ID A0A067KVF8_JATCU Unreviewed; 805 AA.
AC A0A067KVF8;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=1,3-beta-glucan synthase {ECO:0008006|Google:ProtNLM};
GN ORFNames=JCGZ_09973 {ECO:0000313|EMBL:KDP36220.1};
OS Jatropha curcas (Barbados nut).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Malpighiales; Euphorbiaceae; Crotonoideae; Jatropheae;
OC Jatropha.
OX NCBI_TaxID=180498 {ECO:0000313|EMBL:KDP36220.1, ECO:0000313|Proteomes:UP000027138};
RN [1] {ECO:0000313|EMBL:KDP36220.1, ECO:0000313|Proteomes:UP000027138}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. GZQX0401 {ECO:0000313|Proteomes:UP000027138};
RC TISSUE=Young leaves {ECO:0000313|EMBL:KDP36220.1};
RX PubMed=24837971; DOI=10.1371/journal.pone.0097878;
RA Zhang L., Zhang C., Wu P., Chen Y., Li M., Jiang H., Wu G.;
RT "Global Analysis of Gene Expression Profiles in Physic Nut (Jatropha curcas
RT L.) Seedlings Exposed to Salt Stress.";
RL PLoS ONE 9:E97878-E97878(2014).
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DR EMBL; KK914449; KDP36220.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A067KVF8; -.
DR STRING; 180498.A0A067KVF8; -.
DR Proteomes; UP000027138; 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:InterPro.
DR GO; GO:0006075; P:(1->3)-beta-D-glucan biosynthetic process; IEA:InterPro.
DR InterPro; IPR003440; Glyco_trans_48.
DR PANTHER; PTHR12741:SF22; CALLOSE SYNTHASE 8-RELATED; 1.
DR PANTHER; PTHR12741; LYST-INTERACTING PROTEIN LIP5 DOPAMINE RESPONSIVE PROTEIN DRG-1; 1.
DR Pfam; PF02364; Glucan_synthase; 1.
PE 4: Predicted;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000027138};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 373..395
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 460..481
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 542..566
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 617..638
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 650..667
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 687..707
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 714..735
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 755..776
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 805 AA; 93053 MW; DE5236217A0FD96F CRC64;
MQKIYPDEWK NFLERLDYDS SELFKDESKK EELRNWASFR GQTLSRTVRG MMYYREALRV
QAFLDMADDE DILEGYAAAE RNNRTLFAQL DALADLKFTY VISCQIYGSQ KSSGDPHAND
ILEVMKRYPS VRVAYVEEKE EIVNDKPRKA YSSILVKAVN GLDQEIYRIK LPGPPNIGEG
KPENQNHAII FTRGEALQTI DMNQDNYLEE AFKMRNLLQE FFLQRGRRPP TILGLREHIF
TGSVSSLAWF MSYQETSFVT IGQRLLANPL RVRFHYGHPD VFDRLFHITR GGISKASKTI
NLSEDVFAGF NSTLRRGCVT YHEYLQVGKG RDVGLNQISK FEAKVANGNS EQTLSRDIYR
LGRWFDFFRM LSCYFTTIGF YFSNLIAVIG VYVFLYGQLY LVLSGLQKAL VVEARIHNIQ
SLETALASQS FIQLGLLTGL PMVMEIGLEK GFLTAFKDFI LMQLQLAAVF FTFSLGTKIH
YYGRTILYGG AKYRPTGRKV VVFHASFTEN YRLYSRSHFV KGFELVLLLI VYDLFRRSYQ
SSVAYVLITY SIWFMSITWL FAPFLFNPSG FSWDKIVDDW KDWNKWIREQ GGIGIQQDKS
WQSWWNDEQA HLRRPGLGAR FFEIVLSARF FMYQYGLVYH LDISQHSKNF LVYLLSWVVI
FAVFLLFKAV NMGRNKFSAN YHLGFRLFKA FLFIAVVSII VTLSHICKLS LKDLIVCCLA
FLPTGWGLIL IAQAVRPKIE NTGVWDFTQV LAKAYDYGMG IVLFAPIAIL AWLPIISAFQ
TRFLFNEAFN RHLQIQPILA GKKKK
//
