HYAS1_XENTR
ID HYAS1_XENTR Reviewed; 590 AA.
AC B1WB39;
DT 23-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 1.
DT 03-AUG-2022, entry version 51.
DE RecName: Full=Hyaluronan synthase 1 {ECO:0000250|UniProtKB:Q92839};
DE EC=2.4.1.212;
DE AltName: Full=Hyaluronate synthase 1 {ECO:0000250|UniProtKB:Q92839};
DE AltName: Full=Hyaluronic acid synthase 1 {ECO:0000250|UniProtKB:Q92839};
DE Short=HA synthase 1 {ECO:0000250|UniProtKB:Q92839};
GN Name=has1;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1] {ECO:0000312|EMBL:AAI61605.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Gastrula {ECO:0000312|EMBL:AAI61605.1};
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the addition of GlcNAc or GlcUA monosaccharides to
CC the nascent hyaluronan polymer. Therefore, it is essential to
CC hyaluronan synthesis a major component of most extracellular matrices
CC that has a structural role in tissues architectures and regulates cell
CC adhesion, migration and differentiation. Also able to catalyze the
CC synthesis of chito-oligosaccharide depending on the substrate (By
CC similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[hyaluronan](n) + UDP-N-acetyl-alpha-D-glucosamine = H(+) + N-
CC acetyl-beta-D-glucosaminyl-(1->4)-[hyaluronan](n) + UDP;
CC Xref=Rhea:RHEA:20465, Rhea:RHEA-COMP:12583, Rhea:RHEA-COMP:12585,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57705, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:132153, ChEBI:CHEBI:132154; EC=2.4.1.212;
CC Evidence={ECO:0000250|UniProtKB:Q92839};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N-acetyl-beta-D-glucosaminyl-(1->4)-[hyaluronan](n) + UDP-
CC alpha-D-glucuronate = [hyaluronan](n+1) + H(+) + UDP;
CC Xref=Rhea:RHEA:12528, Rhea:RHEA-COMP:12585, Rhea:RHEA-COMP:12587,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:58052, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:132153, ChEBI:CHEBI:132154; EC=2.4.1.212;
CC Evidence={ECO:0000250|UniProtKB:Q92839};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q92839};
CC -!- PATHWAY: Glycan biosynthesis; hyaluronan biosynthesis.
CC {ECO:0000250|UniProtKB:Q92839}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255, ECO:0000305}; Multi-pass
CC membrane protein {ECO:0000255, ECO:0000305}.
CC -!- SIMILARITY: Belongs to the NodC/HAS family. {ECO:0000305}.
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DR EMBL; BC161605; AAI61605.1; -; mRNA.
DR RefSeq; NP_001120590.1; NM_001127118.1.
DR AlphaFoldDB; B1WB39; -.
DR CAZy; GT2; Glycosyltransferase Family 2.
DR PRIDE; B1WB39; -.
DR GeneID; 100145746; -.
DR KEGG; xtr:100145746; -.
DR CTD; 3036; -.
DR Xenbase; XB-GENE-961588; has1.
DR InParanoid; B1WB39; -.
DR Reactome; R-XTR-2142850; Hyaluronan biosynthesis and export.
DR UniPathway; UPA00341; -.
DR Proteomes; UP000008143; Chromosome 3.
DR Proteomes; UP000790000; Unplaced.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0050501; F:hyaluronan synthase activity; ISS:UniProtKB.
DR GO; GO:0085029; P:extracellular matrix assembly; ISS:UniProtKB.
DR GO; GO:0045226; P:extracellular polysaccharide biosynthetic process; ISS:UniProtKB.
DR GO; GO:0030213; P:hyaluronan biosynthetic process; IBA:GO_Central.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR SUPFAM; SSF53448; SSF53448; 1.
PE 2: Evidence at transcript level;
KW Glycosyltransferase; Membrane; Reference proteome; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..590
FT /note="Hyaluronan synthase 1"
FT /id="PRO_0000392432"
FT TOPO_DOM 1..31
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 32..52
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 53..60
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 61..81
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 82..401
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 402..422
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 423..425
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 426..446
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 447..456
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 457..477
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 478..505
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 506..526
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 527..543
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 544..564
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 565..588
FT /note="Extracellular"
FT /evidence="ECO:0000255"
SQ SEQUENCE 590 AA; 68928 MW; DA4BD83743EFC723 CRC64;
MKDKAAATME IPEDPGIPKN LERKRPIVWR MIYYSFAVLL LAAFTAAYVT EFQILTHEDV
LFSLGLYGLV MFLHLMMQSL FAYLEIRRIN KTDLPCSFKK TVALTIAGYQ ENPDYLKHCL
DSCRYVKYPK DKLKIILVID GNTEDDAYMM EMFKDVFHGD DVGTYVWKGN YHTGVKETQD
GSCPEVSKPL NEDEGIRIVE ELVRTKRCVC IMQQWGGKRE VMYTAFRAIG TTMDYVQVCD
SDTKLDELAT VEMVKVLEAN ELCGAVGGDV RILNPYDSFI SFMSSLRYWM AFNVERACQS
YFDCVSCISG PLGMYRNDIL QVFLEAWHSQ KFLGTYCTLG DDRHLTNRVL SMGYRTKYTP
KCRAFSETPS QYLRWLNQQT RWTKSYFREW LYNAQWWYKH HIWMTYESVV HFIFPFFITA
TVIRLLYAST IWNVVWLLLC IQIMSVLKSL YACWLRGNPI MLLMSLYSML YMTGLLPSKY
FAMLTINKSG WGTSGRKKIV GNYMPVLPLS IWMAVLCGGV GYSIYMDCHQ DWSTPEKQKE
LYHLLYGCIS YTLYWVLMAL MYWVWVKRCC RKRSQTVTLV HDIPERLVCK
