ID A0A453Q8M3_AEGTS Unreviewed; 1888 AA.
AC A0A453Q8M3;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 19.
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 Aegilops tauschii subsp. strangulata (Goatgrass).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Triticinae; Aegilops.
OX NCBI_TaxID=200361 {ECO:0000313|EnsemblPlants:AET6Gv21015200.3, ECO:0000313|Proteomes:UP000015105};
RN [1] {ECO:0000313|Proteomes:UP000015105}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. AL8/78 {ECO:0000313|Proteomes:UP000015105};
RX PubMed=25035499; DOI=10.1126/science.1250092;
RG International Wheat Genome Sequencing Consortium,;
RA Marcussen T., Sandve S.R., Heier L., Spannagl M., Pfeifer M.,
RA Jakobsen K.S., Wulff B.B., Steuernagel B., Mayer K.F., Olsen O.A.;
RT "Ancient hybridizations among the ancestral genomes of bread wheat.";
RL Science 345:1250092-1250092(2014).
RN [2] {ECO:0000313|Proteomes:UP000015105}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. AL8/78 {ECO:0000313|Proteomes:UP000015105};
RX PubMed=29158546; DOI=10.1038/s41477-017-0067-8;
RA Zhao G., Zou C., Li K., Wang K., Li T., Gao L., Zhang X., Wang H., Yang Z.,
RA Liu X., Jiang W., Mao L., Kong X., Jiao Y., Jia J.;
RT "The Aegilops tauschii genome reveals multiple impacts of transposons.";
RL Nat. Plants 3:946-955(2017).
RN [3] {ECO:0000313|EnsemblPlants:AET6Gv21015200.3}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (MAR-2019) 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; AET6Gv21015200.3; AET6Gv21015200.3; AET6Gv21015200.
DR Gramene; AET6Gv21015200.3; AET6Gv21015200.3; AET6Gv21015200.
DR Proteomes; UP000015105; Chromosome 6D.
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:UP000015105};
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 422..438
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 458..480
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 492..512
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 537..561
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 597..618
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 649..666
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1447..1469
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1498..1517
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1529..1550
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1616..1640
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1694..1712
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1724..1741
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1761..1781
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1788..1809
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1829..1850
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 253..369
FT /note="1,3-beta-glucan synthase component FKS1-like"
FT /evidence="ECO:0000259|SMART:SM01205"
SQ SEQUENCE 1888 AA; 218116 MW; 60A8B9D82B6D605F CRC64;
GGFEKAHRLD PLSNGRGVRQ FKIALLQRLE RENDPTLKGR VKQSDAREMQ SFYQHYYKKY
IQALQNAADK ADRAQLTKAY QTAAVLFEVL KAVNVSQKIE VDQAILETHN QVEEKKKLYL
PYNILPLDPD SAANQAIMRY PEIQASFHAL RNTRGLPWPK DHEKKDDADL LEWLQALFGF
QKDNVSNQRE HLILLLANVH IREMSKPDQQ SKLDDHALDI VMKKLFKNYK RWCKYLGRKS
SLWLPTIQQE VQQRKLLYMG LYLLIWGEAA NLRFMPECLC YIYHHMAFEL YGMLAGNVSP
TTGENVKPAY GGAEEAFLKK VVTPIYKIIE MEAERSKTMK SKHSHWRNYD DLNEYFWSRD
CFRLGWPMRA DADFFKTPNF VLNPRDQTNG EHRPAGNDHW MGKVNFVEIR SFWHIFRSFD
RMWSFLILSL QAMVIVAWNG GTPGDIFDAG VFKQVLSIFI TAAVMKMGQA ILDIVLSWKA
RRSMSLAVKL RYILKLLSGA AWVVILPVTY AYTSDNPTGL NRTIKSWFGD GRNQPSLYIL
AVVIYLSPNM LAATLFIFPV LRRFLEKSNL KVVALIMWWS QPRLFVGRGM HEGAFSLFKY
TMFWVVLLAT KLVVSFYVEI RPLVQPTKDI MKVPITTFQW HEFFPHAKNN IGVVIALWAP
IILVYFMDTQ IWYAIFSTLV GGIYGACRRL GEIRTLGMLR SRFESLPKAF NDHLIPNDSK
RRGFRSAFSS KPYKKPEDGK EEDKIAARFA QIWNLIITSF RQEDLIDNRE KDLLLVPYCK
DREMDMIQWP PFLLASKIPI ALDMAADSGG KDRDLKKRMN SDPYFTYAIK ECYASFKNVI
YAVVVGPRER DVIQKIFKVV DDLVAADTLI KDLHMSNLPT LSKKFIELLV ILQKNNKDDL
GQVIILFQDM LEVVTRDIME DQLTELLEPV HGGNNRKHEG ITPLDQQEQE QLFTKAVEFE
FPVKASDAWK EKIKRLHLLL TVKESAMDVP TNLDARRRIS FFANSLFMDM PKAPKVRNML
PFSVLTPYYK EDVLFSSQAL EEENEDGVSI LFYLQKIYPD EWKNFLERVD CKNEEELRET
EQTEDELRLW ASYRGQTLTR TVRGMMYYRQ ALVLQSCLDM APENDLMEGF RAADILSEES
HLLTQSKAVA DMKFTYVVSC QSYGIQKRSG DARAQDILRL MTTYPSLRVA YIDEVEETSK
EGEASKDRSK KIEKVYYSAL VKAAVTKPDD PGQKLDQDIY RIKLPGNAML GEGKPENQNH
AIIFTRGEGL QTIDMNQEHY MEETLKMRNL LQEFTKKHDG VRYPTILGVR EHIFTGSVSS
LAWFMSNQET SFVTIGQRVL ANPLRVRFHY GHPDIFDRLF HLTRGGVSKA SKIINLSEDI
FAGFNSTLRE GNVTHHEYMQ VGKGRDVGLN QISLFEAKIA YGNGEQTLSR DIYRLGHRFD
FFRMLSCYYT TIGFYFSTMI TVWTVYVFLY GRLYLVLSGL DEGLATGRRF IHNDPLQVAL
ASQSFVQLGF LMALPMMMEI GLERGFRTAL SDFVLMQLQL ASVFFTFSLG TKTHYYGKTL
LHGGAEYRAT GRGFVVFHAK FAENYRLYSR SHFVKGIELM ILLIVFEIFG QSYRGAIAYI
FITFSMWFMV VTWLFAPFLF NPSGFEWQKI VDDWTDWNKW ISNRGGIGVS PDKSWESWWE
KEHEPLKYSG KRGTVLEIVL AVRFFIYQYG LVYHLNITKH TKSVLVYCLS WVVIFFILLV
MKAVSVGRRK FSAEFQLVFR LLKGLIFIVF ISTIVILIVI PHMTIQDIFV CILAFMPTGW
GLLLVAQALK PAIMSVGLWG SIRALARGYE IIMGLLLFTP IAFLAWFPFV SEFQTRMLFN
QAFSRGLQIS RILGGHKKDR AALSKDDR
//
