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Q8CF93 (GLT13_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 106. 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·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Polypeptide N-acetylgalactosaminyltransferase 13

EC=2.4.1.41
Alternative name(s):
Polypeptide GalNAc transferase 13
Short name=GalNAc-T13
Short name=pp-GaNTase 13
Protein-UDP acetylgalactosaminyltransferase 13
UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 13
Gene names
Name:Galnt13
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length556 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. Has a much stronger activity than GALNT1 to transfer GalNAc to mucin peptides, such as Muc5Ac and Muc7. Able to glycosylate SDC3. Probably responsible for the synthesis of Tn antigen in neuronal cells. Ref.1 Ref.3

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.

Tissue specificity

Specifically expressed in neuronal cells. Not expressed in glial cells such as astrocytes. Expressed at low level. Ref.1 Ref.4

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.

Disruption phenotype

No visible phenotype. It however abolishes Tn antigen in neuronal cells. Ref.3

Sequence similarities

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

Contains 1 ricin B-type lectin domain.

Caution

Was initially wrongly assigned as Galnt8.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q8CF93-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q8CF93-2)

The sequence of this isoform differs from the canonical sequence as follows:
     466-466: V → VHDLCLSAPSLGVGAEECCSNHPLYGLVYTPTINEQV
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 556556Polypeptide N-acetylgalactosaminyltransferase 13
PRO_0000059131

Regions

Topological domain1 – 44Cytoplasmic Potential
Transmembrane5 – 2723Helical; Signal-anchor for type II membrane protein; Potential
Topological domain28 – 556529Lumenal Potential
Domain428 – 550123Ricin B-type lectin
Region114 – 224111Catalytic subdomain A
Region284 – 34663Catalytic subdomain B

Sites

Metal binding2081Manganese By similarity
Metal binding2101Manganese By similarity
Metal binding3431Manganese By similarity
Binding site1551Substrate By similarity
Binding site1851Substrate By similarity
Binding site3151Substrate By similarity
Binding site3461Substrate By similarity
Binding site3511Substrate By similarity

Amino acid modifications

Glycosylation941N-linked (GlcNAc...) Potential
Glycosylation1161N-linked (GlcNAc...) Potential
Glycosylation5511N-linked (GlcNAc...) Potential
Disulfide bond105 ↔ 338 By similarity
Disulfide bond329 ↔ 407 By similarity
Disulfide bond441 ↔ 458 By similarity
Disulfide bond481 ↔ 496 By similarity
Disulfide bond522 ↔ 539 By similarity

Natural variations

Alternative sequence4661V → VHDLCLSAPSLGVGAEECCS NHPLYGLVYTPTINEQV in isoform 2.
VSP_011220

Experimental info

Sequence conflict4571N → K in BAC32353. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: 593934CFD0AED148

FASTA55663,983
        10         20         30         40         50         60 
MRRFVYCKVV LATSLMWVLV DVFLLLYFSE CNKCDDKKER SLLPALRAVI SRNQEGPGEM 

        70         80         90        100        110        120 
GKAVLIPKDD QEKMKELFKI NQFNLMASDL IALNRSLPDV RLEGCKTKVY PDELPNTSVV 

       130        140        150        160        170        180 
IVFHNEAWST LLRTVYSVIN RSPHYLLSEV ILVDDASERD FLKLTLENYV KTLEVPVKII 

       190        200        210        220        230        240 
RMEERSGLIR ARLRGAAASK GQVITFLDAH CECTLGWLEP LLARIKEDRK TVVCPIIDVI 

       250        260        270        280        290        300 
SDDTFEYMAG SDMTYGGFNW KLNFRWYPVP QREMDRRKGD RTLPVRTPTM AGGLFSIDRN 

       310        320        330        340        350        360 
YFEEIGTYDA GMDIWGGENL EMSFRIWQCG GSLEIVTCSH VGHVFRKATP YTFPGGTGHV 

       370        380        390        400        410        420 
INKNNRRLAE VWMDEFKDFF YIISPGVVKV DYGDVSVRKT LRENLKCKPF SWYLENIYPD 

       430        440        450        460        470        480 
SQIPRRYYSL GEIRNVETNQ CLDNMGRKEN EKVGIFNCHG MGGNQVFSYT ADKEIRTDDL 

       490        500        510        520        530        540 
CLDVSRLSGP VIMLKCHHMR GNQLWEYDAE RLTLRHANSN QCLDEPSEED KMVPTMQDCS 

       550 
GSRSQQWLLR NMTLGT 

« Hide

Isoform 2 [UniParc].

