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O00219 (HYAS3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 124. 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·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Hyaluronan synthase 3

EC=2.4.1.212
Alternative name(s):
Hyaluronate synthase 3
Hyaluronic acid synthase 3
Short name=HA synthase 3
Gene names
Name:HAS3
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length553 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the addition of GlcNAc or GlcUA monosaccharides to the nascent hyaluronan polymer. Therefore, it is essential to hyaluronan synthesis a major component of most extracellular matrices that has a structural role in tissues architectures and regulates cell adhesion, migration and differentiation. This is one of the isozymes catalyzing that reaction By similarity.

Catalytic activity

UDP-alpha-N-acetyl-D-glucosamine + beta-D-glucuronosyl-(1->3)-N-acetyl-beta-D-glucosaminyl-(1->4)-(nascent hyaluronan) = UDP + N-acetyl-beta-D-glucosaminyl-(1->4)-beta-D-glucuronosyl-(1->3)-N-acetyl-beta-D-glucosaminyl-(1->4)-(nascent hyaluronan).

UDP-alpha-D-glucuronate + N-acetyl-beta-D-glucosaminyl-(1->4)-beta-D-glucuronosyl-(1->3)-(nascent hyaluronan) = UDP + beta-D-glucuronosyl-(1->3)-N-acetyl-beta-D-glucosaminyl-(1->4)-beta-D-glucuronosyl-(1->3)-(nascent hyaluronan).

Cofactor

Magnesium.

Pathway

Glycan biosynthesis; hyaluronan biosynthesis.

Subcellular location

Membrane; Multi-pass membrane protein Probable.

Sequence similarities

Belongs to the NodC/HAS family.

Ontologies

Keywords
   Cellular componentMembrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainTransmembrane
Transmembrane helix
   Molecular functionGlycosyltransferase
Transferase
   PTMGlycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcarbohydrate metabolic process

Traceable author statement. Source: Reactome

extracellular matrix assembly

Inferred from sequence or structural similarity. Source: UniProtKB

extracellular polysaccharide biosynthetic process

Inferred from sequence or structural similarity. Source: UniProtKB

glycosaminoglycan metabolic process

Traceable author statement. Source: Reactome

hyaluronan biosynthetic process

Inferred from direct assay PubMed 16900089. Source: UniProtKB

hyaluronan metabolic process

Traceable author statement. Source: Reactome

positive regulation of hyaluranon cable assembly

Inferred from direct assay PubMed 16900089. Source: UniProtKB

positive regulation of transcription, DNA-templated

Inferred from direct assay PubMed 16900089. Source: UniProtKB

small molecule metabolic process

Traceable author statement. Source: Reactome

   Cellular_componenthyaluranon cable

Inferred from direct assay PubMed 16900089. Source: UniProtKB

integral component of membrane

Traceable author statement Ref.6. Source: ProtInc

integral component of plasma membrane

Traceable author statement PubMed 9169154. Source: ProtInc

plasma membrane

Traceable author statement. Source: Reactome

   Molecular_functionhyaluronan synthase activity

Inferred from direct assay PubMed 16900089. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O00219-1)

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: O00219-2)

The sequence of this isoform differs from the canonical sequence as follows:
     247-553: ILNKYDSWIS...EQYSLAFAEV → PPGKGMAVEDDQVQAAQVRATEAWSVHQRHVSREQ
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 553553Hyaluronan synthase 3
PRO_0000197178

Regions

Topological domain1 – 1515Cytoplasmic Potential
Transmembrane16 – 3621Helical; Name=1; Potential
Topological domain37 – 448Extracellular Potential
Transmembrane45 – 6521Helical; Name=2; Potential
Topological domain66 – 377312Cytoplasmic Potential
Transmembrane378 – 39821Helical; Name=3; Potential
Topological domain399 – 40810Extracellular Potential
Transmembrane409 – 42921Helical; Name=4; Potential
Topological domain430 – 44011Cytoplasmic Potential
Transmembrane441 – 46121Helical; Name=5; Potential
Topological domain462 – 47312Extracellular Potential
Transmembrane474 – 49421Helical; Name=6; Potential
Topological domain495 – 51521Cytoplasmic Potential
Transmembrane516 – 53621Helical; Name=7; Potential
Topological domain537 – 55317Extracellular Potential

Amino acid modifications

Glycosylation4621N-linked (GlcNAc...) Potential

Natural variations

Alternative sequence247 – 553307ILNKY…AFAEV → PPGKGMAVEDDQVQAAQVRA TEAWSVHQRHVSREQ in isoform 2.
VSP_042022
Natural variant1731R → H.
Corresponds to variant rs2232229 [ dbSNP | Ensembl ].
VAR_049317

Experimental info

Sequence conflict4931G → E in AAF36984. Ref.1

Sequences

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

Last modified September 23, 2008. Version 3.
Checksum: 82F3B0C932EE9EA3

FASTA55362,998
        10         20         30         40         50         60 
MPVQLTTALR VVGTSLFALA VLGGILAAYV TGYQFIHTEK HYLSFGLYGA ILGLHLLIQS 

        70         80         90        100        110        120 
LFAFLEHRRM RRAGQALKLP SPRRGSVALC IAAYQEDPDY LRKCLRSAQR ISFPDLKVVM 

       130        140        150        160        170        180 
VVDGNRQEDA YMLDIFHEVL GGTEQAGFFV WRSNFHEAGE GETEASLQEG MDRVRDVVRA 

