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Polypeptide N-acetylgalactosaminyltransferase 2 (EC 2.4.1.41) (Polypeptide GalNAc transferase 2) (GalNAc-T2) (pp-GaNTase 2) (Protein-UDP acetylgalactosaminyltransferase 2) (UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 2) [Cleaved into: Polypeptide N-acetylgalactosaminyltransferase 2 soluble form]

 GALT2_HUMAN             Reviewed;         571 AA.
Q10471; A8K1Y3; B7Z8V8; C5HU00; Q9NPY4;
16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
30-AUG-2017, entry version 163.
RecName: Full=Polypeptide N-acetylgalactosaminyltransferase 2;
EC=2.4.1.41;
AltName: Full=Polypeptide GalNAc transferase 2;
Short=GalNAc-T2;
Short=pp-GaNTase 2;
AltName: Full=Protein-UDP acetylgalactosaminyltransferase 2;
AltName: Full=UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 2;
Contains:
RecName: Full=Polypeptide N-acetylgalactosaminyltransferase 2 soluble form;
Name=GALNT2;
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), PROTEIN SEQUENCE OF 52-93;
104-120; 170-182; 193-218; 303-323; 421-424 AND 510-546, FUNCTION,
COFACTOR, CATALYTIC ACTIVITY, AND TISSUE SPECIFICITY.
TISSUE=Gastric carcinoma;
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).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
MET-554.
TISSUE=Hippocampus, and Trachea;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[4]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
NHLBI resequencing and genotyping service (RS&G);
Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Lymph;
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).
[7]
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).
[8]
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).
[9]
FUNCTION.
PubMed=12438318; DOI=10.1074/jbc.M211097200;
Iwasaki H., Zhang Y., Tachibana K., Gotoh M., Kikuchi N., Kwon Y.-D.,
Togayachi A., Kudo T., Kubota T., Narimatsu H.;
"Initiation of O-glycan synthesis in IgA1 hinge region is determined
by a single enzyme, UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-
acetylgalactosaminyltransferase 2.";
J. Biol. Chem. 278:5613-5621(2003).
[10]
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).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-536, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[14]
X-RAY CRYSTALLOGRAPHY (1.64 ANGSTROMS) OF 75-571 IN COMPLEX WITH UDP;
PEPTIDE SUBSTRATE AND MANGANESE, FUNCTION, CATALYTIC ACTIVITY,
COFACTOR, AND DISULFIDE BONDS.
PubMed=16434399; DOI=10.1074/jbc.M513590200;
Fritz T.A., Raman J., Tabak L.A.;
"Dynamic association between the catalytic and lectin domains of human
UDP-GalNAc:polypeptide alpha-N-acetylgalactosaminyltransferase-2.";
J. Biol. Chem. 281:8613-8619(2006).
-!- 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. Probably involved in O-linked
glycosylation of the immunoglobulin A1 (IgA1) hinge region.
{ECO:0000269|PubMed:12438318, ECO:0000269|PubMed:16434399,
ECO:0000269|PubMed:7592619, ECO:0000269|PubMed:9295285}.
-!- CATALYTIC ACTIVITY: UDP-N-acetyl-alpha-D-galactosamine +
polypeptide = UDP + N-acetyl-alpha-D-galactosaminyl-polypeptide.
{ECO:0000269|PubMed:16434399, ECO:0000269|PubMed:7592619}.
-!- COFACTOR:
Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
Evidence={ECO:0000269|PubMed:16434399,
ECO:0000269|PubMed:7592619};
-!- PATHWAY: Protein modification; protein glycosylation.
