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Q8C102

- GALT5_MOUSE

UniProt

Q8C102 - GALT5_MOUSE

Protein

Polypeptide N-acetylgalactosaminyltransferase 5

Gene

Galnt5

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 101 (01 Oct 2014)
      Sequence version 2 (27 Jul 2011)
      Previous versions | rss
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    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. Has activity toward EA2 peptide substrate, but has a weak activity toward Muc2 or Muc1b substrates 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 sitei526 – 5261SubstrateBy similarity
    Binding sitei555 – 5551SubstrateBy similarity
    Metal bindingi578 – 5781ManganeseBy similarity
    Binding sitei579 – 5791SubstrateBy similarity
    Metal bindingi580 – 5801ManganeseBy similarity
    Binding sitei685 – 6851SubstrateBy similarity
    Metal bindingi713 – 7131ManganeseBy similarity
    Binding sitei716 – 7161SubstrateBy similarity
    Binding sitei721 – 7211SubstrateBy 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

    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 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 namesi
    Name:Galnt5
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 2

    Organism-specific databases

    MGIiMGI:2179403. Galnt5.

    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 – 930930Polypeptide N-acetylgalactosaminyltransferase 5PRO_0000059111Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi198 – 1981N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi213 – 2131N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi283 – 2831N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi287 – 2871N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi309 – 3091N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi355 – 3551N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi387 – 3871N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi476 ↔ 708PROSITE-ProRule annotation
    Glycosylationi568 – 5681N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi699 ↔ 779PROSITE-ProRule annotation
    Glycosylationi766 – 7661N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi812 ↔ 825PROSITE-ProRule annotation
    Glycosylationi817 – 8171N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi835 – 8351N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi848 ↔ 863PROSITE-ProRule annotation
    Disulfide bondi898 ↔ 913PROSITE-ProRule annotation
    Glycosylationi902 – 9021N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    MaxQBiQ8C102.
    PRIDEiQ8C102.

    PTM databases

    PhosphoSiteiQ8C102.

    Expressioni

    Tissue specificityi

    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.1 Publication

    Gene expression databases

    BgeeiQ8C102.
    GenevestigatoriQ8C102.

    Interactioni

    Subunit structurei

    Interacts with EXT2. Does not interact with EXT1, EXTL1 or EXTL3 By similarity.By similarity

    Protein-protein interaction databases

    STRINGi10090.ENSMUSP00000028171.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8C102.
    SMRiQ8C102. Positions 429-925.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 1212CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini36 – 930895LumenalSequence 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
    Domaini794 – 925132Ricin B-type lectinPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni485 – 594110Catalytic subdomain AAdd
    BLAST
    Regioni654 – 71663Catalytic 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

    eggNOGiNOG307550.
    GeneTreeiENSGT00740000115054.
    HOGENOMiHOG000231869.
    HOVERGENiHBG051698.
    InParanoidiA2AS75.
    KOiK00710.
    OMAiSHVVIIT.
    OrthoDBiEOG7J9VP2.
    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.

