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Q9D2N8

- GLT15_MOUSE

UniProt

Q9D2N8 - GLT15_MOUSE

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Protein
Polypeptide N-acetylgalactosaminyltransferase 15
Gene
Galnt15, Galntl2
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. 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 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 sitei231 – 2311Substrate By similarity
Binding sitei260 – 2601Substrate By similarity
Metal bindingi283 – 2831Manganese By similarity
Metal bindingi285 – 2851Manganese By similarity
Metal bindingi416 – 4161Manganese By similarity
Binding sitei419 – 4191Substrate By similarity

GO - Molecular functioni

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

GO - Biological processi

  1. protein glycosylation Source: UniProtKB-UniPathway
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 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 namesi
Name:Galnt15
Synonyms:Galntl2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 14

Organism-specific databases

MGIiMGI:1926004. Galnt15.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1212Cytoplasmic Reviewed prediction
Add
BLAST
Transmembranei13 – 3523Helical; Signal-anchor for type II membrane protein; Reviewed prediction
Add
BLAST
Topological domaini36 – 638603Lumenal Reviewed prediction
Add
BLAST

GO - Cellular componenti

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

Keywords - Cellular componenti

Golgi apparatus, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 638638Polypeptide N-acetylgalactosaminyltransferase 15
PRO_0000059138Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi181 ↔ 411 By similarity
Disulfide bondi402 ↔ 481 By similarity
Disulfide bondi516 ↔ 535 By similarity
Disulfide bondi561 ↔ 574 By similarity
Glycosylationi573 – 5731N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi602 ↔ 619 By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PRIDEiQ9D2N8.

PTM databases

PhosphoSiteiQ9D2N8.

Expressioni

Tissue specificityi

Specifically expressed in testis.1 Publication

Gene expression databases

ArrayExpressiQ9D2N8.
BgeeiQ9D2N8.
GenevestigatoriQ9D2N8.

Structurei

3D structure databases

ProteinModelPortaliQ9D2N8.
SMRiQ9D2N8. Positions 128-631.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini503 – 630128Ricin B-type lectin
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni190 – 299110Catalytic subdomain A
Add
BLAST
Regioni357 – 41963Catalytic subdomain B
Add
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

eggNOGiNOG282033.
GeneTreeiENSGT00750000117451.
HOGENOMiHOG000038227.
HOVERGENiHBG051699.
InParanoidiA3KN88.
KOiK00710.
OMAiETWLGSF.
OrthoDBiEOG7X3QQH.
PhylomeDBiQ9D2N8.
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]

Sequencei

Sequence statusi: Complete.

Q9D2N8-1 [UniParc]FASTAAdd to Basket

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MLPRKRPRSG RSRLQFLLLF LTLGCVLMMV ILLHPPPPTL HQAVTAQASK    50
HSPDTGYRLD FGDSQEWVLE AETEGDEYSL LDGLPSFISL QEDQLLVAVA 100
SPRARRSQSQ GRRQGSYQFI KHRSRRWDEE ALEKDWRTEE DGEESEEVLT 150
PLGPDSDGLN KPLSARLPLR RVLPEVRHPL CLQQHPTSGL PTASVILCFH 200
DEAWPTLLRT VHSILDTAPR ALLQEIILVD DLSQQELLKS ALSEYVARLE 250
AVKLLRSNRR LGTIGARMLG ATRATGDVLV FMDAHCECHP GWLEPLLSRI 300
ADDRSRVVSP VIDVIDWKTL QYSASKLHRG TLDWKLDFRW KPLGEQEQKA 350
LPSPISPVRS PVVPREVVAV DRHYFQNTGA YDPLLSLGDS ENLEMSFKAW 400
LCGGSVEILP CSRVGHIYRS QDASSRPDPE VALKNKIIIA ETWLSSFKET 450
FYRHIPEAFT LSKVAKPDCT ERLKLQRRLG CRTFHWFLAN VYPELYPSDH 500
RPRFSGKLHN TGFGLCADCQ ADGDILGCPM TLAPCSNNRQ QQNLEHTGRK 550
EILFGGPQRL CFDVRGGRVI LQNCTEEGPA IHQQHWDFQE DGMIIHVLSG 600
KCMEAGVQPS NKDLYLRQCD GKTSQLWRFD QIHPVDER 638
Length:638
Mass (Da):72,321
Last modified:June 1, 2001 - v1
Checksum:i421617F0C8556976
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK019470 mRNA. Translation: BAB31741.1.
BC133711 mRNA. Translation: AAI33712.1.
CCDSiCCDS36859.1.
RefSeqiNP_084442.1. NM_030166.3.
UniGeneiMm.40681.

Genome annotation databases

EnsembliENSMUST00000022460; ENSMUSP00000022460; ENSMUSG00000021903.
GeneIDi78754.
KEGGimmu:78754.
UCSCiuc007syb.1. mouse.

Cross-referencesi

Web resourcesi

Functional Glycomics Gateway - GTase

Polypeptide N-acetylgalactosaminyltransferase-like protein 2

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK019470 mRNA. Translation: BAB31741.1 .
BC133711 mRNA. Translation: AAI33712.1 .
CCDSi CCDS36859.1.
RefSeqi NP_084442.1. NM_030166.3.
UniGenei Mm.40681.

3D structure databases

ProteinModelPortali Q9D2N8.
SMRi Q9D2N8. Positions 128-631.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

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

PTM databases

PhosphoSitei Q9D2N8.

Proteomic databases

PRIDEi Q9D2N8.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000022460 ; ENSMUSP00000022460 ; ENSMUSG00000021903 .
GeneIDi 78754.
KEGGi mmu:78754.
UCSCi uc007syb.1. mouse.

Organism-specific databases

CTDi 117248.
MGIi MGI:1926004. Galnt15.

Phylogenomic databases

eggNOGi NOG282033.
GeneTreei ENSGT00750000117451.
HOGENOMi HOG000038227.
HOVERGENi HBG051699.
InParanoidi A3KN88.
KOi K00710.
OMAi ETWLGSF.
OrthoDBi EOG7X3QQH.
PhylomeDBi Q9D2N8.
TreeFami TF313267.

Enzyme and pathway databases

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

Miscellaneous databases

NextBioi 349440.
PROi Q9D2N8.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9D2N8.
Bgeei Q9D2N8.
Genevestigatori Q9D2N8.

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. "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].
    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.

Entry informationi

Entry nameiGLT15_MOUSE
AccessioniPrimary (citable) accession number: Q9D2N8
Secondary accession number(s): A3KN88
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: June 1, 2001
Last modified: September 3, 2014
This is version 98 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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