Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-10090-00232
Entry Name
UniProt Accession
Theoretical PI
8.8
Molecular Weight
64514.5
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
Polypeptide N-acetylgalactosaminyltransferase 2 soluble form
Protein Synonyms/Alias
2.4.1.41; Polypeptide GalNAc transferase 2; GalNAc-T2; pp-GaNTase 2; Protein-UDP acetylgalactosaminyltransferase 2; UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 2;
Gene Name
Galnt2
Gene Synonyms/Alias
Created Date
16-AUG-2004
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
10
Canonical
RRSRMLLCFALLWVL
[1]
S-Palmitoylation
226
Canonical
LTFLDSHCECNERWL
[1]
S-Palmitoylation
Organism
Mus musculus (Mouse)
NCBI Taxa ID
10090
Reference
[1] Predicted from GPS-Lipid
Functional Description
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 (By similarity).
Sequence Annotation
Topological domain: 1 6 Cytoplasmic.
Transmembrane: 7 24 Helical; Signal-anchor for type IImembrane protein.
Topological domain: 25 570 Lumenal.
Domain: 442 565 Ricin B-type lectin.
Region: 134 239 Catalytic subdomain A.
Region: 299 361 Catalytic subdomain B.
Metal binding site: 223 223 Manganese.
Metal binding site: 225 225 Manganese.
Metal binding site: 358 358 Manganese.
Binding site: 142 142 Substrate.
Binding site: 175 175 Substrate.
Binding site: 200 200 Substrate.
Binding site: 224 224 Substrate.
Binding site: 330 330 Substrate.
Binding site: 361 361 Substrate.
Binding site: 364 364 Substrate.
Binding site: 366 366 Substrate.
Protein Length
570 AA.
Protein Sequence
(Canonical)
MRRRSRMLLC FALLWVLGIA YYMYSGGGSA LAAGGGGAGR KGDWNDIDSI KKKDLHHSRG  60
DEKAQGVETL PPGKVRWPDF NQEAYVGGTM VRSGQDPYAR NKFNQVESDK LHMDRGIPDT  120
RHDQCQRKQW RVDLPATSVV ITFHNEARSA LLRTVVSVLK RSPPHLIKEI ILVDDYSNDP  180
EDGALLGKIE KVRVLRNDRR EGLMRSRVRG ADAAQAKVLT FLDSHCECNE RWLEPLLERV  240
AEDRTRVVSP IIDVINMDNF QYVGASADLK GGFDWNLVFK WDYMTPEQRR SRQGNPVAPI  300
KTPMIAGGLF VMDKLYFEEL GKYDMMMDVW GGENLEISFR VWQCGGSLEI IPCSRVGHVF  360
RKQHPYTFPG GSGTVFARNT RRAAEVWMDE YKHFYYAAVP SARNVPYGNI QSRLELRKKL  420
GCKPFKWYLD NVYPELRVPD HQDIAFGALQ QGTNCLDTLG HFADGVVGIY ECHNAGGNQE  480
WALTKEKSVK HMDLCLTVVD RSPGSLIRLQ GCRENDSRQK WEQIEGNSKL RHVGSNLCLD  540
SRTAKSGGLS VEVCGPALSQ QWKFSLNLQQ                                   570
FASTA
(Canonical)
>LipidDB-10090-00232|Q6PB93
MRRRSRMLLCFALLWVLGIAYYMYSGGGSALAAGGGGAGRKGDWNDIDSIKKKDLHHSRG
DEKAQGVETLPPGKVRWPDFNQEAYVGGTMVRSGQDPYARNKFNQVESDKLHMDRGIPDT
RHDQCQRKQWRVDLPATSVVITFHNEARSALLRTVVSVLKRSPPHLIKEIILVDDYSNDP
EDGALLGKIEKVRVLRNDRREGLMRSRVRGADAAQAKVLTFLDSHCECNERWLEPLLERV
AEDRTRVVSPIIDVINMDNFQYVGASADLKGGFDWNLVFKWDYMTPEQRRSRQGNPVAPI
KTPMIAGGLFVMDKLYFEELGKYDMMMDVWGGENLEISFRVWQCGGSLEIIPCSRVGHVF
RKQHPYTFPGGSGTVFARNTRRAAEVWMDEYKHFYYAAVPSARNVPYGNIQSRLELRKKL
GCKPFKWYLDNVYPELRVPDHQDIAFGALQQGTNCLDTLGHFADGVVGIYECHNAGGNQE
WALTKEKSVKHMDLCLTVVDRSPGSLIRLQGCRENDSRQKWEQIEGNSKLRHVGSNLCLD
SRTAKSGGLSVEVCGPALSQQWKFSLNLQQ
Gene Ontology
GO:0005576; C:extracellular region; IEA:UniProtKB-KW
GO:0005796; C:Golgi lumen; TAS:MGI
GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW
GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW
GO:0030145; F:manganese ion binding; ISS:UniProtKB
GO:0004653; F:polypeptide N-acetylgalactosaminyltransferase activity; ISS:UniProtKB
GO:0006493; P:protein O-linked glycosylation; ISS:UniProtKB
Interpro
InterPro; IPR001173; Glyco_trans_2-like
InterPro; IPR029044; Nucleotide-diphossugar_trans
InterPro; IPR000772; Ricin_B_lectin
Pfam
Pfam; PF00535; Glycos_transf_2;
Pfam; PF00652; Ricin_B_lectin;
SMART
SMART; SM00458; RICIN;
PROSITE
PROSITE; PS50231; RICIN_B_LECTIN;
PRINTS