Q86SF2 (GALT7_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:

GALNT7

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	657 AA.
Sequence status	Complete.
Protein existence	Evidence 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. Calcium 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.

Ontologies

Keywords
Cellular component	Golgi apparatus Membrane
Domain	Signal-anchor Transmembrane Transmembrane helix
Ligand	Calcium Lectin Manganese
Molecular function	Glycosyltransferase Transferase
PTM	Disulfide bond
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	O-glycan processing Traceable author statement. Source: Reactome post-translational protein modification Traceable author statement. Source: Reactome
Cellular_component	Golgi membrane Traceable author statement. Source: Reactome integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	polypeptide N-acetylgalactosaminyltransferase activity Traceable author statement Ref.1. Source: ProtInc
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 657	657	N-acetylgalactosaminyltransferase 7		PRO_0000059116
Regions
	Topological domain	1 – 6	6	Cytoplasmic Potential
	Transmembrane	7 – 29	23	Helical; Signal-anchor for type II membrane protein; Potential
	Topological domain	30 – 657	628	Lumenal Potential
	Domain	532 – 652	121	Ricin B-type lectin
	Region	206 – 317	112	Catalytic subdomain A
	Region	381 – 443	63	Catalytic subdomain B
Amino acid modifications
	Disulfide bond	545 ↔ 562		By similarity
	Disulfide bond	585 ↔ 600		By similarity
	Disulfide bond	625 ↔ 640		By similarity
Experimental info
	Sequence conflict	188	1	S → N in CAB60270. Ref.1
	Sequence conflict	392	1	F → C in CAB60270. Ref.1
	Sequence conflict	408	1	G → S in CAB60270. Ref.1
	Sequence conflict	508	1	K → Q in CAB60270. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q86SF2 [UniParc]. Last modified June 1, 2003. Version 1. Checksum: D78CB5CBDA4B02FA	FASTA	657	75,389
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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.
IPI	IPI00328391.
RefSeq	NP_059119.2. NM_017423.2.
UniGene	Hs.548088.
3D structure databases
ProteinModelPortal	Q86SF2.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q86SF2. 1 interaction.
STRING	9606.ENSP00000265000.
Protein family/group databases
CAZy	CBM13. Carbohydrate-Binding Module Family 13. GT27. Glycosyltransferase Family 27.
PTM databases
PhosphoSite	Q86SF2.
Polymorphism databases
DMDM	51315961.
Proteomic databases
PaxDb	Q86SF2.
PeptideAtlas	Q86SF2.
PRIDE	Q86SF2.
Protocols and materials databases
DNASU	51809.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000265000; ENSP00000265000; ENSG00000109586.
GeneID	51809.
KEGG	hsa:51809.
UCSC	uc003isz.4. human.
Organism-specific databases
CTD	51809.
GeneCards	GC04P174089.
H-InvDB	HIX0031463.
HGNC	HGNC:4129. GALNT7.
MIM	605005. gene.
neXtProt	NX_Q86SF2.
PharmGKB	PA28542.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG248127.
HOGENOM	HOG000038227.
HOVERGEN	HBG051699.
InParanoid	Q86SF2.
KO	K00710.
OrthoDB	EOG44MXRP.
PhylomeDB	Q86SF2.
Enzyme and pathway databases
Reactome	REACT_17015. Metabolism of proteins.
UniPathway	UPA00378.
Gene expression databases
ArrayExpress	Q86SF2.
Bgee	Q86SF2.
CleanEx	HS_GALNT7.
Genevestigator	Q86SF2.
GermOnline	ENSG00000109586. Homo sapiens.
Family and domain databases
InterPro	IPR003859. Galactosyl_T_2_met. IPR001173. Glyco_trans_2. IPR000772. Ricin_B_lectin. [Graphical view]
Pfam	PF02709. Glyco_transf_7C. 1 hit. PF00535. Glycos_transf_2. 1 hit. PF00652. Ricin_B_lectin. 1 hit. [Graphical view]
SMART	SM00458. RICIN. 1 hit. [Graphical view]
SUPFAM	SSF50370. RicinB_like. 1 hit.
PROSITE	PS50231. RICIN_B_LECTIN. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	51809.
NextBio	55940.
SOURCE	Search...

Entry information

Entry name

GALT7_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 96 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.