ID A0A0D2S572_GOSRA Unreviewed; 1539 AA.
AC A0A0D2S572;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 19.
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_012G187400 {ECO:0000313|EMBL:KJB78277.1};
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:KJB78277.1, ECO:0000313|Proteomes:UP000032304};
RN [1] {ECO:0000313|EMBL:KJB78277.1, 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; CM001751; KJB78277.1; -; Genomic_DNA.
DR EnsemblPlants; KJB78277; KJB78277; B456_012G187400.
DR Gramene; KJB78277; KJB78277; B456_012G187400.
DR Proteomes; UP000032304; Chromosome 12.
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 InterPro; IPR026899; FKS1-like_dom1.
DR InterPro; IPR003440; Glyco_trans_48.
DR PANTHER; PTHR12741:SF51; 1,3-BETA-GLUCAN SYNTHASE; 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; 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 Coiled coil {ECO:0000256|SAM:Coils};
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 139..156
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 176..197
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 209..227
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 253..274
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 317..340
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 365..382
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1107..1130
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1273..1295
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1379..1399
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1420..1438
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1483..1502
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1..82
FT /note="1,3-beta-glucan synthase component FKS1-like"
FT /evidence="ECO:0000259|SMART:SM01205"
FT COILED 748..775
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1539 AA; 178794 MW; 0EBA31F0B338721F CRC64;
MPECICYIFH KMADDVNQVF SGDKMIQNPD GSFLSNVIKP IYEILSKEAG KNKGGKASHS
RWSNYDDLNE CFWSGKCSLE LRELIPFTYI YIDLYQFVFF NTVQIFHILE KFTDGWWKSK
INFVEVRTYW QVYRSFDRMW VFFIMALQAM IIVAWTQSGS TSANNEVVLR RVLSIFITYA
ILSFFRAILD VILSIHAWRN SDLTQPLRYI LKLVVAAIWA VVLPVGYSTS VKNPTGPLKF
LNHWARDSHN QSLYNYILVL YMIPDLLAIM LFLLPRLREK MELSDWPVIN IVMWWAQPKL
YVGRGMHVGT FSLLKYTIFW ILVLSVKLAF SYFVEILPLI RPTKVIMKIQ VENYRLHKFV
PNVKHNMGVI IAIWSPIILV YFMDVQVWYT IFSTLLGGVL GAFRHLGEIR TIGMVHSRFE
SISSKFRSCF VPLHSDAVTE TLSTSKEPNE NEYFCCMWNE FIRSMRMEDL ISNRDRELLL
LPPPLANKPG DQLPLFLLAS KIPAAINIAK EFKRKDHAEL EKFIGSDKYT CAAILDCYYT
LKSLIFLLLK DEDDKKIVDE VFHAANGKKL FLQNFNMSGM PLLAVKFEKF LKILMADYGD
EEFKSKITTA LQEIMYIIPE SIDDNSPLKG ALKRDEISHK FKNINTSDIK KNIWSEKVNR
LHLLLTFKES GTDVPLNSEA RRRITFFVNS LFMNMRSAPK VSNMRSFSVL TPHYNEEVVY
SDEELNKENE DGVSTLFYLK TIYPDEWTNF EERMKDKLEE EKKEERRKWV SYRGQTLSRS
VRGMMYYKKA LELQCSMEFT DSISNEEDCI RKQKLPDLKF TYIISCQIYG NLKRSKDPRQ
KDILNLMIMY PSLRVAYIDE VDEALKEKTE GKTEKVYYSV LIKGDTINYS EREIYRIRLP
GSPTKIGEGK PENQNHAIIF TRGEALQTID MNQDNYFEEA FKMRNVLEEF PHSHGAQKPT
ILGLREHVFT GSVSSLAWFM SNQEFSFVTI GQRFLASPLR VRFHYGHPDI FDRIFHITRG
GISKASKTIN LSEDIFAGFN STLRLGSVTH HDYVQVGKGR DVGMNQISIF EAKVANGNGE
QTLTRDVHRL GCHFDFFRML SFYCTTVGFY FNSLVTVLIV YVFLYGRLYM VMTGLEREIL
EDPQIKNNNA LEAALVTQSF IQMGMLLVLP MLMEIGLEKG FRTALGDFFI MQLQLSSVFF
TFQLGTKAHY FGKTILHGGS KYRATGRGFV VRHSKFADNY RLYSRSHFVK ALELGLLLVI
YEVYGESYRS SSLYLFITFS MWFLVGSWLF APFIFNPSGF EWQKTVNDWT DWKWWMGIRG
GVGIQPENSW ESWWDKEQEH LRYTSIRGRV LEILLALRFF VYQYGIVYHL DIAHHSRNLL
VYGLSWCAVL VILIVPKMVS VRRLQMFHMD LQLPLRMLKG LLYLILLAVM IILFKFCGLT
LSDLFASILA FMPTGWAFIL VGQACRPCLH KLLWEPIKEV ARAYDFMMGL LLFTPIAFLS
WLPAVNEFQT RILFNQAFSR GLHISMILAG KKDGGASFN
//
