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Q8CF93

- GLT13_MOUSE

UniProt

Q8CF93 - GLT13_MOUSE

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Protein

Polypeptide N-acetylgalactosaminyltransferase 13

Gene
Galnt13
Organism
Mus musculus (Mouse)
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 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.2 Publications

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 sitei155 – 1551Substrate By similarity
Binding sitei185 – 1851Substrate By similarity
Metal bindingi208 – 2081Manganese By similarity
Metal bindingi210 – 2101Manganese By similarity
Binding sitei315 – 3151Substrate By similarity
Metal bindingi343 – 3431Manganese By similarity
Binding sitei346 – 3461Substrate By similarity
Binding sitei351 – 3511Substrate By similarity

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. polypeptide N-acetylgalactosaminyltransferase activity Source: MGI

GO - Biological processi

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

Keywords - Molecular functioni

Glycosyltransferase, Transferase

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 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 namesi
Name:Galnt13
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 2

Organism-specific databases

MGIiMGI:2139447. Galnt13.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 44Cytoplasmic Reviewed prediction
Transmembranei5 – 2723Helical; Signal-anchor for type II membrane protein; Reviewed predictionAdd
BLAST
Topological domaini28 – 556529Lumenal Reviewed predictionAdd
BLAST

GO - Cellular componenti

  1. Golgi membrane Source: UniProtKB-SubCell
  2. integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Golgi apparatus, Membrane

Pathology & Biotechi

Disruption phenotypei

No visible phenotype. It however abolishes Tn antigen in neuronal cells.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 556556Polypeptide N-acetylgalactosaminyltransferase 13PRO_0000059131Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi94 – 941N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi105 ↔ 338 By similarity
Glycosylationi116 – 1161N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi329 ↔ 407 By similarity
Disulfide bondi441 ↔ 458 By similarity
Disulfide bondi481 ↔ 496 By similarity
Disulfide bondi522 ↔ 539 By similarity
Glycosylationi551 – 5511N-linked (GlcNAc...) Reviewed prediction

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PRIDEiQ8CF93.

PTM databases

PhosphoSiteiQ8CF93.

Expressioni

Tissue specificityi

Specifically expressed in neuronal cells. Not expressed in glial cells such as astrocytes. Expressed at low level.2 Publications

Gene expression databases

ArrayExpressiQ8CF93.
BgeeiQ8CF93.
GenevestigatoriQ8CF93.

Structurei

3D structure databases

ProteinModelPortaliQ8CF93.
SMRiQ8CF93. Positions 56-552.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini428 – 550123Ricin B-type lectinAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni114 – 224111Catalytic subdomain AAdd
BLAST
Regioni284 – 34663Catalytic 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

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG239675.
GeneTreeiENSGT00750000117385.
HOGENOMiHOG000038227.
HOVERGENiHBG051699.
KOiK00710.
OMAiETFEYMA.
OrthoDBiEOG7J9VP2.
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]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q8CF93-1) [UniParc]FASTAAdd to Basket

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.

« Hide

MRRFVYCKVV LATSLMWVLV DVFLLLYFSE CNKCDDKKER SLLPALRAVI    50
SRNQEGPGEM GKAVLIPKDD QEKMKELFKI NQFNLMASDL IALNRSLPDV 100
RLEGCKTKVY PDELPNTSVV IVFHNEAWST LLRTVYSVIN RSPHYLLSEV 150
ILVDDASERD FLKLTLENYV KTLEVPVKII RMEERSGLIR ARLRGAAASK 200
GQVITFLDAH CECTLGWLEP LLARIKEDRK TVVCPIIDVI SDDTFEYMAG 250
SDMTYGGFNW KLNFRWYPVP QREMDRRKGD RTLPVRTPTM AGGLFSIDRN 300
YFEEIGTYDA GMDIWGGENL EMSFRIWQCG GSLEIVTCSH VGHVFRKATP 350
YTFPGGTGHV INKNNRRLAE VWMDEFKDFF YIISPGVVKV DYGDVSVRKT 400
LRENLKCKPF SWYLENIYPD SQIPRRYYSL GEIRNVETNQ CLDNMGRKEN 450
EKVGIFNCHG MGGNQVFSYT ADKEIRTDDL CLDVSRLSGP VIMLKCHHMR 500
GNQLWEYDAE RLTLRHANSN QCLDEPSEED KMVPTMQDCS GSRSQQWLLR 550
NMTLGT 556
Length:556
Mass (Da):63,983
Last modified:March 1, 2003 - v1
Checksum:i593934CFD0AED148
GO
Isoform 2 (identifier: Q8CF93-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     466-466: V → VHDLCLSAPSLGVGAEECCSNHPLYGLVYTPTINEQV

Note: No experimental confirmation available.

Show »
Length:592
Mass (Da):67,796
Checksum:i54A13935542D268C
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei466 – 4661V → VHDLCLSAPSLGVGAEECCS NHPLYGLVYTPTINEQV in isoform 2. VSP_011220

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti457 – 4571N → K in BAC32353. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB082928 mRNA. Translation: BAC54546.1.
AK038387 mRNA. Translation: BAC29981.1.
AK045417 mRNA. Translation: BAC32353.1.
CCDSiCCDS16041.1. [Q8CF93-1]
RefSeqiNP_766618.2. NM_173030.2. [Q8CF93-1]
XP_006498154.1. XM_006498091.1. [Q8CF93-1]
XP_006498155.1. XM_006498092.1. [Q8CF93-1]
UniGeneiMm.330227.

Genome annotation databases

EnsembliENSMUST00000068595; ENSMUSP00000063464; ENSMUSG00000060988. [Q8CF93-1]
ENSMUST00000112634; ENSMUSP00000108253; ENSMUSG00000060988. [Q8CF93-2]
ENSMUST00000112635; ENSMUSP00000108254; ENSMUSG00000060988. [Q8CF93-1]
ENSMUST00000112636; ENSMUSP00000108255; ENSMUSG00000060988. [Q8CF93-1]
GeneIDi271786.
KEGGimmu:271786.
UCSCiuc008jrq.1. mouse. [Q8CF93-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Web resourcesi

Functional Glycomics Gateway - GTase

Polypeptide N-acetylgalactosaminyltransferase 13

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB082928 mRNA. Translation: BAC54546.1 .
AK038387 mRNA. Translation: BAC29981.1 .
AK045417 mRNA. Translation: BAC32353.1 .
CCDSi CCDS16041.1. [Q8CF93-1 ]
RefSeqi NP_766618.2. NM_173030.2. [Q8CF93-1 ]
XP_006498154.1. XM_006498091.1. [Q8CF93-1 ]
XP_006498155.1. XM_006498092.1. [Q8CF93-1 ]
UniGenei Mm.330227.

3D structure databases

ProteinModelPortali Q8CF93.
SMRi Q8CF93. Positions 56-552.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

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

PTM databases

PhosphoSitei Q8CF93.

Proteomic databases

PRIDEi Q8CF93.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000068595 ; ENSMUSP00000063464 ; ENSMUSG00000060988 . [Q8CF93-1 ]
ENSMUST00000112634 ; ENSMUSP00000108253 ; ENSMUSG00000060988 . [Q8CF93-2 ]
ENSMUST00000112635 ; ENSMUSP00000108254 ; ENSMUSG00000060988 . [Q8CF93-1 ]
ENSMUST00000112636 ; ENSMUSP00000108255 ; ENSMUSG00000060988 . [Q8CF93-1 ]
GeneIDi 271786.
KEGGi mmu:271786.
UCSCi uc008jrq.1. mouse. [Q8CF93-1 ]

Organism-specific databases

CTDi 114805.
MGIi MGI:2139447. Galnt13.

Phylogenomic databases

eggNOGi NOG239675.
GeneTreei ENSGT00750000117385.
HOGENOMi HOG000038227.
HOVERGENi HBG051699.
KOi K00710.
OMAi ETFEYMA.
OrthoDBi EOG7J9VP2.
TreeFami TF313267.

Enzyme and pathway databases

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

Miscellaneous databases

ChiTaRSi GALNT13. mouse.
NextBioi 393497.
PROi Q8CF93.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q8CF93.
Bgeei Q8CF93.
Genevestigatori Q8CF93.

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

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiGLT13_MOUSE
AccessioniPrimary (citable) accession number: Q8CF93
Secondary accession number(s): Q8BLE4, Q8BYT3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: March 1, 2003
Last modified: September 3, 2014
This is version 107 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

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