Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q6PB93

- GALT2_MOUSE

UniProt

Q6PB93 - GALT2_MOUSE

Protein

Polypeptide N-acetylgalactosaminyltransferase 2

Gene

Galnt2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 106 (01 Oct 2014)
      Sequence version 1 (05 Jul 2004)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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 a broad spectrum of substrates for peptides such as EA2, Muc5AC, Muc1a, Muc1b. Probably involved in O-linked glycosylation of the immunoglobulin A1 (IgA1) hinge region 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 sitei142 – 1421SubstrateBy similarity
    Binding sitei175 – 1751SubstrateBy similarity
    Binding sitei200 – 2001SubstrateBy similarity
    Metal bindingi223 – 2231ManganeseBy similarity
    Binding sitei224 – 2241SubstrateBy similarity
    Metal bindingi225 – 2251ManganeseBy similarity
    Binding sitei330 – 3301SubstrateBy similarity
    Metal bindingi358 – 3581ManganeseBy similarity
    Binding sitei361 – 3611SubstrateBy similarity
    Binding sitei364 – 3641SubstrateBy similarity
    Binding sitei366 – 3661SubstrateBy similarity

    GO - Molecular functioni

    1. manganese ion binding Source: UniProtKB
    2. polypeptide N-acetylgalactosaminyltransferase activity Source: UniProtKB

    GO - Biological processi

    1. protein O-linked glycosylation Source: UniProtKB

    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 2 (EC:2.4.1.41)
    Alternative name(s):
    Polypeptide GalNAc transferase 2
    Short name:
    GalNAc-T2
    Short name:
    pp-GaNTase 2
    Protein-UDP acetylgalactosaminyltransferase 2
    UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 2
    Cleaved into the following chain:
    Gene namesi
    Name:Galnt2
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 8

    Organism-specific databases

    MGIiMGI:894694. Galnt2.

    Subcellular locationi

    Golgi apparatusGolgi stack membrane; Single-pass type II membrane protein. Secreted
    Note: Resides preferentially in the trans and medial parts of the Golgi stack. A secreted form also exists.

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB-SubCell
    2. Golgi cisterna membrane Source: UniProtKB-SubCell
    3. Golgi lumen Source: MGI
    4. integral component of membrane Source: UniProtKB-KW

    Keywords - Cellular componenti

    Golgi apparatus, Membrane, Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 570570Polypeptide N-acetylgalactosaminyltransferase 2PRO_0000223392Add
    BLAST
    Chaini51 – 570520Polypeptide N-acetylgalactosaminyltransferase 2 soluble formPRO_0000012267Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi125 ↔ 353PROSITE-ProRule annotation
    Disulfide bondi344 ↔ 422PROSITE-ProRule annotation
    Disulfide bondi455 ↔ 472PROSITE-ProRule annotation
    Disulfide bondi495 ↔ 512PROSITE-ProRule annotation
    Glycosylationi515 – 5151N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi538 ↔ 554PROSITE-ProRule annotation

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    MaxQBiQ6PB93.
    PaxDbiQ6PB93.
    PRIDEiQ6PB93.

    PTM databases

    PhosphoSiteiQ6PB93.

    Expressioni

    Tissue specificityi

    Widely expressed at high level.1 Publication

    Gene expression databases

    BgeeiQ6PB93.
    GenevestigatoriQ6PB93.

    Structurei

    3D structure databases

    ProteinModelPortaliQ6PB93.
    SMRiQ6PB93. Positions 74-567.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 66CytoplasmicSequence Analysis
    Topological domaini25 – 570546LumenalSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei7 – 2418Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini442 – 565124Ricin B-type lectinPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni134 – 239106Catalytic subdomain AAdd
    BLAST
    Regioni299 – 36163Catalytic 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

    eggNOGiCOG5533.
    GeneTreeiENSGT00750000117385.
    HOVERGENiHBG051699.
    InParanoidiQ6PB93.
    KOiK00710.
    OMAiDDYSDNP.
    OrthoDBiEOG7J9VP2.
    PhylomeDBiQ6PB93.
    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.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q6PB93-1) [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

    MRRRSRMLLC FALLWVLGIA YYMYSGGGSA LAAGGGGAGR KGDWNDIDSI    50
    KKKDLHHSRG DEKAQGVETL PPGKVRWPDF NQEAYVGGTM VRSGQDPYAR 100
    NKFNQVESDK LHMDRGIPDT RHDQCQRKQW RVDLPATSVV ITFHNEARSA 150
    LLRTVVSVLK RSPPHLIKEI ILVDDYSNDP EDGALLGKIE KVRVLRNDRR 200
    EGLMRSRVRG ADAAQAKVLT FLDSHCECNE RWLEPLLERV AEDRTRVVSP 250
    IIDVINMDNF QYVGASADLK GGFDWNLVFK WDYMTPEQRR SRQGNPVAPI 300
    KTPMIAGGLF VMDKLYFEEL GKYDMMMDVW GGENLEISFR VWQCGGSLEI 350
    IPCSRVGHVF RKQHPYTFPG GSGTVFARNT RRAAEVWMDE YKHFYYAAVP 400
    SARNVPYGNI QSRLELRKKL GCKPFKWYLD NVYPELRVPD HQDIAFGALQ 450
    QGTNCLDTLG HFADGVVGIY ECHNAGGNQE WALTKEKSVK HMDLCLTVVD 500
    RSPGSLIRLQ GCRENDSRQK WEQIEGNSKL RHVGSNLCLD SRTAKSGGLS 550
    VEVCGPALSQ QWKFSLNLQQ 570
    Length:570
    Mass (Da):64,514
    Last modified:July 5, 2004 - v1
    Checksum:i90D5DC02C85A8EEA
    GO
    Isoform 2 (identifier: Q6PB93-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-41: MRRRSRMLLCFALLWVLGIAYYMYSGGGSALAAGGGGAGRK → MALHNPQ

