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Protein

Polypeptide N-acetylgalactosaminyltransferase 14

Gene

Galnt14

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript 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. Displays activity toward mucin-derived peptide substrates such as Muc2, Muc5AC, Muc7, and Muc13 (-58). May be involved in O-glycosylation in kidney (By similarity).By similarity

Catalytic activityi

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

Cofactori

Mn2+By similarity

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 sitei151SubstrateBy similarity1
Binding sitei176SubstrateBy similarity1
Metal bindingi199ManganeseBy similarity1
Binding sitei200SubstrateBy similarity1
Metal bindingi201ManganeseBy similarity1
Binding sitei305SubstrateBy similarity1
Metal bindingi333ManganeseBy similarity1
Binding sitei336SubstrateBy similarity1
Binding sitei339SubstrateBy similarity1
Binding sitei341SubstrateBy similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Ligandi

Lectin, Manganese, Metal-binding

Enzyme and pathway databases

ReactomeiR-MMU-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 14 (EC:2.4.1.41)
Alternative name(s):
Polypeptide GalNAc transferase 14
Short name:
GalNAc-T14
Short name:
pp-GaNTase 14
Protein-UDP acetylgalactosaminyltransferase 14
UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 14
Gene namesi
Name:Galnt14
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 17

Organism-specific databases

MGIiMGI:1918935. Galnt14.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 6CytoplasmicSequence analysis6
Transmembranei7 – 26Helical; Signal-anchor for type II membrane proteinSequence analysisAdd BLAST20
Topological domaini27 – 550LumenalSequence analysisAdd BLAST524

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000591341 – 550Polypeptide N-acetylgalactosaminyltransferase 14Add BLAST550

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi101 ↔ 328PROSITE-ProRule annotation
Disulfide bondi319 ↔ 397PROSITE-ProRule annotation
Disulfide bondi430 ↔ 447PROSITE-ProRule annotation
Disulfide bondi474 ↔ 491PROSITE-ProRule annotation
Disulfide bondi515 ↔ 536PROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond

Proteomic databases

PaxDbiQ8BVG5.
PRIDEiQ8BVG5.

PTM databases

PhosphoSitePlusiQ8BVG5.

Expressioni

Gene expression databases

BgeeiENSMUSG00000024064.
ExpressionAtlasiQ8BVG5. baseline and differential.
GenevisibleiQ8BVG5. MM.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000024858.

Structurei

3D structure databases

ProteinModelPortaliQ8BVG5.
SMRiQ8BVG5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini415 – 548Ricin B-type lectinPROSITE-ProRule annotationAdd BLAST134

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni110 – 215Catalytic subdomain AAdd BLAST106
Regioni274 – 336Catalytic 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 binds to GalNAc and contributes to the glycopeptide specificity.By similarity

Sequence similaritiesi

Contains 1 ricin B-type lectin domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG3738. Eukaryota.
ENOG410XPRX. LUCA.
GeneTreeiENSGT00760000118828.
HOGENOMiHOG000038227.
HOVERGENiHBG051699.
InParanoidiQ8BVG5.
KOiK00710.
PhylomeDBiQ8BVG5.

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]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q8BVG5-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MRRLTRRLAL PIFGVLWITV LLFFWVTKRK LEVPLGPEVQ TPKPSDADWD
60 70 80 90 100
DLWEQFDERR YLNAKKWRVG DDPYKLYAFN QRESERISSN RAVPDTRHKR
110 120 130 140 150
CSLLVYCTDL PPTSIIITFH NEARSTLLRT IRSVLNRTPM HLIQEIILVD
160 170 180 190 200
DFSNDPEDCK QLIKLPKVKC LRNNERQGLV RSRMRGADIA QGTTLTFLDS
210 220 230 240 250
HCEVNRDWLQ PLLHRVKEDY TRVVCPVIDI INLDTFNYIE SASELRGGFD
260 270 280 290 300
WSLHFQWEQL SLEQKALRLD PTEPIRTPII AGGLFVIDKA WFDYLGKYDV
310 320 330 340 350
DMDIWGGENF EISFRVWMCG GGLEIIPCSR VGHVFRKKHP YVFPDGNANT
360 370 380 390 400
YIKNTKRTAE VWMDEYKQYY YAARPFALER PFGNIENRLN LRKNLHCQTF
410 420 430 440 450
KWNLENVYPE LRVPPDSSIQ KGNIRQRQKC LESQKQKKQE ILRLSPCAKV
460 470 480 490 500
KGDGAKSQVW AFTYTQQIIQ EELCLSVVTL FPGAPVVLAL CKNGDERQLW
510 520 530 540 550
TKTGARIEHI ASHLCLDTDM FGDSTEDGKE VVVNPCESSL MSQHWDIVSS
Length:550
Mass (Da):63,989
Last modified:June 13, 2006 - v2
Checksum:iD67054CFE6F332E1
GO
Isoform 2 (identifier: Q8BVG5-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     385-429: IENRLNLRKN...QKGNIRQRQK → SHVTQCCRRR...SSPYYLSSSS
     430-550: Missing.

