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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

Pathway:iprotein 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

  • carbohydrate binding Source: UniProtKB-KW
  • metal ion binding Source: UniProtKB-KW
  • polypeptide N-acetylgalactosaminyltransferase activity Source: ProtInc

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. 2681.
ReactomeiREACT_115606. 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
ProteomesiUP000005640 Componenti: Chromosome 4

Organism-specific databases

HGNCiHGNC:4129. 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

  • extracellular exosome Source: UniProtKB
  • Golgi membrane Source: Reactome
  • integral component of membrane Source: UniProtKB-KW
  • membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA28542.

Polymorphism and mutation databases

BioMutaiGALNT7.
DMDMi51315961.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 657657N-acetylgalactosaminyltransferase 7PRO_0000059116Add
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

MaxQBiQ86SF2.
PaxDbiQ86SF2.
PeptideAtlasiQ86SF2.
PRIDEiQ86SF2.

PTM databases

PhosphoSiteiQ86SF2.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiQ86SF2.
CleanExiHS_GALNT7.
ExpressionAtlasiQ86SF2. baseline and differential.
GenevisibleiQ86SF2. HS.

Organism-specific databases

HPAiHPA064243.
HPA065317.

Interactioni

Protein-protein interaction databases

BioGridi119735. 6 interactions.
IntActiQ86SF2. 2 interactions.
STRINGi9606.ENSP00000265000.

Structurei

3D structure databases

ProteinModelPortaliQ86SF2.
SMRiQ86SF2. Positions 148-656.
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

eggNOGiNOG248127.
GeneTreeiENSGT00760000118828.
HOGENOMiHOG000038227.
HOVERGENiHBG051699.
InParanoidiQ86SF2.
KOiK00710.
OrthoDBiEOG7J9VP2.
PhylomeDBiQ86SF2.
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.

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti188 – 1881S → N in CAB60270 (PubMed:10544240).Curated
Sequence conflicti392 – 3921F → C in CAB60270 (PubMed:10544240).Curated
Sequence conflicti408 – 4081G → S in CAB60270 (PubMed:10544240).Curated
Sequence conflicti508 – 5081K → Q in CAB60270 (PubMed:10544240).Curated

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.

Cross-referencesi

Web resourcesi

GGDB

GlycoGene database

Functional Glycomics Gateway - GTase

N-acetylgalactosaminyltransferase 7

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.

3D structure databases

ProteinModelPortaliQ86SF2.
SMRiQ86SF2. Positions 148-656.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi119735. 6 interactions.
IntActiQ86SF2. 2 interactions.
STRINGi9606.ENSP00000265000.

Protein family/group databases

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

PTM databases

PhosphoSiteiQ86SF2.

Polymorphism and mutation databases

BioMutaiGALNT7.
DMDMi51315961.

Proteomic databases

MaxQBiQ86SF2.
PaxDbiQ86SF2.
PeptideAtlasiQ86SF2.
PRIDEiQ86SF2.

Protocols and materials databases

DNASUi51809.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi51809.
GeneCardsiGC04P174089.
H-InvDBHIX0031463.
HGNCiHGNC:4129. GALNT7.
HPAiHPA064243.
HPA065317.
MIMi605005. gene.
neXtProtiNX_Q86SF2.
PharmGKBiPA28542.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG248127.
GeneTreeiENSGT00760000118828.
HOGENOMiHOG000038227.
HOVERGENiHBG051699.
InParanoidiQ86SF2.
KOiK00710.
OrthoDBiEOG7J9VP2.
PhylomeDBiQ86SF2.
TreeFamiTF352176.

Enzyme and pathway databases

UniPathwayiUPA00378.
BRENDAi2.4.1.41. 2681.
ReactomeiREACT_115606. O-linked glycosylation of mucins.

Miscellaneous databases

ChiTaRSiGALNT7. human.
GenomeRNAii51809.
NextBioi55940.
PROiQ86SF2.
SOURCEiSearch...

Gene expression databases

BgeeiQ86SF2.
CleanExiHS_GALNT7.
ExpressionAtlasiQ86SF2. baseline and differential.
GenevisibleiQ86SF2. HS.

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...

Publicationsi

« Hide 'large scale' publications
  1. "A novel human UDP-N-acetyl-D-galactosamine;polypeptide N-acetylgalactosaminyltransferase, GalNAc-T7, with specificity for partial GalNAc-glycosylated acceptor substrates."
    Bennett E.P., Hassan H., Hollingsworth M.A., Clausen H.
    FEBS Lett. 460:226-230(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], ENZYME ACTIVITY, TISSUE SPECIFICITY.
  2. "Signal sequence and keyword trap in silico for selection of full-length human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA libraries."
    Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J., Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S., Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y.
    , Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S., Isogai T.
    DNA Res. 12:117-126(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Ovary.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Placenta and Testis.
  5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiGALT7_HUMAN
AccessioniPrimary (citable) accession number: Q86SF2
Secondary accession number(s): B3KQU3, Q7Z5W7, Q9UJ28
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: June 1, 2003
Last modified: July 22, 2015
This is version 118 of the entry and version 1 of the sequence. [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

External Data

Dasty 3

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 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.