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Q86SF2 (GALT7_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 107. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:GALNT7
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length657 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Cofactor

Manganese By similarity.

Pathway

Protein modification; protein glycosylation.

Subcellular location

Golgi apparatus membrane; Single-pass type II membrane protein By similarity.

Tissue specificity

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

Domain

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 similarities

Belongs to the glycosyltransferase 2 family. GalNAc-T subfamily.

Contains 1 ricin B-type lectin domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 657657N-acetylgalactosaminyltransferase 7
PRO_0000059116

Regions

Topological domain1 – 66Cytoplasmic Potential
Transmembrane7 – 2923Helical; Signal-anchor for type II membrane protein; Potential
Topological domain30 – 657628Lumenal Potential
Domain532 – 652121Ricin B-type lectin
Region206 – 317112Catalytic subdomain A
Region381 – 44363Catalytic subdomain B

Sites

Metal binding3011Manganese By similarity
Metal binding3031Manganese By similarity
Metal binding4401Manganese By similarity
Binding site2471Substrate By similarity
Binding site2771Substrate By similarity
Binding site4121Substrate By similarity
Binding site4431Substrate By similarity

Amino acid modifications

Disulfide bond197 ↔ 435 By similarity
Disulfide bond426 ↔ 507 By similarity
Disulfide bond545 ↔ 562 By similarity
Disulfide bond585 ↔ 600 By similarity
Disulfide bond625 ↔ 640 By similarity

Experimental info

Sequence conflict1881S → N in CAB60270. Ref.1
Sequence conflict3921F → C in CAB60270. Ref.1
Sequence conflict4081G → S in CAB60270. Ref.1
Sequence conflict5081K → Q in CAB60270. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q86SF2 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: D78CB5CBDA4B02FA

FASTA65775,389
        10         20         30         40         50         60 
MRLKIGFILR SLLVVGSFLG LVVLWSSLTP RPDDPSPLSR MREDRDVNDP MPNRGGNGLA 

        70         80         90        100        110        120 
PGEDRFKPVV PWPHVEGVEV DLESIRRINK AKNEQEHHAG GDSQKDIMQR QYLTFKPQTF 

       130        140        150        160        170        180 
TYHDPVLRPG ILGNFEPKEP EPPGVVGGPG EKAKPLVLGP EFKQAIQASI KEFGFNMVAS 

       190        200        210        220        230        240 
DMISLDRSVN DLRQEECKYW HYDENLLTSS VVIVFHNEGW STLMRTVHSV IKRTPRKYLA 

       250        260        270        280        290        300 
EIVLIDDFSN KEHLKEKLDE YIKLWNGLVK VFRNERREGL IQARSIGAQK AKLGQVLIYL 

       310        320        330        340        350        360 
DAHCEVAVNW YAPLVAPISK DRTICTVPLI DVINGNTYEI IPQGGGDEDG YARGAWDWSM 

       370        380        390        400        410        420 
LWKRVPLTPQ EKRLRKTKTE PYRSPAMAGG LFAIEREFFF ELGLYDPGLQ IWGGENFEIS 

       430        440        450        460        470        480 
YKIWQCGGKL LFVPCSRVGH IYRLEGWQGN PPPIYVGSSP TLKNYVRVVE VWWDEYKDYF 

       490        500        510        520        530        540 
YASRPESQAL PYGDISELKK FREDHNCKSF KWFMEEIAYD ITSHYPLPPK NVDWGEIRGF 

       550        560        570        580        590        600 
ETAYCIDSMG KTNGGFVELG PCHRMGGNQL FRINEANQLM QYDQCLTKGA DGSKVMITHC 

       610        620        630        640        650 
NLNEFKEWQY FKNLHRFTHI PSGKCLDRSE VLHQVFISNC DSSKTTQKWE MNNIHSV 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Web resources

GGDB

GlycoGene database

Functional Glycomics Gateway - GTase

N-acetylgalactosaminyltransferase 7

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS3815.1.
RefSeqNP_059119.2. NM_017423.2.
UniGeneHs.548088.

3D structure databases

ProteinModelPortalQ86SF2.
SMRQ86SF2. Positions 148-656.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid119735. 3 interactions.
IntActQ86SF2. 2 interactions.
STRING9606.ENSP00000265000.

Protein family/group databases

CAZyCBM13. Carbohydrate-Binding Module Family 13.
GT27. Glycosyltransferase Family 27.

PTM databases

PhosphoSiteQ86SF2.

Polymorphism databases

DMDM51315961.

Proteomic databases

MaxQBQ86SF2.
PaxDbQ86SF2.
PeptideAtlasQ86SF2.
PRIDEQ86SF2.

Protocols and materials databases

DNASU51809.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000265000; ENSP00000265000; ENSG00000109586.
GeneID51809.
KEGGhsa:51809.
UCSCuc003isz.4. human.

Organism-specific databases

CTD51809.
GeneCardsGC04P174089.
H-InvDBHIX0031463.
HGNCHGNC:4129. GALNT7.
MIM605005. gene.
neXtProtNX_Q86SF2.
PharmGKBPA28542.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG248127.
HOGENOMHOG000038227.
HOVERGENHBG051699.
InParanoidQ86SF2.
KOK00710.
OrthoDBEOG7J9VP2.
PhylomeDBQ86SF2.
TreeFamTF352176.

Enzyme and pathway databases

ReactomeREACT_17015. Metabolism of proteins.
UniPathwayUPA00378.

Gene expression databases

ArrayExpressQ86SF2.
BgeeQ86SF2.
CleanExHS_GALNT7.
GenevestigatorQ86SF2.

Family and domain databases

Gene3D3.90.550.10. 1 hit.
InterProIPR027791. Galactosyl_T_C.
IPR001173. Glyco_trans_2-like.
IPR029044. Nucleotide-diphossugar_trans.
IPR000772. Ricin_B_lectin.
[Graphical view]
PfamPF02709. Glyco_transf_7C. 1 hit.
PF00535. Glycos_transf_2. 1 hit.
PF00652. Ricin_B_lectin. 1 hit.
[Graphical view]
SMARTSM00458. RICIN. 1 hit.
[Graphical view]
SUPFAMSSF50370. SSF50370. 1 hit.
SSF53448. SSF53448. 1 hit.
PROSITEPS50231. RICIN_B_LECTIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi51809.
NextBio55940.
PROQ86SF2.
SOURCESearch...

Entry information

Entry nameGALT7_HUMAN
AccessionPrimary (citable) accession number: Q86SF2
Secondary accession number(s): B3KQU3, Q7Z5W7, Q9UJ28
Entry history
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: June 1, 2003
Last modified: July 9, 2014
This is version 107 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 4

Human chromosome 4: entries, gene names and cross-references to MIM