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O88829

- SIAT9_MOUSE

UniProt

O88829 - SIAT9_MOUSE

Protein

Lactosylceramide alpha-2,3-sialyltransferase

Gene

St3gal5

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 109 (01 Oct 2014)
      Sequence version 2 (20 May 2008)
      Previous versions | rss
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    Functioni

    Catalyzes the formation of ganglioside GM3 (alpha-N-acetylneuraminyl-2,3-beta-D-galactosyl-1, 4-beta-D-glucosylceramide).1 Publication

    Catalytic activityi

    CMP-N-acetylneuraminate + beta-D-galactosyl-(1->4)-beta-D-glucosyl-(1<->1)-ceramide = CMP + alpha-N-acetylneuraminyl-(2->3)-beta-D-galactosyl-(1->4)-beta-D-glucosyl-(1<->1)-ceramide.

    GO - Molecular functioni

    1. lactosylceramide alpha-2,3-sialyltransferase activity Source: UniProtKB

    GO - Biological processi

    1. protein glycosylation Source: InterPro
    2. sialylation Source: GOC

    Keywords - Molecular functioni

    Glycosyltransferase, Transferase

    Enzyme and pathway databases

    ReactomeiREACT_202500. Sialic acid metabolism.

    Protein family/group databases

    CAZyiGT29. Glycosyltransferase Family 29.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Lactosylceramide alpha-2,3-sialyltransferase (EC:2.4.99.9)
    Alternative name(s):
    CMP-NeuAc:lactosylceramide alpha-2,3-sialyltransferase
    Ganglioside GM3 synthase
    ST3Gal V
    Short name:
    ST3GalV
    Sialyltransferase 9
    Gene namesi
    Name:St3gal5
    Synonyms:GM3S, Siat9
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 6

    Organism-specific databases

    MGIiMGI:1339963. St3gal5.

    Subcellular locationi

    GO - Cellular componenti

    1. integral component of Golgi membrane Source: InterPro

    Keywords - Cellular componenti

    Golgi apparatus, Membrane

    Pathology & Biotechi

    Disruption phenotypei

    Mice are viable and fertile, and do not show any obvious abnormality apart from an increased sensitivity to insulin.1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 414414Lactosylceramide alpha-2,3-sialyltransferasePRO_0000149303Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi194 ↔ 352By similarity
    Glycosylationi235 – 2351N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi279 – 2791N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi389 – 3891N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PaxDbiO88829.
    PRIDEiO88829.

    PTM databases

    PhosphoSiteiO88829.

    Expressioni

    Gene expression databases

    ArrayExpressiO88829.
    BgeeiO88829.
    GenevestigatoriO88829.

    Interactioni

    Protein-protein interaction databases

    STRINGi10090.ENSMUSP00000070414.

    Structurei

    3D structure databases

    ProteinModelPortaliO88829.
    SMRiO88829. Positions 132-363.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 6565CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini87 – 414328LumenalSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei66 – 8621Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glycosyltransferase 29 family.Curated

    Keywords - Domaini

    Signal-anchor, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG257001.
    GeneTreeiENSGT00620000087815.
    HOVERGENiHBG056676.
    InParanoidiB2RRS1.
    KOiK03370.
    OMAiFFWKQVA.
    OrthoDBiEOG76X609.
    PhylomeDBiO88829.
    TreeFamiTF352819.

    Family and domain databases

    InterProiIPR001675. Glyco_trans_29.
    IPR012163. Sialyl_trans.
    [Graphical view]
    PfamiPF00777. Glyco_transf_29. 1 hit.
    [Graphical view]
    PIRSFiPIRSF005557. Sialyl_trans. 1 hit.

