ID A0A0E0C370_9ORYZ Unreviewed; 1833 AA.
AC A0A0E0C370;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 28-JAN-2026, entry version 33.
DE RecName: Full=1,3-beta-glucan synthase {ECO:0000256|ARBA:ARBA00012589};
DE EC=2.4.1.34 {ECO:0000256|ARBA:ARBA00012589};
DE AltName: Full=1,3-beta-glucan synthase {ECO:0000256|ARBA:ARBA00032165};
OS Oryza meridionalis.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=40149 {ECO:0000313|EnsemblPlants:OMERI01G17250.1};
RN [1] {ECO:0000313|EnsemblPlants:OMERI01G17250.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (APR-2015) to UniProtKB.
RN [2] {ECO:0000313|EnsemblPlants:OMERI01G17250.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. OR44 {ECO:0000313|EnsemblPlants:OMERI01G17250.1};
RA Zhang J., Kudrna D., Lee S., Talag J., Welchert J., Wing R.A.;
RT "OmerRS3 (Oryza meridionalis Reference Sequence Version 3).";
RL Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[(1->3)-beta-D-glucosyl](n) + UDP-alpha-D-glucose = [(1->3)-
CC beta-D-glucosyl](n+1) + UDP + H(+); Xref=Rhea:RHEA:21476, Rhea:RHEA-
CC COMP:11146, Rhea:RHEA-COMP:14303, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:37671, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885; EC=2.4.1.34;
CC Evidence={ECO:0000256|ARBA:ARBA00047777};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 48 family.
CC {ECO:0000256|ARBA:ARBA00009040}.
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DR STRING; 40149.A0A0E0C370; -.
DR EnsemblPlants; OMERI01G17250.1; OMERI01G17250.1; OMERI01G17250.
DR Gramene; OMERI01G17250.1; OMERI01G17250.1; OMERI01G17250.
DR eggNOG; KOG0916; Eukaryota.
DR HOGENOM; CLU_000742_1_1_1; -.
DR Proteomes; UP000008021; Chromosome 1.
DR GO; GO:0000148; C:1,3-beta-D-glucan synthase complex; IEA:InterPro.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0003843; F:1,3-beta-D-glucan synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0006075; P:(1->3)-beta-D-glucan biosynthetic process; IEA:InterPro.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR Gene3D; 1.25.40.270; Vacuolar protein sorting-associated protein vta1; 1.
DR InterPro; IPR058851; CALS1_helical.
DR InterPro; IPR026899; FKS1-like_dom1.
DR InterPro; IPR003440; Glyco_trans_48_dom.
DR InterPro; IPR023175; Vta1/CALS_N_sf.
DR PANTHER; PTHR12741:SF13; 1,3-BETA-GLUCAN SYNTHASE; 1.
DR PANTHER; PTHR12741; LYST-INTERACTING PROTEIN LIP5 DOPAMINE RESPONSIVE PROTEIN DRG-1; 1.
DR Pfam; PF25968; CALS1; 1.
DR Pfam; PF14288; FKS1_dom1; 1.
DR Pfam; PF02364; Glucan_synthase; 2.
