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Q8BGT9

- GLT12_MOUSE

UniProt

Q8BGT9 - GLT12_MOUSE

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Protein
Polypeptide N-acetylgalactosaminyltransferase 12
Gene
Galnt12
Organism
Mus musculus (Mouse)
Status
Reviewed - 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.

Catalytic activityi

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

Cofactori

Manganese By similarity.

Pathwayi

Sites

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

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. polypeptide N-acetylgalactosaminyltransferase activity Source: UniProtKB-EC

GO - Biological processi

  1. protein glycosylation Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Ligandi

Lectin, Manganese, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_198517. 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: Chromosome 4

Organism-specific databases

MGIiMGI:2444664. Galnt12.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1919Cytoplasmic Reviewed prediction
Add
BLAST
Transmembranei20 – 3718Helical; Signal-anchor for type II membrane protein; Reviewed prediction
Add
BLAST
Topological domaini38 – 576539Lumenal Reviewed prediction
Add
BLAST

GO - Cellular componenti

  1. Golgi membrane Source: UniProtKB-SubCell
  2. integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus, Membrane

PTM / Processingi

Molecule processing

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

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi120 ↔ 353 By similarity
Disulfide bondi344 ↔ 417 By similarity
Disulfide bondi453 ↔ 474 By similarity
Disulfide bondi501 ↔ 516 By similarity
Disulfide bondi542 ↔ 561 By similarity

Keywords - PTMi

Disulfide bond

Proteomic databases

MaxQBiQ8BGT9.
PRIDEiQ8BGT9.

Expressioni

Gene expression databases

ArrayExpressiQ8BGT9.
BgeeiQ8BGT9.
GenevestigatoriQ8BGT9.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000045721.

Structurei

3D structure databases

ProteinModelPortaliQ8BGT9.
SMRiQ8BGT9. Positions 83-569.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini440 – 572133Ricin B-type lectin
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni130 – 239110Catalytic subdomain A
Add
BLAST
Regioni299 – 36163Catalytic subdomain B
Add
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

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG239675.
GeneTreeiENSGT00750000117451.
HOGENOMiHOG000038227.
HOVERGENiHBG051699.
InParanoidiQ8BGT9.
KOiK00710.
OMAiKELYYHR.
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

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MWGRAVRRRC PRGLRRGREA LLALLALAGL GALLRARSRS GTVDPGPPRT    50
PLPGRHEPVL PRPPLPADAL GAHGEAVRLQ LQGEELRLQE ESVKQHQINI 100
YLSDRISLHR RLPERWNPLC REVKYDYDNL PKTSVVIAFY NEAWSTLLRT 150
VYSVLETSPD ILLEEVILVD DYSDREHLKE RLANELSQLP KVRLIRASRR 200
EGLVRARLLG ASAARGEVLT FLDCHCECHE GWLEPLLQRI HEKESAVVCP 250
VIDVIDWNTF EYLGNSGEPQ IGGFDWRLVF TWHVVPQRER QSMRSPIDVI 300
RSPTMAGGLF AVSKRYFDYL GSYDTGMEVW GGENLEFSFR IWQCGGTLET 350
HPCSHVGHVF PKQAPYSRSK ALANSVRAAE VWMDEFKELY YHRNPQARLE 400
PFGDVTERKK LRAKLQCKDF KWFLDTVYPE LHVPEDRPGF FGMLQNRGLR 450
GYCLDYNPPN ENHVEGHQVL LYLCHGMGQN QFFEYTTRKE IRYNTRQPEA 500
CITVEDGKDT LVMDLCRETV PENQEFILQE DGTLVHKHSR KCVEATEKVL 550
DNGFAPYLRD CTNSDNQRWF FKERMS 576
Length:576
Mass (Da):66,541
Last modified:March 1, 2003 - v1
Checksum:i706310A99FCDACD5
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
AK033638 mRNA. Translation: BAC28401.1 .
AK042133 mRNA. Translation: BAC31179.1 .
BC056425 mRNA. Translation: AAH56425.1 .
CCDSi CCDS18158.1.
RefSeqi NP_766281.1. NM_172693.3.
UniGenei Mm.132246.

3D structure databases

ProteinModelPortali Q8BGT9.
SMRi Q8BGT9. Positions 83-569.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 10090.ENSMUSP00000045721.

Protein family/group databases

CAZyi CBM13. Carbohydrate-Binding Module Family 13.
GT27. Glycosyltransferase Family 27.

Proteomic databases

MaxQBi Q8BGT9.
PRIDEi Q8BGT9.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000045041 ; ENSMUSP00000045721 ; ENSMUSG00000039774 .
GeneIDi 230145.
KEGGi mmu:230145.
UCSCi uc008suk.1. mouse.

Organism-specific databases

CTDi 79695.
MGIi MGI:2444664. Galnt12.

Phylogenomic databases

eggNOGi NOG239675.
GeneTreei ENSGT00750000117451.
HOGENOMi HOG000038227.
HOVERGENi HBG051699.
InParanoidi Q8BGT9.
KOi K00710.
OMAi KELYYHR.
OrthoDBi EOG7J9VP2.
PhylomeDBi Q8BGT9.
TreeFami TF352660.

Enzyme and pathway databases

UniPathwayi UPA00378 .
Reactomei REACT_198517. O-linked glycosylation of mucins.

Miscellaneous databases

ChiTaRSi GALNT12. mouse.
NextBioi 379814.
PROi Q8BGT9.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q8BGT9.
Bgeei Q8BGT9.
Genevestigatori Q8BGT9.

Family and domain databases

Gene3Di 3.90.550.10. 1 hit.
InterProi IPR001173. Glyco_trans_2-like.
IPR029044. Nucleotide-diphossugar_trans.
IPR000772. Ricin_B_lectin.
[Graphical view ]
Pfami PF00535. Glycos_transf_2. 1 hit.
PF00652. Ricin_B_lectin. 1 hit.
[Graphical view ]
SMARTi SM00458. RICIN. 1 hit.
[Graphical view ]
SUPFAMi SSF50370. SSF50370. 1 hit.
SSF53448. SSF53448. 1 hit.
PROSITEi PS50231. RICIN_B_LECTIN. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: September 3, 2014
This is version 100 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

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