese1 Publication1
Binding sitei316SubstrateBy similarity1
Metal bindingi344Manganese1 Publication1
Binding sitei347SubstrateBy similarity1
Binding sitei352SubstrateBy 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

BRENDAi2.4.1.41. 3474.
ReactomeiR-MMU-6811436. COPI-independent Golgi-to-ER retrograde traffic.
R-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 1 (EC:2.4.1.41)
Alternative name(s):
Polypeptide GalNAc transferase 1
Short name:
GalNAc-T1
Short name:
pp-GaNTase 1
Protein-UDP acetylgalactosaminyltransferase 1
UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 1
Cleaved into the following chain:
Gene namesi
Name:Galnt1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 18

Organism-specific databases

MGIiMGI:894693. Galnt1.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 9CytoplasmicSequence analysis9
Transmembranei10 – 28Helical; Signal-anchor for type II membrane proteinSequence analysisAdd BLAST19
Topological domaini29 – 559LumenalSequence analysisAdd BLAST531

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus, Membrane, Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi125H → F: No effect. 1 Publication1
Mutagenesisi125H → Q: Induces a strong decrease in activity. 1 Publication1
Mutagenesisi127E → Q: Loss of enzyme activity. 1 Publication1
Mutagenesisi150E → Q: No effect. 1 Publication1
Mutagenesisi155D → N: No effect; specificity not affected. 1 Publication1
Mutagenesisi156D → Q: Loss of enzyme activity. 1 Publication1
Mutagenesisi209D → N, A or E: Loss of enzyme activity. 1 Publication1
Mutagenesisi211H → A or D: Loss of enzyme activity. 1 Publication1
Mutagenesisi213E → Q: Loss of enzyme activity. 1 Publication1
Mutagenesisi310D → N: Loss of enzyme activity. 1 Publication1
Mutagenesisi319E → Q: Loss of enzyme activity. 1 Publication1
Mutagenesisi320N → A: No effect. 1 Publication1
Mutagenesisi322E → Q: Loss of enzyme activity. 1 Publication1
Mutagenesisi341H → A, L, V, K or R: Little or no effect. 1 Publication1
Mutagenesisi375D → A or N: Little or no effect. 1 Publication1
Mutagenesisi376E → Q: No effect. 1 Publication1
Mutagenesisi444D → H: Induces a decrease in activity. 1 Publication1
Mutagenesisi455G → V: Induces a slight decrease in activity. 1 Publication1
Mutagenesisi457F → H: Induces a slight decrease in activity. 1 Publication1
Mutagenesisi460H → K or N: Induces a slight decrease in activity. 1 Publication1
Mutagenesisi464G → A: Induces a slight decrease in activity. 1 Publication1
Mutagenesisi465 – 466NQ → QN: Induces a decrease in activity. 2
Mutagenesisi465N → A: Little or no effect. Induces a slight decrease in activity; when associated with A-466. 1 Publication1
Mutagenesisi466Q → A: Little or no effect. Induces a slight decrease in activity; when associated with A-465. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002233881 – 559Polypeptide N-acetylgalactosaminyltransferase 1Add BLAST559
ChainiPRO_000001225941 – 559Polypeptide N-acetylgalactosaminyltransferase 1 soluble formAdd BLAST519

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi95N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi106 ↔ 339PROSITE-ProRule annotation1 Publication
Disulfide bondi330 ↔ 408PROSITE-ProRule annotation1 Publication
Disulfide bondi442 ↔ 459PROSITE-ProRule annotation1 Publication
Disulfide bondi482 ↔ 497PROSITE-ProRule annotation1 Publication
Disulfide bondi523 ↔ 540PROSITE-ProRule annotation1 Publication
Glycosylationi552N-linked (GlcNAc...)1 Publication1

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

EPDiO08912.
MaxQBiO08912.
PaxDbiO08912.
PeptideAtlasiO08912.
PRIDEiO08912.

PTM databases

iPTMnetiO08912.
PhosphoSitePlusiO08912.
SwissPalmiO08912.

Expressioni

Tissue specificityi

Widely expressed at high level. Higher expression in kidney, heart, small intestine and cervix and to a lesser extent in all the other tissues tested.2 Publications

Gene expression databases

BgeeiENSMUSG00000000420.
ExpressionAtlasiO08912. baseline and differential.
GenevisibleiO08912. MM.

