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Q91ZJ9 (HYAL1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 105. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Hyaluronidase-1

Short name=Hyal-1
EC=3.2.1.35
Alternative name(s):
Hyaluronoglucosaminidase-1
Gene names
Name:Hyal1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length462 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May have a role in promoting tumor progression. May block the TGFB1-enhanced cell growth. Ref.2

Catalytic activity

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

Subcellular location

Secreted By similarity. Lysosome By similarity.

Tissue specificity

Highly expressed in liver, kidney, lung and skin. Ref.1 Ref.7

Developmental stage

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

Sequence similarities

Belongs to the glycosyl hydrolase 56 family.

Contains 1 EGF-like domain.

Biophysicochemical properties

pH dependence:

Optimum pH is 3.5-4.0. Ref.1

Ontologies

Keywords
   Cellular componentLysosome
Secreted
   Coding sequence diversityAlternative splicing
   DomainEGF-like domain
Signal
   Molecular functionGlycosidase
Hydrolase
   PTMDisulfide bond
Glycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcarbohydrate metabolic process

Inferred from electronic annotation. Source: InterPro

cartilage development

Inferred from sequence or structural similarity. Source: UniProtKB

cellular response to UV-B

Inferred from sequence or structural similarity. Source: UniProtKB

cellular response to fibroblast growth factor stimulus

Inferred from electronic annotation. Source: Ensembl

cellular response to interleukin-1

Inferred from sequence or structural similarity. Source: UniProtKB

cellular response to pH

Inferred from sequence or structural similarity. Source: UniProtKB

cellular response to platelet-derived growth factor stimulus

Inferred from sequence or structural similarity. Source: UniProtKB

cellular response to tumor necrosis factor

Inferred from electronic annotation. Source: Ensembl

embryonic skeletal joint morphogenesis

Inferred from mutant phenotype PubMed 18772348. Source: MGI

hyaluronan biosynthetic process

Inferred from sequence or structural similarity. Source: UniProtKB

hyaluronan catabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

hyaluronan metabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

inflammatory response

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of cell growth

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of angiogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of cell adhesion

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of cell growth

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of epithelial cell migration

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of epithelial cell proliferation

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of growth

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of hyaluranon cable assembly

Inferred from sequence or structural similarity. Source: UniProtKB

response to antibiotic

Inferred from sequence or structural similarity. Source: UniProtKB

response to reactive oxygen species

Inferred from sequence or structural similarity. Source: UniProtKB

response to virus

Inferred from direct assay PubMed 11296287. Source: UniProtKB

   Cellular_componentcytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

cytoplasmic vesicle

Inferred from sequence or structural similarity. Source: UniProtKB

extracellular space

Inferred from sequence or structural similarity. Source: UniProtKB

hyaluranon cable

Inferred from sequence or structural similarity. Source: UniProtKB

lysosome

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionhyaluronan synthase activity

Inferred from sequence or structural similarity. Source: UniProtKB

hyalurononglucosaminidase activity

Inferred from sequence or structural similarity. Source: UniProtKB

transcription factor binding

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q91ZJ9-1)

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.
Isoform 2 (identifier: Q91ZJ9-2)

The sequence of this isoform differs from the canonical sequence as follows:
     455-462: KWCDKRGM → GSST
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 5252 Potential
Chain53 – 462410Hyaluronidase-1
PRO_0000042624

Regions

Domain446 – 45712EGF-like

Sites

Active site1591Proton donor By similarity

Amino acid modifications

Glycosylation981N-linked (GlcNAc...) Potential
Glycosylation1271N-linked (GlcNAc...) Potential
Glycosylation2441N-linked (GlcNAc...) Potential
Glycosylation2651N-linked (GlcNAc...) Potential
Glycosylation3781N-linked (GlcNAc...) Potential
Disulfide bond71 ↔ 361 By similarity
Disulfide bond235 ↔ 249 By similarity
Disulfide bond386 ↔ 397 By similarity
Disulfide bond391 ↔ 446 By similarity
Disulfide bond448 ↔ 457 By similarity