DR SMART; SM01205; FKS1_dom1; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Cell shape {ECO:0000256|ARBA:ARBA00022960};
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000008021};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 473..491
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 503..524
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 544..568
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 588..609
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 648..669
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 697..717
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 722..741
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1365..1388
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1409..1429
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1441..1461
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1504..1523
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1529..1551
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1605..1623
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1635..1656
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1668..1693
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1699..1717
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1780..1798
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 326..437
FT /note="1,3-beta-glucan synthase component FKS1-like"
FT /evidence="ECO:0000259|SMART:SM01205"
SQ SEQUENCE 1833 AA; 210333 MW; BC5F4CD596471BBA CRC64;
MAASTSTEVV VPAGAGAGAG AGAGRWRRDA LAHTLGSRRL PEGVADAGER VPDAVAPGVM
PFIRAADEVE QDSPRVAFLC RRYAYNKVQR MDPSSVQRGV RQFKTYMSVK LDQDDTQVMG
NDAKEIQRFY KSYCAELSRI SEKRNFEEVA RRYQVASALY EVLRDVTNNK VDSEVMKIAK
VIEEKSVHFK NYKYNIIPLN FPGSSEAIVE LHEIKGAIDA LNSIDGLPMP HMSSMHTDGN
KSIRDLLDWL SLAFGFQKSN VENQRENLVL LLANIGTRTA GQDHPLVDTV NKLWKKILQN
YQSWCSYLHV SSSIMNVETV TQNKQQLMLL HIGLYLLIWG EASNVRFMPE CLCYIFHHMA
RQLHKMIEEN NFQSPPGFEE EGSFLKTAIE PIYKVLQKEA HKSKGGTAGH STWRNYDDLN
EHFWSEKCFA RLNWPWDLTA DFFYQGRTTS TKPKTNFVEV RTFLHIFRSF NRMWMFFILA
FQAMLIVSWS SSGSLSALAD ATVFRSVLSV FITAALLNFI KVTLDIVLTF QAWGNMDWIQ
IVRYLLKFVV AIAWIIILPL AYSSSIRYPS GAGKLLNSWV GNWHNPSVYN VAIIIYIVPD
ILAAFLFLLP QLQNIMERSN WRVIGLIMWW IQPRLYVARG MHEDILSIIK YVFFWVVLLT
CKLAFSFYVE ISPIIGPTKF LLNQGVGNYE WHEIFPFLPH NLGVVITIWA PIVMVYFMDI
QIWYAIFSTA FGGVSGALSH VGEIRTLGML RARFKSMPEA FNKSHATAHR EVPTALHMAM
TSKEGDYHEL IEKIRLDQAR FNAVIECYES LVLILKNLLL DNNDQKIIDA IDKTVLDSVE
NNTLLEDFHM AEIGKVSNTL AKLLHLLSNE STDGTAERKI INALQDFMEI TTRDFMKDGQ
GILKDENERK QRFTHLDMDM IKESFWKEKF VRLHLLLTMK DSAMDVPTNL DARRRITFFA
NSLFMKMPKA PQEVLYSSHE LNKKNEDGIS ILFYLQKIYP DEWKNFLERI GVDPENEEAV
KGYMDDVRIW ASYRGQTLAR TVRGMMYYRR ALELQCYEDM TNAQDGEESA RSKAIADIKF
TYVVSCQLYG MHKASKDSHE KGLYENILNL MLTYPALRIA YIDEKEVPLP NGKMEKQYYS
VLVKGNDEEI YRIRLPGKPT DIGEGKPNNQ NHAIIFTRGE ALQAIDMNQD NYLEEAFKMR
NLLEEFLIKH GKSEPTILGV REHIFTGSVS SLAWFMSNQE TSFVTIGQRV LANTLKVRFH
YGHPDVFDRI FHLTRGGISK ASKVINLSED IFAGFNSTLR QGNVTHHEYI QLGKGRDVGM
NQISNFEAKV ANGNGEQTLC RDIYRLGHRF DFYRMLSLYF TTVGFYFNSM VAVLTVYVFL
YGRLYLVLSG LEKSILQDPQ IKNIKPFENA LATQSIFQLG MLLVLPMMIE VGLEKGFGRA
LGEFVIMQLQ LASVFFTFHL GTKTHYYGRT ILHGGAKYRG TGRGFVVRHA KFAENYRMYS
RSHFVKALEL LILLVVYLAY GISYRSSSLY LYVTISIWFL VFCWLFAPFV FNPSCFEWHK
TVDDWTDWWH WMSNRGGIGL APEQSWEAWW ISEHDHLRNG TIRSLLLEFV LSLRFLIYQY
GIVYHLHIVH GNRSFMVYAL SWLVIAIVLV SLKVVSMGRE KFITNFQLVF RILKGIVFIV
LISLVVILFV VFNLTVSDVG ASILAFIPTG WFILQIAQLC GPLFRRLVTE PLCALFCSCC
TGGTACKGRC CARFRLRSRD VLRKIGPWDS IQEMARMYEY TMGILIFFPI AVLSWFPFVS
EFQTRLLFNQ AFSRGLQISR ILAGQNGSGS KRD
//
