ID A0A022PQP0_ERYGU Unreviewed; 1869 AA.
AC A0A022PQP0;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 24-JAN-2024, entry version 27.
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=MIMGU_mgv1a000082mg {ECO:0000313|EMBL:EYU18041.1};
OS Erythranthe guttata (Yellow monkey flower) (Mimulus guttatus).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Lamiales; Phrymaceae; Erythranthe.
OX NCBI_TaxID=4155 {ECO:0000313|EMBL:EYU18041.1, ECO:0000313|Proteomes:UP000030748};
RN [1] {ECO:0000313|EMBL:EYU18041.1, ECO:0000313|Proteomes:UP000030748}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. DUN x IM62 {ECO:0000313|Proteomes:UP000030748};
RX PubMed=24225854; DOI=10.1073/pnas.1319032110;
RA Hellsten U., Wright K.M., Jenkins J., Shu S., Yuan Y., Wessler S.R.,
RA Schmutz J., Willis J.H., Rokhsar D.S.;
RT "Fine-scale variation in meiotic recombination in Mimulus inferred from
RT population shotgun sequencing.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:19478-19482(2013).
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; KI632341; EYU18041.1; -; Genomic_DNA.
DR STRING; 4155.A0A022PQP0; -.
DR eggNOG; KOG0916; Eukaryota.
DR Proteomes; UP000030748; 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 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:UP000030748};
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 483..505
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 517..537
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 562..583
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 622..639
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 674..691
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1443..1464
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1484..1506
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1518..1538
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1607..1629
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1713..1734
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1746..1765
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1777..1797
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1818..1838
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 320..436
FT /note="1,3-beta-glucan synthase component FKS1-like"
FT /evidence="ECO:0000259|SMART:SM01205"
SQ SEQUENCE 1869 AA; 214905 MW; DA002DBD4393F14C CRC64;
MASGVNFEHT LSRRPSRSAA MTTFSMEVFD NEVVPSSLQS IAPILRVAKE IQNERPRVAY
LCRFYAFEKA HRLDPNSSGR GVRQFKTSLH QRLDRDNAST LASRVKKTDA REIESFYKQY
YEHYVLALNK GEQADRAQLG KAYQTAGVLF EVLCAVNKTE KVEEVAPEIM AAANDVQAKK
EIYSPYNILP LDSAGASQSI MQLDEVKASV SALRNTVGLA WPSSFEQTRQ KAGELDILDW
LRAMFGFQRD NVRNQREHLI LLLANIHTRL VPKPEPQNKL DDRAADALMN KLFKNYKSWC
KYLGRKHSLR LPQAQQEVQQ RKILYMGLYL LIWGEAANVR FMPECLCYIF HNMAYELHGL
LAGNVSIVTG ENIKPSYGGD DESFLRKVIT PIYRVIEKEA KKGKNGKAPH IAWCNYDDLN
EYFWSSDCFS LGWPMRDDGE FFKSVREVPQ GKRAHQKKPG KLGKSYFAET RTLWHTFRSF
DRLWTFLILA LQVSVLDLIL NFPGYLRWKI TDVLRNFLKI IVSLAWSIIL PMCYVSQNNS
PSFSKIKDML PFLNKMKGAS SLYIVVVAVY LLPNLLAAVL FIFPMLRRWI ENSDWLIIRF
LLWWSQPRIY VGRGMHESQF SLLKYTLFWV LLLCSKFAFD YFMMIKPLVK PTQDIMDINH
VDYAWHEFLP NAKHNYGAVV ALWAPVILVY FMDTQIFYAI FSTLYGGFIG AFDRLGEIRT
LGMLRSRFQS LPGAFNAHLV PSNKARKRGY SLSKQSKEVN ESRRCEAAKF AQLWNETGAK
LGIIYLREMD LLLVPYSSDP SLKLIQWPPF LLASKIPIAL DMAAQFKSKD ADLWKRICAD
EYMKCAVIEC YESFKLVLNA LIVGETEKRI IGIIIKEVES NITKNTLLTN FRMRSLPDLC
KKFVELVEIL KDSDPSKKDR VVLLLQDMLE VVSRDMMVNE IRELAEVGQG SKDSAKQLFA
NIVFPPPNTA QWDEQIRRLY LLLTVKESAI DVPTNLEARR RIAFFTNSLF MYMPRAPRVR
KMLSFSVMTP YYSEETVYSK SDLEMENEDG VSIIYYLQKI YPDEWNNFVE RLNCKVSEIW
ENEEKILQLR HWASLRGQTL SRTIRGMMYY RRALKLQAFL DMATEDEILE GYKTIIEPSA
EDKKSQRSVY TQLEAVADMK FTYVATCQNY GNQKLSGDRR ATDILNLMVN NPSLRVAYID
EVEERESGKN QKVYYSVLVK AVDNLDQEIY RIKLPGSAKV GEGKPENQNH AIIFTRGEAL
QTIDMNQDNY LEEAFKMRNL LEEFNEDHGV RSPTILGVRE HIFTGSVSSL AWFMSNQETS
FVTIGQRVLA RPLKVRFHYG HPDVFDRIFH ITRGGISKAS RGINLSEDIF AGFNSTLRRG
NITHHEYIQV GKGRDVGLNQ ISLFEAKVAC GNGEQTLSRD IYRLGHRFDF FRMLSCYYTT
TGFYVSSMLV VLTVYAYLYG KLYLSLSGLE KTIVRHARAR GDDALTAVMA SQSIVQLGIL
MTLPMVMEIG LERGFTTAAG DVIIMQLQLA AVFFTFSLGT KLHYFGRTVL HGGAKYRATG
RGFVVRHEKF AENYRMYSRS HFTKALELMI LLIVYHAYGT ATPNSKAYLF LTFSMWFLVI
SWLFSPFLFN PSGFEWQKIV EDLEDWTKWI SNHGGIGVPA TKSWESWWDE EQEHLQYTGF
SGRFWEIVLS LRFFLYQYGV VYQLHVTQND KSIVVYGLSW LVIVAVVIIL KIVSMGRKKF
SADFQLMFRL LKLFLFIAFI IGLIISIKFL ELTIGDIFAS LLGFLPTGWA LLLIAQACRP
ITKGLGMWGS VKALARGYEY LMGFVIFAPV AILAWFPFVS EFQTRLLFNQ AFSRGLQIQR
ILAGGKKNK
//