ID A0A0D9Z0M5_9ORYZ Unreviewed; 1980 AA.
AC A0A0D9Z0M5;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 34.
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:OGLUM02G39620.1};
RN [1] {ECO:0000313|EnsemblPlants:OGLUM02G39620.1}
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:OGLUM02G39620.1}
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 STRING; 40148.A0A0D9Z0M5; -.
DR EnsemblPlants; OGLUM02G39620.1; OGLUM02G39620.1; OGLUM02G39620.
DR Gramene; OGLUM02G39620.1; OGLUM02G39620.1; OGLUM02G39620.
DR eggNOG; KOG0916; Eukaryota.
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:SF103; 1,3-BETA-GLUCAN SYNTHASE; 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; 1.
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 525..541
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 561..583
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 595..615
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 640..664
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 700..721
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 752..769
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 775..794
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1541..1563
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1592..1611
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1623..1644
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1710..1734
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1788..1806
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1818..1835
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1855..1875
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1882..1903
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1923..1944
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 349..474
FT /note="1,3-beta-glucan synthase component FKS1-like"
FT /evidence="ECO:0000259|SMART:SM01205"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1980 AA; 228072 MW; 8951F839374E00F4 CRC64;
MASSSSGRRV GGPRGGGESS PSPAAXXXXX XXXXXXXXXX AASGGRRILR TQTAGNLGES
IFDSEVVPSS LVEIAPILRV ANEVEGSNPR VAYLCRFYAF EKAHRLDPTS SGRGVRQFKT
ALLQRLEREN DPTLKGRVKQ SDAREMQSFY QHYYKKYIQA LQNAADKADR AQLTKAYQTA
AVLFEVLKAV NVSQKIEVDQ AILETHNQVE EKKKLYLPYN ILPLDPDSAN QAIMRYPEIQ
AAFHALRNTR GLPWPKDHEK KPDADLLGWL QAMFGFQKDN VSNQREHLIL LLANVHIRQI
PKPDQQPKLD DRALDTVMKK LFKNYKRWCK YLGRKSSLWL PTIQQEVQQR KLLYMGLYLL
IWGEAANLRF MPECLCYIYH HMAFELYGML AGNVSPTTGE NVKPAYGGDE EAFLKKVVTP
IYKVIEKEAE RSESSERSER SKTTKSKHSH WRNYDDLNEY FWSRDCFRLG WPMRADADFF
KTPDYAYHDE VSGENRRVGS GQWMGKVNFV EIRSFWHIFR SFDRMWSFLI LSLQAMIIIA
WNGGTPSDIF DAGVFKQVLS IFITAAILKL GQAILDIILS WKARRSMSLA GKLRYILKLI
SAAAWVVILP VTYAYTWENP TGLARTIKSW LGDGQNQPSL YILAVVIYLA PNMLSAVLFL
FPVLRRALER SNLKVVTFMM WWSQPRLFVG RGMHEGAFSL FKYTMFWVLL LATKLIVSYY
VEIKPLVRPT KDIMKEPIRT FQWHEFFPHG NNNIGIVIAL WAPIILVYFM DTQIWYAIFS
TLIGGIYGAC RRLGEIRTLG MLRSRFESLP KAFNQRLIPS DSNKRRGIRA AFSSKPTKTP
EDSKEEEKIA ARFAQIWNLI ITSFREEDLI DNREKDLLLV PYCKDRDMDI IQWPPFLLAS
KIPIALDMAA DSEGKDRDLK KRVKSDPYFT YAIKECYASF KNIIYTLVVG AKERDVIQKI
FTAVDDHIAQ DTLIKELNMS NLPTLSKKFI ELLELLQKNN KEDQGQVIIL FQDMLEVVTR
DIMDEQLSGL LESVHGGNNR RYEGITPLDQ QDQLFTKAID FPVKESHAWT EKIKRLQLLL
TVKESAMDVP TNLDARRRIS FFANSLFMDM PSAPKVRHML PFSVLTPYYK EDVLFSSQAL
EDQNEDGVSI LFYLQKIYPD EWKHFLQRVD CNTEEELRET EQLEDELRLW ASYRGQTLTR
TVRGMMYYRQ ALVLQAFLDM ARDEDLREGF RAADLLNDES PLLTQCKAIA DMKFTYVVSC
QQYGIQKRSG DHRAQDILRL MTTYPSLRVA YIDEVEEPSK DRNKKIEKVY YSALVKAAVT
KPDDPGQKLD QDIYRIKLPG NAMLGEGKPE NQNHAIIFTR GEGLQTIDMN QEHYMEETLK
MRNLLQEFLK KHDGVRYPSI LGVREHIFTG SVSSLAWFMS NQETSFVTIG QRVLANPLRV
RFHYGHPDIF DRLFHLTRGG VSKASKIINL SEDIFAGFNS TLREGNVTHH EYMQVGKGRD
VGLNQISLFE AKIANGNGEQ TLSRDVYRLG HRFDFFRMLS CYYTTIGFYF STMMTVWTVY
VFLYGRLYLV LSGLDEALAT GKRFIHNEPL QVALASQSFV QLGFLMALPM MMEIGLERGF
RTALSDFVLM QLQLASVFFT FSLGTKTHYY GTTLLHGGAE YRATGRGFVV FHAKFAENYR
LYSRSHFVKG IELLILLIVY EIFGQSYRGA IAYIFITFSM WFMVVTWLFA PFLFNPSGFE
WQKIVDDWTD WNKWISNRGG IGVPPEKSWE SWWEKEQEPI KYSGKRGIVL EIVLALRFFI
YQYGLVYHLN ITKHTKSVLV YCLSWVVIFV ILLVMKTVSV GRRKFSADFQ LVFRLIKGLI
FITFISIIII LIAIPHMTVQ DIFVCILAFM PTGWGLLLVA QAIKPVIVRI GLWGSIKALA
RGYEIIMGLL LFTPIAFLAW FPFVSEFQTR MLFNQAFSRG LQISRILGGH KKDRATRNKE
//
