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Q91ZJ9

- HYAL1_MOUSE

UniProt

Q91ZJ9 - HYAL1_MOUSE

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Protein

Hyaluronidase-1

Gene
Hyal1
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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 donor By 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
Complete GO annotation...

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
Complete GO annotation...

Keywords - Cellular componenti

Lysosome, Secreted

PTM / Processingi

Molecule processing

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

Amino acid modifications

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

Family & Domainsi

Domains and Repeats

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

Sequence similaritiesi

Contains 1 EGF-like domain.

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

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei455 – 4628KWCDKRGM → GSST in isoform 2. VSP_015923

Sequence conflict

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

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 108 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

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