-!- INTERACTION:
Q8N6L0:CCDC155; NbExp=5; IntAct=EBI-10226985, EBI-749265;
Q9HC29:NOD2; NbExp=2; IntAct=EBI-10226985, EBI-7445625;
-!- SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane
{ECO:0000269|PubMed:9394011}; Single-pass type II membrane protein
{ECO:0000269|PubMed:9394011}. Secreted
{ECO:0000269|PubMed:9394011}. Note=Resides preferentially in the
trans and medial parts of the Golgi stack. A secreted form also
exists.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q10471-1; Sequence=Displayed;
Name=2;
IsoId=Q10471-2; Sequence=VSP_056491, VSP_056492, VSP_056493;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Widely expressed.
{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 binds to GalNAc and
contributes to the glycopeptide specificity. {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 2;
URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_hum_484";
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EMBL; X85019; CAA59381.1; -; mRNA.
EMBL; AK290048; BAF82737.1; -; mRNA.
EMBL; AK304029; BAH14094.1; -; mRNA.
EMBL; AL592228; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL078646; CAC00585.2; -; Genomic_DNA.
EMBL; AL117349; CAC00585.2; JOINED; Genomic_DNA.
EMBL; AL136988; CAC00585.2; JOINED; Genomic_DNA.
EMBL; AL117349; CAI22902.1; -; Genomic_DNA.
EMBL; AL078646; CAI22902.1; JOINED; Genomic_DNA.
EMBL; AL136988; CAI22902.1; JOINED; Genomic_DNA.
EMBL; AL136988; CAI23447.1; -; Genomic_DNA.
EMBL; AL078646; CAI23447.1; JOINED; Genomic_DNA.
EMBL; AL117349; CAI23447.1; JOINED; Genomic_DNA.
EMBL; FJ515852; ACS13744.1; -; Genomic_DNA.
EMBL; CH471098; EAW69911.1; -; Genomic_DNA.
EMBL; BC041120; AAH41120.1; -; mRNA.
CCDS; CCDS1582.1; -. [Q10471-1]
PIR; I37405; I37405.
RefSeq; NP_001278795.1; NM_001291866.1.
RefSeq; NP_004472.1; NM_004481.4. [Q10471-1]
UniGene; Hs.743964; -.
PDB; 2FFU; X-ray; 1.64 A; A=75-571.
PDB; 2FFV; X-ray; 2.75 A; A/B=75-571.
PDB; 4D0T; X-ray; 2.45 A; A/B/C/D/E/F=1-571.
PDB; 4D0Z; X-ray; 2.20 A; A/B/C/D/E/F=1-571.
PDB; 4D11; X-ray; 2.85 A; A/B/C/D/E/F=1-571.
PDB; 5AJN; X-ray; 1.67 A; A=1-571.
PDB; 5AJO; X-ray; 1.48 A; A=1-571.
PDB; 5AJP; X-ray; 1.65 A; A=1-571.
PDB; 5FV9; X-ray; 2.07 A; A/B/C/D/E/F=1-571.
PDBsum; 2FFU; -.
PDBsum; 2FFV; -.
PDBsum; 4D0T; -.
PDBsum; 4D0Z; -.
PDBsum; 4D11; -.
PDBsum; 5AJN; -.
PDBsum; 5AJO; -.
PDBsum; 5AJP; -.
PDBsum; 5FV9; -.
ProteinModelPortal; Q10471; -.
SMR; Q10471; -.
BioGrid; 108862; 30.
IntAct; Q10471; 19.
MINT; MINT-3026412; -.
STRING; 9606.ENSP00000355632; -.
CAZy; CBM13; Carbohydrate-Binding Module Family 13.
CAZy; GT27; Glycosyltransferase Family 27.
iPTMnet; Q10471; -.
PhosphoSitePlus; Q10471; -.
SwissPalm; Q10471; -.
BioMuta; GALNT2; -.
DMDM; 51315838; -.
EPD; Q10471; -.
MaxQB; Q10471; -.
PaxDb; Q10471; -.
PeptideAtlas; Q10471; -.
PRIDE; Q10471; -.
DNASU; 2590; -.
Ensembl; ENST00000366672; ENSP00000355632; ENSG00000143641. [Q10471-1]
GeneID; 2590; -.