       190        200        210        220        230        240 
STFSCIMQKW GGKREVMYTA FKALGDSVDY IQVCDSDTVL DPACTIEMLR VLEEDPQVGG 

       250        260        270        280        290        300 
VGGDVQILNK YDSWISFLSS VRYWMAFNVE RACQSYFGCV QCISGPLGMY RNSLLQQFLE 

       310        320        330        340        350        360 
DWYHQKFLGS KCSFGDDRHL TNRVLSLGYR TKYTARSKCL TETPTKYLRW LNQQTRWSKS 

       370        380        390        400        410        420 
YFREWLYNSL WFHKHHLWMT YESVVTGFFP FFLIATVIQL FYRGRIWNIL LFLLTVQLVG 

       430        440        450        460        470        480 
IIKATYACFL RGNAEMIFMS LYSLLYMSSL LPAKIFAIAT INKSGWGTSG RKTIVVNFIG 

       490        500        510        520        530        540 
LIPVSIWVAV LLGGLAYTAY CQDLFSETEL AFLVSGAILY GCYWVALLML YLAIIARRCG 

       550 
KKPEQYSLAF AEV 

« Hide

Isoform 2 [UniParc].

Checksum: BD9AA4E19847764B
Show »

FASTA28131,200

References

« Hide 'large scale' references
[1]"Molecular characterization of hyaluronan synthase 3."
Spicer A.P.
Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Brain.
[3]"The sequence and analysis of duplication-rich human chromosome 16."
Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J. expand/collapse author list , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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 2).
Tissue: Prostate.
[6]"Molecular cloning and characterization of a cDNA encoding the third putative mammalian hyaluronan synthase."
Spicer A.P., Olson J.S., McDonald J.A.
J. Biol. Chem. 272:8957-8961(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 275-464.
+Additional computationally mapped references.

Web resources

GGDB

GlycoGene database

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF232772 mRNA. Translation: AAF36984.1.
AK291400 mRNA. Translation: BAF84089.1.
AC009027 Genomic DNA. No translation available.
CH471092 Genomic DNA. Translation: EAW83247.1.
CH471092 Genomic DNA. Translation: EAW83248.1.
BC021853 mRNA. Translation: AAH21853.1.
U86409 Genomic DNA. Translation: AAC51209.1.
CCDSCCDS10870.1. [O00219-2]
CCDS10871.1. [O00219-1]
RefSeqNP_001186209.1. NM_001199280.1. [O00219-1]
NP_005320.2. NM_005329.2. [O00219-1]
NP_619515.1. NM_138612.2. [O00219-2]
XP_005255977.1. XM_005255920.2. [O00219-1]
XP_005255978.1. XM_005255921.1. [O00219-1]
UniGeneHs.592069.

3D structure databases

ProteinModelPortalO00219.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109288. 2 interactions.
STRING9606.ENSP00000304440.

Protein family/group databases

CAZyGT2. Glycosyltransferase Family 2.

PTM databases

PhosphoSiteO00219.

Proteomic databases

MaxQBO00219.
PaxDbO00219.
PRIDEO00219.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000219322; ENSP00000219322; ENSG00000103044. [O00219-2]
ENST00000306560; ENSP00000304440; ENSG00000103044. [O00219-1]
ENST00000569188; ENSP00000454731; ENSG00000103044. [O00219-1]
GeneID3038.
KEGGhsa:3038.
UCSCuc002ewk.3. human. [O00219-2]
uc002ewl.3. human. [O00219-1]

Organism-specific databases

CTD3038.
GeneCardsGC16P069140.
HGNCHGNC:4820. HAS3.
HPACAB033850.
HPA031554.
MIM602428. gene.
neXtProtNX_O00219.
PharmGKBPA29196.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1215.
HOGENOMHOG000112847.
HOVERGENHBG000189.
InParanoidO00219.
KOK00752.
OMAFIHTEQH.
OrthoDBEOG77WWBZ.
PhylomeDBO00219.
TreeFamTF332506.

Enzyme and pathway databases

BRENDA2.4.1.212. 2681.
ReactomeREACT_111217. Metabolism.
REACT_116125. Disease.
UniPathwayUPA00341.

Gene expression databases

ArrayExpressO00219.
BgeeO00219.
CleanExHS_HAS3.
GenevestigatorO00219.

Family and domain databases

Gene3D3.90.550.10. 2 hits.
InterProIPR026108. HA_synthase_3.
IPR026107. HAS/NodC.
IPR029044. Nucleotide-diphossugar_trans.
[Graphical view]
PANTHERPTHR22913. PTHR22913. 1 hit.
PTHR22913:SF6. PTHR22913:SF6. 1 hit.
SUPFAMSSF53448. SSF53448. 2 hits.
ProtoNetSearch...

Other

GeneWikiHAS3.
GenomeRNAi3038.
NextBio12028.
PROO00219.
SOURCESearch...

Entry information

Entry nameHYAS3_HUMAN
AccessionPrimary (citable) accession number: O00219
Secondary accession number(s): A8K5T5, Q8WTZ0, Q9NYP0
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: September 23, 2008
Last modified: July 9, 2014
This is version 124 of the entry and version 3 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

PATHWAY comments

Index of metabolic and biosynthesis pathways

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 16

Human chromosome 16: entries, gene names and cross-references to MIM