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Q8C7U7 (GALT6_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 101. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Polypeptide N-acetylgalactosaminyltransferase 6

EC=2.4.1.41
Alternative name(s):
Polypeptide GalNAc transferase 6
Short name=GalNAc-T6
Short name=pp-GaNTase 6
Protein-UDP acetylgalactosaminyltransferase 6
UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 6
Gene names
Name:Galnt6
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length622 AA.
Sequence statusComplete.
Protein existenceEvidence 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-alpha-D-galactosamine + polypeptide = UDP + N-acetyl-alpha-D-galactosaminyl-polypeptide.

Cofactor

Manganese 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 622622Polypeptide N-acetylgalactosaminyltransferase 6
PRO_0000059115

Regions

Topological domain1 – 88Cytoplasmic Potential
Transmembrane9 – 2820Helical; Signal-anchor for type II membrane protein; Potential
Topological domain29 – 622594Lumenal Potential
Domain496 – 622127Ricin B-type lectin
Region176 – 285110Catalytic subdomain A
Region348 – 41063Catalytic subdomain B

Sites

Metal binding2691Manganese By similarity
Metal binding2711Manganese By similarity
Metal binding4071Manganese By similarity
Binding site2171Substrate By similarity
Binding site2461Substrate By similarity
Binding site3791Substrate By similarity
Binding site4101Substrate By similarity

Amino acid modifications

Glycosylation861N-linked (GlcNAc...) Potential
Glycosylation4761N-linked (GlcNAc...) Potential
Disulfide bond165 ↔ 402 By similarity
Disulfide bond393 ↔ 474 By similarity
Disulfide bond509 ↔ 527 By similarity
Disulfide bond553 ↔ 566 By similarity
Disulfide bond597 ↔ 610 By similarity

Experimental info

Sequence conflict141A → T in CAB55352. Ref.1
Sequence conflict1001K → R in CAB55352. Ref.1
Sequence conflict2101K → N in BAC25984. Ref.2
Sequence conflict2151V → M in BAC25984. Ref.2
Sequence conflict2471K → G in BAC25984. Ref.2
Sequence conflict263 – 27513EVLTF…HCECF → KGAHVSWTPTVSVS Ref.1
Sequence conflict2921A → P in CAB55352. Ref.1
Sequence conflict3361E → Q in CAB55352. Ref.1
Sequence conflict3981E → G in BAC25984. Ref.2
Sequence conflict4671R → Q in CAB55352. Ref.1
Sequence conflict5621G → S in CAB55352. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q8C7U7 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: 6DBCA3A2CCFDBDAA

FASTA62271,537
        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 

« Hide

References

« Hide '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] [Europe PMC] [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. expand/collapse author list , 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] [Europe PMC] [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] [Europe PMC] [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

EMBL
GenBank
DDBJ
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.
RefSeqNP_001155239.1. NM_001161767.1.
NP_001155240.1. NM_001161768.1.
NP_766039.2. NM_172451.3.
UniGeneMm.22969.

3D structure databases

ProteinModelPortalQ8C7U7.
SMRQ8C7U7. Positions 117-622.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000056705.

Protein family/group databases

CAZyCBM13. Carbohydrate-Binding Module Family 13.
GT27. Glycosyltransferase Family 27.

PTM databases

PhosphoSiteQ8C7U7.

Proteomic databases

PaxDbQ8C7U7.
PRIDEQ8C7U7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000052069; ENSMUSP00000056705; ENSMUSG00000037280.
ENSMUST00000159715; ENSMUSP00000123848; ENSMUSG00000037280.
ENSMUST00000161514; ENSMUSP00000124793; ENSMUSG00000037280.
GeneID207839.
KEGGmmu:207839.
UCSCuc007xrz.2. mouse.

Organism-specific databases

CTD11226.
MGIMGI:1891640. Galnt6.

Phylogenomic databases

eggNOGNOG239675.
GeneTreeENSGT00750000117451.
HOGENOMHOG000038227.
HOVERGENHBG051699.
InParanoidQ0VE84.
KOK00710.
OMANQCLDVG.
OrthoDBEOG7J9VP2.
PhylomeDBQ8C7U7.
TreeFamTF313267.

Enzyme and pathway databases

UniPathwayUPA00378.

Gene expression databases

BgeeQ8C7U7.
GenevestigatorQ8C7U7.

Family and domain databases

InterProIPR001173. Glyco_trans_2-like.
IPR000772. Ricin_B_lectin.
[Graphical view]
PfamPF00535. Glycos_transf_2. 1 hit.
PF00652. Ricin_B_lectin. 1 hit.
[Graphical view]
SMARTSM00458. RICIN. 1 hit.
[Graphical view]
SUPFAMSSF50370. SSF50370. 1 hit.
PROSITEPS50231. RICIN_B_LECTIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio372071.
PROQ8C7U7.
SOURCESearch...

Entry information

Entry nameGALT6_MOUSE
AccessionPrimary (citable) accession number: Q8C7U7
Secondary accession number(s): Q0VE84 expand/collapse secondary AC list , Q3TWF0, Q8CED2, Q9QZ16
Entry history
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: March 1, 2003
Last modified: April 16, 2014
This is version 101 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot