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Q05A56 (HYAL4_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 65. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Hyaluronidase-4

Short name=Hyal-4
EC=3.2.1.35
Alternative name(s):
Chondroitin sulfate endo-beta-N-acetylgalactosaminidase
Chondroitin sulfate hydrolase
Short name=CSHY
Hyaluronoglucosaminidase-4
Gene names
Name:Hyal4
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length481 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Endo-hyaluronidase that degrades hyaluronan to smaller oligosaccharide fragments. Has also chondroitin sulfate hydrolase activity, The best substrate being the galactosaminidic linkage in the sequence of a trisulfated tetrasaccharide By similarity.

Catalytic activity

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

Subcellular location

Membrane; Multi-pass membrane protein Potential.

Sequence similarities

Belongs to the glycosyl hydrolase 56 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 481481Hyaluronidase-4
PRO_0000302000

Regions

Topological domain1 – 1111Cytoplasmic Potential
Transmembrane12 – 3221Helical; Potential
Topological domain33 – 455423Extracellular Potential
Transmembrane456 – 47621Helical; Potential
Topological domain477 – 4815Cytoplasmic Potential
Compositional bias459 – 4646Poly-Ser

Sites

Active site1471Proton donor By similarity

Amino acid modifications

Glycosylation641N-linked (GlcNAc...) Potential
Glycosylation1151N-linked (GlcNAc...) Potential
Glycosylation2321N-linked (GlcNAc...) Potential
Glycosylation3431N-linked (GlcNAc...) Potential
Disulfide bond59 ↔ 351 By similarity
Disulfide bond223 ↔ 237 By similarity
Disulfide bond376 ↔ 387 By similarity
Disulfide bond381 ↔ 435 By similarity
Disulfide bond437 ↔ 446 By similarity

Experimental info

Sequence conflict124 – 1263KAA → GAG in BAB29454. Ref.1
Sequence conflict316 – 3172LS → PF in BAB29454. Ref.1
Sequence conflict3761C → S in BAB29454. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q05A56 [UniParc].

Last modified November 14, 2006. Version 1.
Checksum: 388B46DDD9EFDB40

FASTA48154,385
        10         20         30         40         50         60 
MQLLPEGQLR LCVFQPVHLT SGLLILFILK SISSLKPARL PVYQRKPFIA AWNAPTDLCL 

        70         80         90        100        110        120 
IKYNLTLNLK VFQMVGSPRL KDRGQNVVIF YANRLGYYPW YTSEGVPING GLPQNTSLQV 

       130        140        150        160        170        180 
HLKKAAQDIN YYIPSENFSG LAVIDWEYWR PQWARNWNTK DIYRQKSRTL ISDMKENISA 

       190        200        210        220        230        240 
ADIEYSAKAT FEKSAKAFME ETIKLGSKSR PKGLWGYYLY PDCHNYNVYA TNYTGSCPEE 

       250        260        270        280        290        300 
EVLRNNDLSW LWNSSTALYP AVSIRKSFAD SENTLHFSRF RVRESLRIST MTSQDYALPV 

       310        320        330        340        350        360 
FVYTQLGYKE EPLLFLSKQD LISTIGESAA LGAAGIVVWG DMNLTSSEEN CTKVNRFVNS 

       370        380        390        400        410        420 
DFGSYIINVT RAAEVCSRHL CKNNGRCVRK TWKAAHYLHL NPASYHIEAS EDGEFIVRGR 

       430        440        450        460        470        480 
ASDTDLAVMA ENFLCHCYEG YEGADCREMT EASGPSGLSL SSSSVITLCL LVLAGYQSIQ 


L 

« Hide

References

[1]"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].
Strain: C57BL/6J.
Tissue: Skin.
[2]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK014599 mRNA. Translation: BAB29454.1.
BC125402 mRNA. Translation: AAI25403.1.
BC132096 mRNA. Translation: AAI32097.1.
CCDSCCDS39441.1.
RefSeqNP_084124.1. NM_029848.1.
UniGeneMm.66017.

3D structure databases

ProteinModelPortalQ05A56.
SMRQ05A56. Positions 39-446.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000031691.

Protein family/group databases

CAZyGH56. Glycoside Hydrolase Family 56.

PTM databases

PhosphoSiteQ05A56.

Proteomic databases

PaxDbQ05A56.
PRIDEQ05A56.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000031691; ENSMUSP00000031691; ENSMUSG00000029680.
GeneID77042.
KEGGmmu:77042.
UCSCuc009bbx.1. mouse.

Organism-specific databases

CTD23553.
MGIMGI:1924292. Hyal4.

Phylogenomic databases

eggNOGNOG77606.
GeneTreeENSGT00550000074476.
HOGENOMHOG000015133.
HOVERGENHBG052053.
InParanoidQ05A56.
KOK01197.
OMAWNTKDVY.
OrthoDBEOG74J97S.
PhylomeDBQ05A56.
TreeFamTF321598.

Gene expression databases

BgeeQ05A56.
CleanExMM_HYAL4.
GenevestigatorQ05A56.

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

NextBio346362.
PROQ05A56.
SOURCESearch...

Entry information

Entry nameHYAL4_MOUSE
AccessionPrimary (citable) accession number: Q05A56
Secondary accession number(s): Q9D660
Entry history
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: November 14, 2006
Last modified: July 9, 2014
This is version 65 of the entry and version 1 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