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Q921L8

- GLT11_MOUSE

UniProt

Q921L8 - GLT11_MOUSE

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Protein

Polypeptide N-acetylgalactosaminyltransferase 11

Gene

Galnt11

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

Functioni

Polypeptide N-acetylgalactosaminyltransferase that catalyzes the initiation of protein O-linked glycosylation and is involved in left/right asymmetry by mediating O-glycosylation of NOTCH1. O-glycosylation of NOTCH1 promotes activation of NOTCH1, modulating the balance between motile and immotile (sensory) cilia at the left-right organiser (LRO). Polypeptide N-acetylgalactosaminyltransferases catalyze the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. Displays the same enzyme activity toward MUC1, MUC4, and EA2 than GALNT1. Not involved in glycosylation of erythropoietin (EPO) By similarity.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 sitei191 – 1911SubstrateBy similarity
Binding sitei222 – 2221SubstrateBy similarity
Metal bindingi245 – 2451ManganeseBy similarity
Binding sitei246 – 2461SubstrateBy similarity
Metal bindingi247 – 2471ManganeseBy similarity
Binding sitei350 – 3501SubstrateBy similarity
Metal bindingi378 – 3781ManganeseBy similarity
Binding sitei381 – 3811SubstrateBy similarity
Binding sitei386 – 3861SubstrateBy similarity

GO - Molecular functioni

  1. carbohydrate binding Source: UniProtKB-KW
  2. metal ion binding Source: UniProtKB-KW
  3. Notch binding Source: UniProtKB
  4. polypeptide N-acetylgalactosaminyltransferase activity Source: UniProtKB

GO - Biological processi

  1. cilium morphogenesis Source: UniProtKB
  2. determination of left/right symmetry Source: UniProtKB
  3. Notch receptor processing Source: UniProtKB
  4. Notch signaling involved in heart development Source: UniProtKB
  5. protein O-linked glycosylation via threonine Source: UniProtKB
  6. regulation of Notch signaling pathway Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Biological processi

Notch signaling pathway

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 11 (EC:2.4.1.41)
Alternative name(s):
Polypeptide GalNAc transferase 11
Short name:
GalNAc-T11
Short name:
pp-GaNTase 11
Protein-UDP acetylgalactosaminyltransferase 11
UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 11
Gene namesi
Name:Galnt11
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 5

Organism-specific databases

MGIiMGI:2444392. Galnt11.

Subcellular locationi

GO - Cellular componenti

  1. Golgi apparatus Source: UniProtKB-KW
  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 – 608608Polypeptide N-acetylgalactosaminyltransferase 11PRO_0000059126Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi141 ↔ 373PROSITE-ProRule annotation
Disulfide bondi364 ↔ 441PROSITE-ProRule annotation
Glycosylationi423 – 4231N-linked (GlcNAc...)Sequence Analysis
Glycosylationi428 – 4281N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi493 ↔ 512PROSITE-ProRule annotation
Disulfide bondi536 ↔ 553PROSITE-ProRule annotation
Disulfide bondi578 ↔ 596PROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiQ921L8.
PaxDbiQ921L8.
PRIDEiQ921L8.

PTM databases

PhosphoSiteiQ921L8.

Expressioni

Tissue specificityi

Mainly expressed in kidney. Weakly expressed in other tissues.1 Publication

Developmental stagei

At E8.0, present in the left-right organiser (LRO) node, with enrichment in crown cells compared to pit cells (at protein level).1 Publication

Gene expression databases

BgeeiQ921L8.
ExpressionAtlasiQ921L8. baseline and differential.
GenevestigatoriQ921L8.

Interactioni

Subunit structurei

Interacts with NOTCH1.By similarity

Protein-protein interaction databases

IntActiQ921L8. 2 interactions.
MINTiMINT-4096164.

Structurei

3D structure databases

ProteinModelPortaliQ921L8.
SMRiQ921L8. Positions 114-606.
ModBaseiSearch...
MobiDBiSearch...

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 66CytoplasmicSequence Analysis
Topological domaini30 – 608579LumenalSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei7 – 2923Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini476 – 607132Ricin B-type lectinPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni150 – 261112Catalytic subdomain AAdd
BLAST
Regioni319 – 38163Catalytic 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.
InParanoidiQ921L8.
KOiK00710.
OMAiMIFNERD.
OrthoDBiEOG7J9VP2.
PhylomeDBiQ921L8.
TreeFamiTF313267.

