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Q7TT15

- GLTL3_MOUSE

UniProt

Q7TT15 - GLTL3_MOUSE

Protein

Putative polypeptide N-acetylgalactosaminyltransferase-like protein 3

Gene

Wbscr17

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 107 (01 Oct 2014)
      Sequence version 1 (01 Oct 2003)
      Previous versions | rss
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    Functioni

    May catalyze 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.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 sitei192 – 1921SubstrateBy similarity
    Binding sitei223 – 2231SubstrateBy similarity
    Metal bindingi246 – 2461ManganeseBy similarity
    Metal bindingi248 – 2481ManganeseBy similarity
    Metal bindingi378 – 3781ManganeseBy similarity
    Binding sitei381 – 3811SubstrateBy similarity
    Binding sitei386 – 3861SubstrateBy 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

    Keywords - Molecular functioni

    Glycosyltransferase, Transferase

    Keywords - Ligandi

    Lectin, Manganese, Metal-binding

    Enzyme and pathway databases

    UniPathwayiUPA00378.

    Protein family/group databases

    CAZyiCBM13. Carbohydrate-Binding Module Family 13.
    GT27. Glycosyltransferase Family 27.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Putative polypeptide N-acetylgalactosaminyltransferase-like protein 3 (EC:2.4.1.41)
    Alternative name(s):
    Polypeptide GalNAc transferase-like protein 3
    Short name:
    GalNAc-T-like protein 3
    Short name:
    pp-GaNTase-like protein 3
    Protein-UDP acetylgalactosaminyltransferase-like protein 3
    UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase-like protein 3
    Williams-Beuren syndrome chromosomal region 17 protein homolog
    Gene namesi
    Name:Wbscr17
    Synonyms:Galntl3
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 5

    Organism-specific databases

    MGIiMGI:2137594. Wbscr17.

    Subcellular locationi

    GO - Cellular componenti

    1. Golgi membrane Source: UniProtKB-SubCell
    2. integral component of membrane Source: UniProtKB-KW

    Keywords - Cellular componenti

    Golgi apparatus, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 598598Putative polypeptide N-acetylgalactosaminyltransferase-like protein 3PRO_0000059140Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi50 – 501N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi142 ↔ 373PROSITE-ProRule annotation
    Disulfide bondi364 ↔ 443PROSITE-ProRule annotation
    Glycosylationi461 – 4611N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi478 ↔ 494PROSITE-ProRule annotation
    Glycosylationi486 – 4861N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi526 ↔ 541PROSITE-ProRule annotation
    Disulfide bondi568 ↔ 586PROSITE-ProRule annotation

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PaxDbiQ7TT15.
    PRIDEiQ7TT15.

    PTM databases

    PhosphoSiteiQ7TT15.

    Expressioni

    Gene expression databases

    BgeeiQ7TT15.
    GenevestigatoriQ7TT15.

    Structurei

    3D structure databases

    ProteinModelPortaliQ7TT15.
    SMRiQ7TT15. Positions 93-595.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 66CytoplasmicSequence Analysis
    Topological domaini28 – 598571LumenalSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei7 – 2721Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini465 – 594130Ricin B-type lectinPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni151 – 262112Catalytic subdomain AAdd
    BLAST
    Regioni319 – 38163Catalytic 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

    eggNOGiNOG259711.
    GeneTreeiENSGT00670000097647.
    HOGENOMiHOG000038228.
    HOVERGENiHBG051699.
    InParanoidiQ7TT15.
    KOiK00710.
    OMAiRYENSGH.
    OrthoDBiEOG7JX33Q.
    PhylomeDBiQ7TT15.
    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]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q7TT15-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MASLRRVKVL LVLNLIAVAG FVIFLAKCRP IAVRSGDAFH EIRPRAEVAN    50
    LSAHSASPIQ DAVLKRLSLL EDIVYRQLNG LSKSLGLIEG YGGRGKGGLP 100
    ATLSPSEEEK AKGPHEKYGY NSYLSEKISL DRSIPDYRPT KCKELKYSKE 150
    LPQISIIFIF VNEALSVILR SVHSAVNHTP THLLKEIILV DDNSDEEELK 200
    APLEEYVHKR YPGLVKVVRN QKREGLIRAR IEGWKAATGQ VTGFFDAHVE 250
    FTAGWAEPVL SRIQENRKRV ILPSIDNIKQ DNFEVQRYEN SAHGYSWELW 300
    CMYISPPKDW WDAGDPSLPI RTPAMIGCSF VVNRKFFGEI GLLDPGMDVY 350
    GGENIELGIK VWLCGGSMEV LPCSRVAHIE RKKKPYNSNI GFYTKRNALR 400
    VAEVWMDDYK SHVYIAWNLP LENPGIDIGD VSERKALRKS LKCKNFQWYL 450
    DHVYPEMRRY NNTIAYGELR NNKAKDVCLD QGPLENHTAI LYPCHGWGPQ 500
    LARYTKEGFL HLGALGTTTL LPDTRCLVDN SKSRLPQLLD CDKVKSSLYK 550
    RWNFIQNGAI MNKGTGRCLE VENRGLAGID LILRSCTGQR WAIKNPIK 598
    Length:598
    Mass (Da):67,691
    Last modified:October 1, 2003 - v1
    Checksum:i66F91B355EF571F5
    GO
    Isoform 2 (identifier: Q7TT15-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         194-196: SDE → R

