ID A0A0E0AEQ1_9ORYZ Unreviewed; 1867 AA.
AC A0A0E0AEQ1;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
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:OGLUM06G29540.5};
RN [1] {ECO:0000313|EnsemblPlants:OGLUM06G29540.5}
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:OGLUM06G29540.5}
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; OGLUM06G29540.5; OGLUM06G29540.5; OGLUM06G29540.
DR Gramene; OGLUM06G29540.5; OGLUM06G29540.5; OGLUM06G29540.
DR HOGENOM; CLU_000742_0_0_1; -.
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:SF48; CALLOSE SYNTHASE 3; 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 490..515
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 527..547
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 572..592
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 676..694
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1445..1467
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1496..1515
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1527..1548
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1614..1638
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1693..1713
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1738..1761
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1767..1790
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1810..1830
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 336..447
FT /note="1,3-beta-glucan synthase component FKS1-like"
FT /evidence="ECO:0000259|SMART:SM01205"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1867 AA; 214292 MW; 2C88B3204EDAFACF CRC64;
MAAPGGARRP DFSSAASPSP SPAGAAGRRL LRTQTVGNLG ESIFDSEVVP SSLVEIAPIL
RVANEVEATN PRVAYLCRFY AFEKAHRLDP TSSGRGVRQF KTALLQRLER ENDPTLKGRV
HQSDAREMQR FYREYYKKYI QALQNAADKA DRALLTKAYQ TAAVLFEVLK AVNVSQSVEV
DQAILDTHNK VEEKKKLYVP YNILPLDPES TYQPIMQYPE IQAAVNALRN IRGLPWPKEH
EKKPDEKKTG KDLLDWLQAM FGFQKDNVSN QREHLILLLA NVHIRQSPKT EQQAKLDDRA
LDAVMKKLFK NYKKWCKYLG RKSSLWLPTI QQEVQQRKLL YMGLYLLIWG EAANLRCLQF
YVLMAFELYG MLAGNVSPMT GENVKPAYGG DEEAFLMKVV TPIYKVIEKE AERSKTIKSK
HSHWRNYDDL NEYFWSVDCF RLGWPMRADA DFFKTPEDAY PSRLNGAMII IAWNGGTPSD
IFDVGVFKQV LSIFITAAVL KLGQAILDIV FGWKARRSMS FAVKLRYVLK LISSSAWVVI
LPVTYAYTWD SPTGLARIIK SWLGNGQNQP SLYILAVVIY LAPNMLAAML FLFPFLRRFL
ESSNVKVITF IMWWSQPRLF VGRGMHEGAF SLFKYTMFWV LLLAMKLTIK PLVQPTKDIM
KEPIRDFQWH EFFPRANNNI GVVIALWAPI ILVYFMDTQI WYALFSTLIG GIYGAYRRLG
EIRTLGMLRS RFESLPEAFN EHLIPSDSHK SKGLRAAFTG KPSKTSGDEQ EKEKIAARFA
QMWNLIITSF REEDLIDNRE MDLLLVPYCK DRELNIFQWP PFLLASKIPI ALDMAADSGG
KDRDLKKRMR SDPYFSYAIR ECYGSFKNII NTLVFGQREK IVIQQIFTIV DEHIEGGSLI
KDLNMRSLPA LSKKFIELLE LLQKNKEEDL GQVVILFQDM LEVVTRDIMD EQDQLGGLLD
SVHGGNRKHE GMTSLDQQDQ LFTKAIRFPV EESNAWTEKI KRLHLLLTVK ESAMDVPTNL
DARRRISFFA NSLFMEMPNA PKVRHMLPFS VLTPYYKEDV LFSSHNLEEP NEDGVSILFY
LQKIYPDEWK NFLDRVDRKS EEELREDETL EEELRLWASY RGQTLTRTVR GMMYYRKALE
LQAFLDMAKD NGYRATELMS EDSQLMTQCK AIADMKFTYV VSCQQYGIQK RSGEACAHDI
LRLMTVYPSL RVAYIDEVEA PSQDRNKKTD KVYYSALVKA SVTKPNEPGQ SLDQVIYKIK
LPGNAILGEG KPENQNHAII FTRGECLQTI DMNQEHYMEE ALKMRNLLDE FLKKHDGVRY
PSILGVREHI FTGSVSSLAW FMSNQETSFV TIGQRVLANP LRGGVSKASK IINLSEDIFA
GFNSTLREGN VTHHEYMQVG KGRDVGLNQI SLFEAKIANG NGEQTLSRDI YRLGHRFDFF
RMLSCYYTTI GFYFSTMITV WTVYVFLYGR LYLVLSGLDQ ALATGKKFVH NAPLQVALAS
ESFVQLGFLM ALPMMMEIGL ERGFRTALSD FVLMQLQLAS VFFTFSLGTK THYYGRTLLH
GGAEYRATGR GFVVFHAKFA DNYRLYSRSH FVKGIELMIL LVVYEIFGQS YRGAITYIFI
TVSMWFMVGT WLFAPFLFNP SGFEWQKIVD DWTDWNKWIS NRGGIGVAPT KSWESWWEKE
QEPLRYSGKR GTFLEILLAL RFFVYQYGLV YHLNITKHTR SVLTVSVGRR RFSAEFQLVF
RLIKGLIFIT FVAIVVILIA IPHMTVLDIF VCILAFMPTG WGLLLIAQAI KPAVQAIGLW
GSIKALARGY EILMGLLLFT PIAFLAWFPF VSEFQTRMLF NQAFSRGLQI SRILGGHKKD
RSTRNKE
//
