ID A0A1U7Z7F3_NELNU Unreviewed; 1787 AA.
AC A0A1U7Z7F3;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
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 Name=LOC104587134 {ECO:0000313|RefSeq:XP_010242908.1,
GN ECO:0000313|RefSeq:XP_010242909.1};
GN ORFNames=HUJ06_024359 {ECO:0000313|EMBL:DAD22896.1};
OS Nelumbo nucifera (Sacred lotus).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Proteales; Nelumbonaceae; Nelumbo.
OX NCBI_TaxID=4432 {ECO:0000313|Proteomes:UP000189703, ECO:0000313|RefSeq:XP_010242909.1};
RN [1] {ECO:0000313|EMBL:DAD22896.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf {ECO:0000313|EMBL:DAD22896.1};
RX PubMed=32343808;
RA Shi T., Rahmani R.S., Gugger P.F., Wang M., Li H., Zhang Y., Li Z.,
RA Wang Q., Van de Peer Y., Marchal K., Chen J.;
RT "Distinct Expression and Methylation Patterns for Genes with Different
RT Fates following a Single Whole-Genome Duplication in Flowering Plants.";
RL Mol. Biol. Evol. 37:2394-2413(2020).
RN [2] {ECO:0000313|RefSeq:XP_010242908.1, ECO:0000313|RefSeq:XP_010242909.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) 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 EMBL; DUZY01000001; DAD22896.1; -; Genomic_DNA.
DR RefSeq; XP_010242908.1; XM_010244606.2.
DR RefSeq; XP_010242909.1; XM_010244607.2.
DR STRING; 4432.A0A1U7Z7F3; -.
DR GeneID; 104587134; -.
DR KEGG; nnu:104587134; -.
DR eggNOG; KOG0916; Eukaryota.
DR OrthoDB; 354539at2759; -.
DR Proteomes; UP000189703; Unplaced.
DR Proteomes; UP000607653; Unassembled WGS sequence.
DR GO; GO:0000148; C:1,3-beta-D-glucan synthase complex; IEA:InterPro.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0003843; F:1,3-beta-D-glucan synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0046527; F:glucosyltransferase activity; IBA:GO_Central.
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:SF7; CALLOSE SYNTHASE 12; 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:UP000189703};
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 392..410
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 431..454
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 466..482
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 494..514
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 539..560
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 565..584
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1354..1382
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1403..1423
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1435..1453
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1522..1545
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1596..1617
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1629..1650
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1662..1683
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1690..1713
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1733..1752
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 172..284
FT /note="1,3-beta-glucan synthase component FKS1-like"
FT /evidence="ECO:0000259|SMART:SM01205"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1787 AA; 206815 MW; 20E294E06065ABFE CRC64;
MNLRQRPAVP RGGPGYGSVY GPNHGLDGSA PFPTPVSSES FNIIPVHSHL AVADHHSLRC
PEVRAVAGAL RNVGDLRMPP FVPWREGMDL LDWLGVSFGF QRDNVRNQRE HLVLYIANAQ
MRLHPPPVDV DVLDLNVLRR FRRKLLHNYT SWCSYLGRKS SVLLRSRRDD SRRELLYTSL
YLLVWGEAAN LRFVPECICY IFHHMAKELN AILDDYVDGP PTPFTCGENG FLIHVVTPIY
RIISAEVDRS RNGTAPHSAW RNYDDINEYF WSHRCFRRLG WPLNLNSKFF QTKGKDKGVG
KTGFVEQRSF WNIFRSFDRL WVMHILFLQA AIIVAWEGTE FPWTSLESRD VQVRLFTVFI
TWGCLRFLQS VLDAGTQYSL VTRETWLVGV RMVLKSIVAI VWTVVFGVFY GRIWSQRNHD
GRWSDEANRR LVAFLEAALV FIFPELLALA LFIVPWIRNF LEETNFILFY ILTWWFQSRT
FVGRGLREGL VENIRYTSFW VAVLASKFTF SYFLQIKPMV APTKAVLNLR NVSYNWHEFF
GNTNRVAVFF LWLPVVLIYL MDLQIWYSIF TSIVGAIVGL FSHLGEIRNM EQLRLRFQFF
ASAIQFNLMP KEQLLNARGT LLGRLHDAIH LLKLRYGLGR PFMKIESNQV EGKKFALLWN
EIIKTFREED IISDREVELL ELTPNMWNIR VIRWPCFLLC NELLLALSHA AELVDAPDQW
LWYKIGKNEY RRCAIVEAYD SIKYMLIQIV KHGTEEHSIV RHVFLEIDSA LNIGNFTKTY
KTTALPQLHA KLVTLVELLT KPNKDVNKAV NVLQALYEIY IRDFPKVKRT MEQLREDGLM
PLKPVTSREL LFENAVQLPD IADVSFYRQV QRLQTILTSR DSMHNIPRNF EARRRLAFFS
NSLFMNMPHA PPVEKMMAFS VLTPYYNEEV LYSKEQLRTE NEDGISTLFY LQKIYEDDWG
NFIERMRRQG MVGDEEIWTK KLRDLRLWAS YRGQTLSRTV RGMMYYYKAL KMLAFLDSAS
EMEIREGAQK LASVGSVGLD GILNGHSSGI QESSWSLSGA NSDASILFKG HEYGSALMKY
TYVVACQIYG TQKAKKDPRA EDILYLMKCN EALRVAYVDE VHKGRNEVEY YSVLVKYDQQ
LQKEVEIYRV RLPGPLKLGE GKPENQNHAI IFTRGDAVQT IDMNQDNFFE EALKMRNLLE
EYNTYYGIRK PTILGVREHI FTGSVSSLAW FMSAQETSFV TLGQRVLANP LKVRMHYGHP
DVFDRLWFLT RGGISKASRV INISEDIYAG FNCTLRGGNV THHEYIQVGK GRDVGLNQIS
MFEAKVASGN GEQVLSRDVY RLGHRLDFFR MLSFYYSTVG FFFNTMTVIL TVFAFLWGRL
YLALSGLEKA MKNNSNNNKA LGAILNQQFI IQLGLFTALP MIVENSLEHG FLPAVWDFLT
MQFQLASVFY TFSMGTRTHF FGRTILHGGA KYRATGRGFV VQHKSFAENY RLYARSHFVK
AIELGVILTV YASHSVVAKD TFVYIAMSIS SWFLVVSWFM APFVFNPSGF DWLKTVYDFE
DFMNWIWYRG EIFTKAEQSW ETWWYEEQDH LRTTGLWGKL LEIILDLRFF FFQYGIVYQL
GISAGNTAIS VYLLSWIGIV AGVGTYMIIA YAQDKYAAKE HIYYRLVQLL VITVTVLVII
VFLEFTHFQF FDIIACLMAF IPTGWGLISI AQVLRPFLQS TVVWDTVVSL ARLYDMLFGV
IVMAPMALLA WLPGFQSMQT RILFNQAFSR GLQISRILTG KRSNVDL
//
