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Protein

Polypeptide N-acetylgalactosaminyltransferase 5

Gene

Galnt5

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: -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. Has activity toward EA2 peptide substrate, but has a weak activity toward Muc2 or Muc1b substrates (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 sitei526SubstrateBy similarity1
Binding sitei555SubstrateBy similarity1
Metal bindingi578ManganeseBy similarity1
Binding sitei579SubstrateBy similarity1
Metal bindingi580ManganeseBy similarity1
Binding sitei685SubstrateBy similarity1
Metal bindingi713ManganeseBy similarity1
Binding sitei716SubstrateBy similarity1
Binding sitei721SubstrateBy similarity1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionGlycosyltransferase, Transferase
LigandLectin, 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 5 (EC:2.4.1.41)
Alternative name(s):
Polypeptide GalNAc transferase 5
Short name:
GalNAc-T5
Short name:
pp-GaNTase 5
Protein-UDP acetylgalactosaminyltransferase 5
UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 5
Gene namesi
Name:Galnt5
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:2179403 Galnt5

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 – 12CytoplasmicSequence analysisAdd BLAST12
Transmembranei13 – 35Helical; Signal-anchor for type II membrane proteinSequence analysisAdd BLAST23
Topological domaini36 – 930LumenalSequence analysisAdd BLAST895

Keywords - Cellular componenti

Golgi apparatus, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000591111 – 930Polypeptide N-acetylgalactosaminyltransferase 5Add BLAST930

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi198N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi213N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi283N-linked (GlcNAc...) asparagineSequence analysis1
Modified residuei285PhosphoserineBy similarity1
Glycosylationi287N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi309N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi355N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi387N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi476 ↔ 708PROSITE-ProRule annotation
Glycosylationi568N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi699 ↔ 779PROSITE-ProRule annotation
Glycosylationi766N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi812 ↔ 825PROSITE-ProRule annotation
Glycosylationi817N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi835N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi848 ↔ 863PROSITE-ProRule annotation
Disulfide bondi898 ↔ 913PROSITE-ProRule annotation
Glycosylationi902N-linked (GlcNAc...) asparagineSequence analysis1

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiQ8C102
PaxDbiQ8C102
PRIDEiQ8C102

PTM databases

iPTMnetiQ8C102
PhosphoSitePlusiQ8C102

Expressioni

Tissue specificityi

Expressed at low level. Not expressed before E7.5 during embryogenesis. Expressed in dental mesenchyme and tongue. Accumulates in a subset of mesenchymal cells at the ventral-most portions of the E12.5 maxilla and mandible underlying the dental lamina.1 Publication

Gene expression databases

BgeeiENSMUSG00000026828
GenevisibleiQ8C102 MM

Interactioni

Subunit structurei

Interacts with EXT2. Does not interact with EXT1, EXTL1 or EXTL3 (By similarity).By similarity

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000108235

Structurei

3D structure databases

ProteinModelPortaliQ8C102
SMRiQ8C102
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini794 – 925Ricin B-type lectinPROSITE-ProRule annotationAdd BLAST132

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni485 – 594Catalytic subdomain AAdd BLAST110
Regioni654 – 716Catalytic 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

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG3736 Eukaryota
ENOG410XPMK LUCA
GeneTreeiENSGT00760000118828
HOGENOMiHOG000231869
HOVERGENiHBG051698
InParanoidiQ8C102
KOiK00710
OMAiSHVVIIT
OrthoDBiEOG091G085O
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.

Q8C102-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNKIRKFFRG SGRVLAFIFA ASVIWLLFDM AALRLSFSEI NAGLLKEDII
60 70 80 90 100
RREHTGFRVE PDQVKVLYTS IRGMGLPRNG AWGKENFRKA ENHELKVEEN
110 120 130 140 150
MDQVQRKGKM QNLLGRRKAV PLWHLAHLQT LPVTIPMQKT QGRDSKPEVS
160 170 180 190 200
SQYMMSKWMT VLESEKTPFT ASRGVPLTKI AGRTETFDKK QEAPQNYNVS
210 220 230 240 250
SDTSKQASER TLNMTISVKT DRSKQKSQTV TKLRMHFASP PILKSEEVTV
260 270 280 290 300
IKKAEAQSKD LKHEALKALP LLKFIADMGH LKNQSTNETQ LGRLPEDDAA
310 320 330 340 350
KVAPGKKLNF SESHVVIITK EEELKTDTKE VPNSKTQTVF PKLLGGSPHK
360 370 380 390 400
QIPRNQSKTS SSPPALKKAV SQSKPTISGG LHTARSNLTA KAPTVGYQQS
410 420 430 440 450
HANIPENPGM HHVFRIDVTL SPRDLNAPGQ FGRPVVVPPE KKKEAEQRWK
460 470 480 490 500
EGNFNVYLSD LIPVDRAIED TRPAGCAEQL VHNDLPTTSI IMCFVDEVWS
510 520 530 540 550
ALLRSVHSVL NRSPPHLIKE ILLVDDFSTK EYLKADLDKY MSQFPKVRIL
560 570 580 590 600
RLKERHGLIR ARLAGAQNAT GDVLTFLDSH VECNVGWLEP LLERVYLNRK
610 620 630 640 650
KVACPVIEVI NDKDMSYMTV DNFQRGVFTW PMNFGWKTIP PDVVAKNGIK
660 670 680 690 700
ETDIIRCPVM AGGLFSIDKS YFYELGTYDP GLDVWGGENM ELSFKVWMCG
710 720 730 740 750
GEIEIIPCSR VGHIFRNDNP YSFPKDRMKT VERNLVRVAE VWLDDYRELF
760 770 780 790 800
YGHGDHLIDQ GLDVGNLTQQ RELRKKLKCK SFKWYLDNVF PDLKAPVVRA
810 820 830 840 850
SGVLINMALG KCVSIENITV TLEDCDGSSQ LQQFNYTWVR LIKHGEWCVA
860 870 880 890 900
PIPEKGSLTL YHCDNRNNRL KWLHKSASAF HPELVDHIVF ENYQQLLCME
910 920 930
GNFSQKTLKL AACNPMELQQ KWKFEKYYEV
Length:930
Mass (Da):105,780
Last modified:July 27, 2011 - v2
Checksum:iC5851F6E13CDF5D7
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti705I → L in BAC26396 (PubMed:16141072).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK029323 mRNA Translation: BAC26396.1
AL928564, AL929144 Genomic DNA Translation: CAM18783.1
AL929144, AL928564 Genomic DNA Translation: CAM24473.1
CH466519 Genomic DNA Translation: EDL26932.1
CCDSiCCDS38125.1
RefSeqiNP_766443.2, NM_172855.3
XP_006498111.1, XM_006498048.3
XP_006498112.1, XM_006498049.2
UniGeneiMm.484118

Genome annotation databases

EnsembliENSMUST00000112616; ENSMUSP00000108235; ENSMUSG00000026828
ENSMUST00000166729; ENSMUSP00000131362; ENSMUSG00000026828
GeneIDi241391
KEGGimmu:241391
UCSCiuc012bvo.1 mouse

Similar proteinsi

Entry informationi

Entry nameiGALT5_MOUSE
AccessioniPrimary (citable) accession number: Q8C102
Secondary accession number(s): A2AS75
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: July 27, 2011
Last modified: April 25, 2018
This is version 122 of the entry and version 2 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. 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
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