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O08650 (HAS3_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 96. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·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
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length554 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Plays a role in hyaluronan/hyaluronic acid (HA) synthesis.

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.

Developmental stage

Expressed at E17.5 day.

Sequence similarities

Belongs to the NodC/HAS family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 554554Hyaluronan synthase 3
PRO_0000197179

Regions

Topological domain1 – 1515Cytoplasmic Potential
Transmembrane16 – 3621Helical; Name=1; Potential
Topological domain37 – 448Extracellular Potential
Transmembrane45 – 6521Helical; Name=2; Potential
Topological domain66 – 378313Cytoplasmic Potential
Transmembrane379 – 39921Helical; Name=3; Potential
Topological domain400 – 40910Extracellular Potential
Transmembrane410 – 43021Helical; Name=4; Potential
Topological domain431 – 44111Cytoplasmic Potential
Transmembrane442 – 46221Helical; Name=5; Potential
Topological domain463 – 47412Extracellular Potential
Transmembrane475 – 49521Helical; Name=6; Potential
Topological domain496 – 51621Cytoplasmic Potential
Transmembrane517 – 53721Helical; Name=7; Potential
Topological domain538 – 55417Extracellular Potential

Amino acid modifications

Glycosylation4631N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict851P → S in AAC53128. Ref.1

Sequences

Sequence LengthMass (Da)Tools
O08650 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: BFFF239C901251DE

FASTA55463,349
        10         20         30         40         50         60 
MPVQLTTALR VVGTSLFALV VLGGILAAYV TGYQFIHTEK HYLSFGLYGA ILGLHLLIQS 

        70         80         90        100        110        120 
LFAFLEHRRM RRAGRPLKLH CSQRPRSVAL CIAAYQEDPE YLRKCLRSAQ RIAFPNLKVV 

       130        140        150        160        170        180 
MVVDGNRQED TYMLDIFHEV LGGTEQAGFF VWRSNFHEAG EGETEASLQE GMERVRAVVW 

       190        200        210        220        230        240 
ASTFSCIMQK WGGKREVMYT AFKALGNSVD YIQVCDSDTV LDPACTIEML RVLEEDPQVG 

       250        260        270        280        290        300 
GVGGDVQILN KYDSWISFLS SVRYWMAFNV ERACQSYFGC VQCISGPLGM YRNSLLQQFL 

       310        320        330        340        350        360 
EDWYHQKFLG SKCSFGDDRH LTNRVLSLGY RTKYTARSKC LTETPTRYLR WLNQQTRWSK 

       370        380        390        400        410        420 
SYFREWLYNS LWFHKHHLWM TYESVVTGFF PFFLIATVIQ LFYRGRIWNI LLFLLTVQLV 

       430        440        450        460        470        480 
GIIKATYACF LRGNAEMIFM SLYSLLYMSS LLPAKIFAIA TINKSGWGTS GRKTIVVNFI 

       490        500        510        520        530        540 
GLIPVSIWVA VLLGGLAYTA YCQDLFSETE LAFLVSGAIL YGCYWVALLM LYLAIIARRC 

       550 
GKKPEQYSLA FAEV

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		U86408 mRNA. Translation: AAC53128.1.
AK028582 mRNA. Translation: BAC26017.1.
BC138152 mRNA. Translation: AAI38153.1.
IPIIPI00114919.
RefSeqNP_032243.2. NM_008217.4.
UniGeneMm.56986.

3D structure databases

ProteinModelPortalO08650.
ModBaseSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000034385.

Protein family/group databases

CAZyGT2. Glycosyltransferase Family 2.

PTM databases

PhosphoSiteO08650.

Proteomic databases

PRIDEO08650.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000034385; ENSMUSP00000034385; ENSMUSG00000031910.
ENSMUST00000176144; ENSMUSP00000135303; ENSMUSG00000031910.
GeneID15118.
KEGGmmu:15118.

Organism-specific databases

CTD3038.
MGIMGI:109599. Has3.

Phylogenomic databases

eggNOGCOG1215.
GeneTreeENSGT00390000010337.
HOGENOMHOG000112847.
HOVERGENHBG000189.
InParanoidQ8CEB9.
KOK00752.
OMAFIHTEQH.
OrthoDBEOG4BG8VQ.

Enzyme and pathway databases

BRENDA2.4.1.212. 3474.
UniPathwayUPA00341.

Gene expression databases

ArrayExpressO08650.
BgeeO08650.
CleanExMM_HAS3.
GenevestigatorO08650.
GermOnlineENSMUSG00000031910. Mus musculus.

Family and domain databases

InterProIPR026108. HA_synthase_3.
IPR026107. HAS/NodC.
[Graphical view]
PANTHERPTHR22913. PTHR22913. 1 hit.
PTHR22913:SF6. PTHR22913:SF6. 1 hit.
ProtoNetSearch...

Other

NextBio287538.
SOURCESearch...

Entry information

Entry nameHAS3_MOUSE
AccessionPrimary (citable) accession number: O08650
Secondary accession number(s): Q8CEB9
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: July 27, 2011
Last modified: April 3, 2013
This is version 96 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents