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Q8BVG5 (GLT14_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·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Polypeptide N-acetylgalactosaminyltransferase 14

EC=2.4.1.41
Alternative name(s):
Polypeptide GalNAc transferase 14
Short name=GalNAc-T14
Short name=pp-GaNTase 14
Protein-UDP acetylgalactosaminyltransferase 14
UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 14
Gene names
Name:Galnt14
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length550 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. Displays activity toward mucin-derived peptide substrates such as Muc2, Muc5AC, Muc7, and Muc13 (-58). May be involved in O-glycosylation in kidney 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.

Ontologies

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q8BVG5-1)

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: Q8BVG5-2)

The sequence of this isoform differs from the canonical sequence as follows:
     385-429: IENRLNLRKN...QKGNIRQRQK → SHVTQCCRRR...SSPYYLSSSS
     430-550: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 550550Polypeptide N-acetylgalactosaminyltransferase 14
PRO_0000059134

Regions

Topological domain1 – 66Cytoplasmic Potential
Transmembrane7 – 2620Helical; Signal-anchor for type II membrane protein; Potential
Topological domain27 – 550524Lumenal Potential
Domain415 – 548134Ricin B-type lectin
Region110 – 215106Catalytic subdomain A
Region274 – 33663Catalytic subdomain B

Sites

Metal binding1991Manganese By similarity
Metal binding2011Manganese By similarity
Metal binding3331Manganese By similarity
Binding site1511Substrate By similarity
Binding site1761Substrate By similarity
Binding site2001Substrate By similarity
Binding site3051Substrate By similarity
Binding site3361Substrate By similarity
Binding site3391Substrate By similarity
Binding site3411Substrate By similarity

Amino acid modifications

Disulfide bond101 ↔ 328 By similarity
Disulfide bond319 ↔ 397 By similarity
Disulfide bond430 ↔ 447 By similarity
Disulfide bond474 ↔ 491 By similarity
Disulfide bond515 ↔ 536 By similarity

Natural variations

Alternative sequence385 – 42945IENRL…RQRQK → SHVTQCCRRRILIRGTSFRG VVPPTNLPVESPTDPSSPYY LSSSS in isoform 2.
VSP_011225
Alternative sequence430 – 550121Missing in isoform 2.
VSP_011226

Experimental info

Sequence conflict1121P → H in BAC37208. Ref.2
Sequence conflict1731N → H in BAD52069. Ref.1
Sequence conflict2601L → I in BAB22325. Ref.2
Sequence conflict3811P → H in BAC37208. Ref.2
Sequence conflict4031N → Y in BAD52069. Ref.1

Sequences

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

Last modified June 13, 2006. Version 2.
Checksum: D67054CFE6F332E1

FASTA55063,989
        10         20         30         40         50         60 
MRRLTRRLAL PIFGVLWITV LLFFWVTKRK LEVPLGPEVQ TPKPSDADWD DLWEQFDERR 

        70         80         90        100        110        120 
YLNAKKWRVG DDPYKLYAFN QRESERISSN RAVPDTRHKR CSLLVYCTDL PPTSIIITFH 

       130        140        150        160        170        180 
NEARSTLLRT IRSVLNRTPM HLIQEIILVD DFSNDPEDCK QLIKLPKVKC LRNNERQGLV 

       190        200        210        220        230        240 
RSRMRGADIA QGTTLTFLDS HCEVNRDWLQ PLLHRVKEDY TRVVCPVIDI INLDTFNYIE 

       250        260        270        280        290        300 
SASELRGGFD WSLHFQWEQL SLEQKALRLD PTEPIRTPII AGGLFVIDKA WFDYLGKYDV 

       310        320        330        340        350        360 
DMDIWGGENF EISFRVWMCG GGLEIIPCSR VGHVFRKKHP YVFPDGNANT YIKNTKRTAE 

       370        380        390        400        410        420 
VWMDEYKQYY YAARPFALER PFGNIENRLN LRKNLHCQTF KWNLENVYPE LRVPPDSSIQ 

       430        440        450        460        470        480 
KGNIRQRQKC LESQKQKKQE ILRLSPCAKV KGDGAKSQVW AFTYTQQIIQ EELCLSVVTL 

       490        500        510        520        530        540 
FPGAPVVLAL CKNGDERQLW TKTGARIEHI ASHLCLDTDM FGDSTEDGKE VVVNPCESSL 

       550 
MSQHWDIVSS 

« Hide

Isoform 2 [UniParc].

Checksum: B14F4BE219C5B7B0
Show »

FASTA42950,057

References

« Hide 'large scale' references
[1]"Mouse UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase, mpp-GalNAc-T14."
Zhang Y., Kwon Y., Kikuchi N., Narimatsu H.
Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[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: Kidney and Olfactory bulb.
+Additional computationally mapped references.

Web resources

Functional Glycomics Gateway - GTase

Polypeptide N-acetylgalactosaminyltransferase 14

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB175681 mRNA. Translation: BAD52069.1.
AK002747 mRNA. Translation: BAB22325.1.
AK078292 mRNA. Translation: BAC37208.1.
RefSeqNP_082140.2. NM_027864.2.
XP_006525002.1. XM_006524939.1.
UniGeneMm.271953.
Mm.450771.

3D structure databases

ProteinModelPortalQ8BVG5.
SMRQ8BVG5. Positions 53-545.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

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

PTM databases

PhosphoSiteQ8BVG5.

Proteomic databases

PRIDEQ8BVG5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000112591; ENSMUSP00000108210; ENSMUSG00000024064. [Q8BVG5-2]
GeneID71685.
KEGGmmu:71685.

Organism-specific databases

CTD79623.
MGIMGI:1918935. Galnt14.

Phylogenomic databases

eggNOGNOG239675.
GeneTreeENSGT00750000117385.
HOGENOMHOG000038227.
HOVERGENHBG051699.
InParanoidQ8BVG5.
KOK00710.
PhylomeDBQ8BVG5.

Enzyme and pathway databases

UniPathwayUPA00378.

Gene expression databases

BgeeQ8BVG5.
GenevestigatorQ8BVG5.

Family and domain databases

InterProIPR027791. Galactosyl_T_C.
IPR001173. Glyco_trans_2-like.
IPR000772. Ricin_B_lectin.
[Graphical view]
PfamPF02709. Glyco_transf_7C. 1 hit.
PF00535. 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

NextBio334229.
PROQ8BVG5.
SOURCESearch...

Entry information

Entry nameGLT14_MOUSE
AccessionPrimary (citable) accession number: Q8BVG5
Secondary accession number(s): Q60GT2, Q8BTI6, Q9DCJ2
Entry history
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: June 13, 2006
Last modified: April 16, 2014
This is version 93 of the entry and version 2 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