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Q9D2N8

- GLT15_MOUSE

UniProt

Q9D2N8 - GLT15_MOUSE

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Protein

Polypeptide N-acetylgalactosaminyltransferase 15

Gene

Galnt15

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).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 – 2311SubstrateBy similarity
Binding sitei260 – 2601SubstrateBy similarity
Metal bindingi283 – 2831ManganeseBy similarity
Metal bindingi285 – 2851ManganeseBy similarity
Metal bindingi416 – 4161ManganeseBy similarity
Binding sitei419 – 4191SubstrateBy similarity

GO - Molecular functioni

  1. carbohydrate binding Source: UniProtKB-KW
  2. metal ion binding Source: UniProtKB-KW
  3. 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

GO - Cellular componenti

  1. Golgi apparatus Source: UniProtKB-KW
  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 15PRO_0000059138Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi181 ↔ 411PROSITE-ProRule annotation
Disulfide bondi402 ↔ 481PROSITE-ProRule annotation
Disulfide bondi516 ↔ 535PROSITE-ProRule annotation
Disulfide bondi561 ↔ 574PROSITE-ProRule annotation
Glycosylationi573 – 5731N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi602 ↔ 619PROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PRIDEiQ9D2N8.

PTM databases

PhosphoSiteiQ9D2N8.

Expressioni

Tissue specificityi

Specifically expressed in testis.1 Publication

Gene expression databases

BgeeiQ9D2N8.
ExpressionAtlasiQ9D2N8. baseline and differential.
GenevestigatoriQ9D2N8.

Structurei

3D structure databases

ProteinModelPortaliQ9D2N8.
SMRiQ9D2N8. Positions 128-631.
ModBaseiSearch...
MobiDBiSearch...

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1212CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini36 – 638603LumenalSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei13 – 3523Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini503 – 630128Ricin B-type lectinPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni190 – 299110Catalytic subdomain AAdd
BLAST
Regioni357 – 41963Catalytic subdomain BAdd
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

Contains 1 ricin B-type lectin domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG282033.
GeneTreeiENSGT00760000118828.
HOGENOMiHOG000038227.
HOVERGENiHBG051699.
InParanoidiQ9D2N8.
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

« Hide

        10         20         30         40         50
MLPRKRPRSG RSRLQFLLLF LTLGCVLMMV ILLHPPPPTL HQAVTAQASK
60 70 80 90 100
HSPDTGYRLD FGDSQEWVLE AETEGDEYSL LDGLPSFISL QEDQLLVAVA
110 120 130 140 150
SPRARRSQSQ GRRQGSYQFI KHRSRRWDEE ALEKDWRTEE DGEESEEVLT
160 170 180 190 200
PLGPDSDGLN KPLSARLPLR RVLPEVRHPL CLQQHPTSGL PTASVILCFH
210 220 230 240 250
DEAWPTLLRT VHSILDTAPR ALLQEIILVD DLSQQELLKS ALSEYVARLE
260 270 280 290 300
AVKLLRSNRR LGTIGARMLG ATRATGDVLV FMDAHCECHP GWLEPLLSRI
310 320 330 340 350
ADDRSRVVSP VIDVIDWKTL QYSASKLHRG TLDWKLDFRW KPLGEQEQKA
360 370 380 390 400
LPSPISPVRS PVVPREVVAV DRHYFQNTGA YDPLLSLGDS ENLEMSFKAW
410 420 430 440 450
LCGGSVEILP CSRVGHIYRS QDASSRPDPE VALKNKIIIA ETWLSSFKET
460 470 480 490 500
FYRHIPEAFT LSKVAKPDCT ERLKLQRRLG CRTFHWFLAN VYPELYPSDH
510 520 530 540 550
RPRFSGKLHN TGFGLCADCQ ADGDILGCPM TLAPCSNNRQ QQNLEHTGRK
560 570 580 590 600
EILFGGPQRL CFDVRGGRVI LQNCTEEGPA IHQQHWDFQE DGMIIHVLSG
610 620 630
KCMEAGVQPS NKDLYLRQCD GKTSQLWRFD QIHPVDER
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 ENSGT00760000118828.
HOGENOMi HOG000038227.
HOVERGENi HBG051699.
InParanoidi Q9D2N8.
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

Bgeei Q9D2N8.
ExpressionAtlasi Q9D2N8. baseline and differential.
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: October 29, 2014
This is version 100 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