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O08912

- GALT1_MOUSE

UniProt

O08912 - GALT1_MOUSE

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Protein

Polypeptide N-acetylgalactosaminyltransferase 1

Gene

Galnt1

Organism
Mus musculus (Mouse)
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 Muc7.1 Publication

Catalytic activityi

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

Cofactori

Manganese.1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei156 – 1561SubstrateBy similarity
Binding sitei186 – 1861SubstrateBy similarity
Metal bindingi209 – 2091Manganese1 Publication
Metal bindingi211 – 2111Manganese1 Publication
Binding sitei316 – 3161SubstrateBy similarity
Metal bindingi344 – 3441Manganese1 Publication
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: MGI

GO - Biological processi

  1. protein O-linked glycosylation Source: MGI
  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_198517. 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
ProteomesiUP000000589: Chromosome 18

Organism-specific databases

MGIiMGI:894693. Galnt1.

Subcellular locationi

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-KW
  2. Golgi apparatus Source: UniProtKB-KW
  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
Mutagenesisi125 – 1251H → F: No effect. 1 Publication
Mutagenesisi125 – 1251H → Q: Induces a strong decrease in activity. 1 Publication
Mutagenesisi127 – 1271E → Q: Loss of enzyme activity. 1 Publication
Mutagenesisi150 – 1501E → Q: No effect. 1 Publication
Mutagenesisi155 – 1551D → N: No effect; specificity not affected. 1 Publication
Mutagenesisi156 – 1561D → Q: Loss of enzyme activity. 1 Publication
Mutagenesisi209 – 2091D → N, A or E: Loss of enzyme activity. 1 Publication
Mutagenesisi211 – 2111H → A or D: Loss of enzyme activity. 1 Publication
Mutagenesisi213 – 2131E → Q: Loss of enzyme activity. 1 Publication
Mutagenesisi310 – 3101D → N: Loss of enzyme activity. 1 Publication
Mutagenesisi319 – 3191E → Q: Loss of enzyme activity. 1 Publication
Mutagenesisi320 – 3201N → A: No effect. 1 Publication
Mutagenesisi322 – 3221E → Q: Loss of enzyme activity. 1 Publication
Mutagenesisi341 – 3411H → A, L, V, K or R: Little or no effect. 1 Publication
Mutagenesisi375 – 3751D → A or N: Little or no effect. 1 Publication
Mutagenesisi376 – 3761E → Q: No effect. 1 Publication
Mutagenesisi444 – 4441D → H: Induces a decrease in activity. 1 Publication
Mutagenesisi455 – 4551G → V: Induces a slight decrease in activity. 1 Publication
Mutagenesisi457 – 4571F → H: Induces a slight decrease in activity. 1 Publication
Mutagenesisi460 – 4601H → K or N: Induces a slight decrease in activity. 1 Publication
Mutagenesisi464 – 4641G → A: Induces a slight decrease in activity. 1 Publication
Mutagenesisi465 – 4662NQ → QN: Induces a decrease in activity.
Mutagenesisi465 – 4651N → A: Little or no effect. Induces a slight decrease in activity; when associated with A-466. 1 Publication
Mutagenesisi466 – 4661Q → A: Little or no effect. Induces a slight decrease in activity; when associated with A-465. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 559559Polypeptide N-acetylgalactosaminyltransferase 1PRO_0000223388Add
BLAST
Chaini41 – 559519Polypeptide N-acetylgalactosaminyltransferase 1 soluble formPRO_0000012259Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi95 – 951N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi106 ↔ 3391 PublicationPROSITE-ProRule annotation
Disulfide bondi330 ↔ 4081 PublicationPROSITE-ProRule annotation
Disulfide bondi442 ↔ 4591 PublicationPROSITE-ProRule annotation
Disulfide bondi482 ↔ 4971 PublicationPROSITE-ProRule annotation
Disulfide bondi523 ↔ 5401 PublicationPROSITE-ProRule annotation
Glycosylationi552 – 5521N-linked (GlcNAc...)1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiO08912.
PaxDbiO08912.
PRIDEiO08912.

PTM databases

PhosphoSiteiO08912.

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

BgeeiO08912.
ExpressionAtlasiO08912. baseline and differential.
GenevestigatoriO08912.

Interactioni

Protein-protein interaction databases

IntActiO08912. 1 interaction.
MINTiMINT-4095517.

Structurei

Secondary structure

1
559
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi104 – 1074Combined sources
Beta strandi118 – 1269Combined sources
Helixi129 – 14113Combined sources
Helixi145 – 1473Combined sources
Beta strandi148 – 1558Combined sources
Helixi161 – 1633Combined sources
Helixi165 – 1728Combined sources
Beta strandi173 – 1764Combined sources
Beta strandi178 – 1825Combined sources
Helixi189 – 19911Combined sources
Beta strandi202 – 21413Combined sources
Helixi219 – 22810Combined sources
Beta strandi232 – 24110Combined sources
Beta strandi243 – 2453Combined sources
Beta strandi255 – 2595Combined sources
Beta strandi265 – 2695Combined sources
Helixi272 – 2776Combined sources
Turni278 – 2803Combined sources
Beta strandi293 – 2997Combined sources
Helixi300 – 3056Combined sources
Helixi322 – 3298Combined sources
Beta strandi333 – 34513Combined sources
Helixi360 – 37314Combined sources
Helixi375 – 3784Combined sources
Helixi379 – 3835Combined sources
Helixi388 – 3903Combined sources
Helixi397 – 4059Combined sources
Helixi411 – 4177Combined sources
Beta strandi426 – 4327Combined sources
Beta strandi434 – 4363Combined sources
Turni437 – 4393Combined sources
Beta strandi441 – 4444Combined sources
Beta strandi455 – 4584Combined sources
Helixi464 – 4663Combined sources
Beta strandi468 – 4714Combined sources
Beta strandi476 – 4783Combined sources
Beta strandi481 – 4844Combined sources
Beta strandi493 – 4964Combined sources
Helixi502 – 5043Combined sources
Beta strandi506 – 5094Combined sources
Turni510 – 5134Combined sources
Beta strandi514 – 5207Combined sources
Beta strandi522 – 5265Combined sources
Beta strandi529 – 5313Combined sources
Beta strandi536 – 5394Combined sources
Helixi544 – 5463Combined sources
Beta strandi548 – 5503Combined sources

