ID A0A2T7CIL2_9POAL Unreviewed; 1906 AA.
AC A0A2T7CIL2;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 16.
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};
GN ORFNames=GQ55_9G639500 {ECO:0000313|EMBL:PUZ43152.1};
OS Panicum hallii var. hallii.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Panicodae; Paniceae; Panicinae; Panicum;
OC Panicum sect. Panicum.
OX NCBI_TaxID=1504633 {ECO:0000313|EMBL:PUZ43152.1, ECO:0000313|Proteomes:UP000244336};
RN [1] {ECO:0000313|EMBL:PUZ43152.1, ECO:0000313|Proteomes:UP000244336}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. HAL2 {ECO:0000313|Proteomes:UP000244336};
RA Lovell J., Jenkins J., Lowry D., Mamidi S., Sreedasyam A., Weng X.,
RA Barry K., Bonette J., Campitelli B., Daum C., Gordon S., Gould B.,
RA Lipzen A., MacQueen A., Palacio-Mejia J., Plott C., Shakirov E., Shu S.,
RA Yoshinaga Y., Zane M., Rokhsar D., Grimwood J., Schmutz J., Juenger T.;
RT "WGS assembly of Panicum hallii var. hallii HAL2.";
RL Submitted (APR-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) + 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 EMBL; CM009757; PUZ43152.1; -; Genomic_DNA.
DR STRING; 1504633.A0A2T7CIL2; -.
DR EnsemblPlants; PUZ43152; PUZ43152; GQ55_9G639500.
DR Gramene; PUZ43152; PUZ43152; GQ55_9G639500.
DR Proteomes; UP000244336; Chromosome 9.
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; PF14288; FKS1_dom1; 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:UP000244336};
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 498..517
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 537..556
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 568..586
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 598..618
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 661..682
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 721..747
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1472..1496
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1531..1557
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1620..1638
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1750..1769
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1781..1806
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1812..1832
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1852..1873
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 345..457
FT /note="1,3-beta-glucan synthase component FKS1-like"
FT /evidence="ECO:0000259|SMART:SM01205"
SQ SEQUENCE 1906 AA; 217552 MW; 82952F8613F969C0 CRC64;
MSRAEANWER LVRAALRGER FAGVYGQPVT GIAGNVPSSL GNNVHIEEVL RAADEIQDED
PTVARILCEH AYSLAQNLDP NSEGRGVLQF KTGLMSVIRQ KLAKREGGAI DRSQDIAKLQ
EFYKLYREKH KVDELIEDEM KLRESAVFSG NLGELERKTL KRKKVLATLK VLWSVIEDMT
KEISPEDAKN LISEEMKKVM QKDAARTEDV VPYNIIPLDA LSSTTNAIVT FPEVRAAIST
LQYHRDLPRL PGTFSVPDAR NSDMLDLLQC IFGFQEGNVK NQREHIVHLL ANEQSRVGKP
SGNEPKIDEG AVHAVFSKAL DNYIKWCSYL PLRPVWNNTD SLTKEKKLLY VCLYYLMWGE
AANVRFLPEG LCYIFHHLAR ELEEILRKQT AEPAESCSSN GSVSFLENVI SPLYDIIAAE
AANNRNGRAP HSAWRNYDDF NEFFWSLKCF HLGWPWKLDN PFFSKPSKKE KGMFGRGHHY
GKTSFVEHRT FLHLYHSFHR LWMFLIMMFQ GLTIIAFNNG SFDMKTVLQL LSLGPTYVAM
KFIESLLDIL MMYGAYSTSR GSAITRVLWR FCWFTVASLT ICYLYVKALQ DGTQSATFKI
YVFVISAYAG VQIILSLLMS VPCCHGLTEA CYRWSAVRLV KWMHQENNYV GRGMHESPLD
YIKYVAFWIA ILGAKFSFTY FLQIKPLVKP TRAIINFKGL QYAWHDFVSK NNHNAITILS
LWAPVVSIYL LDIHVFYTVM SAIYGFLLGA RDRLGEISSV EAVHRFFEKF PGAFMDKLHV
AVPKRKQLLS SSQLTELNKF DASRFSPFWN EIVRNLREED YISNAELELL LMPKNDGVLP
IVQWPLFLLA SKVFLAKDIA ADCKDSQEEL WLRISKDEYM QYAVVECFHS VYHILTSILE
KEGRLWVERI YGGIQESISK KNIQSDLHFS KLHIVIAKLV AVLGILRGTT ESSDMKKGAV
NAIQDLYEVV HHEVFSVDIR DYLDEWTQIN RARAEGRLFN NLKWPKDPVL KDLIKRLYSL
LTIKESAASV PKNLEARRRL QFFTNSLFMQ MPVARPASEM FSFSVFTPYY SEIVLYSMDE
LQKKNEDGIT TLFYLQKIYP DEWKNFLTRI NRDENAADSE LFGNPNDILE LRLWASYRGQ
TLARTVRGMM YYRKALMLQS YLERIQSEDR ESTFASAGSA DTHFELSPEA RAQADLKFTY
VLTCQIYGKQ KGEGKPEAAD IALLMQRNEA LRVAYIDEVE SVKNGKPSTE YYSKLVKADI
HGKDKEIYSI KLPGNPKLGE GKPENQNHAI IFTRGNAVQT IDMNQDNYFE EALKMRNLLE
EFSLKRGKHY PSILGVREHV FTGSVSSLAS FMSNQETSFV TLGQRVLANP LKVRMHYGHP
DVFDRIFHIT RGGISKASRS INISEDIYAG FNSTLRQGSI THHEYIQVGK GRDVGLNQIA
VFEGKVAGGN GEQVLSRDIY RLGQLFDFFR MLSFYVTTVG FYFCTMLTVL TVYIFLYGKT
YLALSGVGES IQNRADILQN TALNTALNTQ FLFQIGVFTA VPMILGFILE SGVLTAFVQF
ITMQFQLCSV FFTFSLGTRT HYFGRAILHG GAKYRATGRG FVVRHIKFAE NYRLYSRSHF
VKGMEVALLL VIFLAYGFNN GGAVGYILLS ISSWFMALSW LFAPYLFNPS GFEWQKIVED
FRDWTNWLFY RGGIGVKGEE SWEAWWEEEL QHIYTIRGRI LETILSLRFF IFQYGVVYHM
DASDDSTALL VYWISWAVLG GLLVLLLVFG LNPKAMVHFQ LFLRLVKSIA LLMVLAGLIV
AIVFTNLSVT DVFASILAFV PTGWGILSIA VAWKPVVKKL GLWKTMRSLA RLYDAGMGMI
IFVPIAICSW FPFISTFQTR LLFNQAFSRG LEISLILAGN NPNAGM
//