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Protein

Polypeptide N-acetylgalactosaminyltransferase 15

Gene

Galnt15

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. Although it displays a much weaker activity toward all substrates tested compared to GALNT2, it is able to transfer up to seven GalNAc residues to the Muc5AC peptide, suggesting that it can fill vicinal Thr/Ser residues in cooperation with other GALNT proteins. Prefers Muc1a as substrate (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 sitei231SubstrateBy similarity1
Binding sitei260SubstrateBy similarity1
Metal bindingi283ManganeseBy similarity1
Metal bindingi285ManganeseBy similarity1
Metal bindingi416ManganeseBy similarity1
Binding sitei419SubstrateBy 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 15 (EC:2.4.1.41)
Alternative name(s):
Polypeptide GalNAc transferase-like protein 2
Short name:
GalNAc-T-like protein 2
Short name:
pp-GaNTase-like protein 2
Polypeptide N-acetylgalactosaminyltransferase-like protein 2
Protein-UDP acetylgalactosaminyltransferase-like protein 2
UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase-like protein 2
Gene namesi
Name:Galnt15
Synonyms:Galntl2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 14

Organism-specific databases

MGIiMGI:1926004 Galnt15

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 – 638LumenalSequence analysisAdd BLAST603

Keywords - Cellular componenti

Golgi apparatus, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000591381 – 638Polypeptide N-acetylgalactosaminyltransferase 15Add BLAST638

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi181 ↔ 411PROSITE-ProRule annotation
Disulfide bondi402 ↔ 481PROSITE-ProRule annotation
Disulfide bondi516 ↔ 535PROSITE-ProRule annotation
Disulfide bondi561 ↔ 574PROSITE-ProRule annotation
Glycosylationi573N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi602 ↔ 619PROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ9D2N8
PRIDEiQ9D2N8

PTM databases

iPTMnetiQ9D2N8
PhosphoSitePlusiQ9D2N8

Expressioni

Tissue specificityi

Specifically expressed in testis.1 Publication

Gene expression databases

BgeeiENSMUSG00000021903
ExpressionAtlasiQ9D2N8 baseline and differential
GenevisibleiQ9D2N8 MM

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000022460

Structurei

3D structure databases

ProteinModelPortaliQ9D2N8
SMRiQ9D2N8
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini503 – 630Ricin B-type lectinPROSITE-ProRule annotationAdd BLAST128

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni190 – 299Catalytic subdomain AAdd BLAST110
Regioni357 – 419Catalytic 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
GeneTreeiENSGT00900000140827
HOGENOMiHOG000038227
HOVERGENiHBG051699
InParanoidiQ9D2N8
KOiK00710
OMAiMLAPCSD
OrthoDBiEOG091G04OC
PhylomeDBiQ9D2N8
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.

Q9D2N8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLPRKRPRSG RSRLQFLLLF LTLGCVLMMV ILLHPPPPTL HQAVTAQASK
60 70 80 90 100
HSPDTGYRLD FGDSQEWVLE AETEGDEYSL LDGLPSFISL QEDQLLVAVA
110 120 130 140 150
SPRARRSQSQ GRRQGSYQFI KHRSRRWDEE ALEKDWRTEE DGEESEEVLT
160 170 180 190 200
PLGPDSDGLN KPLSARLPLR RVLPEVRHPL CLQQHPTSGL PTASVILCFH
210 220 230 240 250
DEAWPTLLRT VHSILDTAPR ALLQEIILVD DLSQQELLKS ALSEYVARLE
260 270 280 290 300
AVKLLRSNRR LGTIGARMLG ATRATGDVLV FMDAHCECHP GWLEPLLSRI
310 320 330 340 350
ADDRSRVVSP VIDVIDWKTL QYSASKLHRG TLDWKLDFRW KPLGEQEQKA
360 370 380 390 400
LPSPISPVRS PVVPREVVAV DRHYFQNTGA YDPLLSLGDS ENLEMSFKAW
410 420 430 440 450
LCGGSVEILP CSRVGHIYRS QDASSRPDPE VALKNKIIIA ETWLSSFKET
460 470 480 490 500
FYRHIPEAFT LSKVAKPDCT ERLKLQRRLG CRTFHWFLAN VYPELYPSDH
510 520 530 540 550
RPRFSGKLHN TGFGLCADCQ ADGDILGCPM TLAPCSNNRQ QQNLEHTGRK
560 570 580 590 600
EILFGGPQRL CFDVRGGRVI LQNCTEEGPA IHQQHWDFQE DGMIIHVLSG
610 620 630
KCMEAGVQPS NKDLYLRQCD GKTSQLWRFD QIHPVDER
Length:638
Mass (Da):72,321
Last modified:June 1, 2001 - v1
Checksum:i421617F0C8556976
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK019470 mRNA Translation: BAB31741.1
BC133711 mRNA Translation: AAI33712.1
CCDSiCCDS36859.1
RefSeqiNP_084442.1, NM_030166.3
UniGeneiMm.40681

Genome annotation databases

EnsembliENSMUST00000022460; ENSMUSP00000022460; ENSMUSG00000021903
GeneIDi78754
KEGGimmu:78754
UCSCiuc007syb.1 mouse

Similar proteinsi

Entry informationi

Entry nameiGLT15_MOUSE
AccessioniPrimary (citable) accession number: Q9D2N8
Secondary accession number(s): A3KN88
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: June 1, 2001
Last modified: March 28, 2018
This is version 120 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
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Main funding by: National Institutes of Health