ID A0A1V4KJ00_PATFA Unreviewed; 587 AA.
AC A0A1V4KJ00;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 17.
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};
GN Name=HAS2 {ECO:0000313|EMBL:OPJ83817.1};
GN ORFNames=AV530_006637 {ECO:0000313|EMBL:OPJ83817.1};
OS Patagioenas fasciata monilis.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Columbiformes; Columbidae; Patagioenas.
OX NCBI_TaxID=372326 {ECO:0000313|EMBL:OPJ83817.1, ECO:0000313|Proteomes:UP000190648};
RN [1] {ECO:0000313|EMBL:OPJ83817.1, ECO:0000313|Proteomes:UP000190648}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BTP2013 {ECO:0000313|EMBL:OPJ83817.1};
RC TISSUE=Blood {ECO:0000313|EMBL:OPJ83817.1};
RA Soares A.E., Novak B.J., Rice E.S., O'Connell B., Chang D., Weber S.,
RA Shapiro B.;
RT "Band-tailed pigeon sequencing and assembly.";
RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OPJ83817.1}.
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DR EMBL; LSYS01003169; OPJ83817.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V4KJ00; -.
DR STRING; 372326.A0A1V4KJ00; -.
DR UniPathway; UPA00341; -.
DR Proteomes; UP000190648; Unassembled WGS sequence.
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; IEA:UniProtKB-EC.
DR GO; GO:0030213; P:hyaluronan biosynthetic process; IEA:UniProtKB-UniPathway.
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:UP000190648};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 41..66
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 78..101
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 410..432
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 438..454
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 466..490
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 510..532
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 544..568
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 587 AA; 67474 MW; 098FE85A2003DF61 CRC64;
MERLSLATDQ TVNITSDRGK QQQEKLNSAF GRTSKMHCER FICILRILGT TLFGVSLLLG
ITAAYIVGYQ FIQTDNYYFS FGLYGAILAS HLIIQSLFAY LEHRKMKRSL ETPIKLNKTV
ALCIAAYQED PDYLRKCLLS VKRLTYPGIK VVMVIDGNSE DDVYMMDIFT EIMGRDKSAT
YIWSNNFHDK GPGETDESHR ESMQHVSQLV LSNKSVCIMQ KWGGKREVMY TAFKALGRSV
DYVQVCDSDT MLDPASSVEM VKVLEEDPMV GGVGGDVQIL NKYDSWISFL SSVRYWMAFN
IERACQSYFG CVQCISGPLG MYRNSLLHEF VEDWYNQEFM GSQCSFGDDR HLTNRVLSLG
YATKYTARSK CLTETPIEYL RWLNQQTRWS KSYFREWLYN AMWFHKHHLW MTYEAVITGF
FPFFLIATVI QLFYRGKIWN ILLFLLTVQL VGLIKSSFAS FLRGNVVMVF MSLYSVLYMS
SLLPAKMFAI ATINKAGWGT SGRKTIVVNF IGLIPVSIWF TILLGGVIFT IYKESKKPFS
ESTQTVLIIG TILYACYWVM LLTLYFALIN KCGRRKKEPH FDMVLDV
//