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1XHBX-ray2.50A88-559[»]
ProteinModelPortaliO08912.
SMRiO08912. Positions 95-553.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO08912.

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 99CytoplasmicSequence Analysis
Topological domaini29 – 559531LumenalSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei10 – 2819Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini429 – 551123Ricin B-type lectinPROSITE-ProRule annotationAdd
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.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

eggNOGiNOG239675.
GeneTreeiENSGT00760000118828.
HOGENOMiHOG000038227.
HOVERGENiHBG051699.
InParanoidiO08912.
KOiK00710.
OMAiIKHDRKT.
OrthoDBiEOG7J9VP2.
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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti81 – 811I → T in AAH56215. (PubMed:15489334)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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_006525650.1.
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:
EMBL
GenBank
DDBJ
Links Updated
U73820 mRNA. Translation: AAB58477.1 .
BC056215 mRNA. Translation: AAH56215.1 .
BC090962 mRNA. Translation: AAH90962.1 .
CCDSi CCDS29100.1.
RefSeqi NP_001153876.1. NM_001160404.1.
NP_038842.3. NM_013814.3.
XP_006525713.1. XM_006525650.1.
UniGenei Mm.30249.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1XHB X-ray 2.50 A 88-559 [» ]
ProteinModelPortali O08912.
SMRi O08912. Positions 95-553.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi O08912. 1 interaction.
MINTi MINT-4095517.

Protein family/group databases

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

PTM databases

PhosphoSitei O08912.

Proteomic databases

MaxQBi O08912.
PaxDbi O08912.
PRIDEi O08912.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000000430 ; ENSMUSP00000000430 ; ENSMUSG00000000420 .
ENSMUST00000170243 ; ENSMUSP00000132142 ; ENSMUSG00000000420 .
ENSMUST00000178605 ; ENSMUSP00000137427 ; ENSMUSG00000000420 .
GeneIDi 14423.
KEGGi mmu:14423.
UCSCi uc008egq.2. mouse.

Organism-specific databases

CTDi 2589.
MGIi MGI:894693. Galnt1.

Phylogenomic databases

eggNOGi NOG239675.
GeneTreei ENSGT00760000118828.
HOGENOMi HOG000038227.
HOVERGENi HBG051699.
InParanoidi O08912.
KOi K00710.
OMAi IKHDRKT.
OrthoDBi EOG7J9VP2.
PhylomeDBi O08912.
TreeFami TF313267.

Enzyme and pathway databases

UniPathwayi UPA00378 .
Reactomei REACT_198517. O-linked glycosylation of mucins.

Miscellaneous databases

ChiTaRSi GALNT1. mouse.
EvolutionaryTracei O08912.
NextBioi 286021.
PROi O08912.
SOURCEi Search...

Gene expression databases

Bgeei O08912.
ExpressionAtlasi O08912. baseline and differential.
Genevestigatori O08912.

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

« Hide 'large scale' publications
  1. "cDNA cloning and expression of a novel UDP-N-acetyl-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase."
    Hagen F.K., Ten Hagen K.G., Beres T.M., Balys M.M., VanWuyckhuyse B.C., Tabak L.A.
    J. Biol. Chem. 272:13843-13848(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR, TISSUE SPECIFICITY.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Brain and Embryo.
  3. "Structure-function analysis of the UDP-N-acetyl-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase. Essential residues lie in a predicted active site cleft resembling a lactose repressor fold."
    Hagen F.K., Hazes B., Raffo R., deSa D., Tabak L.A.
    J. Biol. Chem. 274:6797-6803(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: DOMAIN, MUTAGENESIS OF HIS-125; GLU-127; GLU-150; ASP-155; ASP-156; ASP-209; HIS-211; GLU-213; ASP-310; GLU-319; ASN-320; GLU-322; HIS-341; ASP-375; GLU-376; ASP-444; GLY-455; PHE-457; HIS-460; GLY-464; ASN-465 AND GLN-466.
  4. "Expression of UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase isoforms in murine tissues determined by real-time PCR: a new view of a large family."
    Young W.W. Jr., Holcomb D.R., Ten Hagen K.G., Tabak L.A.
    Glycobiology 13:549-557(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  5. "The beginnings of mucin biosynthesis: the crystal structure of UDP-GalNAc:polypeptide alpha-N-acetylgalactosaminyltransferase-T1."
    Fritz T.A., Hurley J.H., Trinh L.B., Shiloach J., Tabak L.A.
    Proc. Natl. Acad. Sci. U.S.A. 101:15307-15312(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 88-559 IN COMPLEX WITH MANGANESE, GLYCOSYLATION AT ASN-552, DISULFIDE BONDS.

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: October 29, 2014
This is version 142 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

External Data

Dasty 3