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Protein

Polypeptide N-acetylgalactosaminyltransferase 1

Gene

GALNT1

Organism
Bos taurus (Bovine)
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 Muc7.2 Publications

Catalytic activityi

UDP-N-acetyl-alpha-D-galactosamine + polypeptide = UDP + N-acetyl-alpha-D-galactosaminyl-polypeptide.2 Publications

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 bindingi209ManganeseBy similarity1
Metal bindingi211ManganeseBy similarity1
Binding sitei316SubstrateBy similarity1
Metal bindingi344ManganeseBy similarity1
Binding sitei347SubstrateBy similarity1
Binding sitei352SubstrateBy similarity1

GO - Molecular functioni

  • carbohydrate binding Source: UniProtKB-KW
  • manganese ion binding Source: UniProtKB
  • polypeptide N-acetylgalactosaminyltransferase activity Source: UniProtKB

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. 908.
ReactomeiR-BTA-6811436. COPI-independent Golgi-to-ER retrograde traffic.
R-BTA-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
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Chromosome 24

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 – 559LumenalSequence analysisAdd BLAST531

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus, Membrane, Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi95N → Q: Induces decrease in glycosylation. 1 Publication1
Mutagenesisi125H → A: Induces a strong decrease in activity. 1 Publication1
Mutagenesisi137H → A: No effect. 1 Publication1
Mutagenesisi141N → Q: No effect. 1 Publication1
Mutagenesisi146H → A: No effect. 1 Publication1
Mutagenesisi179H → A: No effect. 1 Publication1
Mutagenesisi211H → A: Loss of enzyme activity. 1 Publication1
Mutagenesisi228H → A: No effect. 1 Publication1
Mutagenesisi341H → A: Induces a strong decrease in activity. 1 Publication1
Mutagenesisi344H → A: Loss of enzyme activity. 1 Publication1
Mutagenesisi404H → A: No effect. 1 Publication1
Mutagenesisi427H → A: No effect. 1 Publication1
Mutagenesisi460H → A: No effect. 1 Publication1
Mutagenesisi498H → A: No effect. 1 Publication1
Mutagenesisi499H → A: No effect. 1 Publication1
Mutagenesisi517H → A: No effect. 1 Publication1
Mutagenesisi552N → Q: Induces decrease in glycosylation. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002233861 – 559Polypeptide N-acetylgalactosaminyltransferase 1Add BLAST559
ChainiPRO_000001225541 – 559Polypeptide N-acetylgalactosaminyltransferase 1 soluble formAdd BLAST519

Amino acid modifications

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

Post-translational modificationi

N-glycosylated, contains two N-linked oligosaccharides.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei141Not glycosylatedCurated1

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ07537.
PRIDEiQ07537.

Expressioni

Tissue specificityi

Colostrum contains a soluble form.1 Publication

Gene expression databases

BgeeiENSBTAG00000011206.

Interactioni

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000014882.

Structurei

3D structure databases

ProteinModelPortaliQ07537.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

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.By similarity
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.
InParanoidiQ07537.
KOiK00710.
OMAiPSIRDCT.
OrthoDBiEOG091G085O.
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.

Q07537-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRKFAYCKVV LATSLIWVLL DMFLLLYFSE CNKCDEKKER GLPAGDVLEP
60 70 80 90 100
VQKPHEGPGE MGKPVVIPKE DQEKMKEMFK INQFNLMASE MIALNRSLPD
110 120 130 140 150
VRLEGCKTKV YPDNLPTTSV VIVFHNEAWS TLLRTVHSVI NRSPRHMLEE
160 170 180 190 200
IVLVDDASER DFLKRPLESY VKKLKVPVHV IRMEQRSGLI RARLKGAAVS
210 220 230 240 250
KGQVITFLDA HCECTVGWLE PLLARIKHDR KTVVCPIIDV 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
GLRHKLQCRP FSWYLENIYP DSQIPRHYFS LGEIRNVETN QCLDNMARKE
460 470 480 490 500
NEKVGIFNCH GMGGNQVFSY TANKEIRTDD LCLDVSKLNG PVTMLKCHHL
510 520 530 540 550
KGNQLWEYDP VKLTLQHVNS NQCLDKATDE DSQVPSIRDC SGSRSQQWLL

RNVTLPEIF
Length:559
Mass (Da):64,192
Last modified:November 1, 1995 - v1
Checksum:iE3E538C4DE569B40
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L07780 mRNA. Translation: AAA30532.1.
L17437 mRNA. Translation: AAA68489.1.
PIRiA45987.
RefSeqiNP_803485.1. NM_177519.3.
XP_010816977.1. XM_010818675.2.
UniGeneiBt.65693.
Bt.69942.

Genome annotation databases

EnsembliENSBTAT00000014882; ENSBTAP00000014882; ENSBTAG00000011206.
GeneIDi282241.
KEGGibta:282241.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L07780 mRNA. Translation: AAA30532.1.
L17437 mRNA. Translation: AAA68489.1.
PIRiA45987.
RefSeqiNP_803485.1. NM_177519.3.
XP_010816977.1. XM_010818675.2.
UniGeneiBt.65693.
Bt.69942.

3D structure databases

ProteinModelPortaliQ07537.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000014882.

Protein family/group databases

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

Proteomic databases

PaxDbiQ07537.
PRIDEiQ07537.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000014882; ENSBTAP00000014882; ENSBTAG00000011206.
GeneIDi282241.
KEGGibta:282241.

Organism-specific databases

CTDi2589.

Phylogenomic databases

eggNOGiKOG3736. Eukaryota.
ENOG410XPMK. LUCA.
GeneTreeiENSGT00760000118828.
HOGENOMiHOG000038227.
HOVERGENiHBG051699.
InParanoidiQ07537.
KOiK00710.
OMAiPSIRDCT.
OrthoDBiEOG091G085O.
TreeFamiTF313267.

Enzyme and pathway databases

UniPathwayiUPA00378.
BRENDAi2.4.1.41. 908.
ReactomeiR-BTA-6811436. COPI-independent Golgi-to-ER retrograde traffic.
R-BTA-913709. O-linked glycosylation of mucins.

Gene expression databases

BgeeiENSBTAG00000011206.

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_BOVIN
AccessioniPrimary (citable) accession number: Q07537
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: October 5, 2016
This is version 138 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, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. 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.