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Protein

N-acetylgalactosaminyltransferase 7

Gene

GALNT7

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein 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)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

  • carbohydrate metabolic process Source: ProtInc
  • O-glycan processing Source: Reactome
  • protein O-linked glycosylation Source: ProtInc

Keywordsi

Molecular functionGlycosyltransferase, Transferase
LigandLectin, Manganese, Metal-binding

Enzyme and pathway databases

BRENDAi2.4.1.41. 2681.
ReactomeiR-HSA-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
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 4

Organism-specific databases

EuPathDBiHostDB:ENSG00000109586.11.
HGNCiHGNC:4129. 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

Pathology & Biotechi

Organism-specific databases

DisGeNETi51809.
OpenTargetsiENSG00000109586.
PharmGKBiPA28542.

Polymorphism and mutation databases

BioMutaiGALNT7.
DMDMi51315961.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000591161 – 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

EPDiQ86SF2.
MaxQBiQ86SF2.
PaxDbiQ86SF2.
PeptideAtlasiQ86SF2.
PRIDEiQ86SF2.

PTM databases

iPTMnetiQ86SF2.
PhosphoSitePlusiQ86SF2.

Expressioni

Tissue specificityi

Widely expressed. Expressed in uterus, retina, kidney, small intestine, omentum, stomach and CNS.1 Publication

Gene expression databases

BgeeiENSG00000109586.
CleanExiHS_GALNT7.
ExpressionAtlasiQ86SF2. baseline and differential.
GenevisibleiQ86SF2. HS.

Organism-specific databases

HPAiHPA064243.
HPA065317.

Interactioni

Protein-protein interaction databases

BioGridi119735. 34 interactors.
IntActiQ86SF2. 2 interactors.
STRINGi9606.ENSP00000265000.

Structurei

3D structure databases

ProteinModelPortaliQ86SF2.
SMRiQ86SF2.
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.
GeneTreeiENSGT00760000118828.
HOGENOMiHOG000038227.
HOVERGENiHBG051699.
InParanoidiQ86SF2.
KOiK00710.
OrthoDBiEOG091G085O.
PhylomeDBiQ86SF2.
TreeFamiTF352176.

Family and domain databases

Gene3Di3.90.550.10. 1 hit.
InterProiView protein in InterPro
IPR001173. Glyco_trans_2-like.
IPR029044. Nucleotide-diphossugar_trans.
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.

Q86SF2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRLKIGFILR SLLVVGSFLG LVVLWSSLTP RPDDPSPLSR MREDRDVNDP
60 70 80 90 100
MPNRGGNGLA PGEDRFKPVV PWPHVEGVEV DLESIRRINK AKNEQEHHAG
110 120 130 140 150
GDSQKDIMQR QYLTFKPQTF TYHDPVLRPG ILGNFEPKEP EPPGVVGGPG
160 170 180 190 200
EKAKPLVLGP EFKQAIQASI KEFGFNMVAS DMISLDRSVN DLRQEECKYW
210 220 230 240 250
HYDENLLTSS VVIVFHNEGW STLMRTVHSV IKRTPRKYLA EIVLIDDFSN
260 270 280 290 300
KEHLKEKLDE YIKLWNGLVK VFRNERREGL IQARSIGAQK AKLGQVLIYL
310 320 330 340 350
DAHCEVAVNW YAPLVAPISK DRTICTVPLI DVINGNTYEI IPQGGGDEDG
360 370 380 390 400
YARGAWDWSM LWKRVPLTPQ EKRLRKTKTE PYRSPAMAGG LFAIEREFFF
410 420 430 440 450
ELGLYDPGLQ IWGGENFEIS YKIWQCGGKL LFVPCSRVGH IYRLEGWQGN
460 470 480 490 500
PPPIYVGSSP TLKNYVRVVE VWWDEYKDYF YASRPESQAL PYGDISELKK
510 520 530 540 550
FREDHNCKSF KWFMEEIAYD ITSHYPLPPK NVDWGEIRGF ETAYCIDSMG
560 570 580 590 600
KTNGGFVELG PCHRMGGNQL FRINEANQLM QYDQCLTKGA DGSKVMITHC
610 620 630 640 650
NLNEFKEWQY FKNLHRFTHI PSGKCLDRSE VLHQVFISNC DSSKTTQKWE

MNNIHSV
Length:657
Mass (Da):75,389
Last modified:June 1, 2003 - v1
Checksum:iD78CB5CBDA4B02FA
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti188S → N in CAB60270 (PubMed:10544240).Curated1
Sequence conflicti392F → C in CAB60270 (PubMed:10544240).Curated1
Sequence conflicti408G → S in CAB60270 (PubMed:10544240).Curated1
Sequence conflicti508K → Q in CAB60270 (PubMed:10544240).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ002744 mRNA. Translation: CAB60270.1.
AK075488 mRNA. Translation: BAG52155.1.
CH471056 Genomic DNA. Translation: EAX04761.1.
BC035303 mRNA. Translation: AAH35303.1.
BC046129 mRNA. Translation: AAH46129.1.
BC047468 mRNA. Translation: AAH47468.1.
CCDSiCCDS3815.1.
RefSeqiNP_059119.2. NM_017423.2.
UniGeneiHs.548088.

Genome annotation databases

EnsembliENST00000265000; ENSP00000265000; ENSG00000109586.
GeneIDi51809.
KEGGihsa:51809.
UCSCiuc003isz.4. human.

Similar proteinsi

Entry informationi

Entry nameiGALT7_HUMAN
AccessioniPrimary (citable) accession number: Q86SF2
Secondary accession number(s): B3KQU3, Q7Z5W7, Q9UJ28
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: June 1, 2003
Last modified: September 27, 2017
This is version 136 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 4
    Human chromosome 4: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. SIMILARITY comments
    Index of protein domains and families