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Q91ZJ9

- HYAL1_MOUSE

UniProt

Q91ZJ9 - HYAL1_MOUSE

Protein

Hyaluronidase-1

Gene

Hyal1

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 3 (27 Jul 2011)
      Previous versions | rss
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    Functioni

    May have a role in promoting tumor progression. May block the TGFB1-enhanced cell growth.1 Publication

    Catalytic activityi

    Random hydrolysis of (1->4)-linkages between N-acetyl-beta-D-glucosamine and D-glucuronate residues in hyaluronate.

    pH dependencei

    Optimum pH is 3.5-4.0.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei159 – 1591Proton donorBy similarity

    GO - Molecular functioni

    1. hyaluronan synthase activity Source: UniProtKB
    2. hyalurononglucosaminidase activity Source: UniProtKB
    3. transcription factor binding Source: UniProtKB

    GO - Biological processi

    1. carbohydrate metabolic process Source: InterPro
    2. cartilage development Source: UniProtKB
    3. cellular response to fibroblast growth factor stimulus Source: Ensembl
    4. cellular response to interleukin-1 Source: UniProtKB
    5. cellular response to pH Source: UniProtKB
    6. cellular response to platelet-derived growth factor stimulus Source: UniProtKB
    7. cellular response to tumor necrosis factor Source: Ensembl
    8. cellular response to UV-B Source: UniProtKB
    9. embryonic skeletal joint morphogenesis Source: MGI
    10. hyaluronan biosynthetic process Source: UniProtKB
    11. hyaluronan catabolic process Source: UniProtKB
    12. hyaluronan metabolic process Source: UniProtKB
    13. inflammatory response Source: UniProtKB
    14. negative regulation of cell growth Source: UniProtKB
    15. positive regulation of angiogenesis Source: UniProtKB
    16. positive regulation of cell adhesion Source: UniProtKB
    17. positive regulation of cell growth Source: UniProtKB
    18. positive regulation of epithelial cell migration Source: UniProtKB
    19. positive regulation of epithelial cell proliferation Source: UniProtKB
    20. positive regulation of growth Source: UniProtKB
    21. positive regulation of hyaluranon cable assembly Source: UniProtKB
    22. response to antibiotic Source: UniProtKB
    23. response to reactive oxygen species Source: UniProtKB
    24. response to virus Source: UniProtKB

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Enzyme and pathway databases

    ReactomeiREACT_196554. Hyaluronan uptake and degradation.
    REACT_198981. CS/DS degradation.

    Protein family/group databases

    CAZyiGH56. Glycoside Hydrolase Family 56.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Hyaluronidase-1 (EC:3.2.1.35)
    Short name:
    Hyal-1
    Alternative name(s):
    Hyaluronoglucosaminidase-1
    Gene namesi
    Name:Hyal1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 9

    Organism-specific databases

    MGIiMGI:96298. Hyal1.

    Subcellular locationi

    Secreted By similarity. Lysosome By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. cytoplasmic vesicle Source: UniProtKB
    3. extracellular space Source: UniProtKB
    4. hyaluranon cable Source: UniProtKB
    5. lysosome Source: UniProtKB

    Keywords - Cellular componenti

    Lysosome, Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 5252Sequence AnalysisAdd
    BLAST
    Chaini53 – 462410Hyaluronidase-1PRO_0000042624Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi71 ↔ 361By similarity
    Glycosylationi98 – 981N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi127 – 1271N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi235 ↔ 249By similarity
    Glycosylationi244 – 2441N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi265 – 2651N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi378 – 3781N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi386 ↔ 397By similarity
    Disulfide bondi391 ↔ 446By similarity
    Disulfide bondi448 ↔ 457By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PRIDEiQ91ZJ9.

    Expressioni

    Tissue specificityi

    Highly expressed in liver, kidney, lung and skin.2 Publications

    Developmental stagei

    Detected in embryos of all developmental stages, with high level at the 7 day stage.1 Publication

    Gene expression databases

    BgeeiQ91ZJ9.
    CleanExiMM_HYAL1.
    GenevestigatoriQ91ZJ9.

    Interactioni

    Protein-protein interaction databases

    STRINGi10090.ENSMUSP00000010195.

    Structurei

    3D structure databases

    ProteinModelPortaliQ91ZJ9.
    SMRiQ91ZJ9. Positions 51-462.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini446 – 45712EGF-likeAdd
    BLAST

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 56 family.Curated
    Contains 1 EGF-like domain.Curated

    Keywords - Domaini

    EGF-like domain, Signal

    Phylogenomic databases

    eggNOGiNOG77606.
    GeneTreeiENSGT00550000074476.
    HOVERGENiHBG052053.
    InParanoidiB1AV90.
    KOiK01197.
    OMAiYPSIYMP.
    OrthoDBiEOG74J97S.
    TreeFamiTF321598.

