Reviewed, UniProtKB/Swiss-Prot Q8C7U7 (GALT6_MOUSE)

Names and origin

Protein names

Recommended name:
    Polypeptide N-acetylgalactosaminyltransferase 6
    EC=2.4.1.41
Alternative name(s):
    Polypeptide GalNAc transferase 6
      Short name=pp-GaNTase 6
      Short name=GalNAc-T6
    Protein-UDP acetylgalactosaminyltransferase 6
    UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 6

Gene names

Name:

Galnt6

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	622 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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. May participate in synthesis of oncofetal fibronectin. Has activity toward Muc1a, Muc2, EA2 and fibronectin peptides By similarity.
Catalytic activity	UDP-N-acetyl-D-galactosamine + polypeptide = UDP + N-acetyl-D-galactosaminyl-polypeptide.
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.
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.
Sequence caution	The sequence CAB55352.1 differs from that shown. Reason: Frameshift at position 622.

Ontologies

Keywords
Cellular component	Golgi apparatus Membrane
Domain	Signal-anchor Transmembrane
Ligand	Calcium Lectin Manganese
Molecular function	Glycosyltransferase Transferase
PTM	Disulfide bond Glycoprotein
Gene Ontology (GO)
Cellular component	Golgi apparatus Inferred from electronic annotation. Source: UniProtKB-KW integral to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	calcium ion binding Inferred from electronic annotation. Source: UniProtKB-KW manganese ion binding Inferred from electronic annotation. Source: UniProtKB-KW polypeptide N-acetylgalactosaminyltransferase activity Ref.1 Inferred from direct assay. Source: MGI sugar 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 – 622	622	Polypeptide N-acetylgalactosaminyltransferase 6		PRO_0000059115
Regions
	Topological domain	1 – 8	8	Cytoplasmic Potential
	Transmembrane	9 – 28	20	Signal-anchor for type II membrane protein Potential
	Topological domain	29 – 622	594	Lumenal Potential
	Domain	496 – 622	127	Ricin B-type lectin
	Region	176 – 285	110	Catalytic subdomain A
	Region	348 – 410	63	Catalytic subdomain B
Amino acid modifications
	Glycosylation	86	1	N-linked (GlcNAc...) Potential
	Glycosylation	476	1	N-linked (GlcNAc...) Potential
	Disulfide bond	509 ↔ 527		By similarity
	Disulfide bond	553 ↔ 566		By similarity
	Disulfide bond	597 ↔ 610		By similarity
Experimental info
	Sequence conflict	14	1	A → T in CAB55352. Ref.1
	Sequence conflict	100	1	K → R in CAB55352. Ref.1
	Sequence conflict	210	1	K → N in BAC25984. Ref.2
	Sequence conflict	215	1	V → M in BAC25984. Ref.2
	Sequence conflict	247	1	K → G in BAC25984. Ref.2
	Sequence conflict	263 – 275	13	EVLTF…HCECF → KGAHVSWTPTVSVS Ref.1
	Sequence conflict	292	1	A → P in CAB55352. Ref.1
	Sequence conflict	336	1	E → Q in CAB55352. Ref.1
	Sequence conflict	398	1	E → G in BAC25984. Ref.2
	Sequence conflict	467	1	R → Q in CAB55352. Ref.1
	Sequence conflict	562	1	G → S in CAB55352. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q8C7U7-1 [UniParc]. Last modified March 1, 2003. Version 1. Checksum: 6DBCA3A2CCFDBDAA	FASTA	622	71,537
	10 20 30 40 50 60 MRLLRRRHMS LRLAMLGSVF MLFLFIRQKD VSNQEQAMEK PWLKSLAGQK DQVLDFMLGA 70 80 90 100 110 120 VNNIRDVMPK LQIRAPEPPQ TLVSTNHSCL PGFYTPAELK PFWDRPPQDP NSPGADGKAF 130 140 150 160 170 180 QKKEWTNLET KEKEEGYKKH CFNAFASDRI SLQRSLGPDT RPPECVDQKF RRCPPLPTTS 190 200 210 220 230 240 VIIVFHNEAW STLLRTVYSV LHTSPAILLK EIILVDDAST DEHLKERLEQ YVQQLQIVRV 250 260 270 280 290 300 VRQRERKGLI TARLLGASVA QAEVLTFLDA HCECFHGWLE PLLARIAEDK TAVVSPDIVT 310 320 330 340 350 360 IDLNTFQFSR PVQRGKAHSR GNFDWSLTFG WEMLPEHEKQ RRKDETYPIK SPTFAGGLFS 370 380 390 400 410 420 ISKAYFEHIG TYDNQMEIWG GENVEMSFRV WQCGGQLEII PCSVVGHVFR TKSPHTFPKG 430 440 450 460 470 480 TSVIARNQVR LAEVWMDDYK KIFYRRNLQA AKMVQENNFG DISERLRLRE QLRCHNFSWY 490 500 510 520 530 540 LHNVYPEMFV PDLNPTFYGA IKNLGTNQCL DVGENNRGGK PLIMYVCHNL GGNQYFEYTS 550 560 570 580 590 600 QRDLRHNIGK QLCLHASGST LGLRSCQFVG KNSRVPKDEE WELTQDQLIR NSGSGTCLTS 610 620 QDKKPAMAPC NPRDPYQLWL FV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and characterization of a close homologue of human UDP-N-acetyl--D-galactosamine:polypeptide N-acetylgalactosaminyltransferase-T3, designated GalNAc-T6. Evidence for genetic but not functional redundancy." Bennett E.P., Hassan H., Mandel U., Hollingsworth M.A., Akisawa N., Ikematsu Y., Merkx G., Geurts van Kessel A., Olofsson S., Clausen H. J. Biol. Chem. 274:25362-25370(1999) [PubMed: 10464263] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Gastric carcinoma.
[2]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J and NOD. Tissue: Skin.
[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]. Tissue: Brain.
+	Additional computationally mapped references.

