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Q05A56

- HYAL4_MOUSE

UniProt

Q05A56 - HYAL4_MOUSE

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Protein
Hyaluronidase-4
Gene
Hyal4
Organism
Mus musculus (Mouse)
Status
Reviewed - 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.

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 donor By similarity

GO - Molecular functioni

  1. hyalurononglucosaminidase activity Source: MGI

GO - Biological processi

  1. carbohydrate metabolic process Source: InterPro
  2. 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: Chromosome 6

Organism-specific databases

MGIiMGI:1924292. Hyal4.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1111Cytoplasmic Reviewed prediction
Add
BLAST
Transmembranei12 – 3221Helical; Reviewed prediction
Add
BLAST
Topological domaini33 – 455423Extracellular Reviewed prediction
Add
BLAST
Transmembranei456 – 47621Helical; Reviewed prediction
Add
BLAST
Topological domaini477 – 4815Cytoplasmic Reviewed prediction

GO - Cellular componenti

  1. cell surface Source: MGI
  2. 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-4
PRO_0000302000Add
BLAST

Amino acid modifications

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

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ05A56.
PRIDEiQ05A56.

PTM databases

PhosphoSiteiQ05A56.

Expressioni

Gene expression databases

BgeeiQ05A56.
CleanExiMM_HYAL4.
GenevestigatoriQ05A56.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000031691.

Structurei

3D structure databases

ProteinModelPortaliQ05A56.
SMRiQ05A56. Positions 39-446.

Family & Domainsi

Compositional bias

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

Sequence similaritiesi

Keywords - Domaini

EGF-like domain, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG77606.
GeneTreeiENSGT00550000074476.
HOGENOMiHOG000015133.
HOVERGENiHBG052053.
InParanoidiQ05A56.
KOiK01197.
OMAiWNTKDVY.
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

MQLLPEGQLR LCVFQPVHLT SGLLILFILK SISSLKPARL PVYQRKPFIA    50
AWNAPTDLCL IKYNLTLNLK VFQMVGSPRL KDRGQNVVIF YANRLGYYPW 100
YTSEGVPING GLPQNTSLQV HLKKAAQDIN YYIPSENFSG LAVIDWEYWR 150
PQWARNWNTK DIYRQKSRTL ISDMKENISA ADIEYSAKAT FEKSAKAFME 200
ETIKLGSKSR PKGLWGYYLY PDCHNYNVYA TNYTGSCPEE EVLRNNDLSW 250
LWNSSTALYP AVSIRKSFAD SENTLHFSRF RVRESLRIST MTSQDYALPV 300
FVYTQLGYKE EPLLFLSKQD LISTIGESAA LGAAGIVVWG DMNLTSSEEN 350
CTKVNRFVNS DFGSYIINVT RAAEVCSRHL CKNNGRCVRK TWKAAHYLHL 400
NPASYHIEAS EDGEFIVRGR ASDTDLAVMA ENFLCHCYEG YEGADCREMT 450
EASGPSGLSL SSSSVITLCL LVLAGYQSIQ L 481
Length:481
Mass (Da):54,385
Last modified:November 14, 2006 - v1
Checksum:i388B46DDD9EFDB40
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti124 – 1263KAA → GAG in BAB29454. 1 Publication
Sequence conflicti316 – 3172LS → PF in BAB29454. 1 Publication
Sequence conflicti376 – 3761C → S in BAB29454. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
AK014599 mRNA. Translation: BAB29454.1 .
BC125402 mRNA. Translation: AAI25403.1 .
BC132096 mRNA. Translation: AAI32097.1 .
CCDSi CCDS39441.1.
RefSeqi NP_084124.1. NM_029848.1.
UniGenei Mm.66017.

3D structure databases

ProteinModelPortali Q05A56.
SMRi Q05A56. Positions 39-446.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 10090.ENSMUSP00000031691.

Protein family/group databases

CAZyi GH56. Glycoside Hydrolase Family 56.

PTM databases

PhosphoSitei Q05A56.

Proteomic databases

PaxDbi Q05A56.
PRIDEi Q05A56.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000031691 ; ENSMUSP00000031691 ; ENSMUSG00000029680 .
GeneIDi 77042.
KEGGi mmu:77042.
UCSCi uc009bbx.1. mouse.

Organism-specific databases

CTDi 23553.
MGIi MGI:1924292. Hyal4.

Phylogenomic databases

eggNOGi NOG77606.
GeneTreei ENSGT00550000074476.
HOGENOMi HOG000015133.
HOVERGENi HBG052053.
InParanoidi Q05A56.
KOi K01197.
OMAi WNTKDVY.
OrthoDBi EOG74J97S.
PhylomeDBi Q05A56.
TreeFami TF321598.

Miscellaneous databases

NextBioi 346362.
PROi Q05A56.
SOURCEi Search...

Gene expression databases

Bgeei Q05A56.
CleanExi MM_HYAL4.
Genevestigatori Q05A56.

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

  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 9, 2014
This is version 65 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

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