Natural variations

Alternative sequence455 – 4628KWCDKRGM → GSST in isoform 2.
VSP_015923

Experimental info

Sequence conflict161P → S in AAC15949. Ref.1
Sequence conflict161P → S in AAL17822. Ref.2
Sequence conflict2471G → R in AAC15949. Ref.1
Sequence conflict2841E → G in AAL17822. Ref.2
Sequence conflict2841E → G in AAL54881. Ref.3
Sequence conflict2841E → G in AAL57173. Ref.3
Sequence conflict4501R → C in AAL17822. Ref.2
Sequence conflict4501R → C in AAL54881. Ref.3
Sequence conflict4501R → C in AAL57173. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified July 27, 2011. Version 3.
Checksum: DCE7339D7E0BCB9D

FASTA46252,109
        10         20         30         40         50         60 
MLGLTQHAQK VWRMKPFSPE VSPGSSPATA GHLLRISTLF LTLLELAQVC RGSVVSNRPF 

        70         80         90        100        110        120 
ITVWNGDTHW CLTEYGVDVD VSVFDVVANK EQSFQGSNMT IFYREELGTY PYYTPTGEPV 

       130        140        150        160        170        180 
FGGLPQNASL VTHLAHTFQD IKAAMPEPDF SGLAVIDWEA WRPRWAFNWD SKDIYRQRSM 

       190        200        210        220        230        240 
ELVQAEHPDW PETLVEAAAK NQFQEAAEAW MAGTLQLGQV LRPRGLWGYY GFPDCYNNDF 

       250        260        270        280        290        300 
LSLNYTGQCP VFVRDQNDQL GWLWNQSYAL YPSIYLPAAL MGTEKSQMYV RHRVQEALRV 

       310        320        330        340        350        360 
AIVSRDPHVP VMPYVQIFYE MTDYLLPLEE LEHSLGESAA QGVAGAVLWL SSDKTSTKES 

       370        380        390        400        410        420 
CQAIKAYMDS TLGPFIVNVT SAALLCSEAL CSGHGRCVRH PSYPEALLTL NPASFSIELT 

       430        440        450        460 
HDGRPPSLKG TLSLKDRAQM AMKFRCRCYR GWRGKWCDKR GM 

« Hide

Isoform 2 [UniParc].

Checksum: A510CD568AF4FA5F
Show »

FASTA45851,436

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_032343.2. NM_008317.4.
UniGeneMm.475658.

3D structure databases

ProteinModelPortalQ91ZJ9.
SMRQ91ZJ9. Positions 51-462.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000010195.

Protein family/group databases

CAZyGH56. Glycoside Hydrolase Family 56.

Proteomic databases

PRIDEQ91ZJ9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000010195; ENSMUSP00000010195; ENSMUSG00000010051. [Q91ZJ9-1]
ENSMUST00000112387; ENSMUSP00000108006; ENSMUSG00000010051. [Q91ZJ9-2]
GeneID15586.
KEGGmmu:15586.
UCSCuc009rlv.1. mouse. [Q91ZJ9-1]

Organism-specific databases

CTD3373.
MGIMGI:96298. Hyal1.

Phylogenomic databases

eggNOGNOG77606.
GeneTreeENSGT00550000074476.
HOVERGENHBG052053.
InParanoidB1AV90.
KOK01197.
OMAYPSIYMP.
OrthoDBEOG74J97S.
TreeFamTF321598.

Gene expression databases

BgeeQ91ZJ9.
CleanExMM_HYAL1.
GenevestigatorQ91ZJ9.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
InterProIPR013785. Aldolase_TIM.
IPR000742. EG-like_dom.
IPR017853. Glycoside_hydrolase_SF.
IPR018155. Hyaluronidase.
[Graphical view]
PANTHERPTHR11769. PTHR11769. 1 hit.
PfamPF01630. Glyco_hydro_56. 1 hit.
[Graphical view]
PIRSFPIRSF038193. Hyaluronidase. 1 hit.
PRINTSPR00846. GLHYDRLASE56.
SMARTSM00181. EGF. 1 hit.
[Graphical view]
SUPFAMSSF51445. SSF51445. 1 hit.
PROSITEPS00022. EGF_1. 1 hit.
PS01186. EGF_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio288576.
PROQ91ZJ9.
SOURCESearch...

Entry information

Entry nameHYAL1_MOUSE
AccessionPrimary (citable) accession number: Q91ZJ9
Secondary accession number(s): B1AV90 expand/collapse secondary AC list , O70229, Q8CE62, Q8QZX3, Q8VBW7, Q8VDK0
Entry history
Integrated into UniProtKB/Swiss-Prot: October 25, 2005
Last sequence update: July 27, 2011
Last modified: April 16, 2014
This is version 105 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries