ID A0A4P1QY62_LUPAN Unreviewed; 1639 AA.
AC A0A4P1QY62;
DT 03-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 03-JUL-2019, sequence version 1.
DT 24-JAN-2024, entry version 13.
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=TanjilG_28927 {ECO:0000313|EMBL:OIV97176.1};
OS Lupinus angustifolius (Narrow-leaved blue lupine).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC genistoids sensu lato; core genistoids; Genisteae; Lupinus.
OX NCBI_TaxID=3871 {ECO:0000313|EMBL:OIV97176.1, ECO:0000313|Proteomes:UP000188354};
RN [1] {ECO:0000313|EMBL:OIV97176.1, ECO:0000313|Proteomes:UP000188354}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Tanjil {ECO:0000313|Proteomes:UP000188354};
RC TISSUE=Whole plant {ECO:0000313|EMBL:OIV97176.1};
RX PubMed=27557478; DOI=10.1111/pbi.12615;
RA Hane J.K., Ming Y., Kamphuis L.G., Nelson M.N., Garg G., Atkins C.A.,
RA Bayer P.E., Bravo A., Bringans S., Cannon S., Edwards D., Foley R.,
RA Gao L.L., Harrison M.J., Huang W., Hurgobin B., Li S., Liu C.W.,
RA McGrath A., Morahan G., Murray J., Weller J., Jian J., Singh K.B.;
RT "A comprehensive draft genome sequence for lupin (Lupinus angustifolius),
RT an emerging health food: insights into plant-microbe interactions and
RT legume evolution.";
RL Plant Biotechnol. J. 15:318-330(2017).
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; CM007375; OIV97176.1; -; Genomic_DNA.
DR STRING; 3871.A0A4P1QY62; -.
DR Proteomes; UP000188354; Chromosome LG15.
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 InterPro; IPR026899; FKS1-like_dom1.
DR InterPro; IPR003440; Glyco_trans_48.
DR PANTHER; PTHR12741:SF67; CALLOSE SYNTHASE 10; 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:UP000188354};
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 231..248
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 260..286
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 298..319
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 331..354
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 398..416
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 447..463
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1207..1229
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1264..1287
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1353..1372
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1378..1400
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1482..1502
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1514..1539
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1545..1564
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1585..1606
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 82..195
FT /note="1,3-beta-glucan synthase component FKS1-like"
FT /evidence="ECO:0000259|SMART:SM01205"
SQ SEQUENCE 1639 AA; 187696 MW; AEB486694DD0AEC3 CRC64;
MFDLLESVFG FQKDNVRNQR ENVVLTIANA QSRLGIPAEN DPKIDEKTIN DVFLKVLDNY
IRWCRYLRVR LAWNSLEAIN RDRKLFLVSL YFLIWGEAAN VRFLPECICY IFHHMANELD
AILDHGEAYP APSCITNDGS VKFLEQIICP IYETLVEEAA RNNNGKAAHS AWRNYDDFNE
YFWSPACFEL SWPMRMDSPF LRKPKKSKRT AKSSFVEHRT FLHLYRSFHR LWIFLALMFQ
ALTIIAFNHG RINLDTIKTI LSIGPSFAIM NFIKSCLDVL LTFGAYSTAR GMAVSRLVIR
FFWGGLTSAG VTYLYVKVLQ ERNSHNPDNS LYFRIYILVL GVYAAIRLFF AFLLKFPACH
ALSDMSDQSF FQFFKWIYQE RYFVGRGLYE NMRDYCSYVA YWLVILACKF TFAYFLQIKP
LVKPTNIIVH LPSLTYSWHD IISKKNNNIL TVVSLWAPVM AIYLMDLHIW YTVMSAIIGG
AIGARARLGE IRSIEMMHKR FESFPGAFVK NLASPQIKRV PLNGPSTEES QDTNKAYAAM
FAPFWNEIIK SLREEDFIGN REMELLSMPS NTGSLRLVQW PLFLLSSKIP MAIDLALDCE
DTQADLWSRI SRDEYMAYAV QECYYSIEKI LYSVVDNEGR LWVEKIFREI NNSISEGSVV
LTLSLKKLPL VLSRFTALTG LLIRNDPELA KGAANAMFQL YDVVTHDLVS PDLSEHLDTW
NILARARADG RLFSRIQWPN DPEIKELVKR LHLLLTVKDS ASNVPKNLEA RRRLEFFTNS
LFMDMPSAKP VSEMLPFSVF TPYYSETVLY STSELQKENE DGVSTLFYLQ KIFPDEWDNF
LERIGRGVST GEEELQESST DSLELRFWVS YRGQTLARTV RGMMYYRRAL MLQSYLEGRS
LGVDNYSQNN FITSQGFESS RESRAQADLK FTYVVSCQIY GQQKQRKAQE AADIALLLQR
NEALRVAFIH VDESTTDAKT PSVFYSKLVK ADINGKDQEI YSIKLPGDPK LGEGKPENQN
HAIIFTRGDA VQTIDMNQDN YLEEAMKMRN LLEEFHANHG LRSPTILGVR EHVFTGSVSS
LAWFMSNQET SFVTLGQRVL ANPLKVRMHY GHPDVFDRIF HITRGGISKA SRVINISEDI
YSGFNSTLRQ GNITHHEYIQ VGKGRDVGLN QIALFEGKVA GGNGEQVLSR DIYRLGQLFD
FFRMLSFYFT TVGFYVCTMM TVLTVYVFLY GRAYLAFSGL DEAISHEAKL LGNTALNAAL
NAQFLVQIGV FTAVPMIMGF ILELGLLKAV FSFITMQLQL CSVFFTFSLG TRTHYFGRTI
LHGGAKYRAT GRGFVVRHIK FAENYRLYSR SHFVKALEIA ILLIVYIAYG YAEGGAVTYV
LITLSSWFLV ISWLFAPYIF NPSGFEWQKT VEDFEDWTNW LLYKGGVGVK GDNSWESWWD
EEQIHIQTLR GRILETILSL RFFLFQYGVV YKLNATGKDT SLAVYGFSWA VLVGIVLIFK
IFTYSLKKSS RFHLYVRIAQ GFAALGLVAA VCVVVAFTRL TIRDLFASIL AFIPTGWAIL
SLAITWKRVV WSLGLWDSVR EFARMYDAGM GMIIFAPIAS LSWFPFISTF QSRLLFNQAF
SRGLEISLIL AGNKANVET
//
