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Polypeptide N-acetylgalactosaminyltransferase 1 (EC 2.4.1.41) (Polypeptide GalNAc transferase 1) (GalNAc-T1) (pp-GaNTase 1) (Protein-UDP acetylgalactosaminyltransferase 1) (UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 1) [Cleaved into: Polypeptide N-acetylgalactosaminyltransferase 1 soluble form]

 GALT1_HUMAN             Reviewed;         559 AA.
Q10472; Q86TJ7; Q9UM86;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 1.
25-OCT-2017, entry version 168.
RecName: Full=Polypeptide N-acetylgalactosaminyltransferase 1;
EC=2.4.1.41;
AltName: Full=Polypeptide GalNAc transferase 1;
Short=GalNAc-T1;
Short=pp-GaNTase 1;
AltName: Full=Protein-UDP acetylgalactosaminyltransferase 1;
AltName: Full=UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 1;
Contains:
RecName: Full=Polypeptide N-acetylgalactosaminyltransferase 1 soluble form;
Name=GALNT1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE (ISOFORM 1).
TISSUE=Salivary gland;
PubMed=8690719;
Meurer J.A., Naylor J.M., Baker C.A., Thomsen D.R., Homa F.L.,
Elhammer A.P.;
"cDNA cloning, expression, and chromosomal localization of a human
UDP-GalNAc:polypeptide, N-acetylgalactosaminyltransferase.";
J. Biochem. 118:568-574(1995).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
PubMed=7592619; DOI=10.1074/jbc.270.41.24166;
White T., Bennett E.P., Takio K., Soerensen T., Bonding N.,
Clausen H.;
"Purification and cDNA cloning of a human UDP-N-acetyl-alpha-D-
galactosamine:polypeptide N-acetylgalactosaminyltransferase.";
J. Biol. Chem. 270:24156-24165(1995).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=PNS;
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).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 512-559 (ISOFORM 1).
PubMed=8727794; DOI=10.1093/glycob/6.2.231;
Meurer J.A., Drong R.F., Homa F.L., Slightom J.L., Elhammer A.P.;
"Organization of a human UDP-GalNAc:polypeptide, N-
acetylgalactosaminyltransferase gene and a related processed
pseudogene.";
Glycobiology 6:231-241(1996).
[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]
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 a broad spectrum of substrates for peptides
such as EA2, Muc5AC, Muc1a, Muc1b and Muc7.
{ECO:0000269|PubMed:9295285}.
-!- CATALYTIC ACTIVITY: UDP-N-acetyl-alpha-D-galactosamine +
polypeptide = UDP + N-acetyl-alpha-D-galactosaminyl-polypeptide.
-!- COFACTOR:
Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
-!- PATHWAY: Protein modification; protein glycosylation.
-!- SUBCELLULAR LOCATION: Polypeptide N-
acetylgalactosaminyltransferase 1: Golgi apparatus, Golgi stack
membrane; Single-pass type II membrane protein.
-!- SUBCELLULAR LOCATION: Polypeptide N-
acetylgalactosaminyltransferase 1 soluble form: Secreted.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q10472-1; Sequence=Displayed;
Name=2;
IsoId=Q10472-2; Sequence=VSP_011200;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Widely expressed. Expressed in all tissues
tested. {ECO:0000269|PubMed:7592619}.
-!- 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 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).
{ECO:0000250}.
-!- SIMILARITY: Belongs to the glycosyltransferase 2 family. GalNAc-T
subfamily. {ECO:0000305}.
-!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase;
Note=Polypeptide N-acetylgalactosaminyltransferase 1;
URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_hum_483";
-----------------------------------------------------------------------
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EMBL; U41514; AAC50327.1; -; mRNA.
EMBL; X85018; CAA59380.1; -; mRNA.
EMBL; BC047746; AAH47746.1; -; mRNA.
EMBL; S82597; AAD14406.1; -; Genomic_DNA.
CCDS; CCDS11915.1; -. [Q10472-1]
PIR; JC4223; JC4223.
RefSeq; NP_065207.2; NM_020474.3. [Q10472-1]
RefSeq; XP_005258296.1; XM_005258239.3. [Q10472-1]
RefSeq; XP_016881181.1; XM_017025692.1. [Q10472-1]
UniGene; Hs.514806; -.
ProteinModelPortal; Q10472; -.
SMR; Q10472; -.
BioGrid; 108861; 9.
IntAct; Q10472; 4.
STRING; 9606.ENSP00000269195; -.
CAZy; CBM13; Carbohydrate-Binding Module Family 13.
CAZy; GT27; Glycosyltransferase Family 27.
iPTMnet; Q10472; -.
PhosphoSitePlus; Q10472; -.
SwissPalm; Q10472; -.
BioMuta; GALNT1; -.
DMDM; 1709558; -.
EPD; Q10472; -.
MaxQB; Q10472; -.
PaxDb; Q10472; -.
PeptideAtlas; Q10472; -.
PRIDE; Q10472; -.
Ensembl; ENST00000269195; ENSP00000269195; ENSG00000141429. [Q10472-1]
Ensembl; ENST00000591081; ENSP00000466411; ENSG00000141429. [Q10472-2]
Ensembl; ENST00000591924; ENSP00000465699; ENSG00000141429. [Q10472-2]
GeneID; 2589; -.
KEGG; hsa:2589; -.
UCSC; uc002kza.3; human. [Q10472-1]
CTD; 2589; -.
DisGeNET; 2589; -.
EuPathDB; HostDB:ENSG00000141429.13; -.
