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O43820 (HYAL3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 108. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Hyaluronidase-3

Short name=Hyal-3
EC=3.2.1.35
Alternative name(s):
Hyaluronoglucosaminidase-3
Lung carcinoma protein 3
Short name=LuCa-3
Gene names
Name:HYAL3
Synonyms:LUCA3
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length417 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

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

Bone marrow, testis and kidney. Isoform 4 is detected in all bladder tumor and prostate tumor cells. Ref.1 Ref.2

Sequence similarities

Belongs to the glycosyl hydrolase 56 family.

Contains 1 EGF-like domain.

Sequence caution

The sequence AAC70915.1 differs from that shown. Reason: Frameshift at position 410.

Ontologies

Keywords
   Cellular componentLysosome
Secreted
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainEGF-like domain
Signal
   Molecular functionGlycosidase
Hydrolase
   PTMDisulfide bond
Glycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcarbohydrate metabolic process

Inferred from electronic annotation. Source: InterPro

cartilage development

Inferred from expression pattern PubMed 11944887. Source: UniProtKB

cellular response to UV-B

Inferred from direct assay PubMed 21699545. Source: UniProtKB

cellular response to interleukin-1

Inferred from direct assay PubMed 18390475. Source: UniProtKB

cellular response to tumor necrosis factor

Inferred from expression pattern PubMed 18390475. Source: UniProtKB

hyaluronan catabolic process

Inferred from direct assay PubMed 21699545Ref.2. Source: UniProtKB

inflammatory response

Inferred from direct assay PubMed 18390475. Source: UniProtKB

response to antibiotic

Inferred from expression pattern PubMed 11944887. Source: UniProtKB

response to virus

Inferred from direct assay PubMed 11296287. Source: UniProtKB

   Cellular_componentcytoplasmic vesicle

Inferred from direct assay PubMed 18390475. Source: UniProtKB

extracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

lysosome

Inferred from direct assay PubMed 16600643. Source: UniProtKB

   Molecular_functionhyaluronoglucuronidase activity

Inferred from direct assay PubMed 21699545. Source: UniProtKB

hyalurononglucosaminidase activity

Inferred from direct assay PubMed 11944887PubMed 17170110PubMed 18390475Ref.2. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O43820-1)

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: O43820-2)

Also known as: HYAL3v1;

The sequence of this isoform differs from the canonical sequence as follows:
     299-328: Missing.
Note: Enzymatically inactive.
Isoform 3 (identifier: O43820-3)

Also known as: HYAL3v2;

The sequence of this isoform differs from the canonical sequence as follows:
     1-249: Missing.
     250-250: R → M
Note: Enzymatically inactive.
Isoform 4 (identifier: O43820-4)

Also known as: HYAL3v3;

The sequence of this isoform differs from the canonical sequence as follows:
     1-249: Missing.
     250-250: R → M
     299-328: Missing.
Note: Enzymatically inactive.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 Potential
Chain21 – 417397Hyaluronidase-3
PRO_0000248200

Regions

Domain352 – 40756EGF-like

Sites

Active site1291Proton donor By similarity

Amino acid modifications

Glycosylation691N-linked (GlcNAc...) Potential
Glycosylation2151N-linked (GlcNAc...) Potential
Disulfide bond42 ↔ 331 By similarity
Disulfide bond205 ↔ 220 By similarity
Disulfide bond356 ↔ 367 By similarity
Disulfide bond361 ↔ 395 By similarity
Disulfide bond397 ↔ 406 By similarity

Natural variations

Alternative sequence1 – 249249Missing in isoform 3 and isoform 4.
VSP_020192
Alternative sequence2501R → M in isoform 3 and isoform 4.
VSP_020193
Alternative sequence299 – 32830Missing in isoform 2 and isoform 4.
VSP_020194
Natural variant1131H → Y. Ref.5
Corresponds to variant rs13100173 [ dbSNP | Ensembl ].
VAR_027263

Experimental info

Sequence conflict541A → S in AAH05896. Ref.5

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified June 1, 1998. Version 1.
Checksum: A6E7DE5369EF2BB8

FASTA41746,501
        10         20         30         40         50         60 
MTTQLGPALV LGVALCLGCG QPLPQVPERP FSVLWNVPSA HCEARFGVHL PLNALGIIAN 

        70         80         90        100        110        120 
RGQHFHGQNM TIFYKNQLGL YPYFGPRGTA HNGGIPQALP LDRHLALAAY QIHHSLRPGF 

       130        140        150        160        170        180 
AGPAVLDWEE WCPLWAGNWG RRRAYQAASW AWAQQVFPDL DPQEQLYKAY TGFEQAARAL 

       190        200        210        220        230        240 
MEDTLRVAQA LRPHGLWGFY HYPACGNGWH SMASNYTGRC HAATLARNTQ LHWLWAASSA 

       250        260        270        280        290        300 
LFPSIYLPPR LPPAHHQAFV RHRLEEAFRV ALVGHRHPLP VLAYVRLTHR RSGRFLSQDD 

       310        320        330        340        350        360 
LVQSIGVSAA LGAAGVVLWG DLSLSSSEEE CWHLHDYLVD TLGPYVINVT RAAMACSHQR 

       370        380        390        400        410 
CHGHGRCARR DPGQMEAFLH LWPDGSLGDW KSFSCHCYWG WAGPTCQEPR PGPKEAV 

« Hide

Isoform 2 (HYAL3v1) [UniParc].

Checksum: 32FE18A2329307A6
Show »

FASTA38743,602
Isoform 3 (HYAL3v2) [UniParc].

