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Reviewed, UniProtKB/Swiss-Prot Q91ZJ9 (HYAL1_MOUSE)

Last modified July 7, 2009. Version 62. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMus

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.6

Developmental stage

Detected in embryos of all developmental stages, with high level at the 7 day stage. Ref.6

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.

Ontologies

Keywords
   Cellular componentLysosome
Secreted
   Coding sequence diversityAlternative splicing
   DomainEGF-like domain
Signal
   Molecular functionGlycosidase
Hydrolase
   PTMDisulfide bond
Glycoprotein
Gene Ontology (GO)
   Biological processcarbohydrate metabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

lysosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionhyalurononglucosaminidase activity

Inferred from electronic annotation. Source: EC

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 Ref.1
Sequence conflict161P → S Ref.2
Sequence conflict2471G → R in AAC15949. Ref.1
Sequence conflict2841G → E Ref.1
Sequence conflict2841G → E Ref.4
Sequence conflict2841G → E in AAH21636. Ref.5
Sequence conflict4501R → C Ref.2
Sequence conflict4501R → C Ref.3

Sequences

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

Last modified October 25, 2005. Version 2.
Checksum: 5CE53210C95C9F45

FASTA46252,037
        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 MGTGKSQMYV 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.

Checksum: 0247998E69794DA8
Show »

FASTA45851,364

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: 9503017] [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: 11960552] [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: 16141072] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Strain: C57BL/6J.
Tissue: Skin.
[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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Strain: Czech II.
Tissue: Mammary gland.
[6]"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: 11929860] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 331-462, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
Strain: 129/Sv.
+Additional computationally mapped references.

Cross-references

Sequence databases

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.
BC021636 mRNA. Translation: AAH21636.1.
AF417496 mRNA. Translation: AAM14428.1.
AF417497 mRNA. Translation: AAM14430.1.
AF417498 mRNA. Translation: AAM14432.1.
IPIIPI00453571.
IPI00889928.
UniGeneMm.475658

3D structure databases

HSSPHSSP built from PDB template 1FCQ based on UniProtKB Q08169.
ModBaseSearch...

Protein family/group databases

CAZyGH56. Glycoside Hydrolase Family 56.

Genome annotation databases

EnsemblENSMUSG00000010051. Mus musculus. [Contig view]

Organism-specific databases

MGIMGI:96298. Hyal1.

Phylogenomic databases

HOGENOMQ91ZJ9.
HOVERGENQ91ZJ9.

Enzyme and pathway databases

BRENDA3.2.1.35. 244.

Gene expression databases

ArrayExpressQ91ZJ9.
BgeeQ91ZJ9.
CleanExMM_HYAL1.
GermOnlineENSMUSG00000010051. Mus musculus.

Family and domain databases

InterProIPR013785. Aldolase_TIM.
IPR006210. EGF-like.
IPR013032. EGF-like_reg_CS.
IPR017430. Glyco_hydro_56_Hyaluronidase.
IPR001968. Glycoside_hydrolase_family_56.
IPR018155. Hyaluronidase.
[Graphical view]
Gene3DG3DSA:3.20.20.70. Aldolase_TIM. 1 hit.
PANTHERPTHR11769. Glyco_hydro_56. 1 hit.
PfamPF01630. Glyco_hydro_56. 1 hit.
[Graphical view]
PIRSFPIRSF038193. Hyaluronidase. 1 hit.
PRINTSPR00846. GLHYDRLASE56.
ProDomPD003549. Glyco_hydro_56. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00181. EGF. 1 hit.
[Graphical view]
PROSITEPS00022. EGF_1. 1 hit.
PS01186. EGF_2. 1 hit.
PS50026. EGF_3. False negative.
[Graphical view]
ProtoNetSearch...

Other Resources

SOURCESearch...

Entry information

Entry nameHYAL1_MOUSE
AccessionPrimary (citable) accession number: Q91ZJ9
Secondary accession number(s): O70229 expand/collapse secondary AC list , Q8CE62, Q8QZX3, Q8VBW7, Q8VDK0
Entry history
Integrated into UniProtKB/Swiss-Prot: October 25, 2005
Last sequence update: October 25, 2005
Last modified: July 7, 2009
This is version 62 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

MGD cross-references

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

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents