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Q925R7

- GLT10_RAT

UniProt

Q925R7 - GLT10_RAT

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Protein

Polypeptide N-acetylgalactosaminyltransferase 10

Gene

Galnt10

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 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 Muc5Ac and EA2 peptide substrates.

Catalytic activityi

UDP-N-acetyl-alpha-D-galactosamine + polypeptide = UDP + N-acetyl-alpha-D-galactosaminyl-polypeptide.1 Publication

Cofactori

Mn2+By similarity

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei185 – 1851SubstrateBy similarity
Binding sitei214 – 2141SubstrateBy similarity
Metal bindingi237 – 2371ManganeseBy similarity
Binding sitei238 – 2381SubstrateBy similarity
Metal bindingi239 – 2391ManganeseBy similarity
Binding sitei342 – 3421SubstrateBy similarity
Metal bindingi370 – 3701ManganeseBy similarity
Binding sitei373 – 3731SubstrateBy similarity
Binding sitei378 – 3781SubstrateBy similarity

GO - Molecular functioni

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

GO - Biological processi

  1. protein O-linked glycosylation Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

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 10 (EC:2.4.1.41)
Alternative name(s):
Polypeptide GalNAc transferase 10
Short name:
GalNAc-T10
Short name:
pp-GaNTase 10
Protein-UDP acetylgalactosaminyltransferase 10
UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 10
Gene namesi
Name:Galnt10
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Chromosome 10

Organism-specific databases

RGDi69409. Galnt10.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1111CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei12 – 3120Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST
Topological domaini32 – 603572LumenalSequence 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 – 603603Polypeptide N-acetylgalactosaminyltransferase 10PRO_0000059124Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi124 – 1241N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi135 ↔ 365PROSITE-ProRule annotation
Glycosylationi146 – 1461N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi356 ↔ 432PROSITE-ProRule annotation
Disulfide bondi471 ↔ 488PROSITE-ProRule annotation
Disulfide bondi523 ↔ 538PROSITE-ProRule annotation
Disulfide bondi563 ↔ 578PROSITE-ProRule annotation
Glycosylationi593 – 5931N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ925R7.
PRIDEiQ925R7.

Expressioni

Tissue specificityi

Highly expressed in the sublingual gland, testis, small intestine, colon and ovary. Expressed at intermediate level in heart, brain, spleen, lung, stomach, cervix and uterus.1 Publication

Gene expression databases

GenevestigatoriQ925R7.

Interactioni

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000003447.

Structurei

3D structure databases

ProteinModelPortaliQ925R7.
SMRiQ925R7. Positions 69-603.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini458 – 590133Ricin B-type lectinPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni144 – 253110Catalytic subdomain AAdd
BLAST
Regioni311 – 37363Catalytic subdomain BAdd
BLAST
Regioni373 – 38412Flexible loopBy similarityAdd
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.
InParanoidiQ925R7.
KOiK00710.
OMAiHSRQKKT.
OrthoDBiEOG7J9VP2.
PhylomeDBiQ925R7.
TreeFamiTF313267.

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.

Q925R7-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MRRKEKRLLQ AVALALAALV LLPNVGLWAL YRERQPDGSP GGSGAAVAPE
60 70 80 90 100
AIQELHSRQK KTLFLGAEQR LKDWHNKEAI RRDAQRVGNG EQGKPYPMTD
110 120 130 140 150
AERVDQAYRE NGFNIYVSDK ISLNRSLPDI RHPNCNSKLY LETLPNTSII
160 170 180 190 200
IPFHNEGWSS LLRTVHSVLN RSPPELVAEI VLVDDFSDRE HLKKPLEDYM
210 220 230 240 250
ALFPSVRILR TKKREGLIRT RMLGASAATG DVITFLDSHC EANVNWLPPL
260 270 280 290 300
LDRIARNRKT IVCPMIDVID HDDFRYETQA GDAMRGAFDW EMYYKRIPIP
310 320 330 340 350
PELQKADPSD PFESPVMAGG LFAVDRKWFW ELGGYDPGLE IWGGEQYEIS
360 370 380 390 400
FKVWMCGGRM EDIPCSRVGH IYRKYVPYKV PAGVSLARNL KRVAEVWMDE
410 420 430 440 450
YAEYIYQRRP EYRHLSAGDV VAQKKLRGSL NCKSFKWFMT KIAWDLPKFY
460 470 480 490 500
PPVEPPAAAW GEIRNVGTGL CTDTKHGTLG SPLRLETCIR GRGEAAWNSM
510 520 530 540 550
QVFTFTWRED IRPGDPQHTK KFCFDAVSHT SPVTLYDCHS MKGNQLWKYR
560 570 580 590 600
KDKTLYHPVS GSCMDCSESD HRIFMNTCNP SSLTQQWLFE HTNSTVLENF

NRN
Length:603
Mass (Da):69,117
Last modified:December 1, 2001 - v1
Checksum:i194EDEAA626A4BBF
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF241241 mRNA. Translation: AAK54498.1.
RefSeqiNP_570098.1. NM_130742.1.
UniGeneiRn.60224.

Genome annotation databases

EnsembliENSRNOT00000003447; ENSRNOP00000003447; ENSRNOG00000002488.
GeneIDi170501.
KEGGirno:170501.
UCSCiRGD:69409. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF241241 mRNA. Translation: AAK54498.1 .
RefSeqi NP_570098.1. NM_130742.1.
UniGenei Rn.60224.

3D structure databases

ProteinModelPortali Q925R7.
SMRi Q925R7. Positions 69-603.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 10116.ENSRNOP00000003447.

Protein family/group databases

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

Proteomic databases

PaxDbi Q925R7.
PRIDEi Q925R7.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSRNOT00000003447 ; ENSRNOP00000003447 ; ENSRNOG00000002488 .
GeneIDi 170501.
KEGGi rno:170501.
UCSCi RGD:69409. rat.

Organism-specific databases

CTDi 55568.
RGDi 69409. Galnt10.

Phylogenomic databases

eggNOGi NOG239675.
GeneTreei ENSGT00760000118828.
HOGENOMi HOG000038227.
HOVERGENi HBG051699.
InParanoidi Q925R7.
KOi K00710.
OMAi HSRQKKT.
OrthoDBi EOG7J9VP2.
PhylomeDBi Q925R7.
TreeFami TF313267.

Enzyme and pathway databases

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

Miscellaneous databases

NextBioi 621001.
PROi Q925R7.

Gene expression databases

Genevestigatori Q925R7.

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. "Cloning and characterization of a ninth member of the UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase family, ppGaNTase-T9."
    Ten Hagen K.G., Bedi G.S., Tetaert D., Kingsley P.D., Hagen F.K., Balys M.M., Beres T.M., Degand P., Tabak L.A.
    J. Biol. Chem. 276:17395-17404(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], ENZYME ACTIVITY, TISSUE SPECIFICITY.
    Tissue: Sublingual gland.

Entry informationi

Entry nameiGLT10_RAT
AccessioniPrimary (citable) accession number: Q925R7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: December 1, 2001
Last modified: November 26, 2014
This is version 95 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Caution

According to PubMed:11278534, this enzyme is unable to transfer GalNAc onto serine or threonine residue on the protein receptor, but instead requires the prior addition of a GalNAc on a peptide before adding additional GalNAc moieties, thereby acting as a glycopeptide transferase.Curated
Was originally termed Galnt9/pp-GaNTase 9.1 Publication

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