KEGG; hsa:2590; -.
UCSC; uc010pwa.2; human. [Q10471-1]
CTD; 2590; -.
DisGeNET; 2590; -.
GeneCards; GALNT2; -.
H-InvDB; HIX0001682; -.
HGNC; HGNC:4124; GALNT2.
HPA; HPA011222; -.
MIM; 602274; gene.
neXtProt; NX_Q10471; -.
OpenTargets; ENSG00000143641; -.
PharmGKB; PA28537; -.
eggNOG; KOG3738; Eukaryota.
eggNOG; ENOG410XPRX; LUCA.
GeneTree; ENSGT00760000118828; -.
HOGENOM; HOG000038227; -.
HOVERGEN; HBG051699; -.
InParanoid; Q10471; -.
KO; K00710; -.
OMA; GNQEWAL; -.
OrthoDB; EOG091G085O; -.
PhylomeDB; Q10471; -.
TreeFam; TF313267; -.
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; GALNT2; human.
EvolutionaryTrace; Q10471; -.
GeneWiki; GALNT2; -.
GenomeRNAi; 2590; -.
PRO; PR:Q10471; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000143641; -.
CleanEx; HS_GALNT2; -.
Genevisible; Q10471; HS.
GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005794; C:Golgi apparatus; IDA:BHF-UCL.
GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
GO; GO:0005795; C:Golgi stack; IDA:BHF-UCL.
GO; GO:0030173; C:integral component of Golgi membrane; NAS:BHF-UCL.
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:UniProtKB.
GO; GO:0004653; F:polypeptide N-acetylgalactosaminyltransferase activity; IDA:UniProtKB.
GO; GO:0002378; P:immunoglobulin biosynthetic process; IDA:BHF-UCL.
GO; GO:0016266; P:O-glycan processing; IDA:GO_Central.
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.
Gene3D; 3.90.550.10; -; 1.
InterPro; IPR001173; Glyco_trans_2-like.
InterPro; IPR029044; Nucleotide-diphossugar_trans.
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;
3D-structure; Alternative splicing; Complete proteome;
Direct protein sequencing; Disulfide bond; Glycosyltransferase;
Golgi apparatus; Lectin; Manganese; Membrane; Metal-binding;
Phosphoprotein; Polymorphism; Reference proteome; Secreted;
Signal-anchor; Transferase; Transmembrane; Transmembrane helix.
CHAIN 1 571 Polypeptide N-
acetylgalactosaminyltransferase 2.
/FTId=PRO_0000223391.
CHAIN 52 571 Polypeptide N-
acetylgalactosaminyltransferase 2 soluble
form.
/FTId=PRO_0000012265.
TOPO_DOM 1 6 Cytoplasmic. {ECO:0000255}.
TRANSMEM 7 24 Helical; Signal-anchor for type II
membrane protein. {ECO:0000255}.
TOPO_DOM 25 571 Lumenal. {ECO:0000255}.
DOMAIN 443 566 Ricin B-type lectin.
{ECO:0000255|PROSITE-ProRule:PRU00174}.
REGION 135 240 Catalytic subdomain A.
REGION 300 362 Catalytic subdomain B.
METAL 224 224 Manganese. {ECO:0000269|PubMed:16434399}.
METAL 226 226 Manganese. {ECO:0000269|PubMed:16434399}.
METAL 359 359 Manganese. {ECO:0000269|PubMed:16434399}.
BINDING 143 143 Substrate.
BINDING 176 176 Substrate.
BINDING 201 201 Substrate.
BINDING 225 225 Substrate.
BINDING 331 331 Substrate.
BINDING 362 362 Substrate.
BINDING 365 365 Substrate.
BINDING 367 367 Substrate.
SITE 516 516 Not glycosylated.
MOD_RES 536 536 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
DISULFID 126 354 {ECO:0000255|PROSITE-ProRule:PRU00174,
ECO:0000269|PubMed:16434399}.
