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O08832 (GALT4_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 102. 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 4

EC=2.4.1.41
Alternative name(s):
Polypeptide GalNAc transferase 4
Short name=GalNAc-T4
Short name=pp-GaNTase 4
Protein-UDP acetylgalactosaminyltransferase 4
UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 4
Gene names
Name:Galnt4
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length578 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. Has a highest activity toward EA2 peptide substrate and a much lower activity with EPO-T, Muc2, Muc1a, Muc1b.

Catalytic activity

UDP-N-acetyl-alpha-D-galactosamine + polypeptide = UDP + N-acetyl-alpha-D-galactosaminyl-polypeptide. Ref.1

Cofactor

Manganese By similarity.

Pathway

Protein modification; protein glycosylation.

Subcellular location

Golgi apparatus membrane; Single-pass type II membrane protein By similarity.

Tissue specificity

Highly expressed in sublingual gland, stomach, colon, small intestine and cervix. Expressed at intermediate levels in kidney, ovary, lung and uterus. Weakly expressed in spleen, liver, heart and brain. Not expressed in submandibular and parotid glands, skeletal muscle and testis. Ref.1

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 578578Polypeptide N-acetylgalactosaminyltransferase 4
PRO_0000059109

Regions

Topological domain1 – 1212Cytoplasmic Potential
Transmembrane13 – 3523Helical; Signal-anchor for type II membrane protein; Potential
Topological domain36 – 578543Lumenal Potential
Domain444 – 577134Ricin B-type lectin
Region134 – 243110Catalytic subdomain A
Region303 – 36563Catalytic subdomain B

Sites

Metal binding2271Manganese By similarity
Metal binding2291Manganese By similarity
Metal binding3621Manganese By similarity
Binding site1751Substrate By similarity
Binding site2041Substrate By similarity
Binding site3341Substrate By similarity
Binding site3701Substrate By similarity

Amino acid modifications

Glycosylation4711N-linked (GlcNAc...) Potential
Disulfide bond124 ↔ 357 By similarity
Disulfide bond348 ↔ 421 By similarity
Disulfide bond457 ↔ 477 By similarity
Disulfide bond503 ↔ 518 By similarity
Disulfide bond547 ↔ 565 By similarity

Sequences

Sequence LengthMass (Da)Tools
O08832 [UniParc].

Last modified July 1, 1997. Version 1.
Checksum: 10ADC0D8B8B30835

FASTA57866,555
        10         20         30         40         50         60 
MAVRWTWAGK SCLLLALLTL AYILVEFSVS TLYASPGAGG ARELGPRRLP DLDTREEDLS 

        70         80         90        100        110        120 
QPLYIKPPAD SHALGEWGRA SKLQLNEGEL KQQEELIERY AINIYLSDRI SLHRHIEDKR 

       130        140        150        160        170        180 
MYECKAKKFH YRSLPTTSVI IAFYNEAWST LLRTIHSVLE TSPAVLLKEI ILVDDLSDRI 

       190        200        210        220        230        240 
YLKAQLETYI SNLERVRLIR TNKREGLVRA RLIGATFATG DVLTFLDCHC ECNTGWLEPL 

       250        260        270        280        290        300 
LERISRDETA IVCPVIDTID WNTFEFYMQT GEPMIGGFDW RLTFQWHSVP KHERDRRTSR 

       310        320        330        340        350        360 
IDPIRSPTMA GGLFAVSKKY FQYLGTYDTG MEVWGGENLE LSFRVWQCGG KLEIHPCSHV 

       370        380        390        400        410        420 
GHVFPKRAPY ARPNFLQNTA RAAEVWMDEY KEHFYNRNPP ARKEAYGDLS ERKLLRERLK 

       430        440        450        460        470        480 
CKSFDWYLKN VFSNLHVPED RPGWHGAIRS MGISSECLDY NAPDNNPTGA NLSLFGCHGQ 

       490        500        510        520        530        540 
GGNQFFEYTS NKEIRFNSVT ELCAEVPQQK DYVGMQNCPK DGLPVPVNII WHFKEDGTIF 

       550        560        570 
HPHTRLCLSA YRTAEGRPSV HMKTCDALDK NQLWRFEK 

« Hide

References

« Hide 'large scale' references
[1]"cDNA cloning and expression of a novel UDP-N-acetyl-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase."
Hagen F.K., Ten Hagen K.G., Beres T.M., Balys M.M., VanWuyckhuyse B.C., Tabak L.A.
J. Biol. Chem. 272:13843-13848(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], ENZYME ACTIVITY, TISSUE SPECIFICITY.
Tissue: Spleen.
[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.
Tissue: Bone marrow and Colon.
[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].
Strain: NMRI.
Tissue: Mammary tumor.
+Additional computationally mapped references.

Web resources

Functional Glycomics Gateway - GTase

Polypeptide N-acetylgalactosaminyltransferase 4

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U73819 mRNA. Translation: AAB58301.1.
AK033494 mRNA. Translation: BAC28317.1.
AK148036 mRNA. Translation: BAE28303.1.
AK153253 mRNA. Translation: BAE31844.1.
BC057882 mRNA. Translation: AAH57882.1.
RefSeqNP_056552.1. NM_015737.4.
UniGeneMm.314.

3D structure databases

ProteinModelPortalO08832.
SMRO08832. Positions 75-577.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

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

PTM databases

PhosphoSiteO08832.

Proteomic databases

PRIDEO08832.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000161240; ENSMUSP00000125315; ENSMUSG00000090035.
GeneID14426.
KEGGmmu:14426.
UCSCuc007gxj.2. mouse.

Organism-specific databases

CTD8693.
MGIMGI:894692. Galnt4.

Phylogenomic databases

GeneTreeENSGT00750000117451.
HOGENOMHOG000038227.
HOVERGENHBG051699.
KOK00710.
OMANTFEFYM.
OrthoDBEOG7J9VP2.
PhylomeDBO08832.
TreeFamTF352660.

Enzyme and pathway databases

UniPathwayUPA00378.

Gene expression databases

BgeeO08832.
GenevestigatorO08832.

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

NextBio286029.
PROO08832.
SOURCESearch...

Entry information

Entry nameGALT4_MOUSE
AccessionPrimary (citable) accession number: O08832
Secondary accession number(s): Q3U681
Entry history
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: July 1, 1997
Last modified: April 16, 2014
This is version 102 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