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Polypeptide N-acetylgalactosaminyltransferase 3 (EC 2.4.1.41) (Polypeptide GalNAc transferase 3) (GalNAc-T3) (pp-GaNTase 3) (Protein-UDP acetylgalactosaminyltransferase 3) (UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 3)

 GALT3_HUMAN             Reviewed;         633 AA.
Q14435; Q53TG9; Q7Z476;
16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
14-OCT-2008, sequence version 2.
22-NOV-2017, entry version 161.
RecName: Full=Polypeptide N-acetylgalactosaminyltransferase 3;
EC=2.4.1.41;
AltName: Full=Polypeptide GalNAc transferase 3;
Short=GalNAc-T3;
Short=pp-GaNTase 3;
AltName: Full=Protein-UDP acetylgalactosaminyltransferase 3;
AltName: Full=UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 3;
Name=GALNT3;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ENZYME ACTIVITY, AND TISSUE
SPECIFICITY.
TISSUE=Salivary gland;
PubMed=8663203; DOI=10.1074/jbc.271.29.17006;
Bennett E.P., Hassan H., Clausen H.;
"cDNA cloning and expression of a novel human UDP-N-acetyl-alpha-D-
galactosamine polypeptide N-acetylgalactosaminyltransferase, GalNAc-
T3.";
J. Biol. Chem. 271:17006-17012(1996).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
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., 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.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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., 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.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Lung;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
FUNCTION.
PubMed=9295285; DOI=10.1074/jbc.272.38.23503;
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.;
"Substrate specificities of three members of the human UDP-N-acetyl-
alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase
family, GalNAc-T1, -T2, and -T3.";
J. Biol. Chem. 272:23503-23514(1997).
[6]
SUBCELLULAR LOCATION.
PubMed=9394011;
Roettger S., White J., Wandall H.H., Olivo J.-C., Stark A.,
Bennett E.P., Whitehouse C., Berger E.G., Clausen H., Nilsson T.;
"Localization of three human polypeptide GalNAc-transferases in HeLa
cells suggests initiation of O-linked glycosylation throughout the
Golgi apparatus.";
J. Cell Sci. 111:45-60(1998).
[7]
TISSUE SPECIFICITY.
PubMed=12708471; DOI=10.1111/j.1349-7006.2003.tb01348.x;
Onitsuka K., Shibao K., Nakayama Y., Minagawa N., Hirata K., Izumi H.,
Matsuo K., Nagata N., Kitazato K., Kohno K., Itoh H.;
"Prognostic significance of UDP-N-acetyl-alpha-D-
galactosamine:polypeptide N-acetylgalactosaminyltransferase-3 (GalNAc-
T3) expression in patients with gastric carcinoma.";
Cancer Sci. 94:32-36(2003).
[8]
INVOLVEMENT IN HFTC.
PubMed=15133511; DOI=10.1038/ng1358;
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.;
"Mutations in GALNT3, encoding a protein involved in O-linked
glycosylation, cause familial tumoral calcinosis.";
Nat. Genet. 36:579-581(2004).
[9]
INVOLVEMENT IN HFTC.
PubMed=15599692; DOI=10.1007/s00109-004-0610-8;
Frishberg Y., Topaz O., Bergman R., Behar D., Fisher D., Gordon D.,
Richard G., Sprecher E.;
"Identification of a recurrent mutation in GALNT3 demonstrates that
hyperostosis-hyperphosphatemia syndrome and familial tumoral
calcinosis are allelic disorders.";
J. Mol. Med. 83:33-38(2005).
[10]
FUNCTION.
PubMed=16638743; DOI=10.1074/jbc.M602469200;
Kato K., Jeanneau C., Tarp M.A., Benet-Pages A., Lorenz-Depiereux B.,
Bennett E.P., Mandel U., Strom T.M., Clausen H.;
"Polypeptide GalNAc-transferase T3 and familial tumoral calcinosis.
Secretion of fibroblast growth factor 23 requires O-glycosylation.";
J. Biol. Chem. 281:18370-18377(2006).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
-!- 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. {ECO:0000269|PubMed:16638743,
ECO:0000269|PubMed:9295285}.
-!- CATALYTIC ACTIVITY: UDP-N-acetyl-alpha-D-galactosamine +
polypeptide = UDP + N-acetyl-alpha-D-galactosaminyl-polypeptide.
{ECO:0000269|PubMed:8663203}.
-!- COFACTOR:
Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
-!- PATHWAY: Protein modification; protein glycosylation.
-!- INTERACTION:
Q92624:APPBP2; NbExp=3; IntAct=EBI-10232904, EBI-743771;
-!- SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane
{ECO:0000269|PubMed:9394011}; Single-pass type II membrane protein
{ECO:0000269|PubMed:9394011}. Note=Resides preferentially in the
trans and medial parts of the Golgi stack.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q14435-1; Sequence=Displayed;
Name=2;
IsoId=Q14435-2; Sequence=VSP_011202, VSP_011203;
Note=No experimental confirmation available.;
-!- 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. {ECO:0000269|PubMed:12708471, ECO:0000269|PubMed:8663203}.
