ID A0A0E0CUA9_9ORYZ Unreviewed; 1641 AA.
AC A0A0E0CUA9;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 24-JAN-2024, entry version 26.
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:OMERI03G01500.7};
RN [1] {ECO:0000313|EnsemblPlants:OMERI03G01500.7}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=OR44 {ECO:0000313|EnsemblPlants:OMERI03G01500.7};
RA Wing R.A., Panaud O., Henry R.;
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:OMERI03G01500.7}
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; OMERI03G01500.7; OMERI03G01500.7; OMERI03G01500.
DR Gramene; OMERI03G01500.7; OMERI03G01500.7; OMERI03G01500.
DR HOGENOM; CLU_000742_0_0_1; -.
DR Proteomes; UP000008021; Chromosome 3.
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; IPR023175; Vta1/CALS_N_sf.
DR PANTHER; PTHR12741:SF47; CALLOSE SYNTHASE 9; 1.
DR PANTHER; PTHR12741; LYST-INTERACTING PROTEIN LIP5 DOPAMINE RESPONSIVE PROTEIN DRG-1; 1.
DR Pfam; PF02364; Glucan_synthase; 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: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 1207..1231
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1266..1284
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1290..1311
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1355..1373
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1485..1504
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1516..1541
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1547..1567
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1587..1608
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 344..395
FT /note="1,3-beta-glucan synthase component FKS1-like"
FT /evidence="ECO:0000259|SMART:SM01205"
SQ SEQUENCE 1641 AA; 186941 MW; FC6F1A2AD748C10A CRC64;
MARAAANWER LVRAALRGER LAGAFGVPVT GIAGNVPSSL GNNVHIDEVL RAADEIQDED
PTVARILCEH AYTLAQNLDP NSEGRGVLQF KTGLMSVIRQ KLAKREGGAI DRSQDVAKLQ
EFYKLYREKH KVDELCEDEM KLRESAVFSG NLGELERKTL KRKKVLATLK VLWSVIEEIT
REISPEDADK LISEEMKRVM QKDAERTEDV VAYNIIPLDA LSTTNAIVNF PEVRAAISAL
QYHRELPRLP ATFSVPDARN SDMLDLLHCV FGFQKDNVTN QREHVVHLLA NEQSRLGKLP
GNEPKIDEGA VHVVFSKSLD NYIKWCNYLP LPPVWNNTES LSKEKKLLYV CLYYLIWGEA
ANEAANNDNG RAPHSAWRNY DDFNEFFWHI GHSDDVWCLF NISWICNYQS ALAILKAFQD
GTNSATFKIY VFVISAYVGA KIIIGLLMSV PCCRGLTDYC YRWSVVRLAK WMHQENNYVG
RGMHERPNDY IKSVEAVHRF FEKFPEAFMD KLHVAVPKRK QLLSSSQHSE LNKFDASKFA
PFWNEIVRNM REEDYINNTE LDLLLMPKNN GSLPIVQWPL FLLASKVFLA KDIAIDCKDS
QEELWLRISK DEYMQYAVVE CYHSIHYILT SILDKEGLLW VKRIYDGIQD SISKRNIQSD
LHFSRLPNVI AKLVAVAGIL KETESTDLRK GAINAIQDLY EVVHHEVLSV DMSGNIDEWE
KIKQARAEGR LFNNLKWPTD SGLKDLIKRL YSLLTIKESA ANVPKNLEAR RRLEFFTNSL
FMQMPVARPV SEMLSFSVFT PYYSETVLYS KDELQKRNED GISTLFYLQK IYPDEWKNFL
ARINRDENTT DSELFSSPND MMELRLWASY RGQTLARTVR GMMYYRKALM LQSYLEKLQS
EDIESAVATT GLVLADIHFE LSPEARAQAD LKFTYVVTCQ IYGVQKGERK PEAADIALLM
QRNEALRVAY VDIVESVKNG KPSTEYYSKL VKADIHGKDK EIYSIKLPGN FKLGEGKPEN
QNHAIIFTRG NAVQTIDMNQ DNYFEEALKM RNLLEEFYQN HGKHKPSILG VREHVFTGSV
SSLASFMSNQ ETSFVTLGQR VLANPLKVRM HYGHPDVFDR IFHITRGGIS KASRVINISE
DIYAGFNSTL RLGNITHHEY IQVGKGRDVG LNQIALFEGK VAGGNGEQVL SRDIYRLGQL
FDFFRMLSFY VTTIGFYFCT MLTVWTVYIF LYGKTYLALS GVGESIQNRA DILQNTALNA
ALNTQFLFQI GVFTAIPMIL GFILEFGVLT AFVSFITMQF QLCSVFFTFS LGTRTHYFGR
TILHGGAKYR ATGRGFVVRH IKFAENYRLY SRSHFVKGLE VALLLLIFLA YGFNNGGAVG
YILLSISSWF MSVSWLFAPY IFNPSGFEWQ KVVEDFRDWT NWLFYRGGIG VKGEESWEAW
WDEELAHIHN VGGRILETVL SLRFFIFQYG VVYHMDASGS SKALLIYWIS WAVLGGLFVL
LLVFGLNPKA MVHFQLFLRL IKSIALLMVL AGLVVAVVFT RLSVSDVFAA ILAFVPTGWG
VLSIAVAWKP VVKKLGLWKT VRSLARLYDA GTGMIIFVPI AIFSWFPFIS TFQTRLLFNQ
AFSRGLEISL ILAGNNPNAG V
//
