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Protein

N-acetylgalactosaminyltransferase 7

Gene

Galnt7

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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.

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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei247 – 2471SubstrateBy similarity
Binding sitei277 – 2771SubstrateBy similarity
Metal bindingi301 – 3011ManganeseBy similarity
Metal bindingi303 – 3031ManganeseBy similarity
Binding sitei412 – 4121SubstrateBy similarity
Metal bindingi440 – 4401ManganeseBy similarity
Binding sitei443 – 4431SubstrateBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Ligandi

Lectin, 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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 16

Organism-specific databases

RGDi620362. Galnt7.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 66CytoplasmicSequence analysis
Transmembranei7 – 2923Helical; Signal-anchor for type II membrane proteinSequence analysisAdd
BLAST
Topological domaini30 – 657628LumenalSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 657657N-acetylgalactosaminyltransferase 7PRO_0000059118Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
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)LengthDescriptionGraphical viewFeature identifierActions
Domaini532 – 652121Ricin B-type lectinPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni206 – 317112Catalytic subdomain AAdd
BLAST
Regioni381 – 44363Catalytic subdomain BAdd
BLAST

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

Contains 1 ricin B-type lectin domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG3736. Eukaryota.
ENOG410XPMK. LUCA.
GeneTreeiENSGT00760000118828.
HOGENOMiHOG000038227.
HOVERGENiHBG051699.
InParanoidiQ9R0C5.
KOiK00710.
OMAiIQRQYLT.
OrthoDBiEOG091G085O.
PhylomeDBiQ9R0C5.
TreeFamiTF352176.

Family and domain databases

Gene3Di3.90.550.10. 1 hit.
InterProiIPR027791. Galactosyl_T_C.
IPR001173. Glyco_trans_2-like.
IPR029044. Nucleotide-diphossugar_trans.
IPR000772. Ricin_B_lectin.
[Graphical view]
PfamiPF02709. Glyco_transf_7C. 1 hit.
PF00535. Glycos_transf_2. 1 hit.
PF00652. Ricin_B_lectin. 1 hit.
[Graphical view]
SMARTiSM00458. RICIN. 1 hit.
[Graphical view]
SUPFAMiSSF50370. SSF50370. 1 hit.
SSF53448. SSF53448. 1 hit.
PROSITEiPS50231. RICIN_B_LECTIN. 1 hit.
[Graphical view]

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.

Cross-referencesi

Sequence databases

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

3D structure databases

ProteinModelPortaliQ9R0C5.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000016474.

Protein family/group databases

CAZyiCBM13. Carbohydrate-Binding Module Family 13.
GT27. Glycosyltransferase Family 27.

Proteomic databases

PaxDbiQ9R0C5.
PRIDEiQ9R0C5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi51809.
RGDi620362. Galnt7.

Phylogenomic databases

eggNOGiKOG3736. Eukaryota.
ENOG410XPMK. LUCA.
GeneTreeiENSGT00760000118828.
HOGENOMiHOG000038227.
HOVERGENiHBG051699.
InParanoidiQ9R0C5.
KOiK00710.
OMAiIQRQYLT.
OrthoDBiEOG091G085O.
PhylomeDBiQ9R0C5.
TreeFamiTF352176.

Enzyme and pathway databases

UniPathwayiUPA00378.
BRENDAi2.4.1.41. 5301.
ReactomeiR-RNO-913709. O-linked glycosylation of mucins.

Miscellaneous databases

PROiQ9R0C5.

Gene expression databases

BgeeiENSRNOG00000012037.
GenevisibleiQ9R0C5. RN.

Family and domain databases

Gene3Di3.90.550.10. 1 hit.
InterProiIPR027791. Galactosyl_T_C.
IPR001173. Glyco_trans_2-like.
IPR029044. Nucleotide-diphossugar_trans.
IPR000772. Ricin_B_lectin.
[Graphical view]
PfamiPF02709. Glyco_transf_7C. 1 hit.
PF00535. Glycos_transf_2. 1 hit.
PF00652. Ricin_B_lectin. 1 hit.
[Graphical view]
SMARTiSM00458. RICIN. 1 hit.
[Graphical view]
SUPFAMiSSF50370. SSF50370. 1 hit.
SSF53448. SSF53448. 1 hit.
PROSITEiPS50231. RICIN_B_LECTIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiGALT7_RAT
AccessioniPrimary (citable) accession number: Q9R0C5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: May 1, 2000
Last modified: September 7, 2016
This is version 109 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Caution

Was originally termed Galnt6/pp-GaNTase 6.1 Publication

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.