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Database: UniProt
Entry: A0A2G5DJC3_AQUCA
LinkDB: A0A2G5DJC3_AQUCA
Original site: A0A2G5DJC3_AQUCA 
ID   A0A2G5DJC3_AQUCA        Unreviewed;      1777 AA.
AC   A0A2G5DJC3;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   24-JAN-2024, entry version 18.
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=AQUCO_01900181v1 {ECO:0000313|EMBL:PIA43604.1};
OS   Aquilegia coerulea (Rocky mountain columbine).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Ranunculales; Ranunculaceae; Thalictroideae;
OC   Aquilegia.
OX   NCBI_TaxID=218851 {ECO:0000313|EMBL:PIA43604.1, ECO:0000313|Proteomes:UP000230069};
RN   [1] {ECO:0000313|EMBL:PIA43604.1, ECO:0000313|Proteomes:UP000230069}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Goldsmith {ECO:0000313|Proteomes:UP000230069};
RA   Hodges S., Kramer E., Nordborg M., Tomkins J., Borevitz J., Derieg N.,
RA   Yan J., Mihaltcheva S., Hayes R.D., Rokhsar D.;
RT   "WGS assembly of Aquilegia coerulea Goldsmith.";
RL   Submitted (SEP-2017) 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; KZ305036; PIA43604.1; -; Genomic_DNA.
DR   Proteomes; UP000230069; 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: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:SF29; 1,3-BETA-GLUCAN SYNTHASE COMPONENT FKS1-RELATED; 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:UP000230069};
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        510..529
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        566..586
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        606..631
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        670..692
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        744..763
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1495..1517
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1581..1599
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1641..1659
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1665..1688
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          289..405
FT                   /note="1,3-beta-glucan synthase component FKS1-like"
FT                   /evidence="ECO:0000259|SMART:SM01205"
SQ   SEQUENCE   1777 AA;  204796 MW;  EF67A6E04ED74034 CRC64;
     MANLDGLPPG LTRRPSRSAA TTTFSLEVFD NEVVPSSLQS IVPILRVATE IENERPRVAY
     LCRFYAFEKA HRLDPSSTGR GVRQFKTALL QRLERDNASS LASRVKKSDA REIESFYQQY
     YEHYVRALDR GEQADRAQLG KAYQTAGVLF EVLCAVNKSE KVEEVAPEII AAAKDVQEKK
     DIYTPYNILP LDAAGASQCI MQFEEIKATV SALRNTHGLN WPTAFEQHKQ KTGDLDLLDW
     LRAMFGFQLD DRAVDLIMSK MFKNYKTWCK FLGRKHSLRL PQGQHEVQQR KILYMGLYLL
     IWGEAANIRF MPECLCYVFH NMAYELHGLL AGNVSIVTGE NIKPSYGGDD EAFLRKVVTP
     LYRVLEKEAK KAGHGKAPHS AWCNYDDLNE YFWSPDCFSL GWPMRDDGDF FKSTRELKSA
     KQGTRKKSES TGKSYFVETR TFWHIFRSFD RLWTFYILAL QIQRLVLYFI CSKFSKKKLA
     GFLVDVRGKE YAFRETVKQH ILRTLMRPIL LIKIAFIYLK QFIISSFLFA CHFTFTFSCT
     RSSILELLLN FPGYHRWKFT DVLRTLLKIV VSLAWAIILP ICYLHSLNNA PEKVKEVMNL
     LRQVEGIPPL YAMVVILYLL PNLLAAVLFI FPMLRRWIEN SDWHIVRFLL WWSQPRIYIG
     RGMHESQFSL IKYTLFWVLL LCSKLAFSYF IMIKPLIQPT KDIMSLQRVQ YTWHEFFPNA
     KHNIGAVVSL WAPVIMVYFM DSQIWYSIFS TIYGGISGAF SRLGEIRTLG MLRSRFQSLP
     GAFNAYLVPT EKTRKRGFSF SKRFAEASAN RRTEAAKFAQ LWNEVICSFR EEDLISDRKG
     LLMDLLLVPY TSDPSLKLIQ WPPFLLASKI PIALDMAAQF RAKDSDLWKR ICADEYLKCA
     VIECYESFKL VLNVLVVGEN EKRIVGIIFK EIESNISKNT FLTNFRMAPL PALCKKFVEL
     IGILKDANPS KRGTVVLLLQ DMLEVVTRDM MVNEIRELVE LGHGNKDKQL FAGADPKPAI
     VFPPVATPHW EEQIKRLYLL LTVKESAIDV PTNLEARRRI TFFANSLFMD MPRAPKVSKM
     LSFSVMTPYY SEETVYSKND LEMENEDGVS IIFYLQKIYP DEWNNFMERV NCKRESEVWE
     NDETILQLRH WVSLRGQTLS RTVRGMMYYR RALKLQAFLD MATEKEILEG YKAVTATTEE
     EKKSQRSLYA HLEAIADMKF TYVATCQNYG NQKRSGDRRA TDILNLMVNN PSLRVAYIDE
     VEERDAGRVQ KVYYSVLVKA ADKIDQEIYR IKLPGTAKIG EGKPENQNHA IIFTRGKALQ
     TIDMNQDNYL EEALKMRNLL EEFHEDHGVR PPTILGVREH IFTGSVSSLA WFMSMQETSF
     VTIGQRVLAN PLKIRFHYGH PDVFDRLFHI TRGGISKASQ GINLSEDIFA GFNSTLRRGN
     VTHHEYIQVG KGRDVGLNQI SLFEAKVACG NGEQILSRDI YRLGHRFDMF RMLSCYFTTV
     GFYISSVLVV LTVYFYLYGK LYLSLSGLEK SIIKFAKAKG KNPLQAAMAS QSVVQLGLLT
     ALPMVMEIGL ERGFRTALGD FIIMNLQLAA VFFTFSLGTK VHYFGRTVMH GGAKYRATGR
     GFVVRHEKFG ENYRMYSRSH FVKGLELMVL LVVYELYGSA ATDSISYVLL TGSIWFLVIS
     WLFSPFLFNP SGFEWQKIVE DWDDWTKWIN SRGGIGVPAI KSWESWWAEE QEHLQYTGFL
     GRFWEVVLSL RFFLYQYGIV YHLHIANGNT SIIVSSI
//
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