DISULFID 345 423 {ECO:0000255|PROSITE-ProRule:PRU00174,
ECO:0000269|PubMed:16434399}.
DISULFID 456 473 {ECO:0000255|PROSITE-ProRule:PRU00174,
ECO:0000269|PubMed:16434399}.
DISULFID 496 513 {ECO:0000255|PROSITE-ProRule:PRU00174,
ECO:0000269|PubMed:16434399}.
DISULFID 539 555 {ECO:0000255|PROSITE-ProRule:PRU00174,
ECO:0000269|PubMed:16434399}.
VAR_SEQ 1 90 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_056491.
VAR_SEQ 303 355 TPMIAGGLFVMDKFYFEELGKYDMMMDVWGGENLEISFRVW
QCGGSLEIIPCS -> DLVPRVAVWWQPGDHPVQPCGTRVP
EAAPLHVPGWQWHCLCPKHPPGSRGLDG (in isoform
2). {ECO:0000303|PubMed:14702039}.
/FTId=VSP_056492.
VAR_SEQ 356 571 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_056493.
VARIANT 245 245 R -> H (in dbSNP:rs1923950).
/FTId=VAR_049240.
VARIANT 554 554 V -> M (in dbSNP:rs2273970).
{ECO:0000269|PubMed:14702039}.
/FTId=VAR_019575.
CONFLICT 70 70 T -> G (in Ref. 1; AA sequence).
{ECO:0000305}.
CONFLICT 78 78 W -> D (in Ref. 1; AA sequence).
{ECO:0000305}.
CONFLICT 93 93 R -> G (in Ref. 1; AA sequence).
{ECO:0000305}.
CONFLICT 210 210 R -> W (in Ref. 1; AA sequence).
{ECO:0000305}.
CONFLICT 290 291 RR -> SC (in Ref. 1; AA sequence).
{ECO:0000305}.
CONFLICT 293 293 R -> Q (in Ref. 1; AA sequence).
{ECO:0000305}.
CONFLICT 300 300 P -> H (in Ref. 1; AA sequence).
{ECO:0000305}.
CONFLICT 522 522 W -> A (in Ref. 1; AA sequence).
{ECO:0000305}.
CONFLICT 533 533 H -> M (in Ref. 1; AA sequence).
{ECO:0000305}.
HELIX 78 80 {ECO:0000244|PDB:5AJO}.
HELIX 83 87 {ECO:0000244|PDB:5AJO}.
HELIX 88 90 {ECO:0000244|PDB:5AJO}.
TURN 98 102 {ECO:0000244|PDB:5AJO}.
HELIX 106 111 {ECO:0000244|PDB:5AJO}.
HELIX 124 128 {ECO:0000244|PDB:5AJO}.
STRAND 138 146 {ECO:0000244|PDB:5AJO}.
HELIX 149 162 {ECO:0000244|PDB:5AJO}.
HELIX 165 167 {ECO:0000244|PDB:5AJO}.
STRAND 168 175 {ECO:0000244|PDB:5AJO}.
HELIX 182 185 {ECO:0000244|PDB:5AJO}.
HELIX 186 189 {ECO:0000244|PDB:5AJO}.
STRAND 193 197 {ECO:0000244|PDB:5AJO}.
HELIX 204 214 {ECO:0000244|PDB:5AJO}.
STRAND 217 223 {ECO:0000244|PDB:5AJO}.
STRAND 225 229 {ECO:0000244|PDB:5AJO}.
HELIX 235 243 {ECO:0000244|PDB:5AJO}.
STRAND 247 256 {ECO:0000244|PDB:5AJO}.
TURN 258 260 {ECO:0000244|PDB:5AJO}.
STRAND 270 274 {ECO:0000244|PDB:5AJO}.
STRAND 280 284 {ECO:0000244|PDB:5AJO}.
HELIX 287 295 {ECO:0000244|PDB:5AJO}.
