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Q8C102 (GALT5_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 99. 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 5

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

Protein attributes

Sequence length930 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 activity toward EA2 peptide substrate, but has a weak activity toward Muc2 or Muc1b substrates 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.

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.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.

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

Sites

Metal binding5781Manganese By similarity
Metal binding5801Manganese By similarity
Metal binding7131Manganese By similarity
Binding site5261Substrate By similarity
Binding site5551Substrate By similarity
Binding site5791Substrate By similarity
Binding site6851Substrate By similarity
Binding site7161Substrate By similarity
Binding site7211Substrate By similarity

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 bond476 ↔ 708 By similarity
Disulfide bond699 ↔ 779 By similarity
Disulfide bond812 ↔ 825 By similarity
Disulfide bond848 ↔ 863 By similarity
Disulfide bond898 ↔ 913 By similarity

Experimental info

Sequence conflict7051I → L in BAC26396. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q8C102 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: C5851F6E13CDF5D7

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 GEIEIIPCSR 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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Head.
[2]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[3]Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"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] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
+Additional computationally mapped references.

Web resources

Functional Glycomics Gateway - GTase

Polypeptide N-acetylgalactosaminyltransferase 5

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK029323 mRNA. Translation: BAC26396.1.
AL928564, AL929144 Genomic DNA. Translation: CAM18783.1.
AL929144, AL928564 Genomic DNA. Translation: CAM24473.1.
CH466519 Genomic DNA. Translation: EDL26932.1.
CCDSCCDS38125.1.
RefSeqNP_766443.2. NM_172855.3.
XP_006498111.1. XM_006498048.1.
XP_006498112.1. XM_006498049.1.
UniGeneMm.484118.

3D structure databases

ProteinModelPortalQ8C102.
SMRQ8C102. Positions 429-925.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000028171.

Protein family/group databases

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

PTM databases

PhosphoSiteQ8C102.

Proteomic databases

MaxQBQ8C102.
PRIDEQ8C102.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000112616; ENSMUSP00000108235; ENSMUSG00000026828.
ENSMUST00000166729; ENSMUSP00000131362; ENSMUSG00000026828.
GeneID241391.
KEGGmmu:241391.
UCSCuc012bvo.1. mouse.

Organism-specific databases

CTD11227.
MGIMGI:2179403. Galnt5.

Phylogenomic databases

eggNOGNOG307550.
GeneTreeENSGT00740000115054.
HOGENOMHOG000231869.
HOVERGENHBG051698.
InParanoidA2AS75.
KOK00710.
OMASHVVIIT.
OrthoDBEOG7J9VP2.
TreeFamTF313267.

Enzyme and pathway databases

UniPathwayUPA00378.

Gene expression databases

BgeeQ8C102.
GenevestigatorQ8C102.

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

NextBio384997.
PROQ8C102.
SOURCESearch...

Entry information

Entry nameGALT5_MOUSE
AccessionPrimary (citable) accession number: Q8C102
Secondary accession number(s): A2AS75
Entry history
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: July 27, 2011
Last modified: July 9, 2014
This is version 99 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