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Q8BGT9 (GLT12_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 88. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Polypeptide N-acetylgalactosaminyltransferase 12
EC=2.4.1.41
Alternative name(s):
Polypeptide GalNAc transferase 12
Short name=GalNAc-T12
Short name=pp-GaNTase 12
Protein-UDP acetylgalactosaminyltransferase 12
UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 12
Gene names
Name:Galnt12
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length576 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

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 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.

Catalytic activity

UDP-N-acetyl-alpha-D-galactosamine + polypeptide = UDP + N-acetyl-alpha-D-galactosaminyl-polypeptide.

Cofactor

Manganese By similarity.

Calcium By similarity.

Pathway

Protein modification; protein glycosylation.

Subcellular location

Golgi apparatus membrane; Single-pass type II membrane protein By similarity.

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 By similarity.

The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity By similarity.

Sequence similarities

Belongs to the glycosyltransferase 2 family. GalNAc-T subfamily.

Contains 1 ricin B-type lectin domain.

Ontologies

Keywords
   Cellular componentGolgi apparatus
Membrane
   DomainSignal-anchor
Transmembrane
Transmembrane helix
   LigandCalcium
Lectin
Manganese
   Molecular functionGlycosyltransferase
Transferase
   PTMDisulfide bond
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processprotein glycosylation

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentGolgi membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

integral to membrane

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionpolypeptide N-acetylgalactosaminyltransferase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 576576Polypeptide N-acetylgalactosaminyltransferase 12
PRO_0000059129

Regions

Topological domain1 – 1919Cytoplasmic Potential
Transmembrane20 – 3718Helical; Signal-anchor for type II membrane protein; Potential
Topological domain38 – 576539Lumenal Potential
Domain440 – 572133Ricin B-type lectin
Region130 – 239110Catalytic subdomain A
Region299 – 36163Catalytic subdomain B

Amino acid modifications

Disulfide bond453 ↔ 474 By similarity
Disulfide bond501 ↔ 516 By similarity
Disulfide bond542 ↔ 561 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8BGT9 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: 706310A99FCDACD5

FASTA57666,541
        10         20         30         40         50         60 
MWGRAVRRRC PRGLRRGREA LLALLALAGL GALLRARSRS GTVDPGPPRT PLPGRHEPVL 

        70         80         90        100        110        120 
PRPPLPADAL GAHGEAVRLQ LQGEELRLQE ESVKQHQINI YLSDRISLHR RLPERWNPLC 

       130        140        150        160        170        180 
REVKYDYDNL PKTSVVIAFY NEAWSTLLRT VYSVLETSPD ILLEEVILVD DYSDREHLKE 

       190        200        210        220        230        240 
RLANELSQLP KVRLIRASRR EGLVRARLLG ASAARGEVLT FLDCHCECHE GWLEPLLQRI 

       250        260        270        280        290        300 
HEKESAVVCP VIDVIDWNTF EYLGNSGEPQ IGGFDWRLVF TWHVVPQRER QSMRSPIDVI 

       310        320        330        340        350        360 
RSPTMAGGLF AVSKRYFDYL GSYDTGMEVW GGENLEFSFR IWQCGGTLET HPCSHVGHVF 

       370        380        390        400        410        420 
PKQAPYSRSK ALANSVRAAE VWMDEFKELY YHRNPQARLE PFGDVTERKK LRAKLQCKDF 

       430        440        450        460        470        480 
KWFLDTVYPE LHVPEDRPGF FGMLQNRGLR GYCLDYNPPN ENHVEGHQVL LYLCHGMGQN 

       490        500        510        520        530        540 
QFFEYTTRKE IRYNTRQPEA CITVEDGKDT LVMDLCRETV PENQEFILQE DGTLVHKHSR 

       550        560        570 
KCVEATEKVL DNGFAPYLRD CTNSDNQRWF FKERMS

« Hide

References

[1]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Cecum and Thymus.
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6.
Tissue: Brain.
+Additional computationally mapped references.

Web resources

Functional Glycomics Gateway - GTase

Polypeptide N-acetylgalactosaminyltransferase 12

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AK033638 mRNA. Translation: BAC28401.1.
AK042133 mRNA. Translation: BAC31179.1.
BC056425 mRNA. Translation: AAH56425.1.
IPIIPI00221718.
RefSeqNP_766281.1. NM_172693.3.
UniGeneMm.132246.

3D structure databases

ProteinModelPortalQ8BGT9.
SMRQ8BGT9. Positions 83-569.
ModBaseSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000045721.

Protein family/group databases

CAZyCBM13. Carbohydrate-Binding Module Family 13.
GT27. Glycosyltransferase Family 27.

Proteomic databases

PRIDEQ8BGT9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000045041; ENSMUSP00000045721; ENSMUSG00000039774.
GeneID230145.
KEGGmmu:230145.
UCSCuc008suk.1. mouse.

Organism-specific databases

CTD79695.
MGIMGI:2444664. Galnt12.

Phylogenomic databases

eggNOGNOG239675.
GeneTreeENSGT00700000104138.
HOGENOMHOG000038227.
HOVERGENHBG051699.
InParanoidQ8BGT9.
KOK00710.
OMAQKWFFKE.
OrthoDBEOG43JC4G.

Enzyme and pathway databases

UniPathwayUPA00378.

Gene expression databases

ArrayExpressQ8BGT9.
BgeeQ8BGT9.
GenevestigatorQ8BGT9.
GermOnlineENSMUSG00000039774. Mus musculus.

Family and domain databases

InterProIPR001173. Glyco_trans_2.
IPR000772. Ricin_B_lectin.
[Graphical view]
PfamPF00535. Glycos_transf_2. 1 hit.
PF00652. Ricin_B_lectin. 1 hit.
[Graphical view]
SMARTSM00458. RICIN. 1 hit.
[Graphical view]
SUPFAMSSF50370. RicinB_like. 1 hit.
PROSITEPS50231. RICIN_B_LECTIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSGALNT12. mouse.
NextBio379814.
SOURCESearch...

Entry information

Entry nameGLT12_MOUSE
AccessionPrimary (citable) accession number: Q8BGT9
Entry history
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: March 1, 2003
Last modified: May 29, 2013
This is version 88 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·Documents