    Family and domain databases

    Gene3Di3.20.20.70. 1 hit.
    InterProiIPR013785. Aldolase_TIM.
    IPR000742. EG-like_dom.
    IPR017853. Glycoside_hydrolase_SF.
    IPR018155. Hyaluronidase.
    [Graphical view]
    PANTHERiPTHR11769. PTHR11769. 1 hit.
    PfamiPF01630. Glyco_hydro_56. 1 hit.
    [Graphical view]
    PIRSFiPIRSF038193. Hyaluronidase. 1 hit.
    PRINTSiPR00846. GLHYDRLASE56.
    SMARTiSM00181. EGF. 1 hit.
    [Graphical view]
    SUPFAMiSSF51445. SSF51445. 1 hit.
    PROSITEiPS00022. EGF_1. 1 hit.
    PS01186. EGF_2. 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: Q91ZJ9-1) [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

    MLGLTQHAQK VWRMKPFSPE VSPGSSPATA GHLLRISTLF LTLLELAQVC    50
    RGSVVSNRPF ITVWNGDTHW CLTEYGVDVD VSVFDVVANK EQSFQGSNMT 100
    IFYREELGTY PYYTPTGEPV FGGLPQNASL VTHLAHTFQD IKAAMPEPDF 150
    SGLAVIDWEA WRPRWAFNWD SKDIYRQRSM ELVQAEHPDW PETLVEAAAK 200
    NQFQEAAEAW MAGTLQLGQV LRPRGLWGYY GFPDCYNNDF LSLNYTGQCP 250
    VFVRDQNDQL GWLWNQSYAL YPSIYLPAAL MGTEKSQMYV RHRVQEALRV 300
    AIVSRDPHVP VMPYVQIFYE MTDYLLPLEE LEHSLGESAA QGVAGAVLWL 350
    SSDKTSTKES CQAIKAYMDS TLGPFIVNVT SAALLCSEAL CSGHGRCVRH 400
    PSYPEALLTL NPASFSIELT HDGRPPSLKG TLSLKDRAQM AMKFRCRCYR 450
    GWRGKWCDKR GM 462
    Length:462
    Mass (Da):52,109
    Last modified:July 27, 2011 - v3
    Checksum:iDCE7339D7E0BCB9D
    GO
    Isoform 2 (identifier: Q91ZJ9-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         455-462: KWCDKRGM → GSST

    Note: No experimental confirmation available.

    Show »
    Length:458
    Mass (Da):51,436
    Checksum:iA510CD568AF4FA5F
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti16 – 161P → S in AAC15949. (PubMed:9503017)Curated
    Sequence conflicti16 – 161P → S in AAL17822. (PubMed:11960552)Curated
    Sequence conflicti247 – 2471G → R in AAC15949. (PubMed:9503017)Curated
    Sequence conflicti284 – 2841E → G in AAL17822. (PubMed:11960552)Curated
    Sequence conflicti284 – 2841E → G in AAL54881. 1 PublicationCurated
    Sequence conflicti284 – 2841E → G in AAL57173. 1 PublicationCurated
    Sequence conflicti450 – 4501R → C in AAL17822. (PubMed:11960552)Curated
    Sequence conflicti450 – 4501R → C in AAL54881. 1 PublicationCurated
    Sequence conflicti450 – 4501R → C in AAL57173. 1 PublicationCurated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei455 – 4628KWCDKRGM → GSST in isoform 2. 1 PublicationVSP_015923

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF011567 mRNA. Translation: AAC15949.1.
    AF422176 mRNA. Translation: AAL17822.1.
    AF069741 Genomic DNA. Translation: AAL54881.1.
    AF338323 Genomic DNA. Translation: AAL57173.1.
    AK028942 mRNA. Translation: BAC26206.1.
    AL672219 Genomic DNA. Translation: CAP19319.1.
    BC021636 mRNA. Translation: AAH21636.1.
    AF417496 mRNA. Translation: AAM14428.1.
    AF417497 mRNA. Translation: AAM14430.1.
    AF417498 mRNA. Translation: AAM14432.1.
    CCDSiCCDS23497.1. [Q91ZJ9-1]
    RefSeqiNP_032343.2. NM_008317.4. [Q91ZJ9-1]
    UniGeneiMm.475658.

