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UniProtKB - Q10473 (GALT1_RAT)

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Protein

Polypeptide N-acetylgalactosaminyltransferase 1

Gene

Galnt1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: -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.

Catalytic activityi

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

Cofactori

Mn2+

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: RGD
View the complete GO annotation on QuickGO ...

GO - Biological processi

View the complete GO annotation on QuickGO ...

Keywordsi

Molecular functionGlycosyltransferase, Transferase
LigandLectin, Manganese, Metal-binding

Enzyme and pathway databases

BRENDAi2.4.1.41 5301
ReactomeiR-RNO-6811436 COPI-independent Golgi-to-ER retrograde traffic
R-RNO-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:
Polypeptide N-acetylgalactosaminyltransferase 1 soluble form
Gene namesi
Name:Galnt1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Rattus
Proteomesi
  • UP000002494 Componenti: Chromosome 18

Organism-specific databases

RGDi620358 Galnt1

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

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

Keywords - Cellular componenti

Golgi apparatus, Membrane, Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi106C → A: Loss of enzyme activity. 1 Publication1
Mutagenesisi212C → A: Loss of enzyme activity due to absence of interaction between UDP moiety and UDP-GalNAC. 1 Publication1
Mutagenesisi214C → A: Loss of enzyme activity due to absence of interaction between UDP moiety and UDP-GalNAC. 1 Publication1
Mutagenesisi235C → A: No effect. 1 Publication1
Mutagenesisi330C → A: Loss of enzyme activity. 1 Publication1
Mutagenesisi339C → A: Loss of enzyme activity. 1 Publication1
Mutagenesisi408C → A: Loss of enzyme activity. 1 Publication1
Mutagenesisi442C → A: Loss of enzyme activity. 1 Publication1
Mutagenesisi444D → A: Induces a strong decrease in activity; loss of function; when associated with A-484 and A-525. 2 Publications1
Mutagenesisi455G → Q: Induces a decrease in activity. 1 Publication1
Mutagenesisi457F → A: Little or no effect. 1 Publication1
Mutagenesisi459C → A: Loss of enzyme activity. 1 Publication1
Mutagenesisi465N → A: Little or no effect. 1 Publication1
Mutagenesisi466Q → A: Induces a decrease in activity. 1 Publication1
Mutagenesisi468F → A: Loss of enzyme activity. 1 Publication1
Mutagenesisi468F → W or Y: Little or no effect. 1 Publication1
Mutagenesisi482C → A: Loss of enzyme activity. 1 Publication1
Mutagenesisi484D → A: Loss of enzyme activity; when associated with A-444 and A-525. 2 Publications1
Mutagenesisi497C → A: Loss of enzyme activity. 1 Publication1
Mutagenesisi523C → A: Loss of enzyme activity. 1 Publication1
Mutagenesisi525D → A: Loss of enzyme activity; when associated with A-444 and A-484. 2 Publications1
Mutagenesisi540C → A: Loss of enzyme activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002233901 – 559Polypeptide N-acetylgalactosaminyltransferase 1Add BLAST559
ChainiPRO_000001226341 – 559Polypeptide N-acetylgalactosaminyltransferase 1 soluble formAdd BLAST519

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi95N-linked (GlcNAc...) asparagineSequence analysis1
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...) asparagineSequence analysis1

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ10473
PRIDEiQ10473

Expressioni

Tissue specificityi

Heart, brain, spleen, liver, skeletal muscle and kidney.

Gene expression databases

BgeeiENSRNOG00000016207
GenevisibleiQ10473 RN

Interactioni

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000022117

Structurei

3D structure databases

ProteinModelPortaliQ10473
SMRiQ10473
ModBaseiSearch...
MobiDBiSearch...

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.
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.

Sequence similaritiesi

Belongs to the glycosyltransferase 2 family. GalNAc-T subfamily.Curated

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG3736 Eukaryota
ENOG410XPMK LUCA
GeneTreeiENSGT00760000118828
HOGENOMiHOG000038227
HOVERGENiHBG051699
InParanoidiQ10473
KOiK00710
OMAiIKHDRKT
OrthoDBiEOG091G085O
PhylomeDBiQ10473
TreeFamiTF313267

Family and domain databases

CDDicd00161 RICIN, 1 hit
Gene3Di3.90.550.10, 1 hit
InterProiView protein in InterPro
IPR001173 Glyco_trans_2-like
IPR029044 Nucleotide-diphossugar_trans
IPR035992 Ricin_B-like_lectins
IPR000772 Ricin_B_lectin
PfamiView protein in Pfam
PF00535 Glycos_transf_2, 1 hit
PF00652 Ricin_B_lectin, 1 hit
SMARTiView protein in SMART
SM00458 RICIN, 1 hit
SUPFAMiSSF50370 SSF50370, 1 hit
SSF53448 SSF53448, 1 hit
PROSITEiView protein in PROSITE
PS50231 RICIN_B_LECTIN, 1 hit

Sequencei

Sequence statusi: Complete.

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

Q10473-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRKFAYCKVV LATSLVWVLL DMFLLLYFSE CNKCEEKKER GLPAGDVLEL 
        60         70         80         90        100
VQKPHEGPGE MGKPVVIPKE DQEKMKEMFK INQFNLMASE MIAFNRSLPD 
       110        120        130        140        150
VRLEGCKTKV YPDSLPTTSV VIVFHNEAWS TLLRTVHSVI NRSPRHMIEE 
       160        170        180        190        200
IVLVDDASER DFLKRPLESY VKKLKVPVHV IRMEQRSGLI RARLKGAAVS 
       210        220        230        240        250
KGQVITFLDA HCECTVGWLE 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 VDYGDISSRV 
       410        420        430        440        450
GLRHKLQCKP 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):64,229
Last modified:October 1, 1996 - v1
Checksum:i5E36A95D9422C853
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U35890 mRNA Translation: AAC52511.1
RefSeqiNP_077349.1, NM_024373.1
XP_006254533.1, XM_006254471.3
UniGeneiRn.10266

Genome annotation databases

EnsembliENSRNOT00000022117; ENSRNOP00000022117; ENSRNOG00000016207
GeneIDi79214
KEGGirno:79214
UCSCiRGD:620358 rat

Similar proteinsi

Entry informationi

Entry nameiGALT1_RAT
AccessioniPrimary (citable) accession number: Q10473
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: May 23, 2018
This is version 144 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

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