Checksum: 54A13935542D268C
Show »

FASTA59267,796

References

« Hide 'large scale' references
[1]"Cloning and characterization of a new human UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase, designated pp-GalNAc-T13, that is specifically expressed in neurons and synthesizes GalNAc alpha-serine/threonine antigen."
Zhang Y., Iwasaki H., Wang H., Kudo T., Kalka T.B., Hennet T., Kubota T., Cheng L., Inaba N., Gotoh M., Togayachi A., Guo J.-M., Hisatomi H., Nakajima K., Nishihara S., Nakamura M., Marth J.D., Narimatsu H.
J. Biol. Chem. 278:573-584(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY.
Tissue: Brain.
[2]"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. expand/collapse author list , 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] (ISOFORMS 1 AND 2).
Strain: C57BL/6J.
Tissue: Corpora quadrigemina and Hypothalamus.
[3]"T-cell-specific deletion of a polypeptide N-acetylgalactosaminyl-transferase gene by site-directed recombination."
Hennet T., Hagen F.K., Tabak L.A., Marth J.D.
Proc. Natl. Acad. Sci. U.S.A. 92:12070-12074(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE.
[4]"Expression of UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase isoforms in murine tissues determined by real-time PCR: a new view of a large family."
Young W.W. Jr., Holcomb D.R., Ten Hagen K.G., Tabak L.A.
Glycobiology 13:549-557(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
+Additional computationally mapped references.

Web resources

Functional Glycomics Gateway - GTase

Polypeptide N-acetylgalactosaminyltransferase 13

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB082928 mRNA. Translation: BAC54546.1.
AK038387 mRNA. Translation: BAC29981.1.
AK045417 mRNA. Translation: BAC32353.1.
CCDSCCDS16041.1. [Q8CF93-1]
RefSeqNP_766618.2. NM_173030.2. [Q8CF93-1]
XP_006498154.1. XM_006498091.1. [Q8CF93-1]
XP_006498155.1. XM_006498092.1. [Q8CF93-1]
UniGeneMm.330227.

3D structure databases

ProteinModelPortalQ8CF93.
SMRQ8CF93. Positions 56-552.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

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

PTM databases

PhosphoSiteQ8CF93.

Proteomic databases

PRIDEQ8CF93.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000068595; ENSMUSP00000063464; ENSMUSG00000060988. [Q8CF93-1]
ENSMUST00000112634; ENSMUSP00000108253; ENSMUSG00000060988. [Q8CF93-2]
ENSMUST00000112635; ENSMUSP00000108254; ENSMUSG00000060988. [Q8CF93-1]
ENSMUST00000112636; ENSMUSP00000108255; ENSMUSG00000060988. [Q8CF93-1]
GeneID271786.
KEGGmmu:271786.
UCSCuc008jrq.1. mouse. [Q8CF93-1]

Organism-specific databases

CTD114805.
MGIMGI:2139447. Galnt13.

Phylogenomic databases

eggNOGNOG239675.
GeneTreeENSGT00750000117385.
HOGENOMHOG000038227.
HOVERGENHBG051699.
KOK00710.
OMAETFEYMA.
OrthoDBEOG7J9VP2.
TreeFamTF313267.

Enzyme and pathway databases

UniPathwayUPA00378.

Gene expression databases

ArrayExpressQ8CF93.
BgeeQ8CF93.
GenevestigatorQ8CF93.

Family and domain databases

Gene3D3.90.550.10. 1 hit.
InterProIPR001173. Glyco_trans_2-like.
IPR029044. Nucleotide-diphossugar_trans.
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.
SSF53448. SSF53448. 1 hit.
PROSITEPS50231. RICIN_B_LECTIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSGALNT13. mouse.
NextBio393497.
PROQ8CF93.
SOURCESearch...

Entry information

Entry nameGLT13_MOUSE
AccessionPrimary (citable) accession number: Q8CF93
Secondary accession number(s): Q8BLE4, Q8BYT3
Entry history
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: March 1, 2003
Last modified: July 9, 2014
This is version 106 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