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Protein

Polypeptide N-acetylgalactosaminyltransferase 12

Gene

Galnt12

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

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).By similarity

Catalytic activityi

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

Cofactori

Mn2+By similarity

Pathway:iprotein glycosylation

This protein is involved in the pathway protein glycosylation, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein glycosylation and in Protein modification.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei171 – 1711SubstrateBy similarity
Binding sitei200 – 2001SubstrateBy similarity
Metal bindingi223 – 2231ManganeseBy similarity
Metal bindingi225 – 2251ManganeseBy similarity
Binding sitei330 – 3301SubstrateBy similarity
Metal bindingi358 – 3581ManganeseBy similarity
Binding sitei366 – 3661SubstrateBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Ligandi

Lectin, Manganese, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_278772. O-linked glycosylation of mucins.
UniPathwayiUPA00378.

Protein family/group databases

CAZyiCBM13. Carbohydrate-Binding Module Family 13.
GT27. Glycosyltransferase Family 27.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:Galnt12
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 4

Organism-specific databases

MGIiMGI:2444664. Galnt12.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1919CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei20 – 3718Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST
Topological domaini38 – 576539LumenalSequence AnalysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 576576Polypeptide N-acetylgalactosaminyltransferase 12PRO_0000059129Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi120 ↔ 353PROSITE-ProRule annotation
Disulfide bondi344 ↔ 417PROSITE-ProRule annotation
Disulfide bondi453 ↔ 474PROSITE-ProRule annotation
Disulfide bondi501 ↔ 516PROSITE-ProRule annotation
Disulfide bondi542 ↔ 561PROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond

Proteomic databases

MaxQBiQ8BGT9.
PRIDEiQ8BGT9.

Expressioni

Gene expression databases

BgeeiQ8BGT9.
ExpressionAtlasiQ8BGT9. baseline and differential.
GenevisibleiQ8BGT9. MM.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000045721.

Structurei

3D structure databases

ProteinModelPortaliQ8BGT9.
SMRiQ8BGT9. Positions 83-545.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini440 – 572133Ricin B-type lectinPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni130 – 239110Catalytic subdomain AAdd
BLAST
Regioni299 – 36163Catalytic subdomain BAdd
BLAST

Domaini

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 similaritiesi

Contains 1 ricin B-type lectin domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG239675.
GeneTreeiENSGT00760000118828.
HOGENOMiHOG000038227.
HOVERGENiHBG051699.
InParanoidiQ8BGT9.
KOiK00710.
OMAiEIRYNTH.
OrthoDBiEOG7J9VP2.
PhylomeDBiQ8BGT9.
TreeFamiTF352660.

Family and domain databases

Gene3Di3.90.550.10. 1 hit.
InterProiIPR001173. Glyco_trans_2-like.
IPR029044. Nucleotide-diphossugar_trans.
IPR000772. Ricin_B_lectin.
[Graphical view]
PfamiPF00535. Glycos_transf_2. 1 hit.
PF00652. Ricin_B_lectin. 1 hit.
[Graphical view]
SMARTiSM00458. RICIN. 1 hit.
[Graphical view]
SUPFAMiSSF50370. SSF50370. 1 hit.
SSF53448. SSF53448. 1 hit.
PROSITEiPS50231. RICIN_B_LECTIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8BGT9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MWGRAVRRRC PRGLRRGREA LLALLALAGL GALLRARSRS GTVDPGPPRT
60 70 80 90 100
PLPGRHEPVL PRPPLPADAL GAHGEAVRLQ LQGEELRLQE ESVKQHQINI
110 120 130 140 150
YLSDRISLHR RLPERWNPLC REVKYDYDNL PKTSVVIAFY NEAWSTLLRT
160 170 180 190 200
VYSVLETSPD ILLEEVILVD DYSDREHLKE RLANELSQLP KVRLIRASRR
210 220 230 240 250
EGLVRARLLG ASAARGEVLT FLDCHCECHE GWLEPLLQRI HEKESAVVCP
260 270 280 290 300
VIDVIDWNTF EYLGNSGEPQ IGGFDWRLVF TWHVVPQRER QSMRSPIDVI
310 320 330 340 350
RSPTMAGGLF AVSKRYFDYL GSYDTGMEVW GGENLEFSFR IWQCGGTLET
360 370 380 390 400
HPCSHVGHVF PKQAPYSRSK ALANSVRAAE VWMDEFKELY YHRNPQARLE
410 420 430 440 450
PFGDVTERKK LRAKLQCKDF KWFLDTVYPE LHVPEDRPGF FGMLQNRGLR
460 470 480 490 500
GYCLDYNPPN ENHVEGHQVL LYLCHGMGQN QFFEYTTRKE IRYNTRQPEA
510 520 530 540 550
CITVEDGKDT LVMDLCRETV PENQEFILQE DGTLVHKHSR KCVEATEKVL
560 570
DNGFAPYLRD CTNSDNQRWF FKERMS
Length:576
Mass (Da):66,541
Last modified:March 1, 2003 - v1
Checksum:i706310A99FCDACD5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK033638 mRNA. Translation: BAC28401.1.
AK042133 mRNA. Translation: BAC31179.1.
BC056425 mRNA. Translation: AAH56425.1.
CCDSiCCDS18158.1.
RefSeqiNP_766281.1. NM_172693.3.
UniGeneiMm.132246.

