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Q6P6V1

- GLT11_RAT

UniProt

Q6P6V1 - GLT11_RAT

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Protein

Polypeptide N-acetylgalactosaminyltransferase 11

Gene

Galnt11

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript 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

Mn2+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_196259. 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
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Chromosome 4

Organism-specific databases

RGDi735097. Galnt11.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 66CytoplasmicSequence Analysis
Transmembranei7 – 2923Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST
Topological domaini30 – 608579LumenalSequence AnalysisAdd
BLAST

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_0000059127Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi141 ↔ 373PROSITE-ProRule annotation
Disulfide bondi364 ↔ 441PROSITE-ProRule annotation
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

PRIDEiQ6P6V1.

PTM databases

PhosphoSiteiQ6P6V1.

Expressioni

Gene expression databases

GenevestigatoriQ6P6V1.

Interactioni

Subunit structurei

Interacts with NOTCH1.By similarity

Protein-protein interaction databases

MINTiMINT-4576490.
STRINGi10116.ENSRNOP00000011815.

Structurei

3D structure databases

ProteinModelPortaliQ6P6V1.
ModBaseiSearch...
MobiDBiSearch...

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.
InParanoidiQ6P6V1.
KOiK00710.
OMAiMIFNERD.
OrthoDBiEOG7J9VP2.
PhylomeDBiQ6P6V1.
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.

Q6P6V1-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MGSVTIRYFC YGCLFTSATW TVLLFIYFNF SEVTQPLRNV PIKGSGPHGP
60 70 80 90 100
FPKKFYPRFT RGPGRVLEPQ FKANRMDDLM NNNIEDPDKG LSKSSSELGM
110 120 130 140 150
IFNERDQELR DLGYQKHAFN MLISNRLGYH RDVPDTRNAE CRGKSYPTDL
160 170 180 190 200
PTASVVICFY 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
KWDLVPVSDL GGADSATAPI RSPTMAGGLF AMNRQYFNDL GQYDSGMDIW
360 370 380 390 400
GGENLEISFR IWMCGGKLFI IPCSRVGHIF RKRRPYGSPE GQDTMTHNSL
410 420 430 440 450
RLAHVWLDEY KEQYFSLRPD LKTKSFGNIS ERVELRKKLG CQSFKWYLDN
460 470 480 490 500
VYPEMQVSGP KARLQQPVFI NRGPKRPRVL LRGRLYHLQT NKCLVAQGRS
510 520 530 540 550
SQKGGLVLLK ACDYGDPTQV WIYNEEHELI LNNLLCLDMS ETRSSDPPRL
560 570 580 590 600
MKCHGSGGSQ QWTFGKNNRL YQVSVGQCLR VVDQMDQKGY VGMAICDGSS

SQQWRLEG
Length:608
Mass (Da):69,039
Last modified:July 5, 2004 - v1
Checksum:iED1295AC1EB35751
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC062004 mRNA. Translation: AAH62004.1.
RefSeqiNP_001258248.1. NM_001271319.1.
NP_955425.2. NM_199393.2.
XP_006235984.1. XM_006235922.2.
XP_006235985.1. XM_006235923.2.
UniGeneiRn.211885.

Genome annotation databases

EnsembliENSRNOT00000011814; ENSRNOP00000011815; ENSRNOG00000008117.
GeneIDi311952.
KEGGirno:311952.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC062004 mRNA. Translation: AAH62004.1 .
RefSeqi NP_001258248.1. NM_001271319.1.
NP_955425.2. NM_199393.2.
XP_006235984.1. XM_006235922.2.
XP_006235985.1. XM_006235923.2.
UniGenei Rn.211885.

3D structure databases

ProteinModelPortali Q6P6V1.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

MINTi MINT-4576490.
STRINGi 10116.ENSRNOP00000011815.

Protein family/group databases

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

PTM databases

PhosphoSitei Q6P6V1.

Proteomic databases

PRIDEi Q6P6V1.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSRNOT00000011814 ; ENSRNOP00000011815 ; ENSRNOG00000008117 .
GeneIDi 311952.
KEGGi rno:311952.

Organism-specific databases

CTDi 63917.
RGDi 735097. Galnt11.

Phylogenomic databases

eggNOGi NOG239675.
GeneTreei ENSGT00760000118828.
HOGENOMi HOG000038227.
HOVERGENi HBG051699.
InParanoidi Q6P6V1.
KOi K00710.
OMAi MIFNERD.
OrthoDBi EOG7J9VP2.
PhylomeDBi Q6P6V1.
TreeFami TF313267.

Enzyme and pathway databases

UniPathwayi UPA00378 .
Reactomei REACT_196259. O-linked glycosylation of mucins.

Miscellaneous databases

NextBioi 664505.
PROi Q6P6V1.

Gene expression databases

Genevestigatori Q6P6V1.

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

  1. "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].
    Tissue: Prostate.

Entry informationi

Entry nameiGLT11_RAT
AccessioniPrimary (citable) accession number: Q6P6V1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: July 5, 2004
Last modified: November 26, 2014
This is version 90 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3