Web resources

Functional Glycomics Gateway - GTase

Polypeptide N-acetylgalactosaminyltransferase 6

Cross-references

Sequence databases
EMBLGenBankDDBJ	AJ133523 mRNA. Translation: CAB55352.1. Frameshift. AK028506 mRNA. Translation: BAC25984.1. AK049222 mRNA. Translation: BAC33618.1. AK155008 mRNA. Translation: BAE32989.1. AK159721 mRNA. Translation: BAE35316.1. BC119324 mRNA. Translation: AAI19325.1. BC119326 mRNA. Translation: AAI19327.1.
IPI	IPI00313003.
RefSeq	NP_001155239.1. NP_001155240.1. NP_766039.2.
UniGene	Mm.22969
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q8C7U7.
Protein family/group databases
CAZy	CBM13. Carbohydrate-Binding Module Family 13. GT27. Glycosyltransferase Family 27.
Proteomic databases
PRIDE	Q8C7U7.
Genome annotation databases
Ensembl	ENSMUST00000052069; ENSMUSP00000056705; ENSMUSG00000037280; Mus musculus. [Genome view]
GeneID	207839.
KEGG	mmu:207839.
UCSC	uc007xrz.1. mouse.
Organism-specific databases
CTD	207839.
MGI	MGI:1891640. Galnt6.
Phylogenomic databases
HOGENOM	Q8C7U7.
HOVERGEN	Q8C7U7.
OMA	QDQLIRN.
Enzyme and pathway databases
BRENDA	2.4.1.41. 244.
Gene expression databases
ArrayExpress	Q8C7U7.
Bgee	Q8C7U7.
Genevestigator	Q8C7U7.
GermOnline	ENSMUSG00000037280. Mus musculus.
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]
PROSITE	PS50231. RICIN_B_LECTIN. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	372071.
SOURCE	Search...

Entry information

Entry name

GALT6_MOUSE

Accession

Primary (citable) accession number: Q8C7U7
Secondary accession number(s): Q0VE84 , Q3TWF0, Q8CED2, Q9QZ16

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 16, 2004
Last sequence update:	March 1, 2003
Last modified:	November 3, 2009
This is version 61 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)