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: O88829-1) [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

    MHTEAVGGAA RRPQKLRSQA AAPACRAMPS EFTSAKLRSD CSRTSLQWYT    50
    RTQHKMRRPS LLIKDICKCT LVAFGVWLLY ILILNYTAEE CDMKRMHYVD 100
    PDRIKRAQSY AQEVLQKECR PRYAKTAMAL LFEDRYSINL EPFVQKVPTA 150
    SEAELKYDPP FGFRKFSSKV QSLLDMLPEH DFPEHLRAKA CKRCVVVGNG 200
    GILHGLELGH ALNQFDVVIR LNSAPVEGYS EHVGNKTTIR MTYPEGAPLS 250
    DVEYYANDLF VTVLFKSVDF KWLQAMVKNE SLPFWVRLFF WKQVAEKVPL 300
    QPKHFRILNP VIIKETAFDI LQYSEPQSRF WGHDKNIPTI GVIAVVLATH 350
    LCDEVSLAGF GYDLSQPRTP LHYFDSQCMG AMHWQVMHNV TTETKFLLKL 400
    LKEGVVEDLS GGIH 414
    Length:414
    Mass (Da):47,360
    Last modified:May 20, 2008 - v2
    Checksum:i3BC5AEE20D7627DD
    GO
    Isoform 2 (identifier: O88829-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-26: MHTEAVGGAARRPQKLRSQAAAPACR → MGAPGELRRCGRGAA

    Show »
    Length:403
    Mass (Da):46,127
    Checksum:i9B344FEADD62FCA8
    GO

    Sequence cautioni

    The sequence AAF66147.1 differs from that shown. Reason: Erroneous initiation.
    The sequence BAA33491.1 differs from that shown. Reason: Erroneous initiation.
    The sequence BAA76467.1 differs from that shown. Reason: Erroneous initiation.
    The sequence BAB28571.1 differs from that shown. Reason: Erroneous initiation.
    The sequence BAE34763.1 differs from that shown. Reason: Erroneous initiation.
    The sequence CAA75235.1 differs from that shown. Reason: Erroneous initiation.
    The sequence CAA75236.1 differs from that shown. Reason: Erroneous initiation.
    The sequence CAC79655.1 differs from that shown. Reason: Erroneous gene model prediction.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti139 – 1391N → K in BAE34763. (PubMed:16141072)Curated
    Sequence conflicti183 – 1831P → S in CAA75235. (PubMed:9875239)Curated
    Sequence conflicti183 – 1831P → S in CAA75236. (PubMed:9875239)Curated
    Sequence conflicti232 – 2321H → Y in BAE34763. (PubMed:16141072)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 2626MHTEA…APACR → MGAPGELRRCGRGAA in isoform 2. 1 PublicationVSP_033689Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y15003 mRNA. Translation: CAA75235.1. Different initiation.
    Y15003 mRNA. Translation: CAA75236.1. Different initiation.
    AB018048 mRNA. Translation: BAA33491.1. Different initiation.
    AF119416 mRNA. Translation: AAF66147.1. Different initiation.
    AK012961 mRNA. Translation: BAB28571.1. Different initiation.
    AK159000 mRNA. Translation: BAE34763.1. Different initiation.
    AK165726 mRNA. Translation: BAE38355.1.
    BC138557 mRNA. Translation: AAI38558.1.
    BC138559 mRNA. Translation: AAI38560.1.
    AB013302 mRNA. Translation: BAA76467.1. Different initiation.
    Y18022 Genomic DNA. Translation: CAC79654.1.
    Y18023 Genomic DNA. Translation: CAC79655.1. Sequence problems.
    CCDSiCCDS20237.1. [O88829-1]
    PIRiJE0364.
    RefSeqiNP_001030305.1. NM_001035228.2. [O88829-1]
    NP_035505.2. NM_011375.3.
    XP_006505880.1. XM_006505817.1.
    UniGeneiMm.38248.

    Genome annotation databases

    EnsembliENSMUST00000069994; ENSMUSP00000070414; ENSMUSG00000056091. [O88829-1]
    ENSMUST00000114112; ENSMUSP00000109747; ENSMUSG00000056091.
    GeneIDi20454.
    KEGGimmu:20454.
    UCSCiuc009chy.1. mouse. [O88829-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Web resourcesi

    Functional Glycomics Gateway - GTase

    ST3Gal V

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y15003 mRNA. Translation: CAA75235.1 . Different initiation.
    Y15003 mRNA. Translation: CAA75236.1 . Different initiation.
    AB018048 mRNA. Translation: BAA33491.1 . Different initiation.
    AF119416 mRNA. Translation: AAF66147.1 . Different initiation.
    AK012961 mRNA. Translation: BAB28571.1 . Different initiation.
    AK159000 mRNA. Translation: BAE34763.1 . Different initiation.
    AK165726 mRNA. Translation: BAE38355.1 .
    BC138557 mRNA. Translation: AAI38558.1 .
    BC138559 mRNA. Translation: AAI38560.1 .
    AB013302 mRNA. Translation: BAA76467.1 . Different initiation.
    Y18022 Genomic DNA. Translation: CAC79654.1 .
    Y18023 Genomic DNA. Translation: CAC79655.1 . Sequence problems.
    CCDSi CCDS20237.1. [O88829-1 ]
    PIRi JE0364.
    RefSeqi NP_001030305.1. NM_001035228.2. [O88829-1 ]
    NP_035505.2. NM_011375.3.
    XP_006505880.1. XM_006505817.1.
    UniGenei Mm.38248.

    3D structure databases

    ProteinModelPortali O88829.
    SMRi O88829. Positions 132-363.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 10090.ENSMUSP00000070414.

    Protein family/group databases

    CAZyi GT29. Glycosyltransferase Family 29.

    PTM databases

    PhosphoSitei O88829.

    Proteomic databases

    PaxDbi O88829.
    PRIDEi O88829.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000069994 ; ENSMUSP00000070414 ; ENSMUSG00000056091 . [O88829-1 ]
    ENSMUST00000114112 ; ENSMUSP00000109747 ; ENSMUSG00000056091 .
    GeneIDi 20454.
    KEGGi mmu:20454.
    UCSCi uc009chy.1. mouse. [O88829-1 ]

    Organism-specific databases

    CTDi 8869.
    MGIi MGI:1339963. St3gal5.

    Phylogenomic databases

    eggNOGi NOG257001.
    GeneTreei ENSGT00620000087815.
    HOVERGENi HBG056676.
    InParanoidi B2RRS1.
    KOi K03370.
    OMAi FFWKQVA.
    OrthoDBi EOG76X609.
    PhylomeDBi O88829.
    TreeFami TF352819.

    Enzyme and pathway databases

    Reactomei REACT_202500. Sialic acid metabolism.

    Miscellaneous databases

    ChiTaRSi ST3GAL5. mouse.
    NextBioi 298530.
    PROi O88829.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O88829.
    Bgeei O88829.
    Genevestigatori O88829.

    Family and domain databases

    InterProi IPR001675. Glyco_trans_29.
    IPR012163. Sialyl_trans.
    [Graphical view ]
    Pfami PF00777. Glyco_transf_29. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF005557. Sialyl_trans. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning and characterization of fifth type of beta-galactoside alpha-2,3-sialyltransferase (ST3Gal V; GM3 synthase)."
      Kono M., Takashima S., Liu H., Inoue M., Kojima N., Young-Choon L., Hamamoto T., Tsuji S.
      Biochem. Biophys. Res. Commun. 253:170-175(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
      Strain: ICR.
      Tissue: Brain.
    2. "Mouse GM3 Synthase cDNA."
      Ishii A., Saito M.
      Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Strain: C57BL/6J.
      Tissue: Brain.
    3. "Combinatorial PCR in homologous cloning: cloning of GM3 synthase (ST-I)."
      Kapitonov D., Yu R.K.
      Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Strain: C57BL/6J.
    4. "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/6.
      Tissue: Visual cortex.
    5. "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).
      Tissue: Brain.
    6. "Expression cloning of mouse cDNA of CMP-NeuAc: lactosylceramide alpha2,3-sialyltransferase, an enzyme that initiates the synthesis of gangliosides."
      Fukumoto S., Miyazaki H., Goto G., Urano T., Furukawa K., Furukawa K.
      J. Biol. Chem. 274:9271-9276(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 52-414.
      Strain: BALB/c.
    7. Shuichi T.
      Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 106-414.
      Strain: ICR.
      Tissue: Brain.
    8. Cited for: FUNCTION, DISRUPTION PHENOTYPE.

    Entry informationi

    Entry nameiSIAT9_MOUSE
    AccessioniPrimary (citable) accession number: O88829
    Secondary accession number(s): B2RRS1
    , Q3TMT6, Q3TY01, Q91YF2, Q91YF3, Q9CZ65, Q9QWF8, Q9QWF9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 11, 2002
    Last sequence update: May 20, 2008
    Last modified: October 1, 2014
    This is version 109 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3