HYAS1_XENLA
ID HYAS1_XENLA Reviewed; 588 AA.
AC P13563; Q5D0A1;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Hyaluronan synthase 1;
DE EC=2.4.1.212;
DE AltName: Full=DG42 protein;
DE AltName: Full=Hyaluronate synthase 1;
DE AltName: Full=Hyaluronic acid synthase 1;
DE Short=HA synthase 1;
DE Short=xHAS1;
GN Name=has1;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
RP STAGE.
RC TISSUE=Gastrula;
RX PubMed=3410156; DOI=10.1016/0012-1606(88)90166-2;
RA Rosa F., Sargent T.D., Rebbert M.L., Michaels G.S., Jamrich M., Grunz H.,
RA Jonas E., Winkles J.A., Dawid I.B.;
RT "Accumulation and decay of DG42 gene products follow a gradient pattern
RT during Xenopus embryogenesis.";
RL Dev. Biol. 129:114-123(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND DEVELOPMENTAL
RP STAGE.
RX PubMed=9442026; DOI=10.1074/jbc.273.4.1923;
RA Spicer A.P., McDonald J.A.;
RT "Characterization and molecular evolution of a vertebrate hyaluronan
RT synthase gene family.";
RL J. Biol. Chem. 273:1923-1932(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Neurula;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (MAR-2003) 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.
CC {ECO:0000269|PubMed:3410156, ECO:0000269|PubMed:9442026}.
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:0000269|PubMed:9442026};
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:0000269|PubMed:9442026};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC -!- PATHWAY: Glycan biosynthesis; hyaluronan biosynthesis.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expression moves as a gradient through the embryo.
CC The mRNA is first expressed in the animal region of the blastula, and
CC by early gastrula is found everywhere except in the outer layer of the
CC dorsal blastopore lip. By mid-gastrula, protein is present in the inner
CC ectodermal layer and the endoderm, then disappears from dorsal ectoderm
CC as the neural plate is induced and later decays in a dorsoventral
CC direction. Last expressed in ventral regions of the gut at the tailbud
CC stage (at protein level). {ECO:0000269|PubMed:3410156}.
CC -!- DEVELOPMENTAL STAGE: Expressed during a short window of embryogenesis.
CC Expression of mRNA begins just after mid-blastula, peaks at late
CC gastrula, and declines by the end of neurulation. Protein expression
CC follows that of the mRNA with a time lag of approximately 2 hours:
CC accumulates through gastrula and early neurula stages and peaks at
CC about stage 18 (mid-neurula), then decays in a non-uniform manner,
CC persisting about 12 to 18 hr longer than the RNA (at protein level).
CC {ECO:0000269|PubMed:3410156, ECO:0000269|PubMed:9442026}.
CC -!- SIMILARITY: Belongs to the NodC/HAS family. {ECO:0000305}.
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DR EMBL; M22249; AAA49699.1; -; mRNA.
DR EMBL; BC047963; AAH47963.1; -; mRNA.
DR EMBL; BC108480; AAI08481.1; -; mRNA.
DR PIR; A43740; A43740.
DR RefSeq; NP_001079696.1; NM_001086227.1.
DR AlphaFoldDB; P13563; -.
DR CAZy; GT2; Glycosyltransferase Family 2.
DR DNASU; 379383; -.
DR GeneID; 379383; -.
DR KEGG; xla:379383; -.
DR CTD; 379383; -.
DR Xenbase; XB-GENE-6256069; has1.S.
DR OMA; SIYACYW; -.
DR OrthoDB; 332363at2759; -.
DR UniPathway; UPA00341; -.
DR Proteomes; UP000186698; Chromosome 3S.
DR Bgee; 379383; Expressed in gastrula and 13 other tissues.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0050501; F:hyaluronan synthase activity; IDA: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; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR SUPFAM; SSF53448; SSF53448; 1.
PE 1: Evidence at protein level;
KW Glycosyltransferase; Membrane; Reference proteome; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..588
FT /note="Hyaluronan synthase 1"
FT /id="PRO_0000197171"
FT TOPO_DOM 1..28
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 29..49
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 50..61
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 62..82
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 83..411
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 412..432
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 433
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 434..454
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 455..456
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 457..477
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 478..505
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 506..526
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 527..543
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 544..564
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 565..588
FT /note="Extracellular"
FT /evidence="ECO:0000255"
SQ SEQUENCE 588 AA; 68522 MW; 33DA3B8E331F4CE9 CRC64;
MKEKAAETME IPEGIPKDLE PKHPTLWRII YYSFGVVLLA TITAAYVAEF QVLKHEAILF
SLGLYGLAML LHLMMQSLFA FLEIRRVNKS ELPCSFKKTV ALTIAGYQEN PEYLIKCLES
CKYVKYPKDK LKIILVIDGN TEDDAYMMEM FKDVFHGEDV GTYVWKGNYH TVKKPEETNK
GSCPEVSKPL NEDEGINMVE ELVRNKRCVC IMQQWGGKRE VMYTAFQAIG TSVDYVQVCD
SDTKLDELAT VEMVKVLESN DMYGAVGGDV RILNPYDSFI SFMSSLRYWM AFNVERACQS
YFDCVSCISG PLGMYRNNIL QVFLEAWYRQ KFLGTYCTLG DDRHLTNRVL SMGYRTKYTH
KSRAFSETPS LYLRWLNQQT RWTKSYFREW LYNAQWWHKH HIWMTYESVV SFIFPFFITA
TVIRLIYAGT IWNVVWLLLC IQIMSLFKSI YACWLRGNFI MLLMSLYSML YMTGLLPSKY
FALLTLNKTG WGTSGRKKIV GNYMPILPLS IWAAVLCGGV GYSIYMDCQN DWSTPEKQKE
MYHLLYGCVG YVMYWVIMAV MYWVWVKRCC RKRSQTVTLV HDIPDMCV