    Q8C102-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNKIRKFFRG SGRVLAFIFA ASVIWLLFDM AALRLSFSEI NAGLLKEDII    50
    RREHTGFRVE PDQVKVLYTS IRGMGLPRNG AWGKENFRKA ENHELKVEEN 100
    MDQVQRKGKM QNLLGRRKAV PLWHLAHLQT LPVTIPMQKT QGRDSKPEVS 150
    SQYMMSKWMT VLESEKTPFT ASRGVPLTKI AGRTETFDKK QEAPQNYNVS 200
    SDTSKQASER TLNMTISVKT DRSKQKSQTV TKLRMHFASP PILKSEEVTV 250
    IKKAEAQSKD LKHEALKALP LLKFIADMGH LKNQSTNETQ LGRLPEDDAA 300
    KVAPGKKLNF SESHVVIITK EEELKTDTKE VPNSKTQTVF PKLLGGSPHK 350
    QIPRNQSKTS SSPPALKKAV SQSKPTISGG LHTARSNLTA KAPTVGYQQS 400
    HANIPENPGM HHVFRIDVTL SPRDLNAPGQ FGRPVVVPPE KKKEAEQRWK 450
    EGNFNVYLSD LIPVDRAIED TRPAGCAEQL VHNDLPTTSI IMCFVDEVWS 500
    ALLRSVHSVL NRSPPHLIKE ILLVDDFSTK EYLKADLDKY MSQFPKVRIL 550
    RLKERHGLIR ARLAGAQNAT GDVLTFLDSH VECNVGWLEP LLERVYLNRK 600
    KVACPVIEVI NDKDMSYMTV DNFQRGVFTW PMNFGWKTIP PDVVAKNGIK 650
    ETDIIRCPVM AGGLFSIDKS YFYELGTYDP GLDVWGGENM ELSFKVWMCG 700
    GEIEIIPCSR VGHIFRNDNP YSFPKDRMKT VERNLVRVAE VWLDDYRELF 750
    YGHGDHLIDQ GLDVGNLTQQ RELRKKLKCK SFKWYLDNVF PDLKAPVVRA 800
    SGVLINMALG KCVSIENITV TLEDCDGSSQ LQQFNYTWVR LIKHGEWCVA 850
    PIPEKGSLTL YHCDNRNNRL KWLHKSASAF HPELVDHIVF ENYQQLLCME 900
    GNFSQKTLKL AACNPMELQQ KWKFEKYYEV 930
    Length:930
    Mass (Da):105,780
    Last modified:July 27, 2011 - v2
    Checksum:iC5851F6E13CDF5D7
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti705 – 7051I → L in BAC26396. (PubMed:16141072)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS38125.1.
    RefSeqiNP_766443.2. NM_172855.3.
    XP_006498111.1. XM_006498048.1.
    XP_006498112.1. XM_006498049.1.
    UniGeneiMm.484118.

    Genome annotation databases

    EnsembliENSMUST00000112616; ENSMUSP00000108235; ENSMUSG00000026828.
    ENSMUST00000166729; ENSMUSP00000131362; ENSMUSG00000026828.
    GeneIDi241391.
    KEGGimmu:241391.
    UCSCiuc012bvo.1. mouse.

    Cross-referencesi

    Web resourcesi

    Functional Glycomics Gateway - GTase

    Polypeptide N-acetylgalactosaminyltransferase 5

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS38125.1.
    RefSeqi NP_766443.2. NM_172855.3.
    XP_006498111.1. XM_006498048.1.
    XP_006498112.1. XM_006498049.1.
    UniGenei Mm.484118.

    3D structure databases

    ProteinModelPortali Q8C102.
    SMRi Q8C102. Positions 429-925.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 10090.ENSMUSP00000028171.

    Protein family/group databases

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

    PTM databases

    PhosphoSitei Q8C102.

    Proteomic databases

    MaxQBi Q8C102.
    PRIDEi Q8C102.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000112616 ; ENSMUSP00000108235 ; ENSMUSG00000026828 .
    ENSMUST00000166729 ; ENSMUSP00000131362 ; ENSMUSG00000026828 .
    GeneIDi 241391.
    KEGGi mmu:241391.
    UCSCi uc012bvo.1. mouse.

    Organism-specific databases

    CTDi 11227.
    MGIi MGI:2179403. Galnt5.

    Phylogenomic databases

    eggNOGi NOG307550.
    GeneTreei ENSGT00740000115054.
    HOGENOMi HOG000231869.
    HOVERGENi HBG051698.
    InParanoidi A2AS75.
    KOi K00710.
    OMAi SHVVIIT.
    OrthoDBi EOG7J9VP2.
    TreeFami TF313267.

    Enzyme and pathway databases

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

    Miscellaneous databases

    NextBioi 384997.
    PROi Q8C102.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q8C102.
    Genevestigatori Q8C102.

    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. "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: Head.
    2. 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.

    Entry informationi

    Entry nameiGALT5_MOUSE
    AccessioniPrimary (citable) accession number: Q8C102
    Secondary accession number(s): A2AS75
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 16, 2004
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 101 of the entry and version 2 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