Note: No experimental confirmation available.
Show »
Length:429
Mass (Da):50,057
Checksum:iB14F4BE219C5B7B0
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti112P → H in BAC37208 (PubMed:16141072).Curated1
Sequence conflicti173N → H in BAD52069 (Ref. 1) Curated1
Sequence conflicti260L → I in BAB22325 (PubMed:16141072).Curated1
Sequence conflicti381P → H in BAC37208 (PubMed:16141072).Curated1
Sequence conflicti403N → Y in BAD52069 (Ref. 1) Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_011225385 – 429IENRL…RQRQK → SHVTQCCRRRILIRGTSFRG VVPPTNLPVESPTDPSSPYY LSSSS in isoform 2. 1 PublicationAdd BLAST45
Alternative sequenceiVSP_011226430 – 550Missing in isoform 2. 1 PublicationAdd BLAST121

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB175681 mRNA. Translation: BAD52069.1.
AK002747 mRNA. Translation: BAB22325.1.
AK078292 mRNA. Translation: BAC37208.1.
CCDSiCCDS28965.1. [Q8BVG5-1]
RefSeqiNP_082140.2. NM_027864.2.
XP_006525002.1. XM_006524939.3. [Q8BVG5-2]
UniGeneiMm.271953.
Mm.450771.

Genome annotation databases

EnsembliENSMUST00000112591; ENSMUSP00000108210; ENSMUSG00000024064. [Q8BVG5-2]
GeneIDi71685.
KEGGimmu:71685.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Web resourcesi

Functional Glycomics Gateway - GTase

Polypeptide N-acetylgalactosaminyltransferase 14

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB175681 mRNA. Translation: BAD52069.1.
AK002747 mRNA. Translation: BAB22325.1.
AK078292 mRNA. Translation: BAC37208.1.
CCDSiCCDS28965.1. [Q8BVG5-1]
RefSeqiNP_082140.2. NM_027864.2.
XP_006525002.1. XM_006524939.3. [Q8BVG5-2]
UniGeneiMm.271953.
Mm.450771.

3D structure databases

ProteinModelPortaliQ8BVG5.
SMRiQ8BVG5.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000024858.

Protein family/group databases

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

PTM databases

PhosphoSitePlusiQ8BVG5.

Proteomic databases

PaxDbiQ8BVG5.
PRIDEiQ8BVG5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000112591; ENSMUSP00000108210; ENSMUSG00000024064. [Q8BVG5-2]
GeneIDi71685.
KEGGimmu:71685.

Organism-specific databases

CTDi79623.
MGIiMGI:1918935. Galnt14.

Phylogenomic databases

eggNOGiKOG3738. Eukaryota.
ENOG410XPRX. LUCA.
GeneTreeiENSGT00760000118828.
HOGENOMiHOG000038227.
HOVERGENiHBG051699.
InParanoidiQ8BVG5.
KOiK00710.
PhylomeDBiQ8BVG5.

Enzyme and pathway databases

UniPathwayiUPA00378.
ReactomeiR-MMU-913709. O-linked glycosylation of mucins.

Miscellaneous databases

PROiQ8BVG5.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000024064.
ExpressionAtlasiQ8BVG5. baseline and differential.
GenevisibleiQ8BVG5. MM.

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 nameiGLT14_MOUSE
AccessioniPrimary (citable) accession number: Q8BVG5
Secondary accession number(s): Q60GT2, Q8BTI6, Q9DCJ2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: June 13, 2006
Last modified: November 2, 2016
This is version 110 of the entry and version 2 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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. 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.