    Note: No experimental confirmation available.

    Show »
    Length:536
    Mass (Da):60,985
    Checksum:i58DC49843190D2E4
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti2 – 21R → L in AAK37548. 1 PublicationCurated
    Sequence conflicti226 – 2261C → Y in BAC32790. (PubMed:16141072)Curated
    Sequence conflicti516 – 5183DSR → NSK in AAK37548. 1 PublicationCurated
    Sequence conflicti564 – 5641F → V in AAK37548. 1 PublicationCurated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 4141MRRRS…GAGRK → MALHNPQ in isoform 2. 1 PublicationVSP_011201Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF348968 mRNA. Translation: AAK37548.1.
    AK046567 mRNA. Translation: BAC32790.1.
    BC007172 mRNA. Translation: AAH07172.1.
    BC053063 mRNA. Translation: AAH53063.1.
    BC059818 mRNA. Translation: AAH59818.1.
    CCDSiCCDS22769.1. [Q6PB93-1]
    RefSeqiNP_644678.2. NM_139272.2. [Q6PB93-1]
    UniGeneiMm.33808.

    Genome annotation databases

    EnsembliENSMUST00000034458; ENSMUSP00000034458; ENSMUSG00000089704. [Q6PB93-1]
    ENSMUST00000127664; ENSMUSP00000118564; ENSMUSG00000092329. [Q6PB93-2]
    GeneIDi108148.
    KEGGimmu:108148.
    UCSCiuc009nwz.2. mouse. [Q6PB93-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Web resourcesi

    Functional Glycomics Gateway - GTase

    Polypeptide N-acetylgalactosaminyltransferase 2

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF348968 mRNA. Translation: AAK37548.1 .
    AK046567 mRNA. Translation: BAC32790.1 .
    BC007172 mRNA. Translation: AAH07172.1 .
    BC053063 mRNA. Translation: AAH53063.1 .
    BC059818 mRNA. Translation: AAH59818.1 .
    CCDSi CCDS22769.1. [Q6PB93-1 ]
    RefSeqi NP_644678.2. NM_139272.2. [Q6PB93-1 ]
    UniGenei Mm.33808.

    3D structure databases

    ProteinModelPortali Q6PB93.
    SMRi Q6PB93. Positions 74-567.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

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

    PTM databases

    PhosphoSitei Q6PB93.

    Proteomic databases

    MaxQBi Q6PB93.
    PaxDbi Q6PB93.
    PRIDEi Q6PB93.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000034458 ; ENSMUSP00000034458 ; ENSMUSG00000089704 . [Q6PB93-1 ]
    ENSMUST00000127664 ; ENSMUSP00000118564 ; ENSMUSG00000092329 . [Q6PB93-2 ]
    GeneIDi 108148.
    KEGGi mmu:108148.
    UCSCi uc009nwz.2. mouse. [Q6PB93-1 ]

    Organism-specific databases

    CTDi 2590.
    MGIi MGI:894694. Galnt2.

    Phylogenomic databases

    eggNOGi COG5533.
    GeneTreei ENSGT00750000117385.
    HOVERGENi HBG051699.
    InParanoidi Q6PB93.
    KOi K00710.
    OMAi DDYSDNP.
    OrthoDBi EOG7J9VP2.
    PhylomeDBi Q6PB93.
    TreeFami TF313267.

    Enzyme and pathway databases

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

    Miscellaneous databases

    NextBioi 360162.
    PROi Q6PB93.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q6PB93.
    Genevestigatori Q6PB93.

    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. Miyahara N., Kanoh A., Irimura T.
      Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Colon adenocarcinoma.
    2. "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] (ISOFORM 1).
      Strain: C57BL/6J.
      Tissue: Adipose tissue.
    3. "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] (ISOFORMS 1 AND 2).
      Strain: C57BL/6 and Czech II.
      Tissue: Brain and Mammary tumor.
    4. "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 nameiGALT2_MOUSE
    AccessioniPrimary (citable) accession number: Q6PB93
    Secondary accession number(s): Q7TSI5
    , Q8BL27, Q922K5, Q99ME1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 16, 2004
    Last sequence update: July 5, 2004
    Last modified: October 1, 2014
    This is version 106 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