ID A0A2H5PX03_CITUN Unreviewed; 1892 AA.
AC A0A2H5PX03;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 24-JAN-2024, entry version 21.
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=CUMW_175300 {ECO:0000313|EMBL:GAY56882.1};
OS Citrus unshiu (Satsuma mandarin) (Citrus nobilis var. unshiu).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Sapindales; Rutaceae; Aurantioideae; Citrus.
OX NCBI_TaxID=55188 {ECO:0000313|EMBL:GAY56882.1, ECO:0000313|Proteomes:UP000236630};
RN [1] {ECO:0000313|EMBL:GAY56882.1, ECO:0000313|Proteomes:UP000236630}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Miyagawa wase {ECO:0000313|Proteomes:UP000236630};
RX PubMed=29259619; DOI=10.3389/fgene.2017.00180;
RA Shimizu T., Tanizawa Y., Mochizuki T., Nagasaki H., Yoshioka T., Toyoda A.,
RA Fujiyama A., Kaminuma E., Nakamura Y.;
RT "Draft sequencing of the heterozygous diploid genome of Satsuma (Citrus
RT unshiu Marc.) using a hybrid assembly approach.";
RL Front. Genet. 8:180-180(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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GAY56882.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BDQV01000148; GAY56882.1; -; Genomic_DNA.
DR STRING; 55188.A0A2H5PX03; -.
DR Proteomes; UP000236630; 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; 2.
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:UP000236630};
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 581..600
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 612..631
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 652..672
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 692..717
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 756..777
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 808..826
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1560..1579
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1661..1682
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1736..1756
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1776..1795
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1841..1861
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 418..534
FT /note="1,3-beta-glucan synthase component FKS1-like"
FT /evidence="ECO:0000259|SMART:SM01205"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 33..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..58
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1892 AA; 216644 MW; 5ED66D2C47E6FFE5 CRC64;
MLIIQNKQNN RRKNQKRHPR SELLRRKEAI KKGIKQTHNP SPQRNGHSHP SRVSCTLSSP
LGPRTWQINK TNYRFSLRLV SSRLAPEAIL IRSFIFCSGL LLNLDQAVTY PAVGRKCRIW
MRADDGGRRE CCAMTTILNG IPSSLGSIAP ILRIATEVES ERPRVAYLCR FYAFEKAHRL
DPSSSGRGVR QFKTSLLQRL ERDNASSLAS RVKKTDAREI QSYYQQYYEH YVRALDQGEQ
ADRAQLGKAY QTAGVLFEVL CAVNKTEKVE EVAPEIIAAA RDVQEKKEIY SPYNILPLDA
AGASQSIMQL EEVKAAVAAL WNTRGLNWPA SFEPQRQKSG DLDLLDWLRA INQREHLILL
LANSHIRLHP KPEPLNKLDE RALDAVMSKL FKNYKTWCKF LGRKHSLRLP QGPQEIQQRK
MLYMGLYLLI WGEAANIRFM PECLCYIFHN MAYELHGLLA GNVSIVTGEN IKPSYGGDDE
AFLRKVVTPI YRVIETEAKK NKDGNAANSD WCNYDDLNEY FWSSDCFSLG WPMRDDGDFF
KSTRNKGQGR KAVQRKSGST GKSNFVEMRS FWHLFRSFDR LWTFYILALQ AMLIAGFQNI
SPMELFEIDS LYALSSIFIT AAFLRLLQSL LDLILNFPGY HRWRFSDVLR NVLKLIVSLA
WVIVLPICYV QSSNYSPVDV KGILPFLPKQ SGIPPLYLLA VALYLLPNLL AACLFLFPML
RRWIENSDWH IIRLLLWWSQ PRIYVGRGMH ESQFSLIKYT LFWVVLLCSK VAFSYYMQIK
PLVKPTKDIM NIKRIKYTWH EFFPEGSGNY GAIFSLWLPM ILIYFMDSQI WYSIYSTLCG
GVIGAFDRLG EIRTLGMLRS RFQSLPGAFN TYLVPSDKTP KRGFSFSKKF AEVTASRRSE
AAKFAQLWNE VICSFREEDL INPSLKIIQW PPFLLASKIP IALDMAAQFR SRDSDLWKRI
CADEYMKCAV IECYETFKIV LNALVVGENE KRIINIIIKE IESNISKNTF LANFRMGPLP
TLCKKVVELV AILKDADPSK KDTVVLLLQD MLEVVTRDMM VNEIRELVEL GHSNKESGRQ
LFAGTDARPA IMFPPVGTAQ WEEQIRRFHL LLTVKESAID VPTNLEARRR ITFFSNSLFM
DMPRAPRVRK MLSFSVLTPY YSEETVYSRA DLELENEDGV SIIYYLQKIF PDEWNNFMER
LNCKKESEVW ENDENILQLR HWVSLRGQTL CRTVRGMMYY RRALKLQAFL DMASETEILE
GYKAITIPSE EEKKSQRSLY AQLEAVADMK FTYVATCQIY GNQKRNGDRR ATDILNLMVN
NPSLRVAYID EVEEREGGKV QKVYYSVLVK AVDNLDQEIY RIKLPGAVKL GEGKPENQNH
AVIFTRGEAL QAIDMNQDNY LEEAFKMRNL LEEFNEDHGV RPPTILGVRE HIFTGSVSSL
AWFMSNQETS FVTIGQRVLA RPLKVRFHYG HPDVFDRIFH ITRGGMSKAS RNVNLSEDIF
AGFNSVLRRG NVTHHEYIQV GKGRDVGLNQ ISLFEAKVAC GNGEQTLSRD IYRLGHRFDF
FRMMSFYFTT IGSYLSSLLK FAETRKDDPL KAVMGSTVPC SIRSFDDLSH VHGDGTGERV
QICIGLIILG ALCCMVEQSI EQLVVVLWYA HVKFAETIGC IQGVTFVKGL EIMILLICYS
VYGFEWQNSD DWMTGKSGLA AGEELVCQQT RAGILYGIVY QLNLTKSSEA GEDLSIIVYG
MSWLVIFALM IILKIVSLGR KKFSADFQLM FRLLKLVLFL AFTVTLVLMF LFLNLKVGDL
LQSLLAYLPT GWALLQIAQA CRPIVKGLGM WGSVKAIARG YEYLMGLVIF VPVGVLAWFP
FVSEFQTRLL FNQAFSRGLQ IQRILAGGKK QN
//