-!- 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. {ECO:0000250}.
-!- DOMAIN: The ricin B-type lectin domain binds to GalNAc and
contributes to the glycopeptide specificity. {ECO:0000250}.
-!- 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.
{ECO:0000269|PubMed:15133511, ECO:0000269|PubMed:15599692}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- MISCELLANEOUS: Overexpressed in many differentiated carcinomas,
suggesting that it may serve as a marker of tumor differentiation.
-!- SIMILARITY: Belongs to the glycosyltransferase 2 family. GalNAc-T
subfamily. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAH56246.1; Type=Erroneous initiation; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase;
Note=Polypeptide N-acetylgalactosaminyltransferase 3;
URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_hum_485";
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EMBL; X92689; CAA63371.1; -; mRNA.
EMBL; AC009495; AAY14678.1; -; Genomic_DNA.
EMBL; CH471058; EAX11324.1; -; Genomic_DNA.
EMBL; BC056246; AAH56246.1; ALT_INIT; mRNA.
EMBL; BC113565; AAI13566.1; -; mRNA.
EMBL; BC113567; AAI13568.1; -; mRNA.
CCDS; CCDS2226.1; -. [Q14435-1]
RefSeq; NP_004473.2; NM_004482.3. [Q14435-1]
RefSeq; XP_005246506.1; XM_005246449.1. [Q14435-1]
RefSeq; XP_011509231.1; XM_011510929.1. [Q14435-1]
RefSeq; XP_016859259.1; XM_017003770.1. [Q14435-1]
UniGene; Hs.170986; -.
ProteinModelPortal; Q14435; -.
BioGrid; 108863; 3.
IntAct; Q14435; 2.
STRING; 9606.ENSP00000376465; -.
CAZy; CBM13; Carbohydrate-Binding Module Family 13.
CAZy; GT27; Glycosyltransferase Family 27.
iPTMnet; Q14435; -.
PhosphoSitePlus; Q14435; -.
BioMuta; GALNT3; -.
DMDM; 209572629; -.
EPD; Q14435; -.
MaxQB; Q14435; -.
PaxDb; Q14435; -.
PeptideAtlas; Q14435; -.
PRIDE; Q14435; -.
DNASU; 2591; -.
Ensembl; ENST00000392701; ENSP00000376465; ENSG00000115339. [Q14435-1]
GeneID; 2591; -.
KEGG; hsa:2591; -.
UCSC; uc010fph.2; human. [Q14435-1]
CTD; 2591; -.
DisGeNET; 2591; -.
EuPathDB; HostDB:ENSG00000115339.13; -.
GeneCards; GALNT3; -.
H-InvDB; HIX0024214; -.
HGNC; HGNC:4125; GALNT3.
HPA; HPA007613; -.
MalaCards; GALNT3; -.
MIM; 211900; phenotype.
MIM; 601756; gene.
neXtProt; NX_Q14435; -.
OpenTargets; ENSG00000115339; -.
Orphanet; 306661; Familial tumoral calcinosis.
PharmGKB; PA28538; -.
eggNOG; KOG3736; Eukaryota.
eggNOG; ENOG410XPMK; LUCA.
GeneTree; ENSGT00760000118828; -.
HOGENOM; HOG000038227; -.
HOVERGEN; HBG051699; -.
InParanoid; Q14435; -.
KO; K00710; -.
OMA; QYFEYSA; -.
OrthoDB; EOG091G085O; -.
PhylomeDB; Q14435; -.
TreeFam; TF313267; -.
BRENDA; 2.4.1.41; 2681.
Reactome; R-HSA-190372; FGFR3c ligand binding and activation.
Reactome; R-HSA-5083625; Defective GALNT3 causes familial hyperphosphatemic tumoral calcinosis (HFTC).
Reactome; R-HSA-913709; O-linked glycosylation of mucins.
UniPathway; UPA00378; -.
ChiTaRS; GALNT3; human.
GeneWiki; GALNT3; -.
GenomeRNAi; 2591; -.
PRO; PR:Q14435; -.
Proteomes; UP000005640; Chromosome 2.
Bgee; ENSG00000115339; -.
CleanEx; HS_GALNT3; -.
ExpressionAtlas; Q14435; baseline and differential.
Genevisible; Q14435; HS.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
GO; GO:0016021; C:integral component of membrane; TAS:ProtInc.
GO; GO:0016020; C:membrane; TAS:ProtInc.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:BHF-UCL.
GO; GO:0005509; F:calcium ion binding; IDA:BHF-UCL.
GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
GO; GO:0030145; F:manganese ion binding; IDA:BHF-UCL.
GO; GO:0004653; F:polypeptide N-acetylgalactosaminyltransferase activity; IDA:BHF-UCL.
GO; GO:0005975; P:carbohydrate metabolic process; NAS:ProtInc.
GO; GO:0008543; P:fibroblast growth factor receptor signaling pathway; TAS:Reactome.
GO; GO:0016266; P:O-glycan processing; TAS:Reactome.
GO; GO:0018242; P:protein O-linked glycosylation via serine; IDA:BHF-UCL.
GO; GO:0018243; P:protein O-linked glycosylation via threonine; IDA:UniProtKB.
CDD; cd00161; RICIN; 1.
Gene3D; 3.90.550.10; -; 1.
InterPro; IPR001173; Glyco_trans_2-like.
InterPro; IPR029044; Nucleotide-diphossugar_trans.
InterPro; IPR035992; Ricin_B-like_lectins.
InterPro; IPR000772; Ricin_B_lectin.
Pfam; PF00535; Glycos_transf_2; 1.
Pfam; PF00652; Ricin_B_lectin; 1.
SMART; SM00458; RICIN; 1.
SUPFAM; SSF50370; SSF50370; 1.
SUPFAM; SSF53448; SSF53448; 1.
PROSITE; PS50231; RICIN_B_LECTIN; 1.
1: Evidence at protein level;
Alternative splicing; Complete proteome; Disulfide bond; Glycoprotein;
Glycosyltransferase; Golgi apparatus; Lectin; Manganese; Membrane;
Metal-binding; Reference proteome; Signal-anchor; Transferase;
Transmembrane; Transmembrane helix.
CHAIN 1 633 Polypeptide N-
acetylgalactosaminyltransferase 3.
/FTId=PRO_0000059106.
TOPO_DOM 1 19 Cytoplasmic. {ECO:0000255}.
TRANSMEM 20 37 Helical; Signal-anchor for type II
membrane protein. {ECO:0000255}.
TOPO_DOM 38 633 Lumenal. {ECO:0000255}.
DOMAIN 504 630 Ricin B-type lectin.
{ECO:0000255|PROSITE-ProRule:PRU00174}.
REGION 184 293 Catalytic subdomain A.
REGION 356 418 Catalytic subdomain B.
METAL 277 277 Manganese. {ECO:0000250}.
METAL 279 279 Manganese. {ECO:0000250}.
METAL 415 415 Manganese. {ECO:0000250}.
BINDING 225 225 Substrate. {ECO:0000250}.
BINDING 254 254 Substrate. {ECO:0000250}.
BINDING 387 387 Substrate. {ECO:0000250}.
BINDING 418 418 Substrate. {ECO:0000250}.
CARBOHYD 132 132 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 297 297 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 484 484 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 173 410 {ECO:0000255|PROSITE-ProRule:PRU00174}.
DISULFID 401 482 {ECO:0000255|PROSITE-ProRule:PRU00174}.
DISULFID 517 535 {ECO:0000255|PROSITE-ProRule:PRU00174}.
DISULFID 561 574 {ECO:0000255|PROSITE-ProRule:PRU00174}.
DISULFID 605 618 {ECO:0000255|PROSITE-ProRule:PRU00174}.
VAR_SEQ 173 192 CIEQKFKRCPPLPTTSVIIV -> YVEEYLLFILYHQALQG
REG (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_011202.
VAR_SEQ 193 633 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_011203.
CONFLICT 481 481 Q -> R (in Ref. 1; CAA63371).
{ECO:0000305}.
SEQUENCE 633 AA; 72610 MW; 3019B2DCCC19A584 CRC64;
MAHLKRLVKL HIKRHYHKKF WKLGAVIFFF IIVLVLMQRE VSVQYSKEES RMERNMKNKN
KMLDLMLEAV NNIKDAMPKM QIGAPVRQNI DAGERPCLQG YYTAAELKPV LDRPPQDSNA
PGASGKAFKT TNLSVEEQKE KERGEAKHCF NAFASDRISL HRDLGPDTRP PECIEQKFKR
CPPLPTTSVI IVFHNEAWST LLRTVHSVLY SSPAILLKEI ILVDDASVDE YLHDKLDEYV
KQFSIVKIVR QRERKGLITA RLLGATVATA ETLTFLDAHC ECFYGWLEPL LARIAENYTA
VVSPDIASID LNTFEFNKPS PYGSNHNRGN FDWSLSFGWE SLPDHEKQRR KDETYPIKTP
TFAGGLFSIS KEYFEYIGSY DEEMEIWGGE NIEMSFRVWQ CGGQLEIMPC SVVGHVFRSK
SPHSFPKGTQ VIARNQVRLA EVWMDEYKEI FYRRNTDAAK IVKQKAFGDL SKRFEIKHRL
QCKNFTWYLN NIYPEVYVPD LNPVISGYIK SVGQPLCLDV GENNQGGKPL IMYTCHGLGG
NQYFEYSAQH EIRHNIQKEL CLHAAQGLVQ LKACTYKGHK TVVTGEQIWE IQKDQLLYNP
FLKMCLSANG EHPSLVSCNP SDPLQKWILS QND


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