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O08650

- HYAS3_MOUSE

UniProt

O08650 - HYAS3_MOUSE

Protein

Hyaluronan synthase 3

Gene

Has3

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 109 (01 Oct 2014)
      Sequence version 2 (27 Jul 2011)
      Previous versions | rss
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    Functioni

    Catalyzes the addition of GlcNAc or GlcUA monosaccharides to the nascent hyaluronan polymer. Therefore, it is essential to hyaluronan synthesis a major component of most extracellular matrices that has a structural role in tissues architectures and regulates cell adhesion, migration and differentiation. This is one of the isozymes catalyzing that reaction.1 Publication

    Catalytic activityi

    UDP-alpha-N-acetyl-D-glucosamine + beta-D-glucuronosyl-(1->3)-N-acetyl-beta-D-glucosaminyl-(1->4)-(nascent hyaluronan) = UDP + N-acetyl-beta-D-glucosaminyl-(1->4)-beta-D-glucuronosyl-(1->3)-N-acetyl-beta-D-glucosaminyl-(1->4)-(nascent hyaluronan).1 Publication
    UDP-alpha-D-glucuronate + N-acetyl-beta-D-glucosaminyl-(1->4)-beta-D-glucuronosyl-(1->3)-(nascent hyaluronan) = UDP + beta-D-glucuronosyl-(1->3)-N-acetyl-beta-D-glucosaminyl-(1->4)-beta-D-glucuronosyl-(1->3)-(nascent hyaluronan).1 Publication

    Cofactori

    Magnesium.

    Kineticsi

    1. KM=0.2 mM for UDP-Glc-NAc (at pH 7.1 and 37 degrees Celsius, in the presence of 15 mM MgCl2)1 Publication
    2. KM=0.3 mM for UDP-Glc-UA (at pH 7.1 and 37 degrees Celsius, in the presence of 15 mM MgCl2)1 Publication

    Pathwayi

    GO - Molecular functioni

    1. hyaluronan synthase activity Source: UniProtKB

    GO - Biological processi

    1. extracellular matrix assembly Source: UniProtKB
    2. extracellular polysaccharide biosynthetic process Source: UniProtKB
    3. hyaluronan biosynthetic process Source: MGI
    4. positive regulation of hyaluranon cable assembly Source: Ensembl
    5. positive regulation of transcription, DNA-templated Source: Ensembl

    Keywords - Molecular functioni

    Glycosyltransferase, Transferase

    Enzyme and pathway databases

    BRENDAi2.4.1.212. 3474.
    ReactomeiREACT_196552. Hyaluronan biosynthesis and export.
    UniPathwayiUPA00341.

    Protein family/group databases

    CAZyiGT2. Glycosyltransferase Family 2.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Hyaluronan synthase 3 (EC:2.4.1.212)
    Alternative name(s):
    Hyaluronate synthase 3
    Hyaluronic acid synthase 3
    Short name:
    HA synthase 3
    Gene namesi
    Name:Has3
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 8

    Organism-specific databases

    MGIiMGI:109599. Has3.

    Subcellular locationi

    GO - Cellular componenti

    1. hyaluranon cable Source: Ensembl
    2. integral component of membrane Source: UniProtKB-KW

    Keywords - Cellular componenti

    Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 554554Hyaluronan synthase 3PRO_0000197179Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi463 – 4631N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Glycoprotein

    Proteomic databases

    PRIDEiO08650.

    PTM databases

    PhosphoSiteiO08650.

    Expressioni

    Developmental stagei

    Expressed at E17.5 day.

    Gene expression databases

    BgeeiO08650.
    CleanExiMM_HAS3.
    GenevestigatoriO08650.

    Interactioni

    Protein-protein interaction databases

    STRINGi10090.ENSMUSP00000034385.

    Structurei

    3D structure databases

    ProteinModelPortaliO08650.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 1515CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini37 – 448ExtracellularSequence Analysis
    Topological domaini66 – 378313CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini400 – 40910ExtracellularSequence Analysis
    Topological domaini431 – 44111CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini463 – 47412ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini496 – 51621CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini538 – 55417ExtracellularSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei16 – 3621Helical; Name=1Sequence AnalysisAdd
    BLAST
    Transmembranei45 – 6521Helical; Name=2Sequence AnalysisAdd
    BLAST
    Transmembranei379 – 39921Helical; Name=3Sequence AnalysisAdd
    BLAST
    Transmembranei410 – 43021Helical; Name=4Sequence AnalysisAdd
    BLAST
    Transmembranei442 – 46221Helical; Name=5Sequence AnalysisAdd
    BLAST
    Transmembranei475 – 49521Helical; Name=6Sequence AnalysisAdd
    BLAST
    Transmembranei517 – 53721Helical; Name=7Sequence AnalysisAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the NodC/HAS family.Curated

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG1215.
    GeneTreeiENSGT00390000010337.
    HOGENOMiHOG000112847.
    HOVERGENiHBG000189.
    InParanoidiQ8CEB9.
    KOiK00752.
    OMAiFIHTEQH.
    OrthoDBiEOG77WWBZ.
    TreeFamiTF332506.

    Family and domain databases

    Gene3Di3.90.550.10. 2 hits.
    InterProiIPR026108. HA_synthase_3.
    IPR026107. HAS/NodC.
    IPR029044. Nucleotide-diphossugar_trans.
    [Graphical view]
    PANTHERiPTHR22913. PTHR22913. 1 hit.
    PTHR22913:SF6. PTHR22913:SF6. 1 hit.
    SUPFAMiSSF53448. SSF53448. 2 hits.

