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Q10473

- GALT1_RAT

UniProt

Q10473 - GALT1_RAT

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Protein

Polypeptide N-acetylgalactosaminyltransferase 1

Gene
Galnt1
Organism
Rattus norvegicus (Rat)
Status
Reviewed - 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.

Catalytic activityi

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

Cofactori

Manganese.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei156 – 1561Substrate By similarity
Binding sitei186 – 1861Substrate By similarity
Metal bindingi209 – 2091Manganese By similarity
Metal bindingi211 – 2111Manganese By similarity
Binding sitei316 – 3161Substrate By similarity
Metal bindingi344 – 3441Manganese By similarity
Binding sitei347 – 3471Substrate By similarity
Binding sitei352 – 3521Substrate By similarity

GO - Molecular functioni

  1. manganese ion binding Source: UniProtKB
  2. polypeptide N-acetylgalactosaminyltransferase activity Source: RGD

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

ReactomeiREACT_196259. 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
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Chromosome 18

Organism-specific databases

RGDi620358. Galnt1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 88Cytoplasmic Reviewed prediction
Transmembranei9 – 2820Helical; Signal-anchor for type II membrane protein; Reviewed predictionAdd
BLAST
Topological domaini29 – 559531Lumenal Reviewed predictionAdd
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
Mutagenesisi106 – 1061C → A: Loss of enzyme activity. 1 Publication
Mutagenesisi212 – 2121C → A: Loss of enzyme activity due to absence of interaction between UDP moiety and UDP-GalNAC. 1 Publication
Mutagenesisi214 – 2141C → A: Loss of enzyme activity due to absence of interaction between UDP moiety and UDP-GalNAC. 1 Publication
Mutagenesisi235 – 2351C → A: No effect. 1 Publication
Mutagenesisi330 – 3301C → A: Loss of enzyme activity. 1 Publication
Mutagenesisi339 – 3391C → A: Loss of enzyme activity. 1 Publication
Mutagenesisi408 – 4081C → A: Loss of enzyme activity. 1 Publication
Mutagenesisi442 – 4421C → A: Loss of enzyme activity. 1 Publication
Mutagenesisi444 – 4441D → A: Induces a strong decrease in activity; loss of function; when associated with A-484 and A-525. 2 Publications
Mutagenesisi455 – 4551G → Q: Induces a decrease in activity. 1 Publication
Mutagenesisi457 – 4571F → A: Little or no effect. 1 Publication
Mutagenesisi459 – 4591C → A: Loss of enzyme activity. 1 Publication
Mutagenesisi465 – 4651N → A: Little or no effect. 1 Publication
Mutagenesisi466 – 4661Q → A: Induces a decrease in activity. 1 Publication
Mutagenesisi468 – 4681F → A: Loss of enzyme activity. 1 Publication
Mutagenesisi468 – 4681F → W or Y: Little or no effect. 1 Publication
Mutagenesisi482 – 4821C → A: Loss of enzyme activity. 1 Publication
Mutagenesisi484 – 4841D → A: Loss of enzyme activity; when associated with A-444 and A-525. 2 Publications
Mutagenesisi497 – 4971C → A: Loss of enzyme activity. 1 Publication
Mutagenesisi523 – 5231C → A: Loss of enzyme activity. 1 Publication
Mutagenesisi525 – 5251D → A: Loss of enzyme activity; when associated with A-444 and A-484. 2 Publications
Mutagenesisi540 – 5401C → A: Loss of enzyme activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 559559Polypeptide N-acetylgalactosaminyltransferase 1PRO_0000223390Add
BLAST
Chaini41 – 559519Polypeptide N-acetylgalactosaminyltransferase 1 soluble formPRO_0000012263Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi95 – 951N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi106 ↔ 339 By similarity
Disulfide bondi330 ↔ 408 By similarity
Disulfide bondi442 ↔ 459 By similarity
Disulfide bondi482 ↔ 497 By similarity
Disulfide bondi523 ↔ 540 By similarity
Glycosylationi552 – 5521N-linked (GlcNAc...) Reviewed prediction

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ10473.
PRIDEiQ10473.

Expressioni

Tissue specificityi

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

Gene expression databases

GenevestigatoriQ10473.

Interactioni

Protein-protein interaction databases

MINTiMINT-4566270.
STRINGi10116.ENSRNOP00000022117.

Structurei

3D structure databases

ProteinModelPortaliQ10473.
SMRiQ10473. Positions 95-553.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini429 – 551123Ricin B-type lectinAdd
BLAST

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.
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

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG239675.
GeneTreeiENSGT00750000117385.
HOGENOMiHOG000038227.
HOVERGENiHBG051699.
InParanoidiQ10473.
KOiK00710.
OMAiIKHDRKT.
OrthoDBiEOG7J9VP2.
PhylomeDBiQ10473.
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.

