Reviewed, UniProtKB/Swiss-Prot Q05A56 (HYAL4_MOUSE)

Names and origin

Protein names

Recommended name:
    Hyaluronidase-4
      Short name=Hyal-4
    EC=3.2.1.35
Alternative name(s):
    Hyaluronoglucosaminidase-4

Gene names

Name:

Hyal4

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	481 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Function	Endo-hyaluronidase that degrades hyaluronan to smaller oligosaccharide fragments. Has also chondroitase activity 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.

Ontologies

Keywords
Cellular component	Membrane
Domain	EGF-like domain Transmembrane
Molecular function	Glycosidase Hydrolase
PTM	Disulfide bond Glycoprotein
Gene Ontology (GO)
Biological process	carbohydrate metabolic process Inferred from electronic annotation. Source: InterPro fusion of sperm to egg plasma membrane Inferred from electronic annotation. Source: InterPro
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	hyalurononglucosaminidase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 481	481	Hyaluronidase-4		PRO_0000302000
Regions
	Topological domain	1 – 11	11	Cytoplasmic Potential
	Transmembrane	12 – 32	21	Potential
	Topological domain	33 – 455	423	Extracellular Potential
	Transmembrane	456 – 476	21	Potential
	Topological domain	477 – 481	5	Cytoplasmic Potential
	Compositional bias	459 – 464	6	Poly-Ser
Sites
	Active site	147	1	Proton donor By similarity
Amino acid modifications
	Glycosylation	64	1	N-linked (GlcNAc...) Potential
	Glycosylation	115	1	N-linked (GlcNAc...) Potential
	Glycosylation	232	1	N-linked (GlcNAc...) Potential
	Glycosylation	343	1	N-linked (GlcNAc...) Potential
	Disulfide bond	59 ↔ 351		By similarity
	Disulfide bond	223 ↔ 237		By similarity
	Disulfide bond	376 ↔ 387		By similarity
	Disulfide bond	381 ↔ 435		By similarity
	Disulfide bond	437 ↔ 446		By similarity
Experimental info
	Sequence conflict	124 – 126	3	KAA → GAG in BAB29454. Ref.1
	Sequence conflict	316 – 317	2	LS → PF in BAB29454. Ref.1
	Sequence conflict	376	1	C → S in BAB29454. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q05A56-1 [UniParc]. Last modified November 14, 2006. Version 1. Checksum: 388B46DDD9EFDB40	FASTA	481	54,385
	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

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. , 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]. 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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AK014599 mRNA. Translation: BAB29454.1. BC125402 mRNA. Translation: AAI25403.1. BC132096 mRNA. Translation: AAI32097.1.
IPI	IPI00317602.
RefSeq	NP_084124.1.
UniGene	Mm.66017
3D structure databases
ModBase	Search...
Protein family/group databases
CAZy	GH56. Glycoside Hydrolase Family 56.
Genome annotation databases
Ensembl	ENSMUSG00000029680. Mus musculus. [Contig view]
GeneID	77042.
KEGG	mmu:77042.
Organism-specific databases
MGI	MGI:1924292. Hyal4.
Phylogenomic databases
HOVERGEN	Q05A56.
OMA	Q05A56. YLAKATF.
Enzyme and pathway databases
BRENDA	3.2.1.35. 244.
Gene expression databases
ArrayExpress	Q05A56.
Bgee	Q05A56.
CleanEx	MM_HYAL4.
Family and domain databases
InterPro	IPR013785. Aldolase_TIM. IPR006210. EGF-like. IPR013032. EGF-like_reg_CS. IPR017430. Glyco_hydro_56_Hyaluronidase. IPR001439. Glyco_hydro_56_PH20. IPR001968. Glycoside_hydrolase_family_56. IPR018155. Hyaluronidase. [Graphical view]
Gene3D	G3DSA:3.20.20.70. Aldolase_TIM. 1 hit.
PANTHER	PTHR11769. Glyco_hydro_56. 1 hit.
Pfam	PF01630. Glyco_hydro_56. 1 hit. [Graphical view]
PIRSF	PIRSF038193. Hyaluronidase. 1 hit.
PRINTS	PR00846. GLHYDRLASE56. PR00848. SPERMPH20.
ProDom	PD003549. Glyco_hydro_56. 1 hit. [Graphical view] [Entries sharing at least one domain]
SMART	SM00181. EGF. 1 hit. [Graphical view]
PROSITE	PS00022. EGF_1. 1 hit. PS01186. EGF_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	346362.
SOURCE	Search...

Entry information

Entry name

HYAL4_MOUSE

Accession

Primary (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:	June 16, 2009
This is version 29 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)