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Database: UniProt
Entry: W9S5R0_9ROSA
LinkDB: W9S5R0_9ROSA
Original site: W9S5R0_9ROSA 
ID   W9S5R0_9ROSA            Unreviewed;      1832 AA.
AC   W9S5R0;
DT   14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT   14-MAY-2014, sequence version 1.
DT   24-JAN-2024, entry version 35.
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=L484_020795 {ECO:0000313|EMBL:EXC11740.1};
OS   Morus notabilis.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Rosales; Moraceae; Moreae; Morus.
OX   NCBI_TaxID=981085 {ECO:0000313|EMBL:EXC11740.1, ECO:0000313|Proteomes:UP000030645};
RN   [1] {ECO:0000313|Proteomes:UP000030645}
RP   NUCLEOTIDE SEQUENCE.
RA   He N., Zhao S.;
RT   "Draft Genome Sequence of a Mulberry Tree, Morus notabilis C.K. Schneid.";
RL   Submitted (JAN-2013) 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; KE345702; EXC11740.1; -; Genomic_DNA.
DR   RefSeq; XP_010106773.1; XM_010108471.1.
DR   STRING; 981085.W9S5R0; -.
DR   eggNOG; KOG0916; Eukaryota.
DR   Proteomes; UP000030645; 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:SF22; CALLOSE SYNTHASE 8-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:UP000030645};
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        1400..1421
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1573..1592
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1643..1664
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1676..1693
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1713..1733
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1740..1761
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1781..1802
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          333..449
FT                   /note="1,3-beta-glucan synthase component FKS1-like"
FT                   /evidence="ECO:0000259|SMART:SM01205"
FT   REGION          460..502
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        468..502
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1832 AA;  211837 MW;  8147F77F1443D2AD CRC64;
     MSHEIVVAEP IFYECEPELP KPASSSSITV SSEIVLDQQQ QHQSVPEPFD SERLPQTVAA
     EIQRFLRVAN LVEIDEPRVA FLCRVHAFEI AHNMDKNSSG RGVRQFKTSL LQRLEQDEEP
     TFRRRKEKSD IRELRRVYHE YKEYIVKHGR TFALESRQKL INACAIASVL FEVLKRITFA
     ANPQALADRE SVNSKSEFFV PYNILPLDHG GIQQAIMQLP EVKAAVAAVR NIRGLPSAED
     FQKHGAFTDL FDFLQYCFGF QEGNVANQRE HLILLLANTH IRKAHKQTSS SKIEDVVVDE
     LMKKFFKNYT NWCKFLGRKS NIRLPYVKQE ALQYKLLYLA LHLLIWGEAA NLRFMPECLC
     YIFHEMAWEL HGMLTGAVNP TTWEKVMPAY GGGSESFLNN VVTPIYKVIK EEANKSKNGT
     TDHSTWRNYD DLNEFFWSPD CFQIGWPMRE DHNFFCVNPS SKPKAKKASK STNAEEKREL
     KEEEKDEELG TNREGDQEQK HEQEWLGKSN FVEIRSFWQI FRSFDRMWIF FILSLQAMII
     MACYELESPL QLFDKAVFED VLSIFITSSI LKLIQVGVYL TPSAIDMVLF FVPAVRKYIE
     ISNSKIFTIF SWTQIIPRKR DARKPGLSAE VYFMDTQIWY SVFCTIFGGL YGILHHLGEW
     SYNDMSQIRT LGMLRSRFHT LPSAFNGCLI PPSKNDQKRG KGLFGNRFHK GPENEKNGVA
     KFVLVWNQII SSIRSEDLIS NKEVDLMIIP MLTDLFAGIV RWPIFLIANK FSTALSITKD
     FVGKDETLVR KIKKDKCMYY AVKECYESLK YILEILIVRD LEKRMISTIL NEIEESMARS
     SLLEDFRMTE LPNLQAKFVE LLELLVEGNV DHYGKVVKVL QDIFEIITND MMIDSSRILE
     LLCHSQRMES NEPYFTRTIE PQLFESDCGE NSIHFPLPDS APLTEQIKRL LLLLTIKDTA
     LDIPTNLDAR RRISFFATSL FMTMPSAPKV RNMLSFSVLT PHYMEDVNFS MKELHSSQRE
     VSIIFYMQKI FPDEWKNFLE RMGCASLDGL KDEGKEEDLR KWASFRGQTL SRTVRGMMYY
     REALKLQAFL DMAEDEDILE GYDTAERENH LLAAQLDALA DLKFTYVVSC QRFGSQKAAG
     DPRAQDIIDL MIRYPALRLA YVEEKEVIVE NKPQKVYSSV LLKAVNGFDQ EIYRVKLPGP
     PEIGEGKPEN QNHAIIFTRG EALQTIDMNQ DSYLEEAFKM RNLLQEFLKC QGRRPPTILG
     LREHIFTESV SSLAWFMSYQ ETSFVTIGQR LLAKPLRVRF HYGHPDIFDR IFHITRGGIS
     KASKTINLSE DIFAGFNSTL RRGCITYHEY MQVGKGRDVG LNQISKFEAK VANGNSEQTL
     SRDIYRLGCQ FDFFRMLSCY FTTIGFYFSS LISIIGIYIF LYGQLYLVLS GLQKALLIEA
     RVQNLESLET ALASQSFIQL GLLTGLPMVM EIGLEKGFLT ALKDFVLMQL QLAAVFFTFS
     FGTKTHHYGR TLLHGGAKYR PTGRKVVVFH TSFTENYRLY SRSHFVKGFE LLLLLIVYDL
     FRRSYESSMA YVLITYSVWF MSITWLFAPF LFNPSGFSWG KIVDDWKDWN KWIRQQGGIG
     IQQDKSWHSW WNDEQAHLRH SGIFSRLFEI LLSLRFFMYQ YGLVYHLDIS QHSKNVLVYV
     LSWIVILVVF FFAKAVNIGR QKLSANYQLL FRLFKAILFI TVLAIIITLS RICQLSLRDL
     IVCCLAFLPT GWGLIMIAQA VRPKIEDTGL WDFTRVLAKA YDYGMGVVLF APIAILAWLP
     IISAFQTRFL FNEAFNRHLQ IQPILAGKRK QK
//
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