ID A0A067FCP7_CITSI Unreviewed; 1512 AA.
AC A0A067FCP7;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, 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};
DE Flags: Fragment;
GN ORFNames=CISIN_1g0003851mg {ECO:0000313|EMBL:KDO60986.1};
OS Citrus sinensis (Sweet orange) (Citrus aurantium var. sinensis).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Sapindales; Rutaceae; Aurantioideae; Citrus.
OX NCBI_TaxID=2711 {ECO:0000313|EMBL:KDO60986.1, ECO:0000313|Proteomes:UP000027120};
RN [1] {ECO:0000313|EMBL:KDO60986.1, ECO:0000313|Proteomes:UP000027120}
RP NUCLEOTIDE SEQUENCE.
RG International Citrus Genome Consortium;
RA Gmitter F., Chen C., Farmerie W., Harkins T., Desany B., Mohiuddin M.,
RA Kodira C., Borodovsky M., Lomsadze A., Burns P., Jenkins J., Prochnik S.,
RA Shu S., Chapman J., Pitluck S., Schmutz J., Rokhsar D.;
RL Submitted (APR-2014) 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; KK784929; KDO60986.1; -; Genomic_DNA.
DR STRING; 2711.A0A067FCP7; -.
DR Proteomes; UP000027120; 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; 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:SF16; CALLOSE SYNTHASE 7; 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 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:UP000027120};
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 289..306
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 326..349
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 361..381
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 405..426
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 465..486
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 515..535
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1282..1304
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1453..1475
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 122..240
FT /note="1,3-beta-glucan synthase component FKS1-like"
FT /evidence="ECO:0000259|SMART:SM01205"
FT NON_TER 1512
FT /evidence="ECO:0000313|EMBL:KDO60986.1"
SQ SEQUENCE 1512 AA; 175654 MW; E7F43C63FA89BC25 CRC64;
MELPEIKAAL RALRNVQNLS MPSVTTNAPH DLPEERNKLD ILDWLSSVFG FQKGNVANQR
EHLILLLANM DVRKRDLADY TELRGSTVPK LMDKIFKNYW SWCNYLRCEQ NTRTPPGSDK
QQIQLIYIGL YLLIWGEASN IRFMPECICY IFHKMAEDVY GILFGNVRPV TGDTYHGSQT
AAPDEETFLR TVITPIYQVL RKEAKRNNGG KASHSRWRNY DDLNEYFWSS KCLSLKWPTG
LKEEFSVHSD VVSPAHETPN RVPAGKSKPK TNFVEARTFW HLYRSFDRMW IFFIMAFQAM
VIVAWTPDGS PAALFDEDVF RSVLTIFITQ AFLNLLQAAL DIVLSFNAWW SLKITQILRY
LLKFAVAAAW AVILPICYAS SVQNPTGVVK FFSNLTENWQ NQGSLYNYAV AIYLIPNILA
ALLFFLPQLR RIMERSNSHV VTPFMWWAQP KLYVGRGLHE GMFQLLKYTL FWIMLLICKL
AFSYYVEILP LVGPSKLIMK LHVDNYEWHE FFPNVTHNIG VVIAIWAPIV LVYFMDTQIW
YSIFSTLFGG IHGALSHLGE IRTLGMLRSR FESVPTAFCR RLVPPSDAAK KDRHMDESVH
RRNIANFSHV WNEFIESMRE EDLISNDDRD LLLVPYSSED VSVVQWPPFL LASKIPIALD
MAKDFKEKED ADLFRKIKND EYMLSAVVEC YETLREIIYG LLEDEIDRSI VRQICYDVDI
NIHQHQFLNE FRMSGMPSLS EKLEKFLKLL LSEYESAEVY KSQIINVLQD IMEIILQDIM
VNGYKILERY HMQIQTNDKK EQRFERLNIT LTQNKSWREK VLLVVRLYLL LTVKESAINV
PTNLDARRRI TFFANSLFMN MPSAPKVRDM ISFSVLTPYF KEDVLYSIDE LNQENEDGIT
TLFYLQKIYP DEWTNFQKRI NDPKLNYSED DKNEATRRWV SYRAQTLSRT VRGMMYYKQA
LELQCFLESA GDNAFFGSYQ AMESSQGDER ASAKALADMK FTYVVSCQLY GAQKKSDDLR
DRSCYNNILN LMIKYPSLRV AYIDEREETV NEKSQKFHYS VLLKGGDKYD EEIYRIKLPG
PPTDIGEGKP ENQNHAIIFT RGEALQTIDM NQDNYFEEAF KMRNVLEEFL KSPSGRREPT
ILGLREHIFT GSVSSLAWFM SNQETSFVTI SQRILAYPLR VRFHYGHPDI FDRIFHITRG
GISKASKTIN LSEDIFAGMN STLRGGYITH HEYIQVGKGR DVGMNQISSF EAKVANGNGE
QTLSRDVYRL GRRFDFFRML SFYFTTVGFY LSSMITVLTV YVFLYGRLYM VMSGLEREIL
ENPSIHQSKA LEQALATQSV FQLGLLLVLP MVMEIGLEKG FRSALGDFII MQLQLASVFF
TFQLGTKVHY FGRTILHGGS KYRATGRGFV VFHEKFSENY RLYSRSHFVK GLELVILLVL
YQVYGHSYRS SNLYLFITIS MWFLVGSWLF APFVFNPSGF DWQKTVDDWT DWKRWMGNRG
GIGIQPNRSW ES
//