    Sequencei

    Sequence statusi: Complete.

    O08650-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPVQLTTALR VVGTSLFALV VLGGILAAYV TGYQFIHTEK HYLSFGLYGA    50
    ILGLHLLIQS LFAFLEHRRM RRAGRPLKLH CSQRPRSVAL CIAAYQEDPE 100
    YLRKCLRSAQ RIAFPNLKVV MVVDGNRQED TYMLDIFHEV LGGTEQAGFF 150
    VWRSNFHEAG EGETEASLQE GMERVRAVVW ASTFSCIMQK WGGKREVMYT 200
    AFKALGNSVD YIQVCDSDTV LDPACTIEML RVLEEDPQVG GVGGDVQILN 250
    KYDSWISFLS SVRYWMAFNV ERACQSYFGC VQCISGPLGM YRNSLLQQFL 300
    EDWYHQKFLG SKCSFGDDRH LTNRVLSLGY RTKYTARSKC LTETPTRYLR 350
    WLNQQTRWSK SYFREWLYNS LWFHKHHLWM TYESVVTGFF PFFLIATVIQ 400
    LFYRGRIWNI LLFLLTVQLV GIIKATYACF LRGNAEMIFM SLYSLLYMSS 450
    LLPAKIFAIA TINKSGWGTS GRKTIVVNFI GLIPVSIWVA VLLGGLAYTA 500
    YCQDLFSETE LAFLVSGAIL YGCYWVALLM LYLAIIARRC GKKPEQYSLA 550
    FAEV 554
    Length:554
    Mass (Da):63,349
    Last modified:July 27, 2011 - v2
    Checksum:iBFFF239C901251DE
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti85 – 851P → S in AAC53128. (PubMed:9083017)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U86408 mRNA. Translation: AAC53128.1.
    AK028582 mRNA. Translation: BAC26017.1.
    BC138152 mRNA. Translation: AAI38153.1.
    CCDSiCCDS22640.1.
    RefSeqiNP_032243.2. NM_008217.4.
    XP_006530762.1. XM_006530699.1.
    XP_006530763.1. XM_006530700.1.
    XP_006530764.1. XM_006530701.1.
    UniGeneiMm.56986.

    Genome annotation databases

    EnsembliENSMUST00000034385; ENSMUSP00000034385; ENSMUSG00000031910.
    ENSMUST00000176144; ENSMUSP00000135303; ENSMUSG00000031910.
    GeneIDi15118.
    KEGGimmu:15118.
    UCSCiuc009ngn.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U86408 mRNA. Translation: AAC53128.1 .
    AK028582 mRNA. Translation: BAC26017.1 .
    BC138152 mRNA. Translation: AAI38153.1 .
    CCDSi CCDS22640.1.
    RefSeqi NP_032243.2. NM_008217.4.
    XP_006530762.1. XM_006530699.1.
    XP_006530763.1. XM_006530700.1.
    XP_006530764.1. XM_006530701.1.
    UniGenei Mm.56986.

    3D structure databases

    ProteinModelPortali O08650.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 10090.ENSMUSP00000034385.

    Protein family/group databases

    CAZyi GT2. Glycosyltransferase Family 2.

    PTM databases

    PhosphoSitei O08650.

    Proteomic databases

    PRIDEi O08650.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000034385 ; ENSMUSP00000034385 ; ENSMUSG00000031910 .
    ENSMUST00000176144 ; ENSMUSP00000135303 ; ENSMUSG00000031910 .
    GeneIDi 15118.
    KEGGi mmu:15118.
    UCSCi uc009ngn.2. mouse.

    Organism-specific databases

    CTDi 3038.
    MGIi MGI:109599. Has3.

    Phylogenomic databases

    eggNOGi COG1215.
    GeneTreei ENSGT00390000010337.
    HOGENOMi HOG000112847.
    HOVERGENi HBG000189.
    InParanoidi Q8CEB9.
    KOi K00752.
    OMAi FIHTEQH.
    OrthoDBi EOG77WWBZ.
    TreeFami TF332506.

    Enzyme and pathway databases

    UniPathwayi UPA00341 .
    BRENDAi 2.4.1.212. 3474.
    Reactomei REACT_196552. Hyaluronan biosynthesis and export.

    Miscellaneous databases

    NextBioi 287538.
    PROi O08650.
    SOURCEi Search...

    Gene expression databases

    Bgeei O08650.
    CleanExi MM_HAS3.
    Genevestigatori O08650.

    Family and domain databases

    Gene3Di 3.90.550.10. 2 hits.
    InterProi IPR026108. HA_synthase_3.
    IPR026107. HAS/NodC.
    IPR029044. Nucleotide-diphossugar_trans.
    [Graphical view ]
    PANTHERi PTHR22913. PTHR22913. 1 hit.
    PTHR22913:SF6. PTHR22913:SF6. 1 hit.
    SUPFAMi SSF53448. SSF53448. 2 hits.
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning and characterization of a cDNA encoding the third putative mammalian hyaluronan synthase."
      Spicer A.P., Olson J.S., McDonald J.A.
      J. Biol. Chem. 272:8957-8961(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: 129/SvJ and C57BL/6.
    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].
      Strain: C57BL/6J.
      Tissue: Skin.
    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].
      Tissue: Brain.
    4. Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, KINETIC PARAMETERS.

    Entry informationi

    Entry nameiHYAS3_MOUSE
    AccessioniPrimary (citable) accession number: O08650
    Secondary accession number(s): Q8CEB9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2000
    Last sequence update: July 27, 2011
    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. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3