Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei141 – 1411Not glycosylatedCurated
Binding sitei156 – 1561SubstrateBy similarity
Binding sitei186 – 1861SubstrateBy similarity
Metal bindingi209 – 2091ManganeseBy similarity
Metal bindingi211 – 2111ManganeseBy similarity
Binding sitei316 – 3161SubstrateBy similarity
Metal bindingi344 – 3441ManganeseBy similarity
Binding sitei347 – 3471SubstrateBy similarity
Binding sitei352 – 3521SubstrateBy 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
  2. protein O-linked glycosylation via serine Source: Ensembl
  3. protein O-linked glycosylation via threonine Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Ligandi

Lectin, Manganese, Metal-binding

Enzyme and pathway databases

BRENDAi2.4.1.41. 908.
ReactomeiREACT_341641. 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
ProteomesiUP000009136 Componenti: Chromosome 24

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 88CytoplasmicSequence Analysis
Transmembranei9 – 2820Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST
Topological domaini29 – 559531LumenalSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-SubCell
  2. Golgi cisterna membrane Source: UniProtKB-SubCell
  3. integral component of membrane Source: UniProtKB-KW
  4. perinuclear region of cytoplasm Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus, Membrane, Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi95 – 951N → Q: Induces decrease in glycosylation. 1 Publication
Mutagenesisi125 – 1251H → A: Induces a strong decrease in activity. 1 Publication
Mutagenesisi137 – 1371H → A: No effect. 1 Publication
Mutagenesisi141 – 1411N → Q: No effect. 1 Publication
Mutagenesisi146 – 1461H → A: No effect. 1 Publication
Mutagenesisi179 – 1791H → A: No effect. 1 Publication
Mutagenesisi211 – 2111H → A: Loss of enzyme activity. 1 Publication
Mutagenesisi228 – 2281H → A: No effect. 1 Publication
Mutagenesisi341 – 3411H → A: Induces a strong decrease in activity. 1 Publication
Mutagenesisi344 – 3441H → A: Loss of enzyme activity. 1 Publication
Mutagenesisi404 – 4041H → A: No effect. 1 Publication
Mutagenesisi427 – 4271H → A: No effect. 1 Publication
Mutagenesisi460 – 4601H → A: No effect. 1 Publication
Mutagenesisi498 – 4981H → A: No effect. 1 Publication
Mutagenesisi499 – 4991H → A: No effect. 1 Publication
Mutagenesisi517 – 5171H → A: No effect. 1 Publication
Mutagenesisi552 – 5521N → Q: Induces decrease in glycosylation. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 559559Polypeptide N-acetylgalactosaminyltransferase 1PRO_0000223386Add
BLAST
Chaini41 – 559519Polypeptide N-acetylgalactosaminyltransferase 1 soluble formPRO_0000012255Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi95 – 951N-linked (GlcNAc...)1 Publication
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
Glycosylationi552 – 5521N-linked (GlcNAc...)1 Publication

Post-translational modificationi

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

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PRIDEiQ07537.

Expressioni

Tissue specificityi

Colostrum contains a soluble form.1 Publication

Interactioni

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000014882.

Structurei

3D structure databases

ProteinModelPortaliQ07537.
SMRiQ07537. Positions 95-553.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni115 – 225111Catalytic subdomain AAdd
BLAST
Regioni285 – 34763Catalytic 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 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

eggNOGiNOG239675.
GeneTreeiENSGT00760000118828.
HOGENOMiHOG000038227.
HOVERGENiHBG051699.
InParanoidiQ07537.
KOiK00710.
OMAiIKHDRKT.
OrthoDBiEOG7J9VP2.
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_010818675.1.
XP_010823837.1. XM_010825535.1.
UniGeneiBt.65693.
Bt.69942.

Genome annotation databases

EnsembliENSBTAT00000014882; ENSBTAP00000014882; ENSBTAG00000011206.
GeneIDi104968722.
282241.
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_010818675.1.
XP_010823837.1. XM_010825535.1.
UniGeneiBt.65693.
Bt.69942.

3D structure databases

ProteinModelPortaliQ07537.
SMRiQ07537. Positions 95-553.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000014882.

Protein family/group databases

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

Proteomic databases

PRIDEiQ07537.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000014882; ENSBTAP00000014882; ENSBTAG00000011206.
GeneIDi104968722.
282241.
KEGGibta:282241.

Organism-specific databases

CTDi2589.

Phylogenomic databases

eggNOGiNOG239675.
GeneTreeiENSGT00760000118828.
HOGENOMiHOG000038227.
HOVERGENiHBG051699.
InParanoidiQ07537.
KOiK00710.
OMAiIKHDRKT.
OrthoDBiEOG7J9VP2.
TreeFamiTF313267.

Enzyme and pathway databases

UniPathwayiUPA00378.
BRENDAi2.4.1.41. 908.
ReactomeiREACT_341641. O-linked glycosylation of mucins.

Miscellaneous databases

NextBioi20806060.

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...

Publicationsi

  1. "Isolation and expression of a cDNA clone encoding a bovine UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase."
    Homa F.L., Hollander T., Lehman D.J., Thomsen D.R., Elhammer A.P.
    J. Biol. Chem. 268:12609-12616(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, PROTEIN SEQUENCE OF 41-74.
    Tissue: Colostrum and Intestine.
  2. "Purification, cloning, and expression of a bovine UDP-GalNAc: polypeptide N-acetyl-galactosaminyltransferase."
    Hagen F.K., van Wuyckhuyse B., Tabak L.A.
    J. Biol. Chem. 268:18960-18965(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 41-559, PARTIAL PROTEIN SEQUENCE.
    Tissue: Colostrum and Placenta.
  3. "Purification and characterization of UDP-N-acetylgalactosamine: polypeptide N-acetylgalactosaminyltransferase from bovine colostrum and murine lymphoma BW5147 cells."
    Elhammer A., Kornfeld S.
    J. Biol. Chem. 261:5249-5255(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBCELLULAR LOCATION, GLYCOSYLATION, TISSUE SPECIFICITY.
  4. "Identification of essential histidine residues in UDP-N-acetyl-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase-T1."
    Wragg S., Hagen F.K., Tabak L.A.
    Biochem. J. 328:193-197(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF ASN-95; HIS-125; HIS-137; ASN-141; HIS-146; HIS-179; HIS-211; HIS-228; HIS-341; HIS-344; HIS-404; HIS-427; HIS-460; HIS-498; HIS-499; HIS-517 AND ASN-552.

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: April 1, 2015
This is version 130 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

External Data

Dasty 3

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 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.