Q10473-1 [UniParc]FASTAAdd to Basket

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MRKFAYCKVV LATSLVWVLL DMFLLLYFSE CNKCEEKKER GLPAGDVLEL    50
VQKPHEGPGE MGKPVVIPKE DQEKMKEMFK INQFNLMASE MIAFNRSLPD 100
VRLEGCKTKV YPDSLPTTSV VIVFHNEAWS TLLRTVHSVI NRSPRHMIEE 150
IVLVDDASER DFLKRPLESY VKKLKVPVHV IRMEQRSGLI RARLKGAAVS 200
KGQVITFLDA HCECTVGWLE PLLARIKHDR RTVVCPIIDV ISDDTFEYMA 250
GSDMTYGGFN WKLNFRWYPV PQREMDRRKG DRTLPVRTPT MAGGLFSIDR 300
DYFQEIGTYD AGMDIWGGEN LEISFRIWQC GGTLEIVTCS HVGHVFRKAT 350
PYTFPGGTGQ IINKNNRRLA EVWMDEFKNF FYIISPGVTK VDYGDISSRV 400
GLRHKLQCKP FSWYLENIYP DSQIPRHYFS LGEIRNVETN QCLDNMARKE 450
NEKVGIFNCH GMGGNQVFSY TANKEIRTDD LCLDVSKLNG PVTMLKCHHL 500
KGNQLWEYDP VKLTLQHVNS NQCLDKATEE DSQVPSIRDC TGSRSQQWLL 550
RNVTLPEIF 559
Length:559
Mass (Da):64,229
Last modified:October 1, 1996 - v1
Checksum:i5E36A95D9422C853
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U35890 mRNA. Translation: AAC52511.1.
RefSeqiNP_077349.1. NM_024373.1.
XP_006254533.1. XM_006254471.1.
UniGeneiRn.10266.

Genome annotation databases

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

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U35890 mRNA. Translation: AAC52511.1 .
RefSeqi NP_077349.1. NM_024373.1.
XP_006254533.1. XM_006254471.1.
UniGenei Rn.10266.

3D structure databases

ProteinModelPortali Q10473.
SMRi Q10473. Positions 95-553.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

MINTi MINT-4566270.
STRINGi 10116.ENSRNOP00000022117.

Protein family/group databases

CAZyi CBM13. Carbohydrate-Binding Module Family 13.
GT27. Glycosyltransferase Family 27.

Proteomic databases

PaxDbi Q10473.
PRIDEi Q10473.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSRNOT00000022117 ; ENSRNOP00000022117 ; ENSRNOG00000016207 .
GeneIDi 79214.
KEGGi rno:79214.
UCSCi RGD:620358. rat.

Organism-specific databases

CTDi 2589.
RGDi 620358. Galnt1.

Phylogenomic databases

eggNOGi NOG239675.
GeneTreei ENSGT00750000117385.
HOGENOMi HOG000038227.
HOVERGENi HBG051699.
InParanoidi Q10473.
KOi K00710.
OMAi IKHDRKT.
OrthoDBi EOG7J9VP2.
PhylomeDBi Q10473.
TreeFami TF313267.

Enzyme and pathway databases

UniPathwayi UPA00378 .
Reactomei REACT_196259. O-linked glycosylation of mucins.

Miscellaneous databases

NextBioi 614616.
PROi Q10473.

Gene expression databases

Genevestigatori Q10473.

Family and domain databases

Gene3Di 3.90.550.10. 1 hit.
InterProi IPR001173. Glyco_trans_2-like.
IPR029044. Nucleotide-diphossugar_trans.
IPR000772. Ricin_B_lectin.
[Graphical view ]
Pfami PF00535. Glycos_transf_2. 1 hit.
PF00652. Ricin_B_lectin. 1 hit.
[Graphical view ]
SMARTi SM00458. RICIN. 1 hit.
[Graphical view ]
SUPFAMi SSF50370. SSF50370. 1 hit.
SSF53448. SSF53448. 1 hit.
PROSITEi PS50231. RICIN_B_LECTIN. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Cloning and sequence homology of a rat UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase."
    Hagen F., Gregorie C.A., Tabak L.A.
    Glycoconj. J. 12:901-909(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Sprague-Dawley.
    Tissue: Sublingual gland.
  2. "Identification of two cysteine residues involved in the binding of UDP-GalNAc to UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 1 (GalNAc-T1)."
    Tenno M., Toba S., Kezdy F.J., Elhammer A.P., Kurosaka A.
    Eur. J. Biochem. 269:4308-4316(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF CYS-106; CYS-212; CYS-214; CYS-235; CYS-330; CYS-339 AND CYS-408.
  3. "The lectin domain of UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 1 is involved in O-glycosylation of a polypeptide with multiple acceptor sites."
    Tenno M., Saeki A., Kezdy F.J., Elhammer A.P., Kurosaka A.
    J. Biol. Chem. 277:47088-47096(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF CYS-442; ASP-444; GLY-455; PHE-457; CYS-459; ASN-465; GLN-466; PHE-468; CYS-482; ASP-484; CYS-497; CYS-523; ASP-525 AND CYS-540.
  4. "Function of the lectin domain of polypeptide N-acetylgalactosaminyltransferase 1."
    Tenno M., Kezdy F.J., Elhammer A.P., Kurosaka A.
    Biochem. Biophys. Res. Commun. 298:755-759(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF ASP-444; ASP-484 AND ASP-525.

Entry informationi

Entry nameiGALT1_RAT
AccessioniPrimary (citable) accession number: Q10473
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: September 3, 2014
This is version 122 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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