ID W5MSA2_LEPOC Unreviewed; 552 AA.
AC W5MSA2;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=Hyaluronan synthase 2 {ECO:0000256|ARBA:ARBA00022262};
DE EC=2.4.1.212 {ECO:0000256|ARBA:ARBA00012207};
DE AltName: Full=Hyaluronate synthase 2 {ECO:0000256|ARBA:ARBA00030887};
DE AltName: Full=Hyaluronic acid synthase 2 {ECO:0000256|ARBA:ARBA00031214};
OS Lepisosteus oculatus (Spotted gar).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Holostei; Semionotiformes; Lepisosteidae;
OC Lepisosteus.
OX NCBI_TaxID=7918 {ECO:0000313|Ensembl:ENSLOCP00000011261.1, ECO:0000313|Proteomes:UP000018468};
RN [1] {ECO:0000313|Proteomes:UP000018468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E.S., Lindblad-Toh K.;
RT "The Draft Genome of Lepisosteus oculatus.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLOCP00000011261.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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:0000256|ARBA:ARBA00033617};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12529;
CC Evidence={ECO:0000256|ARBA:ARBA00033617};
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:0000256|ARBA:ARBA00033606};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20466;
CC Evidence={ECO:0000256|ARBA:ARBA00033606};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- PATHWAY: Glycan biosynthesis; hyaluronan biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004698}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
CC Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004477}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004477}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the NodC/HAS family.
CC {ECO:0000256|ARBA:ARBA00006782}.
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DR EMBL; AHAT01004820; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_006636013.1; XM_006635950.2.
DR AlphaFoldDB; W5MSA2; -.
DR STRING; 7918.ENSLOCP00000011261; -.
DR Ensembl; ENSLOCT00000011277.1; ENSLOCP00000011261.1; ENSLOCG00000009236.1.
DR GeneID; 102682245; -.
DR KEGG; loc:102682245; -.
DR CTD; 3037; -.
DR eggNOG; KOG2571; Eukaryota.
DR GeneTree; ENSGT00390000010337; -.
DR HOGENOM; CLU_029695_3_0_1; -.
DR InParanoid; W5MSA2; -.
DR OMA; KSATYVW; -.
DR OrthoDB; 1361850at2759; -.
DR UniPathway; UPA00341; -.
DR Proteomes; UP000018468; Linkage group LG11.
DR Bgee; ENSLOCG00000009236; Expressed in zone of skin and 7 other cell types or tissues.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0050501; F:hyaluronan synthase activity; IBA:GO_Central.
DR GO; GO:0036302; P:atrioventricular canal development; IEA:Ensembl.
DR GO; GO:0003181; P:atrioventricular valve morphogenesis; IEA:Ensembl.
DR GO; GO:0001568; P:blood vessel development; IEA:Ensembl.
DR GO; GO:0021535; P:cell migration in hindbrain; IEA:Ensembl.
DR GO; GO:0060030; P:dorsal convergence; IEA:Ensembl.
DR GO; GO:0085029; P:extracellular matrix assembly; IBA:GO_Central.
DR GO; GO:0045226; P:extracellular polysaccharide biosynthetic process; IBA:GO_Central.
DR GO; GO:0031101; P:fin regeneration; IEA:Ensembl.
DR GO; GO:0003146; P:heart jogging; IEA:Ensembl.
DR GO; GO:0001947; P:heart looping; IEA:Ensembl.
DR GO; GO:0030213; P:hyaluronan biosynthetic process; IBA:GO_Central.
DR GO; GO:0008078; P:mesodermal cell migration; IEA:Ensembl.
DR GO; GO:0030510; P:regulation of BMP signaling pathway; IEA:Ensembl.
DR GO; GO:0001756; P:somitogenesis; IEA:Ensembl.
DR CDD; cd06434; GT2_HAS; 1.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR PANTHER; PTHR22913; HYALURONAN SYNTHASE; 1.
DR PANTHER; PTHR22913:SF7; HYALURONAN SYNTHASE 2; 1.
DR Pfam; PF03142; Chitin_synth_2; 1.
DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Golgi apparatus {ECO:0000256|ARBA:ARBA00023034};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000018468};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..31
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 43..66
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 375..397
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 431..455
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 475..497
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 509..533
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 552 AA; 63834 MW; 82A22CF61BC4582D CRC64;
MRCDRVITYL RVFGTTMFGV SLLLGITAAY IKGYQFIATD NHYFSFGLYG AILALHLIIQ
SLFAYLEHRK MRRSLETPIK LNKTLALCIA AYQEDPNYLR KCLMSVKRLT YPGIKVIMVI
DGNNEDDNYM MDIFKDVMGR DKAASYIWKS NFHHKGPDET DESHLESMKH VTHLVLSNKC
ICIMQKWGGK REVMYTAFKA LGKSVDYVQV CDSDTMLDPA SSVEMVKVLE EDPMVGGVGG
DVQILNKYES WISFLSSVRY WMAFNIERAC QSYFGCVQCI SGPLGMYRNS LLHEFLEDWY
NQEFLGSQCS FGDDRHLTNR VLSLGYATKY TARSKCLTET PIRYLRWLNQ QTRWSKSYFR
EWLYNAMWFH KHHLWMTYEA VITGFFPFFL IATVIQLFYR GRIWNILLFL LTVQLVGLIK
SSFASCLRGN IVMVFMSFYS VLYMSSLLPA KMFAIATINK AGWGTSGRKT VVVNFIGLIP
ISVWFSILLG GVIFTIYQET KKPFSESEQT ILIIGAILYA CYWVMLLTLY VVLITKCGRR
KKEQQYDMVF DV
//
