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Reviewed, UniProtKB/Swiss-Prot Q8C102 (GALT5_MOUSE)

Last modified October 13, 2009. Version 55. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Polypeptide N-acetylgalactosaminyltransferase 5
    EC=2.4.1.41
Alternative name(s):
    Polypeptide GalNAc transferase 5
      Short name=pp-GaNTase 5
      Short name=GalNAc-T5
    Protein-UDP acetylgalactosaminyltransferase 5
    UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 5
Gene names
Name: Galnt5
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMus

Protein attributes

Sequence length930 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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 activity toward EA2 peptide substrate, but has a weak activity toward Muc2 or Muc1b substrates By similarity.

Catalytic activity

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

Cofactor

Manganese By similarity.

Calcium By similarity.

Pathway

Protein modification; protein glycosylation.

Subunit structure

Interacts with EXT2. Does not interact with EXT1, EXTL1 or EXTL3 By similarity.

Subcellular location

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

Tissue specificity

Expressed at low level. Not expressed before E7.5 during embryogenesis. Expressed in dental mesenchyme and tongue. Accumulates in a subset of mesenchymal cells at the ventral-most portions of the E12.5 maxilla and mandible underlying the dental lamina. Ref.2

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 – 930930Polypeptide N-acetylgalactosaminyltransferase 5
PRO_0000059111

Regions

Topological domain1 – 1212Cytoplasmic Potential
Transmembrane13 – 3523Signal-anchor for type II membrane protein Potential
Topological domain36 – 930895Lumenal Potential
Domain794 – 925132Ricin B-type lectin
Region485 – 594110Catalytic subdomain A
Region654 – 71663Catalytic subdomain B

Amino acid modifications

Glycosylation1981N-linked (GlcNAc...) Potential
Glycosylation2131N-linked (GlcNAc...) Potential
Glycosylation2831N-linked (GlcNAc...) Potential
Glycosylation2871N-linked (GlcNAc...) Potential
Glycosylation3091N-linked (GlcNAc...) Potential
Glycosylation3551N-linked (GlcNAc...) Potential
Glycosylation3871N-linked (GlcNAc...) Potential
Glycosylation5681N-linked (GlcNAc...) Potential
Glycosylation7661N-linked (GlcNAc...) Potential
Glycosylation8171N-linked (GlcNAc...) Potential
Glycosylation8351N-linked (GlcNAc...) Potential
Glycosylation9021N-linked (GlcNAc...) Potential
Disulfide bond812 ↔ 825 By similarity
Disulfide bond848 ↔ 863 By similarity
Disulfide bond898 ↔ 913 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8C102-1 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: AC635A0A458B81B0

FASTA930105,780
        10         20         30         40         50         60 
MNKIRKFFRG SGRVLAFIFA ASVIWLLFDM AALRLSFSEI NAGLLKEDII RREHTGFRVE 

        70         80         90        100        110        120 
PDQVKVLYTS IRGMGLPRNG AWGKENFRKA ENHELKVEEN MDQVQRKGKM QNLLGRRKAV 

       130        140        150        160        170        180 
PLWHLAHLQT LPVTIPMQKT QGRDSKPEVS SQYMMSKWMT VLESEKTPFT ASRGVPLTKI 

       190        200        210        220        230        240 
AGRTETFDKK QEAPQNYNVS SDTSKQASER TLNMTISVKT DRSKQKSQTV TKLRMHFASP 

       250        260        270        280        290        300 
PILKSEEVTV IKKAEAQSKD LKHEALKALP LLKFIADMGH LKNQSTNETQ LGRLPEDDAA 

       310        320        330        340        350        360 
KVAPGKKLNF SESHVVIITK EEELKTDTKE VPNSKTQTVF PKLLGGSPHK QIPRNQSKTS 

       370        380        390        400        410        420 
SSPPALKKAV SQSKPTISGG LHTARSNLTA KAPTVGYQQS HANIPENPGM HHVFRIDVTL 

       430        440        450        460        470        480 
SPRDLNAPGQ FGRPVVVPPE KKKEAEQRWK EGNFNVYLSD LIPVDRAIED TRPAGCAEQL 

       490        500        510        520        530        540 
VHNDLPTTSI IMCFVDEVWS ALLRSVHSVL NRSPPHLIKE ILLVDDFSTK EYLKADLDKY 

       550        560        570        580        590        600 
MSQFPKVRIL RLKERHGLIR ARLAGAQNAT GDVLTFLDSH VECNVGWLEP LLERVYLNRK 

       610        620        630        640        650        660 
KVACPVIEVI NDKDMSYMTV DNFQRGVFTW PMNFGWKTIP PDVVAKNGIK ETDIIRCPVM 

       670        680        690        700        710        720 
AGGLFSIDKS YFYELGTYDP GLDVWGGENM ELSFKVWMCG GEIELIPCSR VGHIFRNDNP 

       730        740        750        760        770        780 
YSFPKDRMKT VERNLVRVAE VWLDDYRELF YGHGDHLIDQ GLDVGNLTQQ RELRKKLKCK 

       790        800        810        820        830        840 
SFKWYLDNVF PDLKAPVVRA SGVLINMALG KCVSIENITV TLEDCDGSSQ LQQFNYTWVR 

       850        860        870        880        890        900 
LIKHGEWCVA PIPEKGSLTL YHCDNRNNRL KWLHKSASAF HPELVDHIVF ENYQQLLCME 

       910        920        930 
GNFSQKTLKL AACNPMELQQ KWKFEKYYEV 

« Hide

References

« Hide 'large scale' references
[1]"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: 16141072] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Head.
[2]"Diverse spatial expression patterns of UDP-GalNAc:polypeptide N-acetylgalactosaminyl-transferase family member mRNAs during mouse development."
Kingsley P.D., Hagen K.G., Maltby K.M., Zara J., Tabak L.A.
Glycobiology 10:1317-1323(2000) [PubMed: 11159923] [Abstract]
Cited for: TISSUE SPECIFICITY.

Web resources

Functional Glycomics Gateway - GTase

Polypeptide N-acetylgalactosaminyltransferase 5

Cross-references

Sequence databases

AK029323 mRNA. Translation: BAC26396.1.
IPIIPI00223910.
UniGeneMm.68639

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGQ8C102.

Protein family/group databases

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

Proteomic databases

PRIDEQ8C102.

Genome annotation databases

EnsemblENSMUST00000028171; ENSMUSP00000028171; ENSMUSG00000026828; Mus musculus. [Genome view]
ENSMUST00000112616; ENSMUSP00000108235; ENSMUSG00000026828; Mus musculus. [Genome view]
UCSCuc008jsg.1. mouse.

Organism-specific databases

MGIMGI:2179403. Galnt5.

Phylogenomic databases

HOGENOMQ8C102.
HOVERGENQ8C102.

Enzyme and pathway databases

BRENDA2.4.1.41. 244.

Gene expression databases

ArrayExpressQ8C102.
BgeeQ8C102.
GenevestigatorQ8C102.

Family and domain databases

InterProIPR001173. Glyco_trans_2.
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]
PROSITEPS50231. RICIN_B_LECTIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

SOURCESearch...

Entry information

Entry nameGALT5_MOUSE
AccessionPrimary (citable) accession number: Q8C102
Entry history
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: March 1, 2003
Last modified: October 13, 2009
This is version 55 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

MGD cross-references

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

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents