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Protein

Hyaluronidase-4

Gene

Hyal4

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

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).By similarity

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei147 – 1471Proton donorBy similarity

GO - Molecular functioni

  • hyalurononglucosaminidase activity Source: MGI

GO - Biological processi

  • carbohydrate metabolic process Source: InterPro
  • chondroitin sulfate catabolic process Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Protein family/group databases

CAZyiGH56. Glycoside Hydrolase Family 56.

Names & Taxonomyi

Protein namesi
Recommended name:
Hyaluronidase-4 (EC:3.2.1.35)
Short name:
Hyal-4
Alternative name(s):
Chondroitin sulfate endo-beta-N-acetylgalactosaminidase
Chondroitin sulfate hydrolase
Short name:
CSHY
Hyaluronoglucosaminidase-4
Gene namesi
Name:Hyal4
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 6

Organism-specific databases

MGIiMGI:1924292. Hyal4.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1111CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei12 – 3221HelicalSequence AnalysisAdd
BLAST
Topological domaini33 – 455423ExtracellularSequence AnalysisAdd
BLAST
Transmembranei456 – 47621HelicalSequence AnalysisAdd
BLAST
Topological domaini477 – 4815CytoplasmicSequence Analysis

GO - Cellular componenti

  • cell surface Source: MGI
  • integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 481481Hyaluronidase-4PRO_0000302000Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi59 ↔ 351By similarity
Glycosylationi64 – 641N-linked (GlcNAc...)Sequence Analysis
Glycosylationi115 – 1151N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi223 ↔ 237By similarity
Glycosylationi232 – 2321N-linked (GlcNAc...)Sequence Analysis
Glycosylationi343 – 3431N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi376 ↔ 387By similarity
Disulfide bondi381 ↔ 435By similarity
Disulfide bondi437 ↔ 446By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ05A56.
PRIDEiQ05A56.

PTM databases

PhosphoSiteiQ05A56.

Expressioni

Gene expression databases

BgeeiQ05A56.
CleanExiMM_HYAL4.
ExpressionAtlasiQ05A56. baseline.
GenevisibleiQ05A56. MM.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000031691.

Structurei

3D structure databases

ProteinModelPortaliQ05A56.
SMRiQ05A56. Positions 39-446.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi459 – 4646Poly-Ser

Sequence similaritiesi

Belongs to the glycosyl hydrolase 56 family.Curated

Keywords - Domaini

EGF-like domain, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG77606.
GeneTreeiENSGT00550000074476.
HOGENOMiHOG000015133.
HOVERGENiHBG052053.
InParanoidiQ05A56.
KOiK01197.
OMAiSEDGEFT.
OrthoDBiEOG74J97S.
PhylomeDBiQ05A56.
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]

Sequencei

Sequence statusi: Complete.

Q05A56-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQLLPEGQLR LCVFQPVHLT SGLLILFILK SISSLKPARL PVYQRKPFIA
60 70 80 90 100
AWNAPTDLCL IKYNLTLNLK VFQMVGSPRL KDRGQNVVIF YANRLGYYPW
110 120 130 140 150
YTSEGVPING GLPQNTSLQV HLKKAAQDIN YYIPSENFSG LAVIDWEYWR
160 170 180 190 200
PQWARNWNTK DIYRQKSRTL ISDMKENISA ADIEYSAKAT FEKSAKAFME
210 220 230 240 250
ETIKLGSKSR PKGLWGYYLY PDCHNYNVYA TNYTGSCPEE EVLRNNDLSW
260 270 280 290 300
LWNSSTALYP AVSIRKSFAD SENTLHFSRF RVRESLRIST MTSQDYALPV
310 320 330 340 350
FVYTQLGYKE EPLLFLSKQD LISTIGESAA LGAAGIVVWG DMNLTSSEEN
360 370 380 390 400
CTKVNRFVNS DFGSYIINVT RAAEVCSRHL CKNNGRCVRK TWKAAHYLHL
410 420 430 440 450
NPASYHIEAS EDGEFIVRGR ASDTDLAVMA ENFLCHCYEG YEGADCREMT
460 470 480
EASGPSGLSL SSSSVITLCL LVLAGYQSIQ L
Length:481
Mass (Da):54,385
Last modified:November 14, 2006 - v1
Checksum:i388B46DDD9EFDB40
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti124 – 1263KAA → GAG in BAB29454 (PubMed:16141072).Curated
Sequence conflicti316 – 3172LS → PF in BAB29454 (PubMed:16141072).Curated
Sequence conflicti376 – 3761C → S in BAB29454 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK014599 mRNA. Translation: BAB29454.1.
BC125402 mRNA. Translation: AAI25403.1.
BC132096 mRNA. Translation: AAI32097.1.
CCDSiCCDS39441.1.
RefSeqiNP_084124.1. NM_029848.1.
UniGeneiMm.66017.

Genome annotation databases

EnsembliENSMUST00000031691; ENSMUSP00000031691; ENSMUSG00000029680.
GeneIDi77042.
KEGGimmu:77042.
UCSCiuc009bbx.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK014599 mRNA. Translation: BAB29454.1.
BC125402 mRNA. Translation: AAI25403.1.
BC132096 mRNA. Translation: AAI32097.1.
CCDSiCCDS39441.1.
RefSeqiNP_084124.1. NM_029848.1.
UniGeneiMm.66017.

3D structure databases

ProteinModelPortaliQ05A56.
SMRiQ05A56. Positions 39-446.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000031691.

Protein family/group databases

CAZyiGH56. Glycoside Hydrolase Family 56.

PTM databases

PhosphoSiteiQ05A56.

Proteomic databases

PaxDbiQ05A56.
PRIDEiQ05A56.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000031691; ENSMUSP00000031691; ENSMUSG00000029680.
GeneIDi77042.
KEGGimmu:77042.
UCSCiuc009bbx.1. mouse.

Organism-specific databases

CTDi23553.
MGIiMGI:1924292. Hyal4.

Phylogenomic databases

eggNOGiNOG77606.
GeneTreeiENSGT00550000074476.
HOGENOMiHOG000015133.
HOVERGENiHBG052053.
InParanoidiQ05A56.
KOiK01197.
OMAiSEDGEFT.
OrthoDBiEOG74J97S.
PhylomeDBiQ05A56.
TreeFamiTF321598.

Miscellaneous databases

NextBioi346362.
PROiQ05A56.
SOURCEiSearch...

Gene expression databases

BgeeiQ05A56.
CleanExiMM_HYAL4.
ExpressionAtlasiQ05A56. baseline.
GenevisibleiQ05A56. MM.

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]
ProtoNetiSearch...

Publicationsi

  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.
    , 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.

Entry informationi

Entry nameiHYAL4_MOUSE
AccessioniPrimary (citable) accession number: Q05A56
Secondary accession number(s): Q9D660
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: November 14, 2006
Last modified: July 22, 2015
This is version 70 of the entry and version 1 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.