    Genome annotation databases

    EnsembliENSMUST00000010195; ENSMUSP00000010195; ENSMUSG00000010051. [Q91ZJ9-1]
    ENSMUST00000112387; ENSMUSP00000108006; ENSMUSG00000010051. [Q91ZJ9-2]
    GeneIDi15586.
    KEGGimmu:15586.
    UCSCiuc009rlv.1. mouse. [Q91ZJ9-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF011567 mRNA. Translation: AAC15949.1 .
    AF422176 mRNA. Translation: AAL17822.1 .
    AF069741 Genomic DNA. Translation: AAL54881.1 .
    AF338323 Genomic DNA. Translation: AAL57173.1 .
    AK028942 mRNA. Translation: BAC26206.1 .
    AL672219 Genomic DNA. Translation: CAP19319.1 .
    BC021636 mRNA. Translation: AAH21636.1 .
    AF417496 mRNA. Translation: AAM14428.1 .
    AF417497 mRNA. Translation: AAM14430.1 .
    AF417498 mRNA. Translation: AAM14432.1 .
    CCDSi CCDS23497.1. [Q91ZJ9-1 ]
    RefSeqi NP_032343.2. NM_008317.4. [Q91ZJ9-1 ]
    UniGenei Mm.475658.

    3D structure databases

    ProteinModelPortali Q91ZJ9.
    SMRi Q91ZJ9. Positions 51-462.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 10090.ENSMUSP00000010195.

    Protein family/group databases

    CAZyi GH56. Glycoside Hydrolase Family 56.

    Proteomic databases

    PRIDEi Q91ZJ9.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000010195 ; ENSMUSP00000010195 ; ENSMUSG00000010051 . [Q91ZJ9-1 ]
    ENSMUST00000112387 ; ENSMUSP00000108006 ; ENSMUSG00000010051 . [Q91ZJ9-2 ]
    GeneIDi 15586.
    KEGGi mmu:15586.
    UCSCi uc009rlv.1. mouse. [Q91ZJ9-1 ]

    Organism-specific databases

    CTDi 3373.
    MGIi MGI:96298. Hyal1.

    Phylogenomic databases

    eggNOGi NOG77606.
    GeneTreei ENSGT00550000074476.
    HOVERGENi HBG052053.
    InParanoidi B1AV90.
    KOi K01197.
    OMAi YPSIYMP.
    OrthoDBi EOG74J97S.
    TreeFami TF321598.

    Enzyme and pathway databases

    Reactomei REACT_196554. Hyaluronan uptake and degradation.
    REACT_198981. CS/DS degradation.

    Miscellaneous databases

    NextBioi 288576.
    PROi Q91ZJ9.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q91ZJ9.
    CleanExi MM_HYAL1.
    Genevestigatori Q91ZJ9.

    Family and domain databases

    Gene3Di 3.20.20.70. 1 hit.
    InterProi IPR013785. Aldolase_TIM.
    IPR000742. EG-like_dom.
    IPR017853. Glycoside_hydrolase_SF.
    IPR018155. Hyaluronidase.
    [Graphical view ]
    PANTHERi PTHR11769. PTHR11769. 1 hit.
    Pfami PF01630. Glyco_hydro_56. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF038193. Hyaluronidase. 1 hit.
    PRINTSi PR00846. GLHYDRLASE56.
    SMARTi SM00181. EGF. 1 hit.
    [Graphical view ]
    SUPFAMi SSF51445. SSF51445. 1 hit.
    PROSITEi PS00022. EGF_1. 1 hit.
    PS01186. EGF_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The hyaluronidase gene HYAL1 maps to chromosome 3p21.2-p21.3 in human and 9F1-F2 in mouse, a conserved candidate tumor suppressor locus."
      Csoka A.B., Frost G.I., Heng H.H.Q., Scherer S.W., Mohapatra G., Stern R.
      Genomics 48:63-70(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES.
    2. "Transforming growth factor-beta1 blocks the enhancement of tumor necrosis factor cytotoxicity by hyaluronidase Hyal-2 in L929 fibroblasts."
      Chang N.-S.
      BMC Cell Biol. 3:8-8(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION.
      Strain: C3H.
    3. "Genomic sequence of the mouse Hyal1 locus encoding the mouse Hyal1, Fus2, and Hyal3 genes."
      Csoka A.B.
      Submitted (JAN-2001) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    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 2).
      Strain: C57BL/6J.
      Tissue: Skin.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    6. "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: Czech II.
      Tissue: Mammary gland.
    7. "Characterization of the murine hyaluronidase gene region reveals complex organization and cotranscription of Hyal1 with downstream genes, Fus2 and Hyal3."
      Shuttleworth T.L., Wilson M.D., Wicklow B.A., Wilkins J.A., Triggs-Raine B.L.
      J. Biol. Chem. 277:23008-23018(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 331-462, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
      Strain: 129/Sv.

    Entry informationi

    Entry nameiHYAL1_MOUSE
    AccessioniPrimary (citable) accession number: Q91ZJ9
    Secondary accession number(s): B1AV90
    , O70229, Q8CE62, Q8QZX3, Q8VBW7, Q8VDK0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 25, 2005
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 109 of the entry and version 3 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. Glycosyl hydrolases
      Classification of glycosyl hydrolase families and list of entries
    2. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3