Family and domain databases

Gene3Di3.90.550.10. 1 hit.
InterProiIPR027791. Galactosyl_T_C.
IPR001173. Glyco_trans_2-like.
IPR029044. Nucleotide-diphossugar_trans.
IPR000772. Ricin_B_lectin.
[Graphical view]
PfamiPF02709. Glyco_transf_7C. 1 hit.
PF00535. Glycos_transf_2. 1 hit.
PF00652. Ricin_B_lectin. 1 hit.
[Graphical view]
SMARTiSM00458. RICIN. 1 hit.
[Graphical view]
SUPFAMiSSF50370. SSF50370. 2 hits.
SSF53448. SSF53448. 1 hit.
PROSITEiPS50231. RICIN_B_LECTIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q921L8-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MGSITVRYFC YGCLFTSATW TVLLFIYFNF SEVTQPLRNV PIKGSGPHGP
60 70 80 90 100
FPKKFYPRFT RGPGRVLDPQ FKANRIDRLM NNHIEDPDKG LSKSSSELGM
110 120 130 140 150
IFNERDQELR DLGYQKHAFN MLISNRLGYH RDVPDTRNAE CRRKSYPTDL
160 170 180 190 200
PTASIVICFY NEAFSALLRT VHSVVDRTPA HLLHEIILVD DSSDFDDLKG
210 220 230 240 250
ELDEYIQRYL PAKVKVIRNM KREGLIRGRM IGAAHATGEV LVFLDSHCEV
260 270 280 290 300
NVMWLQPLLA IILEDPHTVV CPVIDIISAD TLAYSSSPVV RGGFNWGLHF
310 320 330 340 350
KWDLVPVSEL GGPDGATAPI RSPTMAGGLF AMNRQYFNDL GQYDSGMDIW
360 370 380 390 400
GGENLEISFR IWMCGGKLFI LPCSRVGHIF RKRRPYGSPE GQDTMTHNSL
410 420 430 440 450
RLAHVWLDEY KEQYFSLRPD LKNKSFGNIS ERVELRKKLG CQSFKWYLDN
460 470 480 490 500
IYPEMQIPGP NAKPQQPVLI NRGPKRPRVL QRGRLYHLQT NKCLVAQGRS
510 520 530 540 550
SQKGGLVLLK TCDYGDPTQV WIYNEDHELI LNNLLCLDMS ETRSSDPPRL
560 570 580 590 600
MKCHGSGGSQ QWTFGKNNRL YQVSVGQCLR VMDLMDQKGY VGMAICDGSS

SQQWRLEG
Length:608
Mass (Da):69,201
Last modified:December 1, 2001 - v1
Checksum:i0E452FDA1CA5668B
GO

Sequence cautioni

The sequence AAH34184.1 differs from that shown. Reason: Erroneous termination at position 412. Translated as Glu.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti545 – 5451S → L in BAC40096. (PubMed:16141072)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Y12435 mRNA. Translation: CAC79626.1.
AF495528 mRNA. Translation: AAQ06668.1.
AK088014 mRNA. Translation: BAC40096.1.
AK161524 mRNA. Translation: BAE36442.1.
BC011428 mRNA. Translation: AAH11428.1.
BC021504 mRNA. Translation: AAH21504.1.
BC034184 mRNA. Translation: AAH34184.1. Sequence problems.
BC034185 mRNA. Translation: AAH34185.1.
BC036143 mRNA. Translation: AAH36143.1.
BC036145 mRNA. Translation: AAH36145.1.
CCDSiCCDS19133.1.
RefSeqiNP_659157.1. NM_144908.3.
XP_006535744.1. XM_006535681.1.
UniGeneiMm.246718.

Genome annotation databases

EnsembliENSMUST00000045737; ENSMUSP00000036240; ENSMUSG00000038072.
ENSMUST00000114950; ENSMUSP00000110600; ENSMUSG00000038072.
ENSMUST00000114952; ENSMUSP00000110602; ENSMUSG00000038072.
GeneIDi231050.
KEGGimmu:231050.
UCSCiuc008wss.1. mouse.

