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Q14435 (GALT3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 129. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length633 AA.
Sequence statusComplete.
Protein existenceEvidence at protein 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. Probably glycosylates fibronectin in vivo. Glycosylates FGF23. Plays a central role in phosphate homeostasis. Ref.5 Ref.10

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. Note: Resides preferentially in the trans and medial parts of the Golgi stack. Ref.6

Tissue specificity

Expressed in organs that contain secretory epithelial glands. Highly expressed in pancreas, skin, kidney and testis. Weakly expressed in prostate, ovary, intestine and colon. Also expressed in placenta and lung and fetal lung and fetal kidney. Ref.1 Ref.7

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.

Involvement in disease

Tumoral calcinosis, hyperphosphatemic, familial (HFTC) [MIM:211900]: A severe metabolic disorder that manifests with hyperphosphatemia and massive calcium deposits in the skin and subcutaneous tissues. Some patients manifest recurrent, transient, painful swellings of the long bones associated with the radiographic findings of periosteal reaction and cortical hyperostosis and absence of skin involvement.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.8 Ref.9

Miscellaneous

Overexpressed in many differentiated carcinomas, suggesting that it may serve as a marker of tumor differentiation.

Sequence similarities

Belongs to the glycosyltransferase 2 family. GalNAc-T subfamily.

Contains 1 ricin B-type lectin domain.

Sequence caution

The sequence AAH56246.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Cellular componentGolgi apparatus
Membrane
   Coding sequence diversityAlternative splicing
   DomainSignal-anchor
Transmembrane
Transmembrane helix
   LigandLectin
Manganese
Metal-binding
   Molecular functionGlycosyltransferase
Transferase
   PTMDisulfide bond
Glycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processO-glycan processing

Traceable author statement. Source: Reactome

carbohydrate metabolic process

Non-traceable author statement PubMed 9592121. Source: ProtInc

cellular protein metabolic process

Traceable author statement. Source: Reactome

post-translational protein modification

Traceable author statement. Source: Reactome

protein O-linked glycosylation via serine

Inferred from direct assay Ref.5. Source: BHF-UCL

protein O-linked glycosylation via threonine

Inferred from direct assay Ref.10. Source: UniProtKB

   Cellular_componentGolgi cisterna membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

Golgi membrane

Traceable author statement. Source: Reactome

integral component of membrane

Traceable author statement Ref.1. Source: ProtInc

membrane

Traceable author statement Ref.1. Source: ProtInc

perinuclear region of cytoplasm

Inferred from direct assay PubMed 12506059. Source: BHF-UCL

   Molecular_functioncalcium ion binding

Inferred from direct assay Ref.5. Source: BHF-UCL

manganese ion binding

Inferred from direct assay Ref.5. Source: BHF-UCL

polypeptide N-acetylgalactosaminyltransferase activity

Inferred from direct assay Ref.5. Source: BHF-UCL

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q14435-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q14435-2)

The sequence of this isoform differs from the canonical sequence as follows:
     173-192: CIEQKFKRCPPLPTTSVIIV → YVEEYLLFILYHQALQGREG
     193-633: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 633633Polypeptide N-acetylgalactosaminyltransferase 3
PRO_0000059106

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

Glycosylation1321N-linked (GlcNAc...) Potential
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

Natural variations

Alternative sequence173 – 19220CIEQK…SVIIV → YVEEYLLFILYHQALQGREG in isoform 2.
VSP_011202
Alternative sequence193 – 633441Missing in isoform 2.
VSP_011203

Experimental info

Sequence conflict4811Q → R in CAA63371. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 14, 2008. Version 2.
Checksum: 3019B2DCCC19A584

FASTA63372,610
        10         20         30         40         50         60 
MAHLKRLVKL HIKRHYHKKF WKLGAVIFFF IIVLVLMQRE VSVQYSKEES RMERNMKNKN 

        70         80         90        100        110        120 
KMLDLMLEAV NNIKDAMPKM QIGAPVRQNI DAGERPCLQG YYTAAELKPV LDRPPQDSNA 

       130        140        150        160        170        180 
PGASGKAFKT TNLSVEEQKE KERGEAKHCF NAFASDRISL HRDLGPDTRP PECIEQKFKR 

       190        200        210        220        230        240 
CPPLPTTSVI IVFHNEAWST LLRTVHSVLY SSPAILLKEI ILVDDASVDE YLHDKLDEYV 

       250        260        270        280        290        300 
KQFSIVKIVR QRERKGLITA RLLGATVATA ETLTFLDAHC ECFYGWLEPL LARIAENYTA 

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

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

       430        440        450        460        470        480 
SPHSFPKGTQ VIARNQVRLA EVWMDEYKEI FYRRNTDAAK IVKQKAFGDL SKRFEIKHRL 

       490        500        510        520        530        540 
QCKNFTWYLN NIYPEVYVPD LNPVISGYIK SVGQPLCLDV GENNQGGKPL IMYTCHGLGG 

       550        560        570        580        590        600 
NQYFEYSAQH EIRHNIQKEL CLHAAQGLVQ LKACTYKGHK TVVTGEQIWE IQKDQLLYNP 

       610        620        630 
FLKMCLSANG EHPSLVSCNP SDPLQKWILS QND 

« Hide

Isoform 2 [UniParc].

Checksum: 2EEE40B4D6537601
Show »

FASTA19222,212

References

« Hide 'large scale' references
[1]"cDNA cloning and expression of a novel human UDP-N-acetyl-alpha-D-galactosamine polypeptide N-acetylgalactosaminyltransferase, GalNAc-T3."
Bennett E.P., Hassan H., Clausen H.
J. Biol. Chem. 271:17006-17012(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ENZYME ACTIVITY, TISSUE SPECIFICITY.
Tissue: Salivary gland.
[2]"Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. expand/collapse author list , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"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] (ISOFORMS 1 AND 2).
Tissue: Lung.
[5]"Substrate specificities of three members of the human UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase family, GalNAc-T1, -T2, and -T3."
Wandall H.H., Hassan H., Mirgorodskaya E., Kristensen A.K., Roepstorff P., Bennett E.P., Nielsen P.A., Hollingsworth M.A., Burchell J., Taylor-Papadimitriou J., Clausen H.
J. Biol. Chem. 272:23503-23514(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[6]"Localization of three human polypeptide GalNAc-transferases in HeLa cells suggests initiation of O-linked glycosylation throughout the Golgi apparatus."
Roettger S., White J., Wandall H.H., Olivo J.-C., Stark A., Bennett E.P., Whitehouse C., Berger E.G., Clausen H., Nilsson T.
J. Cell Sci. 111:45-60(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[7]"Prognostic significance of UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase-3 (GalNAc-T3) expression in patients with gastric carcinoma."
Onitsuka K., Shibao K., Nakayama Y., Minagawa N., Hirata K., Izumi H., Matsuo K., Nagata N., Kitazato K., Kohno K., Itoh H.
Cancer Sci. 94:32-36(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[8]"Mutations in GALNT3, encoding a protein involved in O-linked glycosylation, cause familial tumoral calcinosis."
Topaz O., Shurman D.L., Bergman R., Indelman M., Ratajczak P., Mizrachi M., Khamaysi Z., Behar D., Petronius D., Friedman V., Zelikovic I., Raimer S., Metzker A., Richard G., Sprecher E.
Nat. Genet. 36:579-581(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN HFTC.
[9]"Identification of a recurrent mutation in GALNT3 demonstrates that hyperostosis-hyperphosphatemia syndrome and familial tumoral calcinosis are allelic disorders."
Frishberg Y., Topaz O., Bergman R., Behar D., Fisher D., Gordon D., Richard G., Sprecher E.
J. Mol. Med. 83:33-38(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN HFTC.
[10]"Polypeptide GalNAc-transferase T3 and familial tumoral calcinosis. Secretion of fibroblast growth factor 23 requires O-glycosylation."
Kato K., Jeanneau C., Tarp M.A., Benet-Pages A., Lorenz-Depiereux B., Bennett E.P., Mandel U., Strom T.M., Clausen H.
J. Biol. Chem. 281:18370-18377(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[11]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Web resources

GGDB

GlycoGene database

Functional Glycomics Gateway - GTase

Polypeptide N-acetylgalactosaminyltransferase 3

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X92689 mRNA. Translation: CAA63371.1.
AC009495 Genomic DNA. Translation: AAY14678.1.
CH471058 Genomic DNA. Translation: EAX11324.1.
BC056246 mRNA. Translation: AAH56246.1. Different initiation.
BC113565 mRNA. Translation: AAI13566.1.
BC113567 mRNA. Translation: AAI13568.1.
RefSeqNP_004473.2. NM_004482.3.
XP_005246506.1. XM_005246449.1.
UniGeneHs.170986.

3D structure databases

ProteinModelPortalQ14435.
SMRQ14435. Positions 122-633.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9606.ENSP00000376465.

Protein family/group databases

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

PTM databases

PhosphoSiteQ14435.

Polymorphism databases

DMDM209572629.

Proteomic databases

PaxDbQ14435.
PRIDEQ14435.

Protocols and materials databases

DNASU2591.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000392701; ENSP00000376465; ENSG00000115339. [Q14435-1]
GeneID2591.
KEGGhsa:2591.
UCSCuc002udi.2. human. [Q14435-2]
uc010fph.1. human. [Q14435-1]

Organism-specific databases

CTD2591.
GeneCardsGC02M166567.
H-InvDBHIX0024214.
HGNCHGNC:4125. GALNT3.
HPAHPA007613.
MIM211900. phenotype.
601756. gene.
neXtProtNX_Q14435.
Orphanet306661. Hypercalcemic tumoral calcinosis.
PharmGKBPA28538.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG239675.
HOGENOMHOG000038227.
HOVERGENHBG051699.
InParanoidQ14435.
KOK00710.
OMAQYFEYSA.
OrthoDBEOG7J9VP2.
PhylomeDBQ14435.
TreeFamTF313267.

Enzyme and pathway databases

BRENDA2.4.1.41. 2681.
ReactomeREACT_17015. Metabolism of proteins.
UniPathwayUPA00378.

Gene expression databases

ArrayExpressQ14435.
BgeeQ14435.
CleanExHS_GALNT3.
GenevestigatorQ14435.

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

ChiTaRSGALNT3. human.
GeneWikiGALNT3.
GenomeRNAi2591.
NextBio10249.
PROQ14435.
SOURCESearch...

Entry information

Entry nameGALT3_HUMAN
AccessionPrimary (citable) accession number: Q14435
Secondary accession number(s): Q53TG9, Q7Z476
Entry history
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: October 14, 2008
Last modified: April 16, 2014
This is version 129 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM