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Protein

Polypeptide N-acetylgalactosaminyltransferase 11

Gene

Galnt11

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Polypeptide N-acetylgalactosaminyltransferase that catalyzes the initiation of protein O-linked glycosylation and is involved in left/right asymmetry by mediating O-glycosylation of NOTCH1. O-glycosylation of NOTCH1 promotes activation of NOTCH1, modulating the balance between motile and immotile (sensory) cilia at the left-right organiser (LRO). Polypeptide N-acetylgalactosaminyltransferases catalyze the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. Displays the same enzyme activity toward MUC1, MUC4, and EA2 than GALNT1. Not involved in glycosylation of erythropoietin (EPO) (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 sitei191SubstrateBy similarity1
Binding sitei222SubstrateBy similarity1
Metal bindingi245ManganeseBy similarity1
Binding sitei246SubstrateBy similarity1
Metal bindingi247ManganeseBy similarity1
Binding sitei350SubstrateBy similarity1
Metal bindingi378ManganeseBy similarity1
Binding sitei381SubstrateBy similarity1
Binding sitei386SubstrateBy similarity1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionGlycosyltransferase, Transferase
Biological processNotch signaling pathway
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 11 (EC:2.4.1.41)
Alternative name(s):
Polypeptide GalNAc transferase 11
Short name:
GalNAc-T11
Short name:
pp-GaNTase 11
Protein-UDP acetylgalactosaminyltransferase 11
UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 11
Gene namesi
Name:Galnt11
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 5

Organism-specific databases

MGIiMGI:2444392 Galnt11

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 – 6CytoplasmicSequence analysis6
Transmembranei7 – 29Helical; Signal-anchor for type II membrane proteinSequence analysisAdd BLAST23
Topological domaini30 – 608LumenalSequence analysisAdd BLAST579

Keywords - Cellular componenti

Golgi apparatus, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000591261 – 608Polypeptide N-acetylgalactosaminyltransferase 11Add BLAST608

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei95PhosphoserineCombined sources1
Disulfide bondi141 ↔ 373PROSITE-ProRule annotation
Disulfide bondi364 ↔ 441PROSITE-ProRule annotation
Glycosylationi423N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi428N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi493 ↔ 512PROSITE-ProRule annotation
Disulfide bondi536 ↔ 553PROSITE-ProRule annotation
Disulfide bondi578 ↔ 596PROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiQ921L8
PaxDbiQ921L8
PRIDEiQ921L8

PTM databases

iPTMnetiQ921L8
PhosphoSitePlusiQ921L8

Expressioni

Tissue specificityi

Mainly expressed in kidney. Weakly expressed in other tissues.1 Publication

Developmental stagei

At E8.0, present in the left-right organiser (LRO) node, with enrichment in crown cells compared to pit cells (at protein level).1 Publication

Gene expression databases

BgeeiENSMUSG00000038072
ExpressionAtlasiQ921L8 baseline and differential
GenevisibleiQ921L8 MM

Interactioni

Subunit structurei

Interacts with NOTCH1.By similarity

GO - Molecular functioni

Protein-protein interaction databases

IntActiQ921L8, 2 interactors
MINTiQ921L8
STRINGi10090.ENSMUSP00000036240

Structurei

3D structure databases

ProteinModelPortaliQ921L8
SMRiQ921L8
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini476 – 607Ricin B-type lectinPROSITE-ProRule annotationAdd BLAST132

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni150 – 261Catalytic subdomain AAdd BLAST112
Regioni319 – 381Catalytic 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
HOGENOMiHOG000038227
HOVERGENiHBG051699
InParanoidiQ921L8
KOiK00710
OMAiGSQQWTF
OrthoDBiEOG091G085O
PhylomeDBiQ921L8
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, 2 hits
SSF53448 SSF53448, 1 hit
PROSITEiView protein in PROSITE
PS50231 RICIN_B_LECTIN, 1 hit

Sequencei

Sequence statusi: Complete.

Q921L8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGSITVRYFC YGCLFTSATW TVLLFIYFNF SEVTQPLRNV PIKGSGPHGP
60 70 80 90 100
FPKKFYPRFT RGPGRVLDPQ FKANRIDRLM NNHIEDPDKG LSKSSSELGM
110 120 130 140 150
IFNERDQELR DLGYQKHAFN MLISNRLGYH RDVPDTRNAE CRRKSYPTDL
160 170 180 190 200
PTASIVICFY NEAFSALLRT VHSVVDRTPA HLLHEIILVD DSSDFDDLKG
210 220 230 240 250
ELDEYIQRYL PAKVKVIRNM KREGLIRGRM IGAAHATGEV LVFLDSHCEV
260 270 280 290 300
NVMWLQPLLA IILEDPHTVV CPVIDIISAD TLAYSSSPVV RGGFNWGLHF
310 320 330 340 350
KWDLVPVSEL GGPDGATAPI RSPTMAGGLF AMNRQYFNDL GQYDSGMDIW
360 370 380 390 400
GGENLEISFR IWMCGGKLFI LPCSRVGHIF RKRRPYGSPE GQDTMTHNSL
410 420 430 440 450
RLAHVWLDEY KEQYFSLRPD LKNKSFGNIS ERVELRKKLG CQSFKWYLDN
460 470 480 490 500
IYPEMQIPGP NAKPQQPVLI NRGPKRPRVL QRGRLYHLQT NKCLVAQGRS
510 520 530 540 550
SQKGGLVLLK TCDYGDPTQV WIYNEDHELI LNNLLCLDMS ETRSSDPPRL
560 570 580 590 600
MKCHGSGGSQ QWTFGKNNRL YQVSVGQCLR VMDLMDQKGY VGMAICDGSS

SQQWRLEG
Length:608
Mass (Da):69,201
Last modified:December 1, 2001 - v1
Checksum:i0E452FDA1CA5668B
GO

Sequence cautioni

The sequence AAH34184 differs from that shown. Reason: Erroneous termination at position 412. Translated as Glu.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti545S → L in BAC40096 (PubMed:16141072).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y12435 mRNA Translation: CAC79626.1
AF495528 mRNA Translation: AAQ06668.1
AK088014 mRNA Translation: BAC40096.1
AK161524 mRNA Translation: BAE36442.1
BC011428 mRNA Translation: AAH11428.1
BC021504 mRNA Translation: AAH21504.1
BC034184 mRNA Translation: AAH34184.1 Sequence problems.
BC034185 mRNA Translation: AAH34185.1
BC036143 mRNA Translation: AAH36143.1
BC036145 mRNA Translation: AAH36145.1
CCDSiCCDS19133.1
RefSeqiNP_659157.1, NM_144908.3
XP_006535744.1, XM_006535681.3
XP_011248066.1, XM_011249764.2
UniGeneiMm.21814
Mm.246718

Genome annotation databases

EnsembliENSMUST00000045737; ENSMUSP00000036240; ENSMUSG00000038072
ENSMUST00000114950; ENSMUSP00000110600; ENSMUSG00000038072
ENSMUST00000114952; ENSMUSP00000110602; ENSMUSG00000038072
GeneIDi231050
KEGGimmu:231050
UCSCiuc008wss.1 mouse

Similar proteinsi

Entry informationi

Entry nameiGLT11_MOUSE
AccessioniPrimary (citable) accession number: Q921L8
Secondary accession number(s): Q3TT83, Q8BU26, Q8K032
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: December 1, 2001
Last modified: March 28, 2018
This is version 133 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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