Checksum: C29CE942F2F784F8
Show »

FASTA16818,764
Isoform 4 (HYAL3v3) [UniParc].

Checksum: 8E94BC56A7606001
Show »

FASTA13815,865

References

« Hide 'large scale' references
[1]"Expression analysis of six paralogous human hyaluronidase genes clustered on chromosomes 3p21 and 7q31."
Csoka A.B., Scherer S.W., Stern R.
Genomics 60:356-361(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
[2]"Regulation of hyaluronidase activity by alternative mRNA splicing."
Lokeshwar V.B., Schroeder G.L., Carey R.I., Soloway M.S., Iida N.
J. Biol. Chem. 277:33654-33663(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3 AND 4), ALTERNATIVE SPLICING, TISSUE SPECIFICITY.
[3]"LUCA-3 a third hyaluronidase gene and candidate tumor suppressor gene located in the 3p21.3 homozygous deletion region."
Fong K., Bader S., Lee C.-C., Latif F., Sekido Y., Duh F.-M., Wei M.-H., Cundiff S., Lerman M.I., Minna J.D.
Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[4]"The DNA sequence, annotation and analysis of human chromosome 3."
Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J. expand/collapse author list , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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), VARIANT TYR-113.
Tissue: Bone marrow and Ovary.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF036035 mRNA. Translation: AAD04257.1.
AF502909 mRNA. Translation: AAM60775.1.
AF502910 mRNA. Translation: AAM60776.1.
AF502911 mRNA. Translation: AAM60777.1.
AF502912 mRNA. Translation: AAM60778.1.
AF040710 mRNA. Translation: AAC70915.1. Frameshift.
U73167 Genomic DNA. Translation: AAC02729.1.
BC005896 mRNA. Translation: AAH05896.1.
BC012892 mRNA. Translation: AAH12892.1.
CCDSCCDS2815.1. [O43820-1]
CCDS56257.1. [O43820-2]
CCDS56259.1. [O43820-4]
CCDS56260.1. [O43820-3]
RefSeqNP_001186958.1. NM_001200029.1. [O43820-1]
NP_001186959.1. NM_001200030.1. [O43820-2]
NP_001186960.1. NM_001200031.1. [O43820-3]
NP_001186961.1. NM_001200032.1. [O43820-4]
NP_003540.2. NM_003549.3. [O43820-1]
UniGeneHs.129910.
Hs.729310.

3D structure databases

ProteinModelPortalO43820.
SMRO43820. Positions 24-407.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid113967. 1 interaction.
IntActO43820. 1 interaction.
STRING9606.ENSP00000337425.

Protein family/group databases

CAZyGH56. Glycoside Hydrolase Family 56.

Proteomic databases

PaxDbO43820.
PRIDEO43820.

Protocols and materials databases

DNASU8372.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000336307; ENSP00000337425; ENSG00000186792. [O43820-1]
ENST00000359051; ENSP00000351946; ENSG00000186792. [O43820-2]
ENST00000415204; ENSP00000401092; ENSG00000186792. [O43820-3]
ENST00000450982; ENSP00000391922; ENSG00000186792. [O43820-2]
ENST00000513170; ENSP00000424633; ENSG00000186792. [O43820-4]
ENST00000571109; ENSP00000459478; ENSG00000261855. [O43820-3]
ENST00000572211; ENSP00000458620; ENSG00000261855. [O43820-2]
ENST00000572961; ENSP00000458171; ENSG00000261855. [O43820-1]
ENST00000576798; ENSP00000460809; ENSG00000261855. [O43820-4]
GeneID8372.
KEGGhsa:8372.
UCSCuc003czd.2. human. [O43820-1]
uc003cze.2. human. [O43820-3]
uc003czf.2. human. [O43820-4]
uc003czg.2. human. [O43820-2]

Organism-specific databases

CTD8372.
GeneCardsGC03M050331.
HGNCHGNC:5322. HYAL3.
HPAHPA049402.
MIM604038. gene.
neXtProtNX_O43820.
PharmGKBPA29573.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG69101.
HOVERGENHBG052053.
KOK01197.
OMAWEEWCPL.
PhylomeDBO43820.
TreeFamTF321598.

Enzyme and pathway databases

BioCycMetaCyc:ENSG00000114366-MONOMER.
BRENDA3.2.1.35. 2681.
ReactomeREACT_111217. Metabolism.
REACT_116125. Disease.

Gene expression databases

BgeeO43820.
CleanExHS_HYAL3.
GenevestigatorO43820.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
InterProIPR013785. Aldolase_TIM.
IPR000742. EG-like_dom.
IPR017853. Glycoside_hydrolase_SF.
IPR018155. Hyaluronidase.
IPR027260. Hyaluronidase-3.
[Graphical view]
PANTHERPTHR11769. PTHR11769. 1 hit.
PfamPF01630. Glyco_hydro_56. 1 hit.
[Graphical view]
PIRSFPIRSF038193. Hyaluronidase. 1 hit.
PIRSF500776. Hyaluronidase_3. 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

GeneWikiHYAL3.
GenomeRNAi8372.
NextBio31358.
PROO43820.
SOURCESearch...

Entry information

Entry nameHYAL3_HUMAN
AccessionPrimary (citable) accession number: O43820
Secondary accession number(s): O60540 expand/collapse secondary AC list , Q8NFK2, Q8NFK3, Q8NFK4, Q96E56, Q9BRW9
Entry history
Integrated into UniProtKB/Swiss-Prot: September 5, 2006
Last sequence update: June 1, 1998
Last modified: July 9, 2014
This is version 108 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries