ID A0A0D2VLH1_GOSRA Unreviewed; 1917 AA.
AC A0A0D2VLH1;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-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 ORFNames=B456_011G119900 {ECO:0000313|EMBL:KJB71385.1};
OS Gossypium raimondii (New World cotton).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Malvoideae; Gossypium.
OX NCBI_TaxID=29730 {ECO:0000313|EMBL:KJB71385.1, ECO:0000313|Proteomes:UP000032304};
RN [1] {ECO:0000313|EMBL:KJB71385.1, ECO:0000313|Proteomes:UP000032304}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23257886; DOI=10.1038/nature11798;
RA Paterson A.H., Wendel J.F., Gundlach H., Guo H., Jenkins J., Jin D.,
RA Llewellyn D., Showmaker K.C., Shu S., Udall J., Yoo M.J., Byers R.,
RA Chen W., Doron-Faigenboim A., Duke M.V., Gong L., Grimwood J., Grover C.,
RA Grupp K., Hu G., Lee T.H., Li J., Lin L., Liu T., Marler B.S., Page J.T.,
RA Roberts A.W., Romanel E., Sanders W.S., Szadkowski E., Tan X., Tang H.,
RA Xu C., Wang J., Wang Z., Zhang D., Zhang L., Ashrafi H., Bedon F.,
RA Bowers J.E., Brubaker C.L., Chee P.W., Das S., Gingle A.R., Haigler C.H.,
RA Harker D., Hoffmann L.V., Hovav R., Jones D.C., Lemke C., Mansoor S.,
RA ur Rahman M., Rainville L.N., Rambani A., Reddy U.K., Rong J.K.,
RA Saranga Y., Scheffler B.E., Scheffler J.A., Stelly D.M., Triplett B.A.,
RA Van Deynze A., Vaslin M.F., Waghmare V.N., Walford S.A., Wright R.J.,
RA Zaki E.A., Zhang T., Dennis E.S., Mayer K.F., Peterson D.G., Rokhsar D.S.,
RA Wang X., Schmutz J.;
RT "Repeated polyploidization of Gossypium genomes and the evolution of
RT spinnable cotton fibres.";
RL Nature 492:423-427(2012).
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; CM001750; KJB71385.1; -; Genomic_DNA.
DR STRING; 29730.A0A0D2VLH1; -.
DR EnsemblPlants; KJB71385; KJB71385; B456_011G119900.
DR Gramene; KJB71385; KJB71385; B456_011G119900.
DR eggNOG; KOG0916; Eukaryota.
DR OMA; WYYMAAN; -.
DR Proteomes; UP000032304; Chromosome 11.
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:UP000032304};
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 482..499
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 549..570
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 597..618
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 657..678
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1484..1507
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1648..1672
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1722..1741
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1761..1781
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1801..1819
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1866..1886
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 321..437
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 1917 AA; 220020 MW; B9D78486E6030EF9 CRC64;
MANAETGPQG LTRRPSRSAS TTTFSTEVFD NEVVPSSLSS SITPILRIAK EIELERPRVA
YLCRLYAFDK ADRLDPNSTG RGVRQFKTGL RQRLERDDAS SLASRVEKSD AGEIGSYYKQ
YYEHYVTALD QGDKADRAQL EKAYQTAGVL FEVLCAVNNT EKVEEVAPEI MATAKDVQEK
KEIYTPYNIL PLDAAGASQS IMQLEEVKAS VVALGNIRGL NWPSGFDPQR QKAGDLDLLD
WLRAMFGFQR DNVRNMREHL ILLLANNHIR LHPKPKPLTM LDERAVDAVM SKLFKNYKTW
CKFLGRKHSL RLPQGSQEIQ QRKILYMGLY LLIWGEAANV RFMPECLCYI FHNMAHELHG
LLAGNVSIVT GENIKPSYGG DDEAFLRKVV KPIYCVIERE AGKNKNGTAS HADWCNYDDL
NEYFWSSDCF SLGWPMRDDG DFFKSTRDTG KKTSRRKCRS TGKSNFVEIR TFWHLFRSFD
RLWTFYILGL QVMIIIAWSG ASLTEIFQKD LLYDISSIFI TAAILRFIQS VLDLAINFPG
YHRWRFTDVL RNVLKIVVSI AWVIILPLFY VRELSFVPEN VKDMLSFLNQ VKGVSPLYVM
AVALYLLPNL LTAALFIFPM LRRWIENSDW HIIRLLLWWS QPRVYVGRGI HESQFALIKY
TLFWLILLCA KFAFSYFVQI KPLVQPTKDI MSIHRVKYAW HEFFPNAENH LGVVSLWAPV
VLVYFMDTQI WYSIFSTIYG GVSGAFDRLG EIRTLGMLRS RFQSLPGAFN AYLVPTDKSR
KRGFSLSKRF AKVTANRRSE AAKFAQLWNE VICSFREEDL ISDRKMDLLL VPYTSDPSLK
LIQWPPFLLA SKIPIALDMA AQFRSKDSEL WKRICADEYM KCAVTECFES FKLVLNTLVV
GENEKRTIRI IIMEIESNIS KNTLLANFRM APLPVLWKKF VELVGILKDG DPSKKDAVVF
LLQDMLEVVT RDMMVNEIRE LVELGHSNKE SGRQLFAGTE EKPALVFPPV LTAHWVEQIR
RLHILLTIKE SGIDIPSNLE ARRRIAFFAN SLFMDMPRAP RVRNMLSFSV LTPYYSEETV
YSKTELEMEN EDGVSIIFYL QKIFPDEWNN FTERLNCKES EIWENDEKIL QLRHWVSLRG
QTLCRTVRGM MYYRRALKIQ AFLDMATENE ILEGYKAILT APDEDKRSQK SLYAQLEAVA
DLKFTYVATC QNYGNQKRNG DRRATDILNL MVNNPSLRVA YIDEVEEREG GRAQKVCYSV
LVKGVDSLDQ ELYRIKLPGN AKLGEGKPEN QNHALIFTRG EALQTIDMNQ DNYLEEAFKM
RNLLEEFNED HGVRPPTILG VREHIFTGSV SSLAWFMSNQ ETSFVTIGQR VLARPLKVRF
HYGHPDVFDR IFHITRGGIS KGSRGINLSE DIFAGFNSTL RRGNITHHEY IQVGKGRDVG
LNQISLFEAK VACGNGEQTL SRDIYRLGHR FDFFRMLSCY FTTVGFYFSS MLVVFTVYFF
LYGRLYLSLS GLEQAILKYA SAKGNDSLKA AMASQSIVQL GVLTVLPMVM EIGLERGFRT
ALGDIIIMQL QLASVFFTFS LGTRVHYFGR TILHGGAKYR ATGRGFVVRH EKFAENYRLY
SRSHFVKGLE LMVLLICYKI YGSAASGAVS YALLSFSMWF LVLSWLFAPF LLNPSGFEWQ
KIVEDWEDWS KWISCRGGIG VPSVKSWESW WEEEQEHLRH TGFMGCLVEI ILSIRFFIYQ
YGIVYHLNMT TSIRQGIRQS IVVYCLSWLV IVGVLIILKI VSMGRMKFSA DFQLMFRLVK
LVMFVGSIVT IAMLFYFLDL TIGDIFQSIL AFVPTGWALL QISQACRTVV KGIGMWGSVK
ALARGYEYMM GVLLFAPITI LAWFPFVSEF QTRLLFNQAF SRGLQIQRIL AGSKMQA
//