Genome annotation databases

EnsembliENSMUST00000045041; ENSMUSP00000045721; ENSMUSG00000039774.
GeneIDi230145.
KEGGimmu:230145.
UCSCiuc008suk.1. mouse.

Cross-referencesi

Web resourcesi

Functional Glycomics Gateway - GTase

Polypeptide N-acetylgalactosaminyltransferase 12

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK033638 mRNA. Translation: BAC28401.1.
AK042133 mRNA. Translation: BAC31179.1.
BC056425 mRNA. Translation: AAH56425.1.
CCDSiCCDS18158.1.
RefSeqiNP_766281.1. NM_172693.3.
UniGeneiMm.132246.

3D structure databases

ProteinModelPortaliQ8BGT9.
SMRiQ8BGT9. Positions 83-545.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000045721.

Protein family/group databases

CAZyiCBM13. Carbohydrate-Binding Module Family 13.
GT27. Glycosyltransferase Family 27.

Proteomic databases

MaxQBiQ8BGT9.
PRIDEiQ8BGT9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000045041; ENSMUSP00000045721; ENSMUSG00000039774.
GeneIDi230145.
KEGGimmu:230145.
UCSCiuc008suk.1. mouse.

Organism-specific databases

CTDi79695.
MGIiMGI:2444664. Galnt12.

Phylogenomic databases

eggNOGiNOG239675.
GeneTreeiENSGT00760000118828.
HOGENOMiHOG000038227.
HOVERGENiHBG051699.
InParanoidiQ8BGT9.
KOiK00710.
OMAiEIRYNTH.
OrthoDBiEOG7J9VP2.
PhylomeDBiQ8BGT9.
TreeFamiTF352660.

Enzyme and pathway databases

UniPathwayiUPA00378.
ReactomeiREACT_278772. O-linked glycosylation of mucins.

Miscellaneous databases

ChiTaRSiGalnt12. mouse.
NextBioi379814.
PROiQ8BGT9.
SOURCEiSearch...

Gene expression databases

BgeeiQ8BGT9.
ExpressionAtlasiQ8BGT9. baseline and differential.
GenevisibleiQ8BGT9. MM.

Family and domain databases

Gene3Di3.90.550.10. 1 hit.
InterProiIPR001173. Glyco_trans_2-like.
IPR029044. Nucleotide-diphossugar_trans.
IPR000772. Ricin_B_lectin.
[Graphical view]
PfamiPF00535. Glycos_transf_2. 1 hit.
PF00652. Ricin_B_lectin. 1 hit.
[Graphical view]
SMARTiSM00458. RICIN. 1 hit.
[Graphical view]
SUPFAMiSSF50370. SSF50370. 1 hit.
SSF53448. SSF53448. 1 hit.
PROSITEiPS50231. RICIN_B_LECTIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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.
    , 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.

Entry informationi

Entry nameiGLT12_MOUSE
AccessioniPrimary (citable) accession number: Q8BGT9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: March 1, 2003
Last modified: July 22, 2015
This is version 107 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.