Q8SPR2 (GGTA1_CEBAP) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
N-acetyllactosaminide alpha-1,3-galactosyltransferase
EC=2.4.1.87

Alternative name(s):
UDP-galactose:beta-D-galactosyl-1,4-N-acetyl-D-glucosaminide alpha-1,3-galactosyltransferase
Short name=Galactosyltransferase

Gene names

Name:

GGTA1

Organism

Cebus apella (Brown-capped capuchin)

Taxonomic identifier

9515 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Platyrrhini › Cebidae › Cebinae › Cebus

Protein attributes

Sequence length	375 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Transfer of galactose from UDP-galactose to an acceptor molecule (R).
Catalytic activity	UDP-galactose + beta-D-galactosyl-(1->4)-beta-N-acetyl-D-glucosaminyl-R = UDP + alpha-D-galactosyl-(1->3)-beta-D-galactosyl-(1->4)-beta-N-acetylglucosaminyl-R.
Cofactor	Manganese By similarity.
Pathway	Protein modification; protein glycosylation.
Subcellular location	Golgi apparatus › Golgi stack membrane; Single-pass type II membrane protein By similarity. Note: Membrane-bound form in trans cisternae of Golgi By similarity.
Domain	The conserved DXD motif is involved in cofactor binding. The manganese ion interacts with the beta-phosphate group of UDP and may also have a role in catalysis By similarity.
Sequence similarities	Belongs to the glycosyltransferase 6 family.

Ontologies

Keywords
Cellular component	Golgi apparatus Membrane
Domain	Signal-anchor Transmembrane Transmembrane helix
Ligand	Manganese Metal-binding
Molecular function	Glycosyltransferase Transferase
PTM	Glycoprotein
Gene Ontology (GO)
Biological process	carbohydrate metabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	Golgi cisterna membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	N-acetyllactosaminide 3-alpha-galactosyltransferase activity Inferred from electronic annotation. Source: EC metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 375	375	N-acetyllactosaminide alpha-1,3-galactosyltransferase		PRO_0000333699
Regions
	Topological domain	1 – 6	6	Cytoplasmic Potential
	Transmembrane	7 – 27	21	Helical; Signal-anchor for type II membrane protein; Potential
	Topological domain	28 – 375	348	Lumenal Potential
Sites
	Metal binding	232	1	Manganese By similarity
	Metal binding	234	1	Manganese By similarity
Amino acid modifications
	Glycosylation	300	1	N-linked (GlcNAc...) Potential

Sequences

	Sequence		Length	Mass (Da)
	Q8SPR2 [UniParc]. Last modified June 1, 2002. Version 1. Checksum: 55F87A88F7059581	FASTA	375	44,392
	10 20 30 40 50 60 MNVKGKVILS MLVVSTVIVV FWEYINSPEG SFLWIYHSKN PEVDDSAQKG WWFPDWFNNG 70 80 90 100 110 120 IHNYQQEEED IDKEKGREEE QRKEDDTTEL QLWDWFNPKK RPEVVTVTKW KAPVVWEGTY 130 140 150 160 170 180 NKAILENYYA KQKITVGLTV FAIGRYIEHY LEEFVTSANR YFMVGHKVIF YVMVDDVSKV 190 200 210 220 230 240 PFIELGPLRS FKVFEVKPEK RWQDISMMRM KTIGEHILAH IQHEVDFLFC MDVDQVFQDH 250 260 270 280 290 300 FGVETLGQSV AQLQAWWYKA DPDDFTYERR RESAAYIPFG QGDFYYHAAV FGGTPIQVLN 310 320 330 340 350 360 ITQECFKGIL LDKKNDIEAE WHDESHLNKY FLLNKPSKIL SPEYCWDYHI GLPSDIKTVK 370 LSWQTKEYNL VRNNV

References

[1]	"Molecular basis of evolutionary loss of the alpha 1,3-galactosyltransferase gene in higher primates." Koike C., Fung J.J., Geller D.A., Kannagi R., Libert T., Luppi P., Nakashima I., Profozich J., Rudert W., Sharma S.B., Starzl T.E., Trucco M. J. Biol. Chem. 277:10114-10120(2002) [PubMed: 11773054] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AY034181 mRNA. Translation: AAK56499.1.
3D structure databases
HSSP	HSSP built from PDB template 1O7Q based on UniProtKB P14769.
ProteinModelPortal	Q8SPR2.
SMR	Q8SPR2. Positions 89-375.
ModBase	Search...
Protein family/group databases
CAZy	GT6. Glycosyltransferase Family 6.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Phylogenomic databases
HOVERGEN	HBG003563.
Family and domain databases
InterPro	IPR005076. Glyco_trans_6. [Graphical view]
PANTHER	PTHR10462. Glyco_trans_6. 1 hit.
Pfam	PF03414. Glyco_transf_6. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

GGTA1_CEBAP

Accession

Primary (citable) accession number: Q8SPR2

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 20, 2008
Last sequence update:	June 1, 2002
Last modified:	January 11, 2011
This is version 33 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program