Q10472 (GALT1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Polypeptide N-acetylgalactosaminyltransferase 1
EC=2.4.1.41

Alternative name(s):
Polypeptide GalNAc transferase 1
Short name=GalNAc-T1
Short name=pp-GaNTase 1
Protein-UDP acetylgalactosaminyltransferase 1
UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 1

Cleaved into the following chain:

1. Polypeptide N-acetylgalactosaminyltransferase 1 soluble form

Gene names

Name:

GALNT1

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	559 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. Has a broad spectrum of substrates for peptides such as EA2, Muc5AC, Muc1a, Muc1b and Muc7. Ref.5
Catalytic activity	UDP-N-acetyl-D-galactosamine + polypeptide = UDP + N-acetyl-D-galactosaminyl-polypeptide.
Cofactor	Manganese. Calcium.
Pathway	Protein modification; protein glycosylation.
Subcellular location	Polypeptide N-acetylgalactosaminyltransferase 1: Golgi apparatus › Golgi stack membrane; Single-pass type II membrane protein Ref.6. Polypeptide N-acetylgalactosaminyltransferase 1 soluble form: Secreted.
Tissue specificity	Widely expressed. Expressed in all tissues tested. Ref.2
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 directs the glycopeptide specificity. It is required in the glycopeptide specificity of enzyme activity but not for activity with naked peptide substrates, suggesting that it triggers the catalytic domain to act on GalNAc-glycopeptide substrates 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 Secreted
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Signal-anchor Transmembrane Transmembrane helix
Ligand	Calcium Lectin Manganese
Molecular function	Glycosyltransferase Transferase
PTM	Disulfide bond Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	protein O-linked glycosylation via serine Inferred from direct assay Ref.5. Source: BHF-UCL protein O-linked glycosylation via threonine Inferred from direct assay Ref.5. Source: BHF-UCL
Cellular component	Golgi cisterna membrane Inferred from electronic annotation. Source: UniProtKB-SubCell extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW perinuclear region of cytoplasm Inferred from direct assay. Source: BHF-UCL
Molecular function	manganese ion binding Inferred from direct assay Ref.5. Source: BHF-UCL polypeptide N-acetylgalactosaminyltransferase activity Inferred from direct assay Ref.5. Source: BHF-UCL sugar binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q10472-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q10472-2)

The sequence of this isoform differs from the canonical sequence as follows:
     106-559: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 559	559	Polypeptide N-acetylgalactosaminyltransferase 1		PRO_0000223387
	Chain	41 – 559	519	Polypeptide N-acetylgalactosaminyltransferase 1 soluble form		PRO_0000012257
Regions
	Topological domain	1 – 8	8	Cytoplasmic Potential
	Transmembrane	9 – 28	20	Helical; Signal-anchor for type II membrane protein; Potential
	Topological domain	29 – 559	531	Lumenal Potential
	Domain	429 – 551	123	Ricin B-type lectin
	Region	115 – 225	111	Catalytic subdomain A
	Region	285 – 347	63	Catalytic subdomain B
Amino acid modifications
	Glycosylation	95	1	N-linked (GlcNAc...) Potential
	Glycosylation	552	1	N-linked (GlcNAc...) Potential
	Disulfide bond	106 ↔ 339		By similarity
	Disulfide bond	330 ↔ 408		By similarity
	Disulfide bond	442 ↔ 459		By similarity
	Disulfide bond	482 ↔ 497		By similarity
	Disulfide bond	523 ↔ 540		By similarity
Natural variations
	Alternative sequence	106 – 559	454	Missing in isoform 2.		VSP_011200
	Natural variant	414	1	Y → D. Corresponds to variant rs34304568 [ dbSNP | Ensembl ].		VAR_033946

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: CD68118CB201EE5B	FASTA	559	64,219
	10 20 30 40 50 60 MRKFAYCKVV LATSLIWVLL DMFLLLYFSE CNKCDEKKER GLPAGDVLEP VQKPHEGPGE 70 80 90 100 110 120 MGKPVVIPKE DQEKMKEMFK INQFNLMASE MIALNRSLPD VRLEGCKTKV YPDNLPTTSV 130 140 150 160 170 180 VIVFHNEAWS TLLRTVHSVI NRSPRHMIEE IVLVDDASER DFLKRPLESY VKKLKVPVHV 190 200 210 220 230 240 IRMEQRSGLI RARLKGAAVS KGQVITFLDA HCECTVGWLE PLLARIKHDR RTVVCPIIDV 250 260 270 280 290 300 ISDDTFEYMA GSDMTYGGFN WKLNFRWYPV PQREMDRRKG DRTLPVRTPT MAGGLFSIDR 310 320 330 340 350 360 DYFQEIGTYD AGMDIWGGEN LEISFRIWQC GGTLEIVTCS HVGHVFRKAT PYTFPGGTGQ 370 380 390 400 410 420 IINKNNRRLA EVWMDEFKNF FYIISPGVTK VDYGDISSRV GLRHKLQCKP FSWYLENIYP 430 440 450 460 470 480 DSQIPRHYFS LGEIRNVETN QCLDNMARKE NEKVGIFNCH GMGGNQVFSY TANKEIRTDD 490 500 510 520 530 540 LCLDVSKLNG PVTMLKCHHL KGNQLWEYDP VKLTLQHVNS NQCLDKATEE DSQVPSIRDC 550 NGSRSQQWLL RNVTLPEIF
	Isoform 2 [UniParc]. Checksum: 01BE501BD11331AF	FASTA	105	12,046
	10 20 30 40 50 60 MRKFAYCKVV LATSLIWVLL DMFLLLYFSE CNKCDEKKER GLPAGDVLEP VQKPHEGPGE 70 80 90 100 MGKPVVIPKE DQEKMKEMFK INQFNLMASE MIALNRSLPD VRLEG

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"cDNA cloning, expression, and chromosomal localization of a human UDP-GalNAc:polypeptide, N-acetylgalactosaminyltransferase." Meurer J.A., Naylor J.M., Baker C.A., Thomsen D.R., Homa F.L., Elhammer A.P. J. Biochem. 118:568-574(1995) [PubMed: 8690719] [Abstract] Cited for: NUCLEOTIDE SEQUENCE (ISOFORM 1). Tissue: Salivary gland.
[2]	"Purification and cDNA cloning of a human UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase." White T., Bennett E.P., Takio K., Soerensen T., Bonding N., Clausen H. J. Biol. Chem. 270:24156-24165(1995) [PubMed: 7592619] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
[3]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: PNS.
[4]	"Organization of a human UDP-GalNAc:polypeptide, N-acetylgalactosaminyltransferase gene and a related processed pseudogene." Meurer J.A., Drong R.F., Homa F.L., Slightom J.L., Elhammer A.P. Glycobiology 6:231-241(1996) [PubMed: 8727794] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 512-559 (ISOFORM 1).
[5]	"Substrate specificities of three members of the human UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase family, GalNAc-T1, -T2, and -T3." Wandall H.H., Hassan H., Mirgorodskaya E., Kristensen A.K., Roepstorff P., Bennett E.P., Nielsen P.A., Hollingsworth M.A., Burchell J., Taylor-Papadimitriou J., Clausen H. J. Biol. Chem. 272:23503-23514(1997) [PubMed: 9295285] [Abstract] Cited for: FUNCTION.
[6]	"Localization of three human polypeptide GalNAc-transferases in HeLa cells suggests initiation of O-linked glycosylation throughout the Golgi apparatus." Roettger S., White J., Wandall H.H., Olivo J.-C., Stark A., Bennett E.P., Whitehouse C., Berger E.G., Clausen H., Nilsson T. J. Cell Sci. 111:45-60(1998) [PubMed: 9394011] [Abstract] Cited for: SUBCELLULAR LOCATION.
[7]	"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: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Web resources

GGDB

GlycoGene database

Functional Glycomics Gateway - GTase

Polypeptide N-acetylgalactosaminyltransferase 1

Cross-references

Sequence databases
EMBL GenBank DDBJ	U41514 mRNA. Translation: AAC50327.1. X85018 mRNA. Translation: CAA59380.1. BC047746 mRNA. Translation: AAH47746.1. S82597 Genomic DNA. Translation: AAD14406.1.
IPI	IPI00025818. IPI00456057.
PIR	JC4223.
RefSeq	NP_065207.2. NM_020474.3.
UniGene	Hs.514806.
3D structure databases
ProteinModelPortal	Q10472.
SMR	Q10472. Positions 59-553.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q10472. 1 interaction.
STRING	Q10472.
Protein family/group databases
CAZy	CBM13. Carbohydrate-Binding Module Family 13. GT27. Glycosyltransferase Family 27.
Polymorphism databases
DMDM	1709558.
Proteomic databases
PeptideAtlas	Q10472.
PRIDE	Q10472.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000269195; ENSP00000269195; ENSG00000141429.
GeneID	2589.
KEGG	hsa:2589.
UCSC	uc002kza.1. human. uc002kzb.1. human.
Organism-specific databases
CTD	2589.
GeneCards	GC18P033161.
H-InvDB	HIX0027372.
HGNC	HGNC:4123. GALNT1.
HPA	HPA012628.
MIM	602273. gene.
neXtProt	NX_Q10472.
PharmGKB	PA30054.
GenAtlas	Search...
Phylogenomic databases
HOGENOM	HBG715048.
HOVERGEN	HBG051699.
InParanoid	Q10472.
OMA	XKLTLQH.
OrthoDB	EOG40P46C.
PhylomeDB	Q10472.
Gene expression databases
ArrayExpress	Q10472.
Bgee	Q10472.
CleanEx	HS_GALNT1.
Genevestigator	Q10472.
GermOnline	ENSG00000141429. Homo sapiens.
Family and domain databases
InterPro	IPR001173. Glyco_trans_2. IPR008997. Ricin_B-rel_lectin. IPR000772. Ricin_B_lectin. [Graphical view]
KO	K00710.
Pfam	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
NextBio	10241.
SOURCE	Search...

Entry information

Entry name

GALT1_HUMAN

Accession

Primary (citable) accession number: Q10472
Secondary accession number(s): Q86TJ7, Q9UM86

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	January 25, 2012
This is version 115 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.