ID A0A0D9YA17_9ORYZ Unreviewed; 1738 AA.
AC A0A0D9YA17;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 24-JAN-2024, entry version 25.
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 glumipatula.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=40148 {ECO:0000313|EnsemblPlants:OGLUM01G21880.5};
RN [1] {ECO:0000313|EnsemblPlants:OGLUM01G21880.5}
RP NUCLEOTIDE SEQUENCE.
RA Wing R.A., Panaud O., Oliveira A.C.;
RT "Oryza genome evolution.";
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:OGLUM01G21880.5}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (APR-2015) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[(1->3)-beta-D-glucosyl](n) + UDP-alpha-D-glucose = [(1->3)-
CC beta-D-glucosyl](n+1) + H(+) + UDP; 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:ARBA00000192};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 48 family.
CC {ECO:0000256|ARBA:ARBA00009040}.
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DR EnsemblPlants; OGLUM01G21880.5; OGLUM01G21880.5; OGLUM01G21880.
DR Gramene; OGLUM01G21880.5; OGLUM01G21880.5; OGLUM01G21880.
DR Proteomes; UP000026961; Unassembled WGS sequence.
DR GO; GO:0000148; C:1,3-beta-D-glucan synthase complex; IEA:InterPro.
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:0071555; P:cell wall organization; IEA:UniProtKB-KW.
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; IPR026899; FKS1-like_dom1.
DR InterPro; IPR003440; Glyco_trans_48.
DR InterPro; IPR039431; Vta1/CALS_N.
DR InterPro; IPR023175; Vta1/CALS_N_sf.
DR PANTHER; PTHR12741:SF16; CALLOSE SYNTHASE 7; 1.
DR PANTHER; PTHR12741; LYST-INTERACTING PROTEIN LIP5 DOPAMINE RESPONSIVE PROTEIN DRG-1; 1.
DR Pfam; PF14288; FKS1_dom1; 1.
DR Pfam; PF02364; Glucan_synthase; 2.
DR Pfam; PF04652; Vta1; 1.
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:UP000026961};
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 482..500
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 512..533
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 553..576
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 596..621
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1302..1324
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1449..1468
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1474..1496
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1580..1600
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1621..1641
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1647..1666
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1687..1705
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 335..434
FT /note="1,3-beta-glucan synthase component FKS1-like"
FT /evidence="ECO:0000259|SMART:SM01205"
FT REGION 1..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1738 AA; 201047 MW; 66794EF7F3C220CB CRC64;
MATGGGGLSG PQPSLRRGLS RASTMRPEGY SGEDGGEYSE ESELVPSSLA PIVPILRAAN
EIEEENPRVA YLCRFTAFEK AHNMDPNSSG RGVRQFKTYL LHRLEKDEHE TQRRLAGTDA
KEIQRFYEHY CKKNLEDGLK TKKPGEMARH YQIASVLYDV LKTVTPEKFH AEFDIYAKEV
EKEKASFSHY NILPLNISGQ RQPVMEIPEI KAAVDLLRKI DGLPMPRLDP VSAEKETDVP
TVRDLLDWLW LTFGFQKGNV ENQKEHLILL LANIDMRKGA NAYQSDRHNH VYGSQMHSDT
VRSLMRKIFE NYISWCRYLH LESNIKIPND ASTQQPEILY IGLYLLIWGE ASNSHQYKNT
IIPIGQDFDP PFRREGSDDA FLQLVIQPIY SVMKQEAAMN KRGRTSHSKW RNYDDLNEYF
WSKRCFKQLK WPMDSAADFF AVPLKIKTEE HHDRVITRRR IPKTNFVEVR TFLHLFRSFD
RMWAFFILAF QAMVIVAWSP SGLPSAIFAP TVFRNVLTIF ITAAFLNFLQ ATLEIILNWK
AWRSLECSQM IRYILKFVVA VAWLIILPTT YMSSIQNSTG LIKFFSSWIG NLQSESIYNF
AVALYMLPNI FSALFFIFLP FRRVLERSNS RIIRFFLWWT QPKLYVARGM YEDTCSLLKF
ILLLDLRGQL CSWDEGNTHG MSSFHTHNLG VVITVWAPIV MIRTLGMLRS RFEAIPIAFG
KHLVPRHDSQ PKRREREEVK NIDKFSDIWN AFIHSLREED LISNSGLLSF SLIPIALDMA
NSVKKRDEEL RKRINQDAYT YYAVVECYET LFSILYSLIV EQSDKKVVDR IHDSIEDSIS
RLSLRTDEDI DPIKTQIANL LQDIMEITTQ DIMKNGQGIL KDKNRENQLF ANINLNSVKD
KTWREKPFCF CISVLTPYFK EEVLFSAEDL YKKNEDGISI LFYLRKIYPD EWKNFLERIE
FQPTDEESLK TKMDEIRPWA SYRGQTLTRT AKLEHRKTVQ SSQEGWASFD MARAIADIKF
TYVVSCQVYG MQKTSKDLKD KACYLNILNL MLTYPSLRVA YIEEVEAPAG NGTTEKTYYS
VLVKGGEKYD EEIYRIKLPG KPTDIGEGKP ENQNHAIVFT RGEALQAIDM NQDNYLEEAF
KMRNVLEEFE SEKYGKRKPT ILGLREHIFT GSVSSLAWFM SNQETSFVTI GQRVLANPLK
VRFHYGHPDI FDRLFHITRG GISKASKTIN LSEDIFSGFN STMREGNVTH HEYMQVGKGR
DVGMNQISSF EAKVANGNGE QTLSRDIYRL GRRFDFYRML SFYFTTVGFY FSSMVTVLTV
YVFLYGRLYL VMSGLERSIL LDPRIEQNIK PLENALASQS FFQLGLLLVL PMVMEVGLEK
GFRTALGEFV IMQLQLASVF FTFQLGTKTH YYGRTILHGG AKYRPTGRGF VVYHAKFADN
YRMYSRSHFV KGLELLILLV VYLVYGSSYR SSSMYLFVTF SIWFLVASWL FAPFIFNPSC
FEWQKTVDDW TDWRKWMGNR GGIGMSVDQS WEAWWISEQE HLRKTSIRSL LLEIILSLRF
LIYQYGIVYH LNIARRNKSI LVYGLSWLVM LSVLVVLKMV SIGRQKFGTD LQLMFRILKG
LLFLGFVSVM AVLFVVCNLT ISDVFASILG FMPTGWCILL IGQACSPLVK KAMLWDSIME
LGRSYENLMG LVLFLPIGLL SWFPFVSEFQ TRLLFNQAFS RGLQISRILA GQKDIGEE
//
