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P70419 (GALT3_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 116. 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 3

EC=2.4.1.41
Alternative name(s):
Polypeptide GalNAc transferase 3
Short name=GalNAc-T3
Short name=pp-GaNTase 3
Protein-UDP acetylgalactosaminyltransferase 3
UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 3
Gene names
Name:Galnt3
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length633 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 activity toward HIV envelope glycoprotein gp120, EA2, Muc2 and Muc5. Glycosylates FGF23 By similarity. Probably glycosylates fibronectin in vivo. May be involved in phosphate homeostasis.

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 apparatusGolgi stack membrane; Single-pass type II membrane protein By similarity. Note: Resides preferentially in the trans and medial parts of the Golgi stack By similarity.

Tissue specificity

Highly expressed in the reproductive tract, principally in the testis and uterus, and to a lesser degree in the cervix with only trace levels in the ovary. Also expressed at high level in sublingual gland, stomach and colon, with more moderate amounts present in the submandibular and parotid gland as well as the kidney. 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 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 annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 633633Polypeptide N-acetylgalactosaminyltransferase 3
PRO_0000059107

Regions

Topological domain1 – 1919Cytoplasmic Potential
Transmembrane20 – 3718Helical; Signal-anchor for type II membrane protein; Potential
Topological domain38 – 633596Lumenal Potential
Domain504 – 630127Ricin B-type lectin
Region184 – 293110Catalytic subdomain A
Region356 – 41863Catalytic subdomain B

Sites

Metal binding2771Manganese By similarity
Metal binding2791Manganese By similarity
Metal binding4151Manganese By similarity
Binding site2251Substrate By similarity
Binding site2541Substrate By similarity
Binding site3871Substrate By similarity
Binding site4181Substrate By similarity

Amino acid modifications

Glycosylation2971N-linked (GlcNAc...) Potential
Glycosylation4841N-linked (GlcNAc...) Potential
Disulfide bond173 ↔ 410 By similarity
Disulfide bond401 ↔ 482 By similarity
Disulfide bond517 ↔ 535 By similarity
Disulfide bond561 ↔ 574 By similarity
Disulfide bond605 ↔ 618 By similarity

Experimental info

Sequence conflict3241S → N in AAH43331. Ref.5
Sequence conflict6331D → E in AAB09579. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P70419 [UniParc].

Last modified July 27, 2011. Version 3.
Checksum: 8BEE7CDDBCF56428

FASTA63372,932
        10         20         30         40         50         60 
MAHLKRLVKL HIKRHYHRKF WKLGAVIFFF LVVLILMQRE VSVQYSKEES KMERNLKNKN 

        70         80         90        100        110        120 
KMLDFMLEAV NNIKDAMPKM QIGAPIKENI DVRERPCLQG YYTAAELKPV FDRPPQDSNA 

       130        140        150        160        170        180 
PGASGKPFKI THLSPEEQKE KERGETKHCF NAFASDRISL HRDLGPDTRP PECIEQKFKR 

       190        200        210        220        230        240 
CPPLPTTSVI IVFHNEAWST LLRTVHSVLY SSPAILLKEI ILVDDASVDD YLHEKLEEYI 

       250        260        270        280        290        300 
KQFSIVKIVR QQERKGLITA RLLGAAVATA ETLTFLDAHC ECFYGWLEPL LARIAENYTA 

       310        320        330        340        350        360 
VVSPDIASID LNTFEFNKPS PYGSNHNRGN FDWSLSFGWE SLPDHEKQRR KDETYPIKTP 

       370        380        390        400        410        420 
TFAGGLFSIS KKYFEHIGSY DEEMEIWGGE NIEMSFRVWQ CGGQLEIMPC SVVGHVFRSK 

       430        440        450        460        470        480 
SPHTFPKGTQ VIARNQVRLA EVWMDEYKEI FYRRNTDAAK IVKQKSFGDL SKRFEIKKRL 

       490        500        510        520        530        540 
QCKNFTWYLN TIYPEAYVPD LNPVISGYIK SVGQPLCLDV GENNQGGKPL ILYTCHGLGG 

       550        560        570        580        590        600 
NQYFEYSAQR EIRHNIQKEL CLHATQGVVQ LKACVYKGHR TIAPGEQIWE IRKDQLLYNP 

       610        620        630 
LFKMCLSSNG EHPNLVPCDA TDLLQKWIFS QND 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and expression of mouse UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase-T3."
Zara J., Hagen F.K., Ten Hagen K.G., Van Wuyckhuyse B.C., Tabak L.A.
Biochem. Biophys. Res. Commun. 228:38-44(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], ENZYME ACTIVITY, TISSUE SPECIFICITY.
Strain: CD-1.
Tissue: Testis.
[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: Muellerian duct.
[3]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[4]Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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: FVB/N.
Tissue: Mammary tumor.
+Additional computationally mapped references.

Web resources

Functional Glycomics Gateway - GTase

Polypeptide N-acetylgalactosaminyltransferase 3

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U70538 mRNA. Translation: AAB09579.1.
AK135489 mRNA. Translation: BAE22551.1.
AL929230, AL928586 Genomic DNA. Translation: CAM20333.1.
AL928586, AL929230 Genomic DNA. Translation: CAM21878.1.
CH466519 Genomic DNA. Translation: EDL27008.1.
BC043331 mRNA. Translation: AAH43331.1.
CCDSCCDS16075.1.
PIRJC5247.
RefSeqNP_056551.2. NM_015736.2.
UniGeneMm.439760.

3D structure databases

ProteinModelPortalP70419.
SMRP70419. Positions 122-633.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP70419. 1 interaction.
MINTMINT-4095534.
STRING10090.ENSMUSP00000028378.

Protein family/group databases

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

PTM databases

PhosphoSiteP70419.

Proteomic databases

MaxQBP70419.
PaxDbP70419.
PRIDEP70419.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000028378; ENSMUSP00000028378; ENSMUSG00000026994.
GeneID14425.
KEGGmmu:14425.
UCSCuc008jwu.2. mouse.

Organism-specific databases

CTD2591.
MGIMGI:894695. Galnt3.

Phylogenomic databases

eggNOGNOG239675.
GeneTreeENSGT00750000117451.
HOGENOMHOG000038227.
HOVERGENHBG051699.
InParanoidQ3UXL2.
KOK00710.
OMAQYFEYSA.
OrthoDBEOG7J9VP2.
TreeFamTF313267.

Enzyme and pathway databases

BRENDA2.4.1.41. 3474.
UniPathwayUPA00378.

Gene expression databases

BgeeP70419.
GenevestigatorP70419.

Family and domain databases

Gene3D3.90.550.10. 1 hit.
InterProIPR001173. Glyco_trans_2-like.
IPR029044. Nucleotide-diphossugar_trans.
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.
SSF53448. SSF53448. 1 hit.
PROSITEPS50231. RICIN_B_LECTIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSGALNT3. mouse.
NextBio286025.
PROP70419.
SOURCESearch...

Entry information

Entry nameGALT3_MOUSE
AccessionPrimary (citable) accession number: P70419
Secondary accession number(s): Q3UXL2, Q80V55
Entry history
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: July 27, 2011
Last modified: July 9, 2014
This is version 116 of the entry and version 3 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