GeneCards; GALNT1; -.
HGNC; HGNC:4123; GALNT1.
HPA; HPA012628; -.
MIM; 602273; gene.
neXtProt; NX_Q10472; -.
OpenTargets; ENSG00000141429; -.
PharmGKB; PA30054; -.
eggNOG; KOG3736; Eukaryota.
eggNOG; ENOG410XPMK; LUCA.
GeneTree; ENSGT00760000118828; -.
HOGENOM; HOG000038227; -.
HOVERGEN; HBG051699; -.
InParanoid; Q10472; -.
KO; K00710; -.
OMA; IMSDDLC; -.
OrthoDB; EOG091G085O; -.
PhylomeDB; Q10472; -.
TreeFam; TF313267; -.
BioCyc; MetaCyc:HS06826-MONOMER; -.
BRENDA; 2.4.1.41; 2681.
Reactome; R-HSA-6811436; COPI-independent Golgi-to-ER retrograde traffic.
Reactome; R-HSA-913709; O-linked glycosylation of mucins.
UniPathway; UPA00378; -.
ChiTaRS; GALNT1; human.
GeneWiki; GALNT1; -.
GenomeRNAi; 2589; -.
PRO; PR:Q10472; -.
Proteomes; UP000005640; Chromosome 18.
Bgee; ENSG00000141429; -.
CleanEx; HS_GALNT1; -.
ExpressionAtlas; Q10472; baseline and differential.
Genevisible; Q10472; HS.
GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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; IEA:UniProtKB-KW.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0048471; C:perinuclear region of cytoplasm; 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:UniProtKB.
GO; GO:0016266; P:O-glycan processing; TAS:Reactome.
GO; GO:0006493; P:protein O-linked glycosylation; IDA:UniProtKB.
GO; GO:0018242; P:protein O-linked glycosylation via serine; IDA:BHF-UCL.
GO; GO:0018243; P:protein O-linked glycosylation via threonine; IDA:BHF-UCL.
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; Polymorphism; Reference proteome; Secreted;
Signal-anchor; Transferase; Transmembrane; Transmembrane helix.
CHAIN 1 559 Polypeptide N-
acetylgalactosaminyltransferase 1.
/FTId=PRO_0000223387.
CHAIN 41 559 Polypeptide N-
acetylgalactosaminyltransferase 1 soluble
form.
/FTId=PRO_0000012257.
TOPO_DOM 1 8 Cytoplasmic. {ECO:0000255}.
TRANSMEM 9 28 Helical; Signal-anchor for type II
membrane protein. {ECO:0000255}.
TOPO_DOM 29 559 Lumenal. {ECO:0000255}.
DOMAIN 429 551 Ricin B-type lectin.
{ECO:0000255|PROSITE-ProRule:PRU00174}.
REGION 115 225 Catalytic subdomain A.
REGION 285 347 Catalytic subdomain B.
METAL 209 209 Manganese. {ECO:0000250}.
METAL 211 211 Manganese. {ECO:0000250}.
METAL 344 344 Manganese. {ECO:0000250}.
BINDING 156 156 Substrate. {ECO:0000250}.
BINDING 186 186 Substrate. {ECO:0000250}.
BINDING 316 316 Substrate. {ECO:0000250}.
BINDING 347 347 Substrate. {ECO:0000250}.
BINDING 352 352 Substrate. {ECO:0000250}.
CARBOHYD 95 95 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 552 552 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 106 339 {ECO:0000255|PROSITE-ProRule:PRU00174}.
DISULFID 330 408 {ECO:0000255|PROSITE-ProRule:PRU00174}.
DISULFID 442 459 {ECO:0000255|PROSITE-ProRule:PRU00174}.
DISULFID 482 497 {ECO:0000255|PROSITE-ProRule:PRU00174}.
DISULFID 523 540 {ECO:0000255|PROSITE-ProRule:PRU00174}.
VAR_SEQ 106 559 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_011200.
VARIANT 414 414 Y -> D (in dbSNP:rs34304568).
/FTId=VAR_033946.
SEQUENCE 559 AA; 64219 MW; CD68118CB201EE5B CRC64;
MRKFAYCKVV LATSLIWVLL DMFLLLYFSE CNKCDEKKER GLPAGDVLEP VQKPHEGPGE
MGKPVVIPKE DQEKMKEMFK INQFNLMASE MIALNRSLPD VRLEGCKTKV YPDNLPTTSV
VIVFHNEAWS TLLRTVHSVI NRSPRHMIEE IVLVDDASER DFLKRPLESY VKKLKVPVHV
IRMEQRSGLI RARLKGAAVS KGQVITFLDA HCECTVGWLE PLLARIKHDR RTVVCPIIDV
ISDDTFEYMA GSDMTYGGFN WKLNFRWYPV PQREMDRRKG DRTLPVRTPT MAGGLFSIDR
DYFQEIGTYD AGMDIWGGEN LEISFRIWQC GGTLEIVTCS HVGHVFRKAT PYTFPGGTGQ
IINKNNRRLA EVWMDEFKNF FYIISPGVTK VDYGDISSRV GLRHKLQCKP FSWYLENIYP
DSQIPRHYFS LGEIRNVETN QCLDNMARKE NEKVGIFNCH GMGGNQVFSY TANKEIRTDD
LCLDVSKLNG PVTMLKCHHL KGNQLWEYDP VKLTLQHVNS NQCLDKATEE DSQVPSIRDC
NGSRSQQWLL RNVTLPEIF


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