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O08650

- HYAS3_MOUSE

UniProt

O08650 - HYAS3_MOUSE

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Protein

Hyaluronan synthase 3

Gene

Has3

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.1 Publication

Catalytic activityi

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).1 Publication
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).1 Publication

Cofactori

Kineticsi

  1. KM=0.2 mM for UDP-Glc-NAc (at pH 7.1 and 37 degrees Celsius, in the presence of 15 mM MgCl2)1 Publication
  2. KM=0.3 mM for UDP-Glc-UA (at pH 7.1 and 37 degrees Celsius, in the presence of 15 mM MgCl2)1 Publication

Pathwayi

GO - Molecular functioni

  1. hyaluronan synthase activity Source: UniProtKB

GO - Biological processi

  1. extracellular matrix assembly Source: UniProtKB
  2. extracellular polysaccharide biosynthetic process Source: UniProtKB
  3. hyaluronan biosynthetic process Source: MGI
  4. positive regulation of hyaluranon cable assembly Source: Ensembl
  5. positive regulation of transcription, DNA-templated Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Enzyme and pathway databases

BRENDAi2.4.1.212. 3474.
ReactomeiREACT_196552. Hyaluronan biosynthesis and export.
UniPathwayiUPA00341.

Protein family/group databases

CAZyiGT2. Glycosyltransferase Family 2.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:Has3
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 8

Organism-specific databases

MGIiMGI:109599. Has3.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1515CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei16 – 3621Helical; Name=1Sequence AnalysisAdd
BLAST
Topological domaini37 – 448ExtracellularSequence Analysis
Transmembranei45 – 6521Helical; Name=2Sequence AnalysisAdd
BLAST
Topological domaini66 – 378313CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei379 – 39921Helical; Name=3Sequence AnalysisAdd
BLAST
Topological domaini400 – 40910ExtracellularSequence Analysis
Transmembranei410 – 43021Helical; Name=4Sequence AnalysisAdd
BLAST
Topological domaini431 – 44111CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei442 – 46221Helical; Name=5Sequence AnalysisAdd
BLAST
Topological domaini463 – 47412ExtracellularSequence AnalysisAdd
BLAST
Transmembranei475 – 49521Helical; Name=6Sequence AnalysisAdd
BLAST
Topological domaini496 – 51621CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei517 – 53721Helical; Name=7Sequence AnalysisAdd
BLAST
Topological domaini538 – 55417ExtracellularSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. hyaluranon cable Source: Ensembl
  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 – 554554Hyaluronan synthase 3PRO_0000197179Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi463 – 4631N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Proteomic databases

PRIDEiO08650.

PTM databases

PhosphoSiteiO08650.

Expressioni

Developmental stagei

Expressed at E17.5 day.

Gene expression databases

BgeeiO08650.
CleanExiMM_HAS3.
ExpressionAtlasiO08650. baseline and differential.
GenevestigatoriO08650.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000034385.

Structurei

3D structure databases

ProteinModelPortaliO08650.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the NodC/HAS family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG1215.
GeneTreeiENSGT00390000010337.
HOGENOMiHOG000112847.
HOVERGENiHBG000189.
InParanoidiO08650.
KOiK00752.
OMAiFIHTEQH.
OrthoDBiEOG77WWBZ.
TreeFamiTF332506.

Family and domain databases

Gene3Di3.90.550.10. 2 hits.
InterProiIPR026108. HA_synthase_3.
IPR026107. HAS/NodC.
IPR029044. Nucleotide-diphossugar_trans.
[Graphical view]
PANTHERiPTHR22913. PTHR22913. 1 hit.
PTHR22913:SF6. PTHR22913:SF6. 1 hit.
SUPFAMiSSF53448. SSF53448. 2 hits.

Sequencei

Sequence statusi: Complete.

