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Protein

Polypeptide N-acetylgalactosaminyltransferase 10

Gene

Galnt10

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 Muc5Ac and EA2 peptide substrates (By similarity).By similarity

Caution

According to experiments made in rat, this enzyme is unable to transfer GalNAc onto serine or threonine residue on the protein receptor, but instead requires the prior addition of a GalNAc on a peptide before adding additional GalNAc moieties, thereby acting as a glycopeptide transferase.Curated

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 sitei185SubstrateBy similarity1
Binding sitei214SubstrateBy similarity1
Metal bindingi237ManganeseBy similarity1
Binding sitei238SubstrateBy similarity1
Metal bindingi239ManganeseBy similarity1
Binding sitei342SubstrateBy similarity1
Metal bindingi370ManganeseBy similarity1
Binding sitei373SubstrateBy similarity1
Binding sitei378SubstrateBy similarity1

GO - Molecular functioni

GO - Biological processi

  • O-glycan processing Source: MGI
  • protein O-linked glycosylation Source: MGI

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 10 (EC:2.4.1.41)
Alternative name(s):
Polypeptide GalNAc transferase 10
Short name:
GalNAc-T10
Short name:
pp-GaNTase 10
Protein-UDP acetylgalactosaminyltransferase 10
UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 10
Gene namesi
Name:Galnt10
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 11

Organism-specific databases

MGIiMGI:1890480 Galnt10

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 – 11CytoplasmicSequence analysisAdd BLAST11
Transmembranei12 – 31Helical; Signal-anchor for type II membrane proteinSequence analysisAdd BLAST20
Topological domaini32 – 603LumenalSequence analysisAdd BLAST572

Keywords - Cellular componenti

Golgi apparatus, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000591231 – 603Polypeptide N-acetylgalactosaminyltransferase 10Add BLAST603

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi124N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi135 ↔ 365PROSITE-ProRule annotation
Glycosylationi146N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi356 ↔ 432PROSITE-ProRule annotation
Disulfide bondi471 ↔ 488PROSITE-ProRule annotation
Disulfide bondi523 ↔ 538PROSITE-ProRule annotation
Disulfide bondi563 ↔ 578PROSITE-ProRule annotation
Glycosylationi593N-linked (GlcNAc...) asparagineSequence analysis1

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiQ6P9S7
PaxDbiQ6P9S7
PRIDEiQ6P9S7

PTM databases

PhosphoSitePlusiQ6P9S7
SwissPalmiQ6P9S7

Expressioni

Tissue specificityi

Expressed at higher level than GALNT9. In the developing hindbrain region of E14.5 embryos it accumulates in the rapidly dividing, undifferentiated ventricular zone adjacent to the pons. It also accumulates in the regions immediately rostral and caudal to the dorsal rhombic lips differentiating into the cerebellum. Not expressed in the developing choroid plexus.1 Publication

Gene expression databases

BgeeiENSMUSG00000020520
ExpressionAtlasiQ6P9S7 baseline and differential
GenevisibleiQ6P9S7 MM

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000065096

Structurei

3D structure databases

ProteinModelPortaliQ6P9S7
SMRiQ6P9S7
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini458 – 590Ricin B-type lectinPROSITE-ProRule annotationAdd BLAST133

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni144 – 253Catalytic subdomain AAdd BLAST110
Regioni311 – 373Catalytic subdomain BAdd BLAST63
Regioni373 – 384Flexible loopBy similarityAdd BLAST12

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
GeneTreeiENSGT00900000140827
HOGENOMiHOG000038227
HOVERGENiHBG051699
InParanoidiQ6P9S7
KOiK00710
OMAiNYRAQDE
OrthoDBiEOG091G085O
PhylomeDBiQ6P9S7
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.

Q6P9S7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRRKEKRLLQ AVALALAALV LLPNVGLWAL YRERQPDGSP GGLGAAVAPA
60 70 80 90 100
AVQELHSRQK KTFFLGAEQR LKDWHNKEAI RRDAQRVGYG EQGKPYPMTD
110 120 130 140 150
AERVDQAYRE NGFNIYVSDK ISLNRSLPDI RHPNCNSKLY LETLPNTSII
160 170 180 190 200
IPFHNEGWSS LLRTVHSVLN RSPPELVAEI VLVDDFSDRE HLKKPLEDYM
210 220 230 240 250
ALFPSVRILR TKKREGLIRT RMLGASAATG DVVTFLDSHC EANVNWLPPL
260 270 280 290 300
LDRIARNRKT IVCPMIDVID HDDFRYETQA GDAMRGAFDW EMYYKRIPIP
310 320 330 340 350
PELQKADPSD PFESPVMAGG LFAVDRKWFW ELGGYDPGLE IWGGEQYEIS
360 370 380 390 400
FKVWMCGGRM EDIPCSRVGH IYRKYVPYKV PAGVSLARNL KRVAEVWMDE
410 420 430 440 450
YAEYIYQRRP EYRHLSAGDV VAQKKLRVSL NCKSFKWFMT KIAWDLPKFY
460 470 480 490 500
PPVEPPAAAW GEIRNVGTGL CTDTKLGTLG SPLRLETCIR GRGEAAWNSM
510 520 530 540 550
QVFTFTWRED IRPGDPQHTK KFCFDAVSHT SPVTLYDCHS MKGNQLWKYR
560 570 580 590 600
KDKTLYHPVS GSCMDCSESD HRVFMNTCNP SSLTQQWLFE HTNSTVLENF

NKN
Length:603
Mass (Da):69,116
Last modified:July 5, 2004 - v1
Checksum:iFF55FBA7E1DD7544
GO

Sequence cautioni

The sequence AAH16585 differs from that shown. Reason: Erroneous initiation.Curated
The sequence BAD21405 differs from that shown. Reason: Erroneous initiation.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti233V → I in BAD21405 (PubMed:15449545).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK131155 mRNA Translation: BAD21405.1 Different initiation.
BC016585 mRNA Translation: AAH16585.1 Different initiation.
BC060617 mRNA Translation: AAH60617.1
AK033515 mRNA Translation: BAC28334.1
CCDSiCCDS24719.1
RefSeqiNP_598950.2, NM_134189.2
UniGeneiMm.271670

Genome annotation databases

EnsembliENSMUST00000066987; ENSMUSP00000065096; ENSMUSG00000020520
GeneIDi171212
KEGGimmu:171212
UCSCiuc007jab.1 mouse

Similar proteinsi

Entry informationi

Entry nameiGLT10_MOUSE
AccessioniPrimary (citable) accession number: Q6P9S7
Secondary accession number(s): Q6KAQ2, Q8BZU8, Q91YJ6
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: July 5, 2004
Last modified: May 23, 2018
This is version 123 of the entry and version 1 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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Main funding by: National Institutes of Health