Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

N-acetylgalactosaminyltransferase 7

Gene

Galnt7

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: -Experimental evidence at transcript leveli

Functioni

Glycopeptide transferase involved in O-linked oligosaccharide biosynthesis, which catalyzes the transfer of an N-acetyl-D-galactosamine residue to an already glycosylated peptide. In contrast to other proteins of the family, it does not act as a peptide transferase that transfers 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. Some peptide transferase activity is however not excluded, considering that its appropriate peptide substrate may remain unidentified.

Caution

Was originally termed Galnt6/pp-GaNTase 6.1 Publication

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 sitei247SubstrateBy similarity1
Binding sitei277SubstrateBy similarity1
Metal bindingi301ManganeseBy similarity1
Metal bindingi303ManganeseBy similarity1
Binding sitei412SubstrateBy similarity1
Metal bindingi440ManganeseBy similarity1
Binding sitei443SubstrateBy similarity1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionGlycosyltransferase, Transferase
LigandLectin, Manganese, Metal-binding

Enzyme and pathway databases

BRENDAi2.4.1.41 5301
ReactomeiR-RNO-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:
N-acetylgalactosaminyltransferase 7 (EC:2.4.1.-)
Alternative name(s):
Polypeptide GalNAc transferase 7
Short name:
GalNAc-T7
Short name:
pp-GaNTase 7
Protein-UDP acetylgalactosaminyltransferase 7
UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 7
Gene namesi
Name:Galnt7
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 16

Organism-specific databases

RGDi620362 Galnt7

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 – 657LumenalSequence analysisAdd BLAST628

Keywords - Cellular componenti

Golgi apparatus, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000591181 – 657N-acetylgalactosaminyltransferase 7Add BLAST657

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi197 ↔ 435PROSITE-ProRule annotation
Disulfide bondi426 ↔ 507PROSITE-ProRule annotation
Disulfide bondi545 ↔ 562PROSITE-ProRule annotation
Disulfide bondi585 ↔ 600PROSITE-ProRule annotation
Disulfide bondi625 ↔ 640PROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond

Proteomic databases

PaxDbiQ9R0C5
PRIDEiQ9R0C5

Expressioni

Tissue specificityi

Highly expressed in sublingual gland. Expressed at lower level in stomach, small intestiine and colon.1 Publication

Gene expression databases

BgeeiENSRNOG00000012037
GenevisibleiQ9R0C5 RN

Interactioni

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000016474

Structurei

3D structure databases

ProteinModelPortaliQ9R0C5
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini532 – 652Ricin B-type lectinPROSITE-ProRule annotationAdd BLAST121

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni206 – 317Catalytic subdomain AAdd BLAST112
Regioni381 – 443Catalytic 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
InParanoidiQ9R0C5
KOiK00710
OMAiNFEYRPV
OrthoDBiEOG091G085O
PhylomeDBiQ9R0C5
TreeFamiTF352176

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.

Q9R0C5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRLKIGFILR SLLVVGSFLG LVVLWSSLSS RPDDPSPLSR MREDRDVNNP
60 70 80 90 100
LPNRGGNGLA PGDDRFKPVV PWPHVEGVEV DLESIRRKNK AKNEQERHAG
110 120 130 140 150
GDSQKDIMQR QYLTFKPQTF TYRDPVLRPG VLGNFEPKEP EPHGVVGGPG
160 170 180 190 200
ENAKPLVLGP EYKQAAQASI KEFGFNMAAS DMISLDRSVN DLRQEECKYW
210 220 230 240 250
HYDENLLTSS VVIVFHNEGW STLMRTVHSV IKRTPRKYLA EIVLIDDFSN
260 270 280 290 300
KEHLKEKLTE YIKLWNGLVK VFRNERREGL IQARSIGAQK AKLGQVLIYL
310 320 330 340 350
DAHCEVAVNW YAPLVAPISK DRTICTVPII DVINGNTYEI IPQGGGDEDG
360 370 380 390 400
YARGAWDWSM LWKRVPLTPR EKRLRKTKTE PYRSPAMAGG LFAIERDFFF
410 420 430 440 450
ELGLYDPGLQ IWGGENFEIS YKIWQCGGKL LFVPCSRVGH IYRLEGWQGN
460 470 480 490 500
PPPLYVGSSP TLKNYVRVVE VWWDEYKDYF YASRPESKAL PYGDISELKK
510 520 530 540 550
FREDHNCKSF KWFMEEIAYD ITAHYPLPPR NVEWGEIRGL ETAYCIDSMG
560 570 580 590 600
KTNGGFVELG PCHRMGGNQL FRINEANQLM QYDQCLTKGP DGSKVMITHC
610 620 630 640 650
NLNEFKEWQY FKNLHRFTHI ASGKCLDRSE VLHQVFISSC DNGKMTQKWE

MNNIHSV
Length:657
Mass (Da):75,335
Last modified:May 1, 2000 - v1
Checksum:i952DE15F0758A625
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF076167 mRNA Translation: AAC99426.1
RefSeqiNP_075215.1, NM_022926.1
UniGeneiRn.207200

Genome annotation databases

EnsembliENSRNOT00000016474; ENSRNOP00000016474; ENSRNOG00000012037
ENSRNOT00000084707; ENSRNOP00000072171; ENSRNOG00000012037
GeneIDi29750
KEGGirno:29750
UCSCiRGD:620362 rat

Similar proteinsi

Entry informationi

Entry nameiGALT7_RAT
AccessioniPrimary (citable) accession number: Q9R0C5
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: May 1, 2000
Last modified: May 23, 2018
This is version 117 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

Cookie policy

We would like to use anonymized google analytics cookies to gather statistics on how uniprot.org is used in aggregate. Learn more

UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health