| Tag |
Content |
LipidDB ID |
LipidDB-10090-01219 |
Entry Name |
|
UniProt Accession |
|
Theoretical PI |
6.84 |
Molecular Weight |
66540.8 |
Genbank Protein ID |
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Genbank Nucleotide ID |
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Protein Name |
Polypeptide N-acetylgalactosaminyltransferase 12 |
Protein Synonyms/Alias |
2.4.1.41; Polypeptide GalNAc transferase 12; GalNAc-T12; pp-GaNTase 12; Protein-UDP acetylgalactosaminyltransferase 12; UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 12; |
Gene Name |
Galnt12 |
Gene Synonyms/Alias |
|
Created Date |
16-AUG-2004 |
| Lipid Modification Sites |
|---|
| Position |
Sequence Form |
Peptide |
References |
Modification Type |
10 | Canonical | GRAVRRRCPRGLRRG | [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 activity toward non-glycosylated peptides such as Muc5AC, Muc1a and EA2, and no detectable activity with Muc2 and Muc7. Displays enzymatic activity toward the Gal-NAc- Muc5AC glycopeptide, but no detectable activity to mono-GalNAc- glycosylated Muc1a, Muc2, Muc7 and EA2. May play an important role in the initial step of mucin-type oligosaccharide biosynthesis in digestive organs (By similarity). |
Sequence Annotation |
Topological domain: 1 19 Cytoplasmic.
Transmembrane: 20 37 Helical; Signal-anchor for type IImembrane protein.
Topological domain: 38 576 Lumenal.
Domain: 440 572 Ricin B-type lectin.
Region: 130 239 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: 171 171 Substrate.
Binding site: 200 200 Substrate.
Binding site: 330 330 Substrate.
Binding site: 366 366 Substrate.
|
Protein Length |
576 AA. |
Protein Sequence
(Canonical) |
MWGRAVRRRC PRGLRRGREA LLALLALAGL GALLRARSRS GTVDPGPPRT PLPGRHEPVL 60
PRPPLPADAL GAHGEAVRLQ LQGEELRLQE ESVKQHQINI YLSDRISLHR RLPERWNPLC 120
REVKYDYDNL PKTSVVIAFY NEAWSTLLRT VYSVLETSPD ILLEEVILVD DYSDREHLKE 180
RLANELSQLP KVRLIRASRR EGLVRARLLG ASAARGEVLT FLDCHCECHE GWLEPLLQRI 240
HEKESAVVCP VIDVIDWNTF EYLGNSGEPQ IGGFDWRLVF TWHVVPQRER QSMRSPIDVI 300
RSPTMAGGLF AVSKRYFDYL GSYDTGMEVW GGENLEFSFR IWQCGGTLET HPCSHVGHVF 360
PKQAPYSRSK ALANSVRAAE VWMDEFKELY YHRNPQARLE PFGDVTERKK LRAKLQCKDF 420
KWFLDTVYPE LHVPEDRPGF FGMLQNRGLR GYCLDYNPPN ENHVEGHQVL LYLCHGMGQN 480
QFFEYTTRKE IRYNTRQPEA CITVEDGKDT LVMDLCRETV PENQEFILQE DGTLVHKHSR 540
KCVEATEKVL DNGFAPYLRD CTNSDNQRWF FKERMS 576
|
FASTA
(Canonical) |
>LipidDB-10090-01219|Q8BGT9
MWGRAVRRRCPRGLRRGREALLALLALAGLGALLRARSRSGTVDPGPPRTPLPGRHEPVL
PRPPLPADALGAHGEAVRLQLQGEELRLQEESVKQHQINIYLSDRISLHRRLPERWNPLC
REVKYDYDNLPKTSVVIAFYNEAWSTLLRTVYSVLETSPDILLEEVILVDDYSDREHLKE
RLANELSQLPKVRLIRASRREGLVRARLLGASAARGEVLTFLDCHCECHEGWLEPLLQRI
HEKESAVVCPVIDVIDWNTFEYLGNSGEPQIGGFDWRLVFTWHVVPQRERQSMRSPIDVI
RSPTMAGGLFAVSKRYFDYLGSYDTGMEVWGGENLEFSFRIWQCGGTLETHPCSHVGHVF
PKQAPYSRSKALANSVRAAEVWMDEFKELYYHRNPQARLEPFGDVTERKKLRAKLQCKDF
KWFLDTVYPELHVPEDRPGFFGMLQNRGLRGYCLDYNPPNENHVEGHQVLLYLCHGMGQN
QFFEYTTRKEIRYNTRQPEACITVEDGKDTLVMDLCRETVPENQEFILQEDGTLVHKHSR
KCVEATEKVLDNGFAPYLRDCTNSDNQRWFFKERMS
|
Gene Ontology |
GO:0005794; C:Golgi apparatus; IEA:UniProtKB-KW GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW GO:0046872; F:metal ion binding; IEA:UniProtKB-KW GO:0004653; F:polypeptide N-acetylgalactosaminyltransferase activity; IEA:UniProtKB-EC GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway |
Interpro |
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Pfam |
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SMART |
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PROSITE |
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PRINTS |
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