Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q9D2N8 (GLT15_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 97. 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 15

EC=2.4.1.41
Alternative name(s):
Polypeptide GalNAc transferase-like protein 2
Short name=GalNAc-T-like protein 2
Short name=pp-GaNTase-like protein 2
Polypeptide N-acetylgalactosaminyltransferase-like protein 2
Protein-UDP acetylgalactosaminyltransferase-like protein 2
UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase-like protein 2
Gene names
Name:Galnt15
Synonyms:Galntl2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length638 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. Although it displays a much weaker activity toward all substrates tested compared to GALNT2, it is able to transfer up to seven GalNAc residues to the Muc5AC peptide, suggesting that it can fill vicinal Thr/Ser residues in cooperation with other GALNT proteins. Prefers Muc1a as substrate 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.

Tissue specificity

Specifically expressed in testis. Ref.3

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 – 638638Polypeptide N-acetylgalactosaminyltransferase 15
PRO_0000059138

Regions

Topological domain1 – 1212Cytoplasmic Potential
Transmembrane13 – 3523Helical; Signal-anchor for type II membrane protein; Potential
Topological domain36 – 638603Lumenal Potential
Domain503 – 630128Ricin B-type lectin
Region190 – 299110Catalytic subdomain A
Region357 – 41963Catalytic subdomain B

Sites

Metal binding2831Manganese By similarity
Metal binding2851Manganese By similarity
Metal binding4161Manganese By similarity
Binding site2311Substrate By similarity
Binding site2601Substrate By similarity
Binding site4191Substrate By similarity

Amino acid modifications

Glycosylation5731N-linked (GlcNAc...) Potential
Disulfide bond181 ↔ 411 By similarity
Disulfide bond402 ↔ 481 By similarity
Disulfide bond516 ↔ 535 By similarity
Disulfide bond561 ↔ 574 By similarity
Disulfide bond602 ↔ 619 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9D2N8 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 421617F0C8556976

FASTA63872,321
        10         20         30         40         50         60 
MLPRKRPRSG RSRLQFLLLF LTLGCVLMMV ILLHPPPPTL HQAVTAQASK HSPDTGYRLD 

        70         80         90        100        110        120 
FGDSQEWVLE AETEGDEYSL LDGLPSFISL QEDQLLVAVA SPRARRSQSQ GRRQGSYQFI 

       130        140        150        160        170        180 
KHRSRRWDEE ALEKDWRTEE DGEESEEVLT PLGPDSDGLN KPLSARLPLR RVLPEVRHPL 

       190        200        210        220        230        240 
CLQQHPTSGL PTASVILCFH DEAWPTLLRT VHSILDTAPR ALLQEIILVD DLSQQELLKS 

       250        260        270        280        290        300 
ALSEYVARLE AVKLLRSNRR LGTIGARMLG ATRATGDVLV FMDAHCECHP GWLEPLLSRI 

       310        320        330        340        350        360 
ADDRSRVVSP VIDVIDWKTL QYSASKLHRG TLDWKLDFRW KPLGEQEQKA LPSPISPVRS 

       370        380        390        400        410        420 
PVVPREVVAV DRHYFQNTGA YDPLLSLGDS ENLEMSFKAW LCGGSVEILP CSRVGHIYRS 

       430        440        450        460        470        480 
QDASSRPDPE VALKNKIIIA ETWLSSFKET FYRHIPEAFT LSKVAKPDCT ERLKLQRRLG 

       490        500        510        520        530        540 
CRTFHWFLAN VYPELYPSDH RPRFSGKLHN TGFGLCADCQ ADGDILGCPM TLAPCSNNRQ 

       550        560        570        580        590        600 
QQNLEHTGRK EILFGGPQRL CFDVRGGRVI LQNCTEEGPA IHQQHWDFQE DGMIIHVLSG 

       610        620        630 
KCMEAGVQPS NKDLYLRQCD GKTSQLWRFD QIHPVDER 

« 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: Skin.
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[3]"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-like protein 2

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK019470 mRNA. Translation: BAB31741.1.
BC133711 mRNA. Translation: AAI33712.1.
CCDSCCDS36859.1.
RefSeqNP_084442.1. NM_030166.3.
UniGeneMm.40681.

3D structure databases

ProteinModelPortalQ9D2N8.
SMRQ9D2N8. Positions 128-631.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

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

PTM databases

PhosphoSiteQ9D2N8.

Proteomic databases

PRIDEQ9D2N8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000022460; ENSMUSP00000022460; ENSMUSG00000021903.
GeneID78754.
KEGGmmu:78754.
UCSCuc007syb.1. mouse.

Organism-specific databases

CTD117248.
MGIMGI:1926004. Galnt15.

Phylogenomic databases

eggNOGNOG282033.
GeneTreeENSGT00750000117451.
HOGENOMHOG000038227.
HOVERGENHBG051699.
InParanoidA3KN88.
KOK00710.
OMAETWLGSF.
OrthoDBEOG7X3QQH.
PhylomeDBQ9D2N8.
TreeFamTF313267.

Enzyme and pathway databases

UniPathwayUPA00378.

Gene expression databases

ArrayExpressQ9D2N8.
BgeeQ9D2N8.
GenevestigatorQ9D2N8.

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

NextBio349440.
PROQ9D2N8.
SOURCESearch...

Entry information

Entry nameGLT15_MOUSE
AccessionPrimary (citable) accession number: Q9D2N8
Secondary accession number(s): A3KN88
Entry history
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: June 1, 2001
Last modified: July 9, 2014
This is version 97 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