Interactioni

Protein-protein interaction databases

IntActiO08912. 1 interactor.
MINTiMINT-4095517.
STRINGi10090.ENSMUSP00000000430.

Structurei

Secondary structure

1559
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi104 – 107Combined sources4
Beta strandi118 – 126Combined sources9
Helixi129 – 141Combined sources13
Helixi145 – 147Combined sources3
Beta strandi148 – 155Combined sources8
Helixi161 – 163Combined sources3
Helixi165 – 172Combined sources8
Beta strandi173 – 176Combined sources4
Beta strandi178 – 182Combined sources5
Helixi189 – 199Combined sources11
Beta strandi202 – 214Combined sources13
Helixi219 – 228Combined sources10
Beta strandi232 – 241Combined sources10
Beta strandi243 – 245Combined sources3
Beta strandi255 – 259Combined sources5
Beta strandi265 – 269Combined sources5
Helixi272 – 277Combined sources6
Turni278 – 280Combined sources3
Beta strandi293 – 299Combined sources7
Helixi300 – 305Combined sources6
Helixi322 – 329Combined sources8
Beta strandi333 – 345Combined sources13
Helixi360 – 373Combined sources14
Helixi375 – 378Combined sources4
Helixi379 – 383Combined sources5
Helixi388 – 390Combined sources3
Helixi397 – 405Combined sources9
Helixi411 – 417Combined sources7
Beta strandi426 – 432Combined sources7
Beta strandi434 – 436Combined sources3
Turni437 – 439Combined sources3
Beta strandi441 – 444Combined sources4
Beta strandi455 – 458Combined sources4
Helixi464 – 466Combined sources3
Beta strandi468 – 471Combined sources4
Beta strandi476 – 478Combined sources3
Beta strandi481 – 484Combined sources4
Beta strandi493 – 496Combined sources4
Helixi502 – 504Combined sources3
Beta strandi506 – 509Combined sources4
Turni510 – 513Combined sources4
Beta strandi514 – 520Combined sources7
Beta strandi522 – 526Combined sources5
Beta strandi529 – 531Combined sources3
Beta strandi536 – 539Combined sources4
Helixi544 – 546Combined sources3
Beta strandi548 – 550Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1XHBX-ray2.50A88-559[»]
ProteinModelPortaliO08912.
SMRiO08912.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO08912.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini429 – 551Ricin B-type lectinPROSITE-ProRule annotationAdd BLAST123

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni115 – 225Catalytic subdomain AAdd BLAST111
Regioni285 – 347Catalytic 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.1 Publication
The ricin B-type lectin domain directs the glycopeptide specificity. It is required in the glycopeptide specificity of enzyme activity but not for activity with naked peptide substrates, suggesting that it triggers the catalytic domain to act on GalNAc-glycopeptide substrates (By similarity).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.
InParanoidiO08912.
KOiK00710.
OMAiPSIRDCT.
OrthoDBiEOG091G085O.
PhylomeDBiO08912.
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.

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

O08912-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRKFAYCKVV LATSLVWVLL DMFLLLYFSE CNKCEEKQER GLPAGDVLEL
60 70 80 90 100
VQKPHEGPGE MGKPVVIPKE DQEKMKEMFK INQFNLMASE MIALNRSLPD
110 120 130 140 150
VRLEGCKTKV YPDNLPTTSV VIVFHNEAWS TLLRTVHSVI NRSPRHMIEE
160 170 180 190 200
IVLVDDASER DFLKRPLESY VKKLKVPVHV IRMEQRSGLI RARLKGAAVS
210 220 230 240 250
RGQVITFLDA HCECTAGWLE PLLARIKHDR RTVVCPIIDV ISDDTFEYMA
260 270 280 290 300
GSDMTYGGFN WKLNFRWYPV PQREMDRRKG DRTLPVRTPT MAGGLFSIDR
310 320 330 340 350
DYFQEIGTYD AGMDIWGGEN LEISFRIWQC GGTLEIVTCS HVGHVFRKAT
360 370 380 390 400
PYTFPGGTGQ IINKNNRRLA EVWMDEFKNF FYIISPGVTK VDYGDISSRL
410 420 430 440 450
GLRRKLQCKP FSWYLENIYP DSQIPRHYFS LGEIRNVETN QCLDNMARKE
460 470 480 490 500
NEKVGIFNCH GMGGNQVFSY TANKEIRTDD LCLDVSKLNG PVTMLKCHHL
510 520 530 540 550
KGNQLWEYDP VKLTLQHVNS NQCLDKATEE DSQVPSIRDC TGSRSQQWLL

RNVTLPEIF
Length:559
Mass (Da):64,255
Last modified:July 1, 1997 - v1
Checksum:iAC5AB655D91F83E4
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti81I → T in AAH56215 (PubMed:15489334).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U73820 mRNA. Translation: AAB58477.1.
BC056215 mRNA. Translation: AAH56215.1.
BC090962 mRNA. Translation: AAH90962.1.
CCDSiCCDS29100.1.
RefSeqiNP_001153876.1. NM_001160404.1.
NP_038842.3. NM_013814.3.
XP_006525713.1. XM_006525650.2.
UniGeneiMm.30249.

Genome annotation databases

EnsembliENSMUST00000000430; ENSMUSP00000000430; ENSMUSG00000000420.
ENSMUST00000170243; ENSMUSP00000132142; ENSMUSG00000000420.
ENSMUST00000178605; ENSMUSP00000137427; ENSMUSG00000000420.
GeneIDi14423.
KEGGimmu:14423.
UCSCiuc008egq.2. mouse.

Cross-referencesi

Web resourcesi

Functional Glycomics Gateway - GTase

Polypeptide N-acetylgalactosaminyltransferase 1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U73820 mRNA. Translation: AAB58477.1.
BC056215 mRNA. Translation: AAH56215.1.
BC090962 mRNA. Translation: AAH90962.1.
CCDSiCCDS29100.1.
RefSeqiNP_001153876.1. NM_001160404.1.
NP_038842.3. NM_013814.3.
XP_006525713.1. XM_006525650.2.
UniGeneiMm.30249.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1XHBX-ray2.50A88-559[»]
ProteinModelPortaliO08912.
SMRiO08912.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiO08912. 1 interactor.
MINTiMINT-4095517.
STRINGi10090.ENSMUSP00000000430.

Protein family/group databases

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

PTM databases

iPTMnetiO08912.
PhosphoSitePlusiO08912.
SwissPalmiO08912.

Proteomic databases

EPDiO08912.
MaxQBiO08912.
PaxDbiO08912.
PeptideAtlasiO08912.
PRIDEiO08912.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000000430; ENSMUSP00000000430; ENSMUSG00000000420.
ENSMUST00000170243; ENSMUSP00000132142; ENSMUSG00000000420.
ENSMUST00000178605; ENSMUSP00000137427; ENSMUSG00000000420.
GeneIDi14423.
KEGGimmu:14423.
UCSCiuc008egq.2. mouse.

Organism-specific databases

CTDi2589.
MGIiMGI:894693. Galnt1.

Phylogenomic databases

eggNOGiKOG3736. Eukaryota.
ENOG410XPMK. LUCA.
GeneTreeiENSGT00760000118828.
HOGENOMiHOG000038227.
HOVERGENiHBG051699.
InParanoidiO08912.
KOiK00710.
OMAiPSIRDCT.
OrthoDBiEOG091G085O.
PhylomeDBiO08912.
TreeFamiTF313267.

Enzyme and pathway databases

UniPathwayiUPA00378.
BRENDAi2.4.1.41. 3474.
ReactomeiR-MMU-6811436. COPI-independent Golgi-to-ER retrograde traffic.
R-MMU-913709. O-linked glycosylation of mucins.

Miscellaneous databases

ChiTaRSiGalnt1. mouse.
EvolutionaryTraceiO08912.
PROiO08912.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000000420.
ExpressionAtlasiO08912. baseline and differential.
GenevisibleiO08912. 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 nameiGALT1_MOUSE
AccessioniPrimary (citable) accession number: O08912
Secondary accession number(s): Q5BKS3, Q7TND1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: July 1, 1997
Last modified: November 2, 2016
This is version 158 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

3D-structure, 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.