Cross-referencesi

Web resourcesi

Functional Glycomics Gateway - GTase

Polypeptide N-acetylgalactosaminyltransferase 11

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Y12435 mRNA. Translation: CAC79626.1 .
AF495528 mRNA. Translation: AAQ06668.1 .
AK088014 mRNA. Translation: BAC40096.1 .
AK161524 mRNA. Translation: BAE36442.1 .
BC011428 mRNA. Translation: AAH11428.1 .
BC021504 mRNA. Translation: AAH21504.1 .
BC034184 mRNA. Translation: AAH34184.1 . Sequence problems.
BC034185 mRNA. Translation: AAH34185.1 .
BC036143 mRNA. Translation: AAH36143.1 .
BC036145 mRNA. Translation: AAH36145.1 .
CCDSi CCDS19133.1.
RefSeqi NP_659157.1. NM_144908.3.
XP_006535744.1. XM_006535681.1.
UniGenei Mm.246718.

3D structure databases

ProteinModelPortali Q921L8.
SMRi Q921L8. Positions 114-606.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi Q921L8. 2 interactions.
MINTi MINT-4096164.

Protein family/group databases

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

PTM databases

PhosphoSitei Q921L8.

Proteomic databases

MaxQBi Q921L8.
PaxDbi Q921L8.
PRIDEi Q921L8.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000045737 ; ENSMUSP00000036240 ; ENSMUSG00000038072 .
ENSMUST00000114950 ; ENSMUSP00000110600 ; ENSMUSG00000038072 .
ENSMUST00000114952 ; ENSMUSP00000110602 ; ENSMUSG00000038072 .
GeneIDi 231050.
KEGGi mmu:231050.
UCSCi uc008wss.1. mouse.

Organism-specific databases

CTDi 63917.
MGIi MGI:2444392. Galnt11.

Phylogenomic databases

eggNOGi NOG239675.
GeneTreei ENSGT00760000118828.
HOGENOMi HOG000038227.
HOVERGENi HBG051699.
InParanoidi Q921L8.
KOi K00710.
OMAi MIFNERD.
OrthoDBi EOG7J9VP2.
PhylomeDBi Q921L8.
TreeFami TF313267.

Enzyme and pathway databases

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

Miscellaneous databases

ChiTaRSi GALNT11. mouse.
NextBioi 380378.
PROi Q921L8.
SOURCEi Search...

Gene expression databases

Bgeei Q921L8.
ExpressionAtlasi Q921L8. baseline and differential.
Genevestigatori Q921L8.

Family and domain databases

Gene3Di 3.90.550.10. 1 hit.
InterProi IPR027791. Galactosyl_T_C.
IPR001173. Glyco_trans_2-like.
IPR029044. Nucleotide-diphossugar_trans.
IPR000772. Ricin_B_lectin.
[Graphical view ]
Pfami PF02709. Glyco_transf_7C. 1 hit.
PF00535. Glycos_transf_2. 1 hit.
PF00652. Ricin_B_lectin. 1 hit.
[Graphical view ]
SMARTi SM00458. RICIN. 1 hit.
[Graphical view ]
SUPFAMi SSF50370. SSF50370. 2 hits.
SSF53448. SSF53448. 1 hit.
PROSITEi PS50231. RICIN_B_LECTIN. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Functional conservation of subfamilies of putative UDP-N-acetylgalactosamine:polypeptide N-acetylgalactosaminyltransferases in Drosophila, Caenorhabditis elegans, and mammals. One subfamily composed of l(2)35Aa is essential in Drosophila."
    Schwientek T., Bennett E.P., Flores C., Thacker J., Hollmann M., Reis C.A., Behrens J., Mandel U., Keck B., Schaefer M.A., Haselmann K., Zubarev R., Roepstorff P., Burchell J.M., Taylor-Papadimitriou J., Hollingsworth M.A., Clausen H.
    J. Biol. Chem. 277:22623-22638(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
  2. "Characterization of a novel mouse UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase."
    Shimoji S., Reynolds P.R., Ten Hagen K.G., Tabak L.A.
    Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: C57BL/6J.
  3. "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 and NOD.
    Tissue: Ovary and Thymus.
  4. "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: FVB/N.
    Tissue: Kidney and Mammary tumor.
  5. "The heterotaxy gene GALNT11 glycosylates Notch to orchestrate cilia type and laterality."
    Boskovski M.T., Yuan S., Pedersen N.B., Goth C.K., Makova S., Clausen H., Brueckner M., Khokha M.K.
    Nature 504:456-459(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: DEVELOPMENTAL STAGE.

Entry informationi

Entry nameiGLT11_MOUSE
AccessioniPrimary (citable) accession number: Q921L8
Secondary accession number(s): Q3TT83, Q8BU26, Q8K032
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: December 1, 2001
Last modified: October 29, 2014
This is version 114 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