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Q8K1B9 (GLT18_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 93. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Polypeptide N-acetylgalactosaminyltransferase 18

EC=2.4.1.41
Alternative name(s):
Polypeptide GalNAc transferase 18
Short name=GalNAc-T18
Polypeptide GalNAc transferase-like protein 4
Short name=GalNAc-T-like protein 4
Short name=pp-GaNTase-like protein 4
Polypeptide N-acetylgalactosaminyltransferase-like protein 4
Protein-UDP acetylgalactosaminyltransferase-like protein 4
UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase-like protein 4
Gene names
Name:Galnt18
Synonyms:Galntl4
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length622 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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 By similarity.

Catalytic activity

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

Cofactor

Manganese By similarity.

Pathway

Protein modification; protein glycosylation.

Subcellular location

Golgi apparatus membrane; Single-pass type II membrane protein By similarity.

Domain

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 similarities

Belongs to the glycosyltransferase 2 family. GalNAc-T subfamily.

Contains 1 ricin B-type lectin domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 622622Polypeptide N-acetylgalactosaminyltransferase 18
PRO_0000059142

Regions

Topological domain1 – 1212Cytoplasmic Potential
Transmembrane13 – 3523Helical; Signal-anchor for type II membrane protein; Potential
Topological domain36 – 622587Lumenal Potential
Domain484 – 614131Ricin B-type lectin
Region153 – 267115Catalytic subdomain A
Region324 – 40077Catalytic subdomain B

Sites

Metal binding2511Manganese By similarity
Metal binding2531Manganese By similarity
Metal binding3971Manganese By similarity
Binding site1941Substrate By similarity
Binding site4001Substrate By similarity
Binding site4051Substrate By similarity

Amino acid modifications

Glycosylation1461N-linked (GlcNAc...) Potential
Glycosylation1951N-linked (GlcNAc...) Potential
Glycosylation3201N-linked (GlcNAc...) Potential
Disulfide bond144 ↔ 392 By similarity
Disulfide bond383 ↔ 462 By similarity
Disulfide bond497 ↔ 513 By similarity
Disulfide bond545 ↔ 558 By similarity
Disulfide bond586 ↔ 606 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8K1B9 [UniParc].

Last modified October 1, 2002. Version 1.
Checksum: 4FE9493795E3A561

FASTA62271,096
        10         20         30         40         50         60 
MVCTRKTKTL VSTCVILSGM TNIICLLYVG WVTNYIASVY VRGQEPVPDK KLEEDKGDTL 

        70         80         90        100        110        120 
KIIERLDHLE NVIKQHIQEA PAKPEEAEAE PFTDSSLFAH WGQELSPEGR RVALKQFQYY 

       130        140        150        160        170        180 
GYNAYLSDRL PLDRPLPDLR PSGCRNLSFP DSLPEVSIVF IFVNEALSVL LRSIHSAMER 

       190        200        210        220        230        240 
TPSHLLKEII LVDDNSSNEE LKEKLTEYVD KVNGQKPGFI KVVRHSKQEG LIRSRVSGWR 

       250        260        270        280        290        300 
AATAPVVALF DAHVEFNVGW AEPVLTRIKE NRKRIISPSF DNIKYDNFEI EEYPLAAQGF 

       310        320        330        340        350        360 
DWELWCRYLN PPKAWWKLEN STAPIRSPAL IGCFIVDRQY FEEIGLLDEG MEVYGGENVE 

       370        380        390        400        410        420 
LGIRVSEISH TGLSSAPMMV WQCGGSVEVL PCSRIAHIER AHKPYTEDLT AHVRRNALRV 

       430        440        450        460        470        480 
AEVWMDEFKS HVYMAWNIPQ EDSGIDIGDI TARKALRKQL QCKTFRWYLV SVYPEMRMYS 

       490        500        510        520        530        540 
DIIAYGVLQN SLKTDLCLDQ GPDTENVPIV YICHGMTPQN VYYTSSQQIH VGILSPTVDD 

       550        560        570        580        590        600 
DDNRCLVDVN SRPRLIECSY AKAKRMKLHW QFSQGGSIQN RKSKRCLELQ ENSDMEFGFQ 

       610        620 
LVLQKCSGQH WTITNVLRSL VS 

« Hide

References

[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].
Strain: FVB/N.
Tissue: Kidney.
+Additional computationally mapped references.

Web resources

Functional Glycomics Gateway - GTase

Putative polypeptide N-acetylgalactosaminyltransferase-like protein 4

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BC024988 mRNA. Translation: AAH24988.1.
RefSeqNP_776100.2. NM_173739.3.
UniGeneMm.323322.

3D structure databases

ProteinModelPortalQ8K1B9.
SMRQ8K1B9. Positions 121-616.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyCBM13. Carbohydrate-Binding Module Family 13.
GT27. Glycosyltransferase Family 27.

PTM databases

PhosphoSiteQ8K1B9.

Proteomic databases

PRIDEQ8K1B9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000049430; ENSMUSP00000043636; ENSMUSG00000038296.
GeneID233733.
KEGGmmu:233733.
UCSCuc009jgc.1. mouse.

Organism-specific databases

CTD374378.
MGIMGI:2446239. Galnt18.

Phylogenomic databases

eggNOGNOG123124.
GeneTreeENSGT00670000097647.
HOGENOMHOG000038228.
HOVERGENHBG051699.
InParanoidQ8K1B9.
KOK00710.
OMAAPDKKLE.
OrthoDBEOG70087G.
PhylomeDBQ8K1B9.
TreeFamTF313267.

Enzyme and pathway databases

UniPathwayUPA00378.

Gene expression databases

ArrayExpressQ8K1B9.
BgeeQ8K1B9.
GenevestigatorQ8K1B9.

Family and domain databases

InterProIPR001173. Glyco_trans_2-like.
IPR000772. Ricin_B_lectin.
[Graphical view]
PfamPF00535. Glycos_transf_2. 1 hit.
PF00652. Ricin_B_lectin. 1 hit.
[Graphical view]
SMARTSM00458. RICIN. 1 hit.
[Graphical view]
SUPFAMSSF50370. SSF50370. 1 hit.
PROSITEPS50231. RICIN_B_LECTIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio381803.
PROQ8K1B9.
SOURCESearch...

Entry information

Entry nameGLT18_MOUSE
AccessionPrimary (citable) accession number: Q8K1B9
Entry history
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: October 1, 2002
Last modified: April 16, 2014
This is version 93 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot