HYAS2_XENLA
ID HYAS2_XENLA Reviewed; 551 AA.
AC O57427;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Hyaluronan synthase 2;
DE EC=2.4.1.212 {ECO:0000250|UniProtKB:Q92819};
DE AltName: Full=Hyaluronate synthase 2;
DE AltName: Full=Hyaluronic acid synthase 2;
DE Short=HA synthase 2;
DE Short=xHAS2;
GN Name=has2;
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].
RX PubMed=10640711; DOI=10.1016/s0925-4773(99)00238-5;
RA Koeprunner M., Muellegger J., Lepperdinger G.;
RT "Synthesis of hyaluronan of distinctly different chain length is regulated
RT by the differential expression of Xhas1 and 2 during early development of
RT Xenopus laevis.";
RL Mech. Dev. 90:275-278(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 272-461.
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).
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 (By similarity). This is one of
CC three isoenzymes responsible for cellular hyaluronan synthesis and it
CC is particularly responsible for the synthesis of high molecular mass
CC hyaluronan (By similarity). {ECO:0000250|UniProtKB:P70312,
CC ECO:0000250|UniProtKB:Q92819}.
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:Q92819};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20466;
CC Evidence={ECO:0000250|UniProtKB:Q92819};
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:Q92819};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12529;
CC Evidence={ECO:0000250|UniProtKB:Q92819};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC -!- PATHWAY: Glycan biosynthesis; hyaluronan biosynthesis.
CC {ECO:0000250|UniProtKB:Q92819}.
CC -!- SUBUNIT: Homodimer; dimerization promotes enzymatic activity.
CC {ECO:0000250|UniProtKB:Q92819}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q92819};
CC Multi-pass membrane protein {ECO:0000255}. Endoplasmic reticulum
CC membrane {ECO:0000250|UniProtKB:Q92819}; Multi-pass membrane protein
CC {ECO:0000255}. Vesicle {ECO:0000250|UniProtKB:Q92819}. Golgi apparatus
CC membrane {ECO:0000250|UniProtKB:Q92819}; Multi-pass membrane protein
CC {ECO:0000255}. Lysosome {ECO:0000250|UniProtKB:Q92819}. Note=Travels
CC from endoplasmic reticulum (ER), Golgi to plasma membrane and either
CC back to endosomes and lysosomes, or out into extracellular vesicles.
CC Post-translational modifications control HAS2 trafficking.
CC {ECO:0000250|UniProtKB:Q92819}.
CC -!- SIMILARITY: Belongs to the NodC/HAS family. {ECO:0000305}.
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DR EMBL; AF168465; AAD45813.1; -; mRNA.
DR EMBL; AF015779; AAB94540.1; -; Genomic_DNA.
DR RefSeq; NP_001083837.1; NM_001090368.1.
DR AlphaFoldDB; O57427; -.
DR CAZy; GT2; Glycosyltransferase Family 2.
DR GeneID; 399146; -.
DR KEGG; xla:399146; -.
DR CTD; 399146; -.
DR Xenbase; XB-GENE-5775604; has2.S.
DR OrthoDB; 332363at2759; -.
DR UniPathway; UPA00341; -.
DR Proteomes; UP000186698; Chromosome 6S.
DR Bgee; 399146; Expressed in gastrula and 7 other tissues.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:1903561; C:extracellular vesicle; ISS:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:InterPro.
DR GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0050501; F:hyaluronan synthase activity; ISS:UniProtKB.
DR GO; GO:0036302; P:atrioventricular canal development; ISS:UniProtKB.
DR GO; GO:0090500; P:endocardial cushion to mesenchymal transition; 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; ISS:UniProtKB.
DR GO; GO:0035810; P:positive regulation of urine volume; ISS:UniProtKB.
DR GO; GO:0070295; P:renal water absorption; ISS:UniProtKB.
DR GO; GO:0001570; P:vasculogenesis; ISS:UniProtKB.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR028371; HAS2.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR PANTHER; PTHR22913:SF7; PTHR22913:SF7; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Endoplasmic reticulum; Glycosyltransferase; Golgi apparatus;
KW Lysosome; Membrane; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..551
FT /note="Hyaluronan synthase 2"
FT /id="PRO_0000197177"
FT TOPO_DOM 1..11
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 12..32
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 33..45
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 46..66
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 67..374
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 375..395
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 396..402
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 403..423
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 424..429
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 430..450
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 451..470
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 471..491
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 492..509
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 510..530
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 531..551
FT /note="Extracellular"
FT /evidence="ECO:0000255"
SQ SEQUENCE 551 AA; 63686 MW; AAD902B3B4802A7D CRC64;
MHCERFICIL RIIGTTLFGV SLLLGISAAY IVGYQFIQTD NYYFSFGLYG AILALHLIIQ
SLFAFLEHRK MKRSLETPIK LNKSVALCIA AYQEDEDYLR KCLLSVKRLT YPGMKVIMVI
DGNSDDDLYM MNIFREIMGN DSCATYVWKN NFHMKGPNET DETHRESMQH VTQMVLSNRN
VCIMQKWNGK REVMYTAFKA LGRSVDYVQV CDSDTVLDPA SSVEMVKVLE EDIMVGGVGG
DVQILNKYDS WISFLSSVRY WMAFNIERAC QSYFGCVQCI SGPLGMYRNS LLHEFIEDWY
NQEFLGSQCS FGDDRHLTNR VLSLGYATKY TARSKCLTET PTEYLRWLNQ QTRWSKSYFR
EWLYNSLWFH KHHLWMTYEA VITGFFPFFL IATVIQLFYR GRIWNILLFL LTVQLVGLIK
SSFASALRGN IVMVFMSFYS VLYMSSLLPA KMFAIATINK AGWGTSGRKT IVVNFIGLIP
ITVWFTILLG GVCYTIWRET KKPFSESEKI VLAVGAILYA CYWVMLLTMY VSLVMKCGRR
RKEPQHDLVL A
