Skip Header

Contribute Send feedback
Read comments (?) or add your own

P70312 (HAS2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 83. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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 2

EC=2.4.1.212
Alternative name(s):
Hyaluronate synthase 2
Hyaluronic acid synthase 2
Short name=HA synthase 2
Gene names
Name:Has2
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length552 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.

Tissue specificity

Expressed in heart, brain, spleen, lung and skeletal muscle.

Developmental stage

Expressed at day 7.5.

Sequence similarities

Belongs to the nodC/HAS family.

Ontologies

Keywords
   Cellular componentMembrane
   DomainTransmembrane
Transmembrane helix
   Molecular functionGlycosyltransferase
Transferase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Cellular componentintegral to membrane

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionhyaluronan synthase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 552552Hyaluronan synthase 2
PRO_0000197174

Regions

Topological domain1 – 1111Cytoplasmic Potential
Transmembrane12 – 3221Helical; Name=1; Potential
Topological domain33 – 4513Extracellular Potential
Transmembrane46 – 6621Helical; Name=2; Potential
Topological domain67 – 374308Cytoplasmic Potential
Transmembrane375 – 39521Helical; Name=3; Potential
Topological domain396 – 4027Extracellular Potential
Transmembrane403 – 42321Helical; Name=4; Potential
Topological domain424 – 4296Cytoplasmic Potential
Transmembrane430 – 45021Helical; Name=5; Potential
Topological domain451 – 47525Extracellular Potential
Transmembrane476 – 49621Helical; Name=6; Potential
Topological domain497 – 51014Cytoplasmic Potential
Transmembrane511 – 53121Helical; Name=7; Potential
Topological domain532 – 55221Extracellular Potential

Experimental info

Sequence conflict1381M → I in AAC53309. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P70312 [UniParc].

Last modified July 27, 2011. Version 4.
Checksum: B840BABC6D2260D5

FASTA55263,510
        10         20         30         40         50         60 
MHCERFLCVL RIIGTTLFGV SLLLGITAAY IVGYQFIQTD NYYFSFGLYG AFLASHLIIQ 

        70         80         90        100        110        120 
SLFAFLEHRK MKKSLETPIK LNKTVALCIA AYQEDPDYLR KCLQSVKRLT YPGIKVVMVI 

       130        140        150        160        170        180 
DGNSDDDLYM MDIFSEVMGR DKSATYIWKN NFHEKGPGET EESHKESSQH VTQLVLSNKS 

       190        200        210        220        230        240 
ICIMQKWGGK REVMYTAFRA LGRSVDYVQV CDSDTMLDPA SSVEMVKVLE EDPMVGGVGG 

       250        260        270        280        290        300 
DVQILNKYDS WISFLSSVRY WMAFNIERAC QSYFGCVQCI SGPLGMYRNS LLHEFVEDWY 

       310        320        330        340        350        360 
NQEFMGNQCS FGDDRHLTNR VLSLGYATKY TARSKCLTET PIEYLRWLNQ QTRWSKSYFR 

       370        380        390        400        410        420 
EWLYNAMWFH KHHLWMTYEA VITGFFPFFL IATVIQLFYR GKIWNILLFL LTVQLVGLIK 

       430        440        450        460        470        480 
SSFASCLRGN IVMVFMSLYS VLYMSSLLPA KMFAIATINK AGWGTSGRKT IVVNFIGLIP 

       490        500        510        520        530        540 
VSVWFTILLG GVIFTIYKES KKPFSESKQT VLIVGTLIYA CYWVMLLTLY VVLINKCGRR 

       550 
KKGQQYDMVL DV 

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning and characterization of a putative mouse hyaluronan synthase."
Spicer A.P., Augustine M.L., McDonald J.A.
J. Biol. Chem. 271:23400-23406(1996) [PubMed: 8798545] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: C57BL/6J.
[2]Spicer A.P., Augustine M.L., McDonald J.A.
Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION TO 138.
[3]"Coding sequence of a hyaluronan synthase homologue expressed during expansion of the mouse cumulus-oocyte complex."
Fueloep C., Salustri A., Hascall V.C.
Arch. Biochem. Biophys. 337:261-266(1997) [PubMed: 9016821] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Swiss CD1.
[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. 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: 16141072] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Thymus.
[5]Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6.
Tissue: Brain.
[7]"Homologs of the Xenopus developmental gene DG42 are present in zebrafish and mouse and are involved in the synthesis of Nod-like chitin oligosaccharides during early embryogenesis."
Semino C.E., Specht C.A., Raimondi A., Robbins P.W.
Proc. Natl. Acad. Sci. U.S.A. 93:4548-4553(1996) [PubMed: 8643441] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 215-348.
Strain: Swiss Webster.
Tissue: Embryo.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U52524 mRNA. Translation: AAC53309.2.
U69695 mRNA. Translation: AAB17609.1.
AK079729 mRNA. Translation: BAC37733.1.
CH466545 Genomic DNA. Translation: EDL29280.1.
BC080281 mRNA. Translation: AAH80281.1.
U53222 Genomic DNA. Translation: AAC52651.1.
IPIIPI00108079.
RefSeqNP_032242.3. NM_008216.3.
UniGeneMm.5148.

3D structure databases

ProteinModelPortalP70312.
ModBaseSearch...

Protein-protein interaction databases

STRINGP70312.

Protein family/group databases

CAZyGT2. Glycosyltransferase Family 2.

PTM databases

PhosphoSiteP70312.

Proteomic databases

PRIDEP70312.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000050544; ENSMUSP00000062212; ENSMUSG00000022367.
GeneID15117.
KEGGmmu:15117.

Organism-specific databases

CTD3037.
MGIMGI:107821. Has2.

Phylogenomic databases

eggNOGroNOG05966.
HOGENOMHBG716008.
HOVERGENHBG000189.
InParanoidP70312.
OrthoDBEOG4KH2TP.

Enzyme and pathway databases

BRENDA2.4.1.212. 3474.

Gene expression databases

ArrayExpressP70312.
BgeeP70312.
CleanExMM_HAS2.
GenevestigatorP70312.
GermOnlineENSMUSG00000022367. Mus musculus.

Family and domain databases

InterProIPR004835. Chitin_synth_fng.
IPR001173. Glyco_trans_2.
[Graphical view]
KOK00752.
PfamPF03142. Chitin_synth_2. 1 hit.
PF00535. Glycos_transf_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio287534.
SOURCESearch...

Entry information

Entry nameHAS2_MOUSE
AccessionPrimary (citable) accession number: P70312
Secondary accession number(s): P70411, Q62405, Q68EF7
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: July 27, 2011
Last modified: December 14, 2011
This is version 83 of the entry and version 4 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