Q29121 (GALT1_PIG) 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

Sus scrofa (Pig) [Reference proteome]

Taxonomic identifier

9823 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Laurasiatheria › Cetartiodactyla › Suina › Suidae › Sus

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 transcript 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 By similarity.
Catalytic activity	UDP-N-acetyl-alpha-D-galactosamine + polypeptide = UDP + N-acetyl-alpha-D-galactosaminyl-polypeptide.
Cofactor	Manganese By similarity. Calcium By similarity.
Pathway	Protein modification; protein glycosylation.
Subcellular location	Polypeptide N-acetylgalactosaminyltransferase 1: Golgi apparatus › Golgi stack membrane; Single-pass type II membrane protein By similarity. Polypeptide N-acetylgalactosaminyltransferase 1 soluble form: Secreted By similarity.
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
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 glycosylation Inferred from electronic annotation. Source: UniProtKB-UniPathway
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
Molecular_function	polypeptide N-acetylgalactosaminyltransferase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 559	559	Polypeptide N-acetylgalactosaminyltransferase 1		PRO_0000223389
	Chain	41 – 559	519	Polypeptide N-acetylgalactosaminyltransferase 1 soluble form By similarity		PRO_0000012261
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

Sequences

	Sequence		Length	Mass (Da)
	Q29121 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 68C2D261A51684C6	FASTA	559	64,119
	10 20 30 40 50 60 MRKFAYCKVV LATSLIWVLL DMFLLLYFSE CNKCDEKKER GLPAGDVLEP VQKPHEGPGE 70 80 90 100 110 120 MGKPVVIPKE DQDKMKEMFK INQFNLMASE MIALNRSLPD VRLEGCKTKV YPDNLPTTSV 130 140 150 160 170 180 VIVFHNEAWS TLLRTVHSVI NRSPRHMLEE IVLVDDASER DFLKRPLESY VKKLKVPVHV 190 200 210 220 230 240 IRMEQRSGLI RARLKGAAVS KGQVITFLDA HCECTVGWLE PLLARIKHDR KTVVCPIIDV 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 EVWMDEFKTF FYIISPGVTK VDYGDISSRL GLRHKLQCRP FSWYLENIYP 430 440 450 460 470 480 DSQIPRHYSS LGEIRNVETN QCLDNMARKE NEKVGIFNCH GMGGNQVFSY TANKEIRTDD 490 500 510 520 530 540 LCLDVSKLNG PVTMLKCHHL KGNQLWEYDP VKLTLQHVNS NQCLDKATEE DSQVPSIRDC 550 SGSRSQQWLL RNVTLPEIF

References

[1]	"Cloning and expression of a porcine UDP-GalNAc: polypeptide N-acetylgalactosaminyl transferase." Yoshida A., Hara T., Ikenaga H., Takeuchi M. Glycoconj. J. 12:824-828(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Lung.

Cross-references

Sequence databases
EMBL GenBank DDBJ	D85389 mRNA. Translation: BAA12800.1.
3D structure databases
ProteinModelPortal	Q29121.
SMR	Q29121. Positions 95-553.
ModBase	Search...
Protein-protein interaction databases
STRING	9823.ENSSSCP00000004051.
Protein family/group databases
CAZy	CBM13. Carbohydrate-Binding Module Family 13. GT27. Glycosyltransferase Family 27.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Phylogenomic databases
eggNOG	NOG239675.
HOGENOM	HOG000038227.
HOVERGEN	HBG051699.
OrthoDB	EOG40P46C.
Enzyme and pathway databases
BRENDA	2.4.1.41. 6170.
UniPathway	UPA00378.
Family and domain databases
InterPro	IPR001173. Glyco_trans_2. IPR000772. Ricin_B_lectin. [Graphical view]
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...

Entry information

Entry name

GALT1_PIG

Accession

Primary (citable) accession number: Q29121

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 27, 2001
Last sequence update:	November 1, 1996
Last modified:	April 3, 2013
This is version 99 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program