O08650-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MPVQLTTALR VVGTSLFALV VLGGILAAYV TGYQFIHTEK HYLSFGLYGA
60 70 80 90 100
ILGLHLLIQS LFAFLEHRRM RRAGRPLKLH CSQRPRSVAL CIAAYQEDPE
110 120 130 140 150
YLRKCLRSAQ RIAFPNLKVV MVVDGNRQED TYMLDIFHEV LGGTEQAGFF
160 170 180 190 200
VWRSNFHEAG EGETEASLQE GMERVRAVVW ASTFSCIMQK WGGKREVMYT
210 220 230 240 250
AFKALGNSVD YIQVCDSDTV LDPACTIEML RVLEEDPQVG GVGGDVQILN
260 270 280 290 300
KYDSWISFLS SVRYWMAFNV ERACQSYFGC VQCISGPLGM YRNSLLQQFL
310 320 330 340 350
EDWYHQKFLG SKCSFGDDRH LTNRVLSLGY RTKYTARSKC LTETPTRYLR
360 370 380 390 400
WLNQQTRWSK SYFREWLYNS LWFHKHHLWM TYESVVTGFF PFFLIATVIQ
410 420 430 440 450
LFYRGRIWNI LLFLLTVQLV GIIKATYACF LRGNAEMIFM SLYSLLYMSS
460 470 480 490 500
LLPAKIFAIA TINKSGWGTS GRKTIVVNFI GLIPVSIWVA VLLGGLAYTA
510 520 530 540 550
YCQDLFSETE LAFLVSGAIL YGCYWVALLM LYLAIIARRC GKKPEQYSLA

FAEV
Length:554
Mass (Da):63,349
Last modified:July 27, 2011 - v2
Checksum:iBFFF239C901251DE
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti85 – 851P → S in AAC53128. (PubMed:9083017)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U86408 mRNA. Translation: AAC53128.1.
AK028582 mRNA. Translation: BAC26017.1.
BC138152 mRNA. Translation: AAI38153.1.
CCDSiCCDS22640.1.
RefSeqiNP_032243.2. NM_008217.4.
XP_006530762.1. XM_006530699.1.
XP_006530763.1. XM_006530700.1.
XP_006530764.1. XM_006530701.1.
UniGeneiMm.56986.

Genome annotation databases

EnsembliENSMUST00000034385; ENSMUSP00000034385; ENSMUSG00000031910.
ENSMUST00000176144; ENSMUSP00000135303; ENSMUSG00000031910.
GeneIDi15118.
KEGGimmu:15118.
UCSCiuc009ngn.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U86408 mRNA. Translation: AAC53128.1 .
AK028582 mRNA. Translation: BAC26017.1 .
BC138152 mRNA. Translation: AAI38153.1 .
CCDSi CCDS22640.1.
RefSeqi NP_032243.2. NM_008217.4.
XP_006530762.1. XM_006530699.1.
XP_006530763.1. XM_006530700.1.
XP_006530764.1. XM_006530701.1.
UniGenei Mm.56986.

3D structure databases

ProteinModelPortali O08650.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 10090.ENSMUSP00000034385.

Protein family/group databases

CAZyi GT2. Glycosyltransferase Family 2.

PTM databases

PhosphoSitei O08650.

Proteomic databases

PRIDEi O08650.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000034385 ; ENSMUSP00000034385 ; ENSMUSG00000031910 .
ENSMUST00000176144 ; ENSMUSP00000135303 ; ENSMUSG00000031910 .
GeneIDi 15118.
KEGGi mmu:15118.
UCSCi uc009ngn.2. mouse.

Organism-specific databases

CTDi 3038.
MGIi MGI:109599. Has3.

Phylogenomic databases

eggNOGi COG1215.
GeneTreei ENSGT00390000010337.
HOGENOMi HOG000112847.
HOVERGENi HBG000189.
InParanoidi O08650.
KOi K00752.
OMAi FIHTEQH.
OrthoDBi EOG77WWBZ.
TreeFami TF332506.

Enzyme and pathway databases

UniPathwayi UPA00341 .
BRENDAi 2.4.1.212. 3474.
Reactomei REACT_196552. Hyaluronan biosynthesis and export.

Miscellaneous databases

NextBioi 287538.
PROi O08650.
SOURCEi Search...

Gene expression databases

Bgeei O08650.
CleanExi MM_HAS3.
ExpressionAtlasi O08650. baseline and differential.
Genevestigatori O08650.

Family and domain databases

Gene3Di 3.90.550.10. 2 hits.
InterProi IPR026108. HA_synthase_3.
IPR026107. HAS/NodC.
IPR029044. Nucleotide-diphossugar_trans.
[Graphical view ]
PANTHERi PTHR22913. PTHR22913. 1 hit.
PTHR22913:SF6. PTHR22913:SF6. 1 hit.
SUPFAMi SSF53448. SSF53448. 2 hits.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "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 [MRNA].
    Strain: 129/SvJ and C57BL/6.
  2. "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.
  3. "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.
  4. Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, KINETIC PARAMETERS.

Entry informationi

Entry nameiHYAS3_MOUSE
AccessioniPrimary (citable) accession number: O08650
Secondary accession number(s): Q8CEB9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: July 27, 2011
Last modified: November 26, 2014
This is version 111 of the entry and version 2 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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3