Q91ZJ9 (HYAL1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Hyaluronidase-1
Short name=Hyal-1
EC=3.2.1.35

Alternative name(s):
Hyaluronoglucosaminidase-1

Gene names

Name:

Hyal1

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	462 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.7
Developmental stage	Detected in embryos of all developmental stages, with high level at the 7 day stage. Ref.7
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. Ref.1

Ontologies

Keywords
Cellular component	Lysosome Secreted
Coding sequence diversity	Alternative splicing
Domain	EGF-like domain Signal
Molecular function	Glycosidase Hydrolase
PTM	Disulfide bond Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	carbohydrate metabolic process Inferred from electronic annotation. Source: InterPro cartilage development Inferred from sequence or structural similarity. Source: UniProtKB cellular response to UV-B Inferred from sequence or structural similarity. Source: UniProtKB cellular response to fibroblast growth factor stimulus Inferred from electronic annotation. Source: Compara cellular response to interleukin-1 Inferred from sequence or structural similarity. Source: UniProtKB cellular response to pH Inferred from sequence or structural similarity. Source: UniProtKB cellular response to platelet-derived growth factor stimulus Inferred from sequence or structural similarity. Source: UniProtKB cellular response to tumor necrosis factor Inferred from electronic annotation. Source: Compara embryonic skeletal joint morphogenesis Inferred from mutant phenotype PubMed 18772348. Source: MGI hyaluronan biosynthetic process Inferred from sequence or structural similarity. Source: UniProtKB hyaluronan catabolic process Inferred from sequence or structural similarity. Source: UniProtKB inflammatory response Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of cell growth Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of S phase of mitotic cell cycle Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of angiogenesis Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of cell adhesion Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of cell growth Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of epithelial cell migration Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of epithelial cell proliferation Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of hyaluranon cable assembly Inferred from sequence or structural similarity. Source: UniProtKB response to antibiotic Inferred from sequence or structural similarity. Source: UniProtKB response to reactive oxygen species Inferred from sequence or structural similarity. Source: UniProtKB response to virus Inferred from direct assay PubMed 11296287. Source: UniProtKB
Cellular_component	cytoplasmic vesicle Inferred from sequence or structural similarity. Source: UniProtKB extracellular space Inferred from sequence or structural similarity. Source: UniProtKB hyaluranon cable Inferred from sequence or structural similarity. Source: UniProtKB lysosome Inferred from sequence or structural similarity. Source: UniProtKB
Molecular_function	hyaluronan synthase activity Inferred from sequence or structural similarity. Source: UniProtKB hyalurononglucosaminidase activity Inferred from sequence or structural similarity. Source: UniProtKB transcription factor binding Inferred from sequence or structural similarity. Source: UniProtKB
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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 52	52	Potential
	Chain	53 – 462	410	Hyaluronidase-1		PRO_0000042624
Regions
	Domain	446 – 457	12	EGF-like
Sites
	Active site	159	1	Proton donor By similarity
Amino acid modifications
	Glycosylation	98	1	N-linked (GlcNAc...) Potential
	Glycosylation	127	1	N-linked (GlcNAc...) Potential
	Glycosylation	244	1	N-linked (GlcNAc...) Potential
	Glycosylation	265	1	N-linked (GlcNAc...) Potential
	Glycosylation	378	1	N-linked (GlcNAc...) Potential
	Disulfide bond	71 ↔ 361		By similarity
	Disulfide bond	235 ↔ 249		By similarity
	Disulfide bond	386 ↔ 397		By similarity
	Disulfide bond	391 ↔ 446		By similarity
	Disulfide bond	448 ↔ 457		By similarity
Natural variations
	Alternative sequence	455 – 462	8	KWCDKRGM → GSST in isoform 2.		VSP_015923
Experimental info
	Sequence conflict	16	1	P → S in AAC15949. Ref.1
	Sequence conflict	16	1	P → S in AAL17822. Ref.2
	Sequence conflict	247	1	G → R in AAC15949. Ref.1
	Sequence conflict	284	1	E → G in AAL17822. Ref.2
	Sequence conflict	284	1	E → G in AAL54881. Ref.3
	Sequence conflict	284	1	E → G in AAL57173. Ref.3
	Sequence conflict	450	1	R → C in AAL17822. Ref.2
	Sequence conflict	450	1	R → C in AAL54881. Ref.3
	Sequence conflict	450	1	R → C in AAL57173. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified July 27, 2011. Version 3. Checksum: DCE7339D7E0BCB9D	FASTA	462	52,109
	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 MGTEKSQMYV 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
	Isoform 2 [UniParc]. Checksum: A510CD568AF4FA5F	FASTA	458	51,436
	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 MGTEKSQMYV 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 HDGRPPSLKG TLSLKDRAQM AMKFRCRCYR GWRGGSST

References

	« Hide 'large scale' referencesShow '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] [Europe PMC] [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] [Europe PMC] [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. , 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] (ISOFORM 2). Strain: C57BL/6J. Tissue: Skin.
[5]	"Lineage-specific biology revealed by a finished genome assembly of the mouse." Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P. PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: C57BL/6J.
[6]	"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] (ISOFORM 1). Strain: Czech II. Tissue: Mammary gland.
[7]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 331-462, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE. Strain: 129/Sv.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	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. AL672219 Genomic DNA. Translation: CAP19319.1. BC021636 mRNA. Translation: AAH21636.1. AF417496 mRNA. Translation: AAM14428.1. AF417497 mRNA. Translation: AAM14430.1. AF417498 mRNA. Translation: AAM14432.1.
IPI	IPI00453571. IPI00889928.
RefSeq	NP_032343.2. NM_008317.4.
UniGene	Mm.10305. Mm.475658.
3D structure databases
ProteinModelPortal	Q91ZJ9.
SMR	Q91ZJ9. Positions 51-462.
ModBase	Search...
Protein-protein interaction databases
STRING	10090.ENSMUSP00000010195.
Protein family/group databases
CAZy	GH56. Glycoside Hydrolase Family 56.
Proteomic databases
PRIDE	Q91ZJ9.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000010195; ENSMUSP00000010195; ENSMUSG00000010051. ENSMUST00000112387; ENSMUSP00000108006; ENSMUSG00000010051.
GeneID	15586.
KEGG	mmu:15586.
Organism-specific databases
CTD	3373.
MGI	MGI:96298. Hyal1.
Phylogenomic databases
eggNOG	NOG77606.
GeneTree	ENSGT00550000074476.
HOVERGEN	HBG052053.
InParanoid	B1AV90.
KO	K01197.
OMA	WVSWENT.
OrthoDB	EOG4VDPZD.
Gene expression databases
ArrayExpress	Q91ZJ9.
Bgee	Q91ZJ9.
CleanEx	MM_HYAL1.
Genevestigator	Q91ZJ9.
GermOnline	ENSMUSG00000010051. Mus musculus.
Family and domain databases
Gene3D	3.20.20.70. 1 hit.
InterPro	IPR013785. Aldolase_TIM. IPR000742. EG-like_dom. IPR017853. Glycoside_hydrolase_SF. IPR018155. Hyaluronidase. [Graphical view]
PANTHER	PTHR11769. PTHR11769. 1 hit.
Pfam	PF01630. Glyco_hydro_56. 1 hit. [Graphical view]
PIRSF	PIRSF038193. Hyaluronidase. 1 hit.
PRINTS	PR00846. GLHYDRLASE56.
SMART	SM00181. EGF. 1 hit. [Graphical view]
SUPFAM	SSF51445. Glyco_hydro_cat. 1 hit.
PROSITE	PS00022. EGF_1. 1 hit. PS01186. EGF_2. 1 hit. PS50026. EGF_3. False negative. [Graphical view]
ProtoNet	Search...
Other
NextBio	288576.
SOURCE	Search...

Entry information

Entry name

HYAL1_MOUSE

Accession

Primary (citable) accession number: Q91ZJ9
Secondary accession number(s): B1AV90 , O70229, Q8CE62, Q8QZX3, Q8VBW7, Q8VDK0

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 25, 2005
Last sequence update:	July 27, 2011
Last modified:	May 1, 2013
This is version 96 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program