STRAND 308 314 {ECO:0000244|PDB:5AJO}.
HELIX 315 320 {ECO:0000244|PDB:5AJO}.
STRAND 330 332 {ECO:0000244|PDB:5AJO}.
HELIX 336 344 {ECO:0000244|PDB:5AJO}.
STRAND 348 360 {ECO:0000244|PDB:5AJO}.
STRAND 363 365 {ECO:0000244|PDB:5AJO}.
TURN 366 368 {ECO:0000244|PDB:2FFV}.
STRAND 369 371 {ECO:0000244|PDB:5AJO}.
HELIX 373 376 {ECO:0000244|PDB:5AJO}.
HELIX 378 388 {ECO:0000244|PDB:5AJO}.
HELIX 390 392 {ECO:0000244|PDB:5AJO}.
HELIX 393 399 {ECO:0000244|PDB:5AJO}.
HELIX 401 403 {ECO:0000244|PDB:5AJO}.
HELIX 412 420 {ECO:0000244|PDB:5AJO}.
HELIX 426 432 {ECO:0000244|PDB:5AJO}.
STRAND 445 452 {ECO:0000244|PDB:5AJO}.
STRAND 455 458 {ECO:0000244|PDB:5AJO}.
TURN 463 465 {ECO:0000244|PDB:2FFV}.
STRAND 469 472 {ECO:0000244|PDB:5AJO}.
HELIX 478 480 {ECO:0000244|PDB:5AJO}.
STRAND 482 484 {ECO:0000244|PDB:5AJO}.
STRAND 490 492 {ECO:0000244|PDB:5AJO}.
STRAND 495 498 {ECO:0000244|PDB:5AJO}.
STRAND 509 512 {ECO:0000244|PDB:5AJO}.
HELIX 518 520 {ECO:0000244|PDB:5AJO}.
STRAND 522 525 {ECO:0000244|PDB:5AJO}.
TURN 526 529 {ECO:0000244|PDB:5AJO}.
STRAND 530 533 {ECO:0000244|PDB:5AJO}.
STRAND 536 541 {ECO:0000244|PDB:5AJO}.
HELIX 545 547 {ECO:0000244|PDB:5AJO}.
STRAND 551 554 {ECO:0000244|PDB:5AJO}.
HELIX 559 561 {ECO:0000244|PDB:5AJO}.
STRAND 564 568 {ECO:0000244|PDB:5AJO}.
SEQUENCE 571 AA; 64733 MW; D9A0F5D17C55BAF2 CRC64;
MRRRSRMLLC FAFLWVLGIA YYMYSGGGSA LAGGAGGGAG RKEDWNEIDP IKKKDLHHSN
GEEKAQSMET LPPGKVRWPD FNQEAYVGGT MVRSGQDPYA RNKFNQVESD KLRMDRAIPD
TRHDQCQRKQ WRVDLPATSV VITFHNEARS ALLRTVVSVL KKSPPHLIKE IILVDDYSND
PEDGALLGKI EKVRVLRNDR REGLMRSRVR GADAAQAKVL TFLDSHCECN EHWLEPLLER
VAEDRTRVVS PIIDVINMDN FQYVGASADL KGGFDWNLVF KWDYMTPEQR RSRQGNPVAP
IKTPMIAGGL FVMDKFYFEE LGKYDMMMDV WGGENLEISF RVWQCGGSLE IIPCSRVGHV
FRKQHPYTFP GGSGTVFARN TRRAAEVWMD EYKNFYYAAV PSARNVPYGN IQSRLELRKK
LSCKPFKWYL ENVYPELRVP DHQDIAFGAL QQGTNCLDTL GHFADGVVGV YECHNAGGNQ
EWALTKEKSV KHMDLCLTVV DRAPGSLIKL QGCRENDSRQ KWEQIEGNSK LRHVGSNLCL
DSRTAKSGGL SVEVCGPALS QQWKFTLNLQ Q


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