Q95158 (GBGT1_CANFA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Globoside alpha-1,3-N-acetylgalactosaminyltransferase 1
EC=2.4.1.88

Alternative name(s):
Forssman glycolipid synthase
pFS-7

Gene names

Name:	GBGT1
Synonyms:	FS

Organism

Canis familiaris (Dog) (Canis lupus familiaris) [Reference proteome]

Taxonomic identifier

9615 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Laurasiatheria › Carnivora › Caniformia › Canidae › Canis › Canis lupus

Protein attributes

Sequence length	347 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Catalyzes the formation of Forssman glycolipid via the addition of N-acetylgalactosamine (GalNAc) in alpha-1,3-linkage to GalNAcb-1,3Gala-1,4Galb-1,4GlcCer (Gb4Cer). Forssman glycolipid (also called Forssman antigen; FG) probably serves for adherence of some pathogens such as E.coli uropathogenic strains.
Catalytic activity	UDP-N-acetyl-alpha-D-galactosamine + N-acetyl-D-galactosaminyl-(1->3)-D-galactosyl-(1->4)-D-galactosyl-(1->4)-D-glucosyl-(1<->1)-ceramide = UDP + N-acetyl-D-galactosaminyl-(1->3)-N-acetyl-D-galactosaminyl-(1->3)-D-galactosyl-(1->4)-D-galactosyl-(1->4)-D-glucosyl-(1<->1)-ceramide. Ref.1
Cofactor	Manganese By similarity.
Pathway	Protein modification; protein glycosylation.
Subcellular location	Golgi apparatus membrane; Single-pass type II membrane protein 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
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	protein glycosylation Inferred from electronic annotation. Source: UniProtKB-UniPathway
Cellular_component	Golgi membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	globoside alpha-N-acetylgalactosaminyltransferase 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 – 347	347	Globoside alpha-1,3-N-acetylgalactosaminyltransferase 1		PRO_0000157294
Regions
	Topological domain	1 – 5	5	Cytoplasmic Potential
	Transmembrane	6 – 26	21	Helical; Signal-anchor for type II membrane protein; Potential
	Topological domain	27 – 347	321	Lumenal Potential
Amino acid modifications
	Glycosylation	108	1	N-linked (GlcNAc...) Potential

Sequences

	Sequence		Length	Mass (Da)
	Q95158 [UniParc]. Last modified February 1, 1997. Version 1. Checksum: 66E6119CCD766739	FASTA	347	40,265
	10 20 30 40 50 60 MRCRRLALGL GFSLLSGIAL WSLWIYMETW LPFSYVPYYL PCPEIFNMKL QYKGEKPFQP 70 80 90 100 110 120 VTRSPHPQPK LLEQRPTELL TLTPWLAPIV SEGTFNPELL QHIYQPLNLT IGLTVFAVGK 130 140 150 160 170 180 YTRFVQHFLE SAEQFFMQGY QVYYYIFTND PAGIPRVPLG PGRLLSIIPI QRHSRWEEIS 190 200 210 220 230 240 TRRMETISRH IAQRAHREVD YLFCVDVDMV FRNPWGPETL GDLVAAIHPG YYAVPRQQFP 250 260 270 280 290 300 YERRHISTAF VAENEGDFYY GGAVFGGRVA KVYEFTTGCH MAILADKANG IMAAWQEESH 310 320 330 340 LNRRFISHKP SKVLSPEYLW DDRKPQPPSL KLIRFSTLDK ATSWLRS

References

[1]	"Expression cloning of Forssman glycolipid synthetase: a novel member of the histo-blood group ABO gene family." Haslam D.B., Baenziger J.U. Proc. Natl. Acad. Sci. U.S.A. 93:10697-10702(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], ENZYME ACTIVITY. Tissue: Kidney.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U66140 mRNA. Translation: AAC48667.1.
PIR	JC6126.
RefSeq	NP_001003193.1. NM_001003193.1.
UniGene	Cfa.3696.
3D structure databases
ProteinModelPortal	Q95158.
ModBase	Search...
Protein-protein interaction databases
STRING	9615.ENSCAFP00000029424.
Protein family/group databases
CAZy	GT6. Glycosyltransferase Family 6.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	403833.
KEGG	cfa:403833.
Organism-specific databases
CTD	26301.
Phylogenomic databases
eggNOG	NOG43612.
HOGENOM	HOG000234339.
HOVERGEN	HBG003563.
InParanoid	Q95158.
KO	K00722.
OrthoDB	EOG4D26Q7.
Enzyme and pathway databases
BRENDA	2.4.1.88. 1154.
UniPathway	UPA00378.
Family and domain databases
InterPro	IPR005076. Glyco_trans_6. [Graphical view]
PANTHER	PTHR10462. PTHR10462. 1 hit.
Pfam	PF03414. Glyco_transf_6. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	20817329.

Entry information

Entry name

GBGT1_CANFA

Accession

Primary (citable) accession number: Q95158

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 10, 2005
Last sequence update:	February 1, 1997
Last modified:	April 3, 2013
This is version 74 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program