    Show »
    Length:596
    Mass (Da):67,516
    Checksum:i2907521731EFC58D
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti74 – 741V → D in BAC33446. (PubMed:16141072)Curated
    Sequence conflicti224 – 2241E → D in BAC33446. (PubMed:16141072)Curated
    Sequence conflicti264 – 2641Q → K in BAC33446. (PubMed:16141072)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei194 – 1963SDE → R in isoform 2. 1 PublicationVSP_011232

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF467979 mRNA. Translation: AAM62404.1.
    AK035817 mRNA. Translation: BAC29197.1.
    AK048758 mRNA. Translation: BAC33446.2.
    AK051281 mRNA. Translation: BAC34591.2.
    BC052469 mRNA. Translation: AAH52469.1.
    CCDSiCCDS39296.1. [Q7TT15-1]
    RefSeqiNP_660253.2. NM_145218.3. [Q7TT15-1]
    UniGeneiMm.299204.

    Genome annotation databases

    EnsembliENSMUST00000086023; ENSMUSP00000083187; ENSMUSG00000034040. [Q7TT15-1]
    GeneIDi212996.
    KEGGimmu:212996.
    UCSCiuc008zuq.1. mouse. [Q7TT15-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Web resourcesi

    Functional Glycomics Gateway - GTase

    Putative polypeptide N-acetylgalactosaminyltransferase-like protein 3

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF467979 mRNA. Translation: AAM62404.1 .
    AK035817 mRNA. Translation: BAC29197.1 .
    AK048758 mRNA. Translation: BAC33446.2 .
    AK051281 mRNA. Translation: BAC34591.2 .
    BC052469 mRNA. Translation: AAH52469.1 .
    CCDSi CCDS39296.1. [Q7TT15-1 ]
    RefSeqi NP_660253.2. NM_145218.3. [Q7TT15-1 ]
    UniGenei Mm.299204.

    3D structure databases

    ProteinModelPortali Q7TT15.
    SMRi Q7TT15. Positions 93-595.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

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

    PTM databases

    PhosphoSitei Q7TT15.

    Proteomic databases

    PaxDbi Q7TT15.
    PRIDEi Q7TT15.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000086023 ; ENSMUSP00000083187 ; ENSMUSG00000034040 . [Q7TT15-1 ]
    GeneIDi 212996.
    KEGGi mmu:212996.
    UCSCi uc008zuq.1. mouse. [Q7TT15-1 ]

    Organism-specific databases

    CTDi 64409.
    MGIi MGI:2137594. Wbscr17.

    Phylogenomic databases

    eggNOGi NOG259711.
    GeneTreei ENSGT00670000097647.
    HOGENOMi HOG000038228.
    HOVERGENi HBG051699.
    InParanoidi Q7TT15.
    KOi K00710.
    OMAi RYENSGH.
    OrthoDBi EOG7JX33Q.
    PhylomeDBi Q7TT15.
    TreeFami TF313267.

    Enzyme and pathway databases

    UniPathwayi UPA00378 .

    Miscellaneous databases

    NextBioi 373790.
    PROi Q7TT15.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q7TT15.
    Genevestigatori Q7TT15.

    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

    1. "Identification of additional transcripts in the Williams-Beuren syndrome critical region."
      Merla G., Ucla C., Guipponi M., Reymond A.
      Hum. Genet. 110:429-438(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    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] (ISOFORM 1).
      Strain: C57BL/6.
      Tissue: Brain.
    3. "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] OF 1-455 (ISOFORM 1).
      Strain: C57BL/6J.
      Tissue: Cerebellum and Embryonic spinal ganglion.
    4. Lubec G., Sunyer B., Chen W.-Q.
      Submitted (JAN-2009) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 128-143, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: OF1.
      Tissue: Hippocampus.

    Entry informationi

    Entry nameiGLTL3_MOUSE
    AccessioniPrimary (citable) accession number: Q7TT15
    Secondary accession number(s): Q8BKN7
    , Q8BUY1, Q8BX73, Q8BZC8, Q8K483
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 16, 2004
    Last sequence update: October 1, 2003
    Last modified: October 1, 2014
    